User:ProteinBoxBot/PBB Log Wiki 11-8-2007-B3-1

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Contents 1 Log file for Protein Box Bot 2 Protein Status Quick Log - Date: 23:26, 18 November 2007 (UTC) 2.1 Proteins without matches (16) 2.2 Proteins with a High Potential Match (1) 2.3 Redirected Proteins (8) 2.4 Manual Inspection (Page not found) (17) 2.5 Updated (8) 3 Protein Status Grid - Date: 23:26, 18 November 2007 (UTC) 4 Vebose Log - Date: 23:26, 18 November 2007 (UTC) 4.1 BACE2 4.2 DFFA 4.3 ECE1 4.4 EEF1D 4.5 GABRA1 4.6 GAD1 4.7 GAP43 4.8 GLI3 4.9 GLRX 4.10 HIST2H3C 4.11 HTR4 4.12 ID3 4.13 ITGAX 4.14 KIR3DL1 4.15 KLK2 4.16 LAMC1 4.17 MAP3K11 4.18 MSX1 4.19 MSX2 4.20 MT2A 4.21 OAS1 4.22 RAPGEF1 4.23 TACSTD1 4.24 TBK1 4.25 TNFRSF9

[edit] Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

[edit] Protein Status Quick Log - Date: 23:26, 18 November 2007 (UTC)

[edit] Proteins without matches (16)

KIR3DL1	ITGAX	MSX2	DFFA	HIST2H3C
GAP43	GLI3	ID3	TBK1	MT2A
GAD1	TACSTD1	GLRX	ECE1	BACE2
LAMC1

[edit] Proteins with a High Potential Match (1)

TNFRSF9

[edit] Redirected Proteins (8)

MSX1	MAP3K11	GABRA1	KLK2	EEF1D
RAPGEF1	OAS1	HTR4

[edit] Manual Inspection (Page not found) (17)

KIR3DL1	ITGAX	MSX2	DFFA	HIST2H3C
GAP43	GLI3	ID3	TBK1	MT2A
GAD1	TACSTD1	GLRX	ECE1	BACE2
LAMC1	TNFRSF9

[edit] Updated (8)

MSX1	MAP3K11	GABRA1	KLK2	EEF1D
RAPGEF1	OAS1	HTR4

[edit] Protein Status Grid - Date: 23:26, 18 November 2007 (UTC)

HUGO Symbol	Action Summary	Target page(s)	WP Symbol Search
KIR3DL1	Manual Inspection (Page not found)	Other Pages: Killer cell immunoglobulin-like receptor (Unknown Data); KIR3DL1 (No Data); KIR (DisAmbig); Kir (Redirect -> KIR); AMB11 (No Data); Amb11 (No Data); CD158E1 (No Data); Cd158e1 (No Data); CD158E2 (No Data); Cd158e2 (No Data); CL-11 (No Data); Cl-11 (No Data); CL-2 (No Data); Cl-2 (No Data); KIR-G1 (No Data); Kir-g1 (No Data); KIR3DS1 (No Data); Kir3ds1 (No Data); MGC119726 (No Data); Mgc119726 (No Data); MGC119728 (No Data); Mgc119728 (No Data); MGC126589 (No Data); Mgc126589 (No Data); MGC126591 (No Data); Mgc126591 (No Data); NKAT10 (No Data); Nkat10 (No Data); NKAT3 (No Data); Nkat3 (No Data); NKB1 (No Data); Nkb1 (No Data); NKB1B (No Data); Nkb1b (No Data);	[1]
ITGAX	Manual Inspection (Page not found)	Other Pages: Integrin (Unknown Data); ITGAX (No Data); CD11C (No Data); Cd11c (No Data);	[2]
MSX2	Manual Inspection (Page not found)	Other Pages: Msh homeobox 2 (No Data); MSX2 (DisAmbig); CRS2 (No Data); Crs2 (No Data); FPP (DisAmbig); Fpp (Redirect -> FPP); HOX8 (No Data); Hox8 (No Data); MSH (DisAmbig); Msh (No Data); PFM (DisAmbig); Pfm (No Data); PFM1 (No Data); Pfm1 (No Data);	[3]
MSX1	Updated	Other Pages: Msh homeobox 1 (No Data); MSX1 (Good Codes + Entrez Match); HOX7 (No Data); Hox7 (No Data); HYD1 (No Data); Hyd1 (No Data);	[4]
DFFA	Manual Inspection (Page not found)	Other Pages: DNA fragmentation factor (No Data); DFFA (No Data); DFF-45 (No Data); Dff-45 (No Data); DFF1 (No Data); Dff1 (No Data); ICAD (Unknown Data); Icad (No Data);	[5]
HIST2H3C	Manual Inspection (Page not found)	Other Pages: Histone cluster 2 (No Data); HIST2H3C (No Data); H3 (DisAmbig); H3.2 (No Data); H3F2 (No Data); H3f2 (No Data); H3FM (No Data); H3fm (No Data); MGC9629 (No Data); Mgc9629 (No Data);	[6]
GAP43	Manual Inspection (Page not found)	Other Pages: Growth associated protein 43 (No Data); GAP43 (No Data); B-50 (Redirect -> B50); PP46 (No Data); Pp46 (No Data); B50 (DisAmbig);	[7]
GLI3	Manual Inspection (Page not found)	Other Pages: GLI-Kruppel family member GLI3 (No Data); GLI3 (No Data); ACLS (DisAmbig); Acls (No Data); GCPS (Redirect -> Greig cephalopolysyndactyly syndrome); Gcps (No Data); PAP-A (No Data); Pap-a (No Data); PAPA (Redirect -> Professional and Amateur Pinball Association); Papa (DisAmbig); PAPA1 (No Data); Papa1 (No Data); PAPB (Unknown Data); Papb (No Data); PHS (DisAmbig); Phs (No Data); PPDIV (No Data); Ppdiv (No Data); Greig cephalopolysyndactyly syndrome (Unknown Data); Professional and Amateur Pinball Association (Unknown Data);	[8]
MAP3K11	Updated	Other Pages: Mitogen-activated protein kinase kinase kinase 11 (No Data); MAP3K11 (Good Codes + Entrez Match); MGC17114 (No Data); Mgc17114 (No Data); MLK-3 (No Data); Mlk-3 (No Data); MLK3 (No Data); Mlk3 (No Data); PTK1 (No Data); Ptk1 (No Data); SPRK (No Data); Sprk (No Data);	[9]
ID3	Manual Inspection (Page not found)	Other Pages: Inhibitor of DNA binding 3 (No Data); ID3 (Unknown Data); HEIR-1 (No Data); Heir-1 (No Data);	[10]
GABRA1	Updated	Other Pages: Gamma-aminobutyric acid A receptor (No Data); GABRA1 (Good Codes + Entrez Match); EJM (No Data); Ejm (No Data);	[11]
TBK1	Manual Inspection (Page not found)	Other Pages: TANK-binding kinase 1 (No Data); TBK1 (No Data); FLJ11330 (No Data); Flj11330 (No Data); NAK (Redirect -> Negative-acknowledge character); Nak (Redirect -> Negative-acknowledge character); T2K (Unknown Data); T2k (No Data); Negative-acknowledge character (Unknown Data);	[12]
MT2A	Manual Inspection (Page not found)	Other Pages: Metallothionein 2A (No Data); MT2A (No Data); MT2 (Redirect -> Wangan Midnight Maximum Tune); Mt2 (No Data); Wangan Midnight Maximum Tune (Unknown Data);	[13]
GAD1	Manual Inspection (Page not found)	Other Pages: Glutamate decarboxylase 1 (No Data); GAD1 (No Data); FLJ45882 (No Data); Flj45882 (No Data); GAD (Redirect -> Gad); Gad (DisAmbig); SCP (DisAmbig); Scp (Redirect -> SCP);	[14]
TACSTD1	Manual Inspection (Page not found)	Other Pages: Tumor-associated calcium signal transducer 1 (No Data); TACSTD1 (No Data); CD326 (No Data); Cd326 (No Data); CO17-1A (No Data); Co17-1a (No Data); EGP (DisAmbig); Egp (No Data); EGP40 (No Data); Egp40 (No Data); Ep-CAM (No Data); Ep-cam (No Data); GA733-2 (No Data); Ga733-2 (No Data); KSA (Redirect -> Saudi Arabia); Ksa (No Data); M4S1 (No Data); M4s1 (No Data); MIC18 (No Data); Mic18 (No Data); MK-1 (No Data); Mk-1 (No Data); TROP1 (No Data); Trop1 (No Data); HEGP-2 (No Data); Hegp-2 (No Data); Saudi Arabia (Unknown Data);	[15]
GLRX	Manual Inspection (Page not found)	Other Pages: Glutaredoxin (Unknown Data); GLRX (No Data); GRX (No Data); Grx (No Data); GRX1 (No Data); Grx1 (No Data); MGC117407 (No Data); Mgc117407 (No Data);	[16]
KLK2	Updated	Other Pages: Kallikrein-related peptidase 2 (No Data); KLK2 (Good Codes + Entrez Match); KLK2A2 (No Data); Klk2a2 (No Data); MGC12201 (No Data); Mgc12201 (No Data); HK2 (No Data); Hk2 (No Data);	[17]
ECE1	Manual Inspection (Page not found)	Other Pages: Endothelin converting enzyme 1 (No Data); ECE1 (No Data); ECE (DisAmbig); Ece (No Data);	[18]
EEF1D	Updated	Other Pages: Eukaryotic translation elongation factor 1 delta (No Data); EEF1D (Good Codes + Entrez Match); EF-1D (No Data); Ef-1d (No Data); FLJ20897 (No Data); Flj20897 (No Data); FP1047 (No Data); Fp1047 (No Data);	[19]
BACE2	Manual Inspection (Page not found)	Other Pages: Beta-site APP-cleaving enzyme 2 (No Data); BACE2 (Unknown Data); AEPLC (No Data); Aeplc (No Data); ALP56 (No Data); Alp56 (No Data); ASP1 (No Data); Asp1 (No Data); ASP21 (No Data); Asp21 (No Data); BAE2 (No Data); Bae2 (No Data); CDA13 (No Data); Cda13 (No Data); CEAP1 (No Data); Ceap1 (No Data); DRAP (No Data); Drap (Unknown Data);	[20]
RAPGEF1	Updated	Other Pages: Rap guanine nucleotide exchange factor 1 (No Data); RAPGEF1 (Good Codes + Entrez Match); C3G (No Data); C3g (No Data); DKFZp781P1719 (No Data); Dkfzp781p1719 (No Data); GRF2 (No Data); Grf2 (No Data);	[21]
OAS1	Updated	Other Pages: 2',5'-oligoadenylate synthetase 1 (No Data); OAS1 (Good Codes + Entrez Match); IFI-4 (No Data); Ifi-4 (No Data); OIAS (No Data); Oias (No Data); OIASI (No Data); Oiasi (No Data);	[22]
LAMC1	Manual Inspection (Page not found)	Other Pages: Laminin (Unknown Data); LAMC1 (No Data); LAMB2 (No Data); Lamb2 (No Data); MGC87297 (No Data); Mgc87297 (No Data);	[23]
TNFRSF9	Manual Inspection (Page not found)	Other Pages: Tumor necrosis factor receptor superfamily (Redirect -> CD120); TNFRSF9 (No Data); 4-1BB (No Data); 4-1bb (No Data); CD137 (Protein Template); Cd137 (No Data); CDw137 (No Data); Cdw137 (No Data); ILA (Redirect -> Ila); Ila (DisAmbig); MGC2172 (No Data); Mgc2172 (No Data); CD120 (Codes Found, but no match[skip]);	[24]
HTR4	Updated	Other Pages: 5-hydroxytryptamine receptor 4 (No Data); HTR4 (Good Codes + Entrez Match); 5-HT4 (Redirect -> 5-HT receptor#Families); 5-ht4 (No Data); 5-HT4R (No Data); 5-ht4r (No Data); 5-HT receptor#Families (Unknown Data);	[25]

[edit] Vebose Log - Date: 23:26, 18 November 2007 (UTC)

[edit] BACE2

• INFO: Beginning work on BACE2... {November 18, 2007 3:16:34 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:17:36 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_BACE2_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ewy.
 | PDB = {{PDB2|2ewy}}
 | Name = Beta-site APP-cleaving enzyme 2
 | HGNCid = 934
 | Symbol = BACE2
 | AltSymbols =; AEPLC; ALP56; ASP1; ASP21; BAE2; CDA13; CEAP1; DRAP
 | OMIM = 605668
 | ECnumber =  
 | Homologene = 22696
 | MGIid = 1860440
 | GeneAtlas_image1 = PBB_GE_BACE2_217867_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0004194 |text = pepsin A activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} {{GNF_GO|id=GO:0009049 |text = aspartic-type signal peptidase activity}} 
 | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006509 |text = membrane protein ectodomain proteolysis}} {{GNF_GO|id=GO:0009306 |text = protein secretion}} {{GNF_GO|id=GO:0016486 |text = peptide hormone processing}} {{GNF_GO|id=GO:0042985 |text = negative regulation of amyloid precursor protein biosynthetic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 25825
    | Hs_Ensembl = ENSG00000182240
    | Hs_RefseqProtein = NP_036237
    | Hs_RefseqmRNA = NM_012105
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 41462061
    | Hs_GenLoc_end = 41569619
    | Hs_Uniprot = Q9Y5Z0
    | Mm_EntrezGene = 56175
    | Mm_Ensembl = ENSMUSG00000040605
    | Mm_RefseqmRNA = NM_019517
    | Mm_RefseqProtein = NP_062390
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 97461672
    | Mm_GenLoc_end = 97543922
    | Mm_Uniprot =  
  }}
}}
'''Beta-site APP-cleaving enzyme 2''', also known as '''BACE2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BACE2 beta-site APP-cleaving enzyme 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25825| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Cerebral deposition of amyloid beta peptide is an early and critical feature of Alzheimer's disease and a frequent complication of Down syndrome. Amyloid beta peptide is generated by proteolytic cleavage of amyloid precursor protein by 2 proteases, one of which is the protein encoded by this gene. This gene localizes to the 'Down critical region' of chromosome 21. The encoded protein, a member of the peptidase A1 protein family, is a type I integral membrane glycoprotein and aspartic protease. Three transcript variants encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: BACE2 beta-site APP-cleaving enzyme 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25825| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Aplin AE, Gibb GM, Jacobsen JS, ''et al.'' |title=In vitro phosphorylation of the cytoplasmic domain of the amyloid precursor protein by glycogen synthase kinase-3beta. |journal=J. Neurochem. |volume=67 |issue= 2 |pages= 699-707 |year= 1996 |pmid= 8764598 |doi=  }}
*{{cite journal  | author=Yan R, Bienkowski MJ, Shuck ME, ''et al.'' |title=Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity. |journal=Nature |volume=402 |issue= 6761 |pages= 533-7 |year= 1999 |pmid= 10591213 |doi= 10.1038/990107 }}
*{{cite journal  | author=Sadik G, Kaji H, Takeda K, ''et al.'' |title=In vitro processing of amyloid precursor protein by cathepsin D. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 11 |pages= 1327-37 |year= 2000 |pmid= 10605825 |doi=  }}
*{{cite journal  | author=Hussain I, Powell D, Howlett DR, ''et al.'' |title=Identification of a novel aspartic protease (Asp 2) as beta-secretase. |journal=Mol. Cell. Neurosci. |volume=14 |issue= 6 |pages= 419-27 |year= 2000 |pmid= 10656250 |doi= 10.1006/mcne.1999.0811 }}
*{{cite journal  | author=Lin X, Koelsch G, Wu S, ''et al.'' |title=Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 4 |pages= 1456-60 |year= 2000 |pmid= 10677483 |doi=  }}
*{{cite journal  | author=Acquati F, Accarino M, Nucci C, ''et al.'' |title=The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region. |journal=FEBS Lett. |volume=468 |issue= 1 |pages= 59-64 |year= 2000 |pmid= 10683441 |doi=  }}
*{{cite journal  | author=Bennett BD, Babu-Khan S, Loeloff R, ''et al.'' |title=Expression analysis of BACE2 in brain and peripheral tissues. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20647-51 |year= 2000 |pmid= 10749877 |doi= 10.1074/jbc.M002688200 }}
*{{cite journal  | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal  | author=Xin H, Stephans JC, Duan X, ''et al.'' |title=Identification of a novel aspartic-like protease differentially expressed in human breast cancer cell lines. |journal=Biochim. Biophys. Acta |volume=1501 |issue= 2-3 |pages= 125-37 |year= 2000 |pmid= 10838186 |doi=  }}
*{{cite journal  | author=Farzan M, Schnitzler CE, Vasilieva N, ''et al.'' |title=BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9712-7 |year= 2000 |pmid= 10931940 |doi= 10.1073/pnas.160115697 }}
*{{cite journal  | author=Iijima K, Ando K, Takeda S, ''et al.'' |title=Neuron-specific phosphorylation of Alzheimer's beta-amyloid precursor protein by cyclin-dependent kinase 5. |journal=J. Neurochem. |volume=75 |issue= 3 |pages= 1085-91 |year= 2000 |pmid= 10936190 |doi=  }}
*{{cite journal  | author=Solans A, Estivill X, de La Luna S |title=A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein beta-secretase. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 3-4 |pages= 177-84 |year= 2000 |pmid= 10965118 |doi=  }}
*{{cite journal  | author=Hussain I, Powell DJ, Howlett DR, ''et al.'' |title=ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site. |journal=Mol. Cell. Neurosci. |volume=16 |issue= 5 |pages= 609-19 |year= 2001 |pmid= 11083922 |doi= 10.1006/mcne.2000.0884 }}
*{{cite journal  | author=Hussain I, Christie G, Schneider K, ''et al.'' |title=Prodomain processing of Asp1 (BACE2) is autocatalytic. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23322-8 |year= 2001 |pmid= 11316808 |doi= 10.1074/jbc.M101069200 }}
*{{cite journal  | author=Yan R, Munzner JB, Shuck ME, Bienkowski MJ |title=BACE2 functions as an alternative alpha-secretase in cells. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 34019-27 |year= 2001 |pmid= 11423558 |doi= 10.1074/jbc.M105583200 }}
*{{cite journal  | author=Grüninger-Leitch F, Schlatter D, Küng E, ''et al.'' |title=Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4687-93 |year= 2002 |pmid= 11741910 |doi= 10.1074/jbc.M109266200 }}
*{{cite journal  | author=Turner RT, Loy JA, Nguyen C, ''et al.'' |title=Specificity of memapsin 1 and its implications on the design of memapsin 2 (beta-secretase) inhibitor selectivity. |journal=Biochemistry |volume=41 |issue= 27 |pages= 8742-6 |year= 2002 |pmid= 12093293 |doi=  }}
*{{cite journal  | author=Kim YT, Downs D, Wu S, ''et al.'' |title=Enzymic properties of recombinant BACE2. |journal=Eur. J. Biochem. |volume=269 |issue= 22 |pages= 5668-77 |year= 2003 |pmid= 12423367 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Kondoh K, Tsuji N, Kamagata C, ''et al.'' |title=A novel aspartic protease gene, ALP56, is up-regulated in human breast cancer independently from the cathepsin D gene. |journal=Breast Cancer Res. Treat. |volume=78 |issue= 1 |pages= 37-44 |year= 2003 |pmid= 12611455 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] DFFA

• INFO: Beginning work on DFFA... {November 18, 2007 2:45:00 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:46:32 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_DFFA_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iyr.
 | PDB = {{PDB2|1iyr}}, {{PDB2|1koy}}
 | Name = DNA fragmentation factor, 45kDa, alpha polypeptide
 | HGNCid = 2772
 | Symbol = DFFA
 | AltSymbols =; DFF-45; DFF1; ICAD
 | OMIM = 601882
 | ECnumber =  
 | Homologene = 3240
 | MGIid = 1196227
 | GeneAtlas_image1 = PBB_GE_DFFA_203277_at_tn.png
 | Function = {{GNF_GO|id=GO:0004537 |text = caspase-activated deoxyribonuclease activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} 
 | Process = {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1676
    | Hs_Ensembl = ENSG00000160049
    | Hs_RefseqProtein = NP_004392
    | Hs_RefseqmRNA = NM_004401
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 10439166
    | Hs_GenLoc_end = 10455200
    | Hs_Uniprot = O00273
    | Mm_EntrezGene = 13347
    | Mm_Ensembl = ENSMUSG00000028974
    | Mm_RefseqmRNA = NM_001025296
    | Mm_RefseqProtein = NP_001020467
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 147947946
    | Mm_GenLoc_end = 147964450
    | Mm_Uniprot = Q8BQC7
  }}
}}
'''DNA fragmentation factor, 45kDa, alpha polypeptide''', also known as '''DFFA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DFFA DNA fragmentation factor, 45kDa, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1676| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: DFFA DNA fragmentation factor, 45kDa, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1676| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Nakanuma Y, Tsuneyama K, Sasaki M, Harada K |title=Destruction of bile ducts in primary biliary cirrhosis. |journal=Baillière's best practice & research. Clinical gastroenterology |volume=14 |issue= 4 |pages= 549-70 |year= 2000 |pmid= 10976014 |doi= 10.1053/bega.2000.0103 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Liu X, Zou H, Slaughter C, Wang X |title=DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. |journal=Cell |volume=89 |issue= 2 |pages= 175-84 |year= 1997 |pmid= 9108473 |doi=  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Enari M, Sakahira H, Yokoyama H, ''et al.'' |title=A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. |journal=Nature |volume=391 |issue= 6662 |pages= 43-50 |year= 1998 |pmid= 9422506 |doi= 10.1038/34112 }}
*{{cite journal  | author=Leek JP, Carr IM, Bell SM, ''et al.'' |title=Assignment of the DNA fragmentation factor gene (DFFA) to human chromosome bands 1p36.3-->p36.2 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 3-4 |pages= 212-3 |year= 1998 |pmid= 9605855 |doi=  }}
*{{cite journal  | author=Liu X, Zou H, Widlak P, ''et al.'' |title=Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 13836-40 |year= 1999 |pmid= 10318789 |doi=  }}
*{{cite journal  | author=Gu J, Dong RP, Zhang C, ''et al.'' |title=Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 20759-62 |year= 1999 |pmid= 10409614 |doi=  }}
*{{cite journal  | author=Oh JJ, Grosshans DR, Wong SG, Slamon DJ |title=Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells. |journal=Nucleic Acids Res. |volume=27 |issue= 20 |pages= 4008-17 |year= 1999 |pmid= 10497265 |doi=  }}
*{{cite journal  | author=McCarty JS, Toh SY, Li P |title=Study of DFF45 in its role of chaperone and inhibitor: two independent inhibitory domains of DFF40 nuclease activity. |journal=Biochem. Biophys. Res. Commun. |volume=264 |issue= 1 |pages= 176-80 |year= 1999 |pmid= 10527860 |doi= 10.1006/bbrc.1999.1497 }}
*{{cite journal  | author=McCarty JS, Toh SY, Li P |title=Multiple domains of DFF45 bind synergistically to DFF40: roles of caspase cleavage and sequestration of activator domain of DFF40. |journal=Biochem. Biophys. Res. Commun. |volume=264 |issue= 1 |pages= 181-5 |year= 1999 |pmid= 10527861 |doi= 10.1006/bbrc.1999.1498 }}
*{{cite journal  | author=Lugovskoy AA, Zhou P, Chou JJ, ''et al.'' |title=Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis. |journal=Cell |volume=99 |issue= 7 |pages= 747-55 |year= 2000 |pmid= 10619428 |doi=  }}
*{{cite journal  | author=Otomo T, Sakahira H, Uegaki K, ''et al.'' |title=Structure of the heterodimeric complex between CAD domains of CAD and ICAD. |journal=Nat. Struct. Biol. |volume=7 |issue= 8 |pages= 658-62 |year= 2000 |pmid= 10932250 |doi= 10.1038/77957 }}
*{{cite journal  | author=Xerri L, Palmerini F, Devilard E, ''et al.'' |title=Frequent nuclear localization of ICAD and cytoplasmic co-expression of caspase-8 and caspase-3 in human lymphomas. |journal=J. Pathol. |volume=192 |issue= 2 |pages= 194-202 |year= 2000 |pmid= 11004695 |doi= 10.1002/1096-9896(2000)9999:9999<::AID-PATH685>3.0.CO;2-M }}
*{{cite journal  | author=Zhou P, Lugovskoy AA, McCarty JS, ''et al.'' |title=Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 11 |pages= 6051-5 |year= 2001 |pmid= 11371636 |doi= 10.1073/pnas.111145098 }}
*{{cite journal  | author=Sharif-Askari E, Alam A, Rhéaume E, ''et al.'' |title=Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation. |journal=EMBO J. |volume=20 |issue= 12 |pages= 3101-13 |year= 2001 |pmid= 11406587 |doi= 10.1093/emboj/20.12.3101 }}
*{{cite journal  | author=Tsukada T, Watanabe M, Yamashima T |title=Implications of CAD and DNase II in ischemic neuronal necrosis specific for the primate hippocampus. |journal=J. Neurochem. |volume=79 |issue= 6 |pages= 1196-206 |year= 2002 |pmid= 11752060 |doi=  }}
*{{cite journal  | author=Abel F, Sjöberg RM, Ejeskär K, ''et al.'' |title=Analyses of apoptotic regulators CASP9 and DFFA at 1P36.2, reveal rare allele variants in human neuroblastoma tumours. |journal=Br. J. Cancer |volume=86 |issue= 4 |pages= 596-604 |year= 2002 |pmid= 11870543 |doi= 10.1038/sj.bjc.6600111 }}
*{{cite journal  | author=Charrier L, Jarry A, Toquet C, ''et al.'' |title=Growth phase-dependent expression of ICAD-L/DFF45 modulates the pattern of apoptosis in human colonic cancer cells. |journal=Cancer Res. |volume=62 |issue= 7 |pages= 2169-74 |year= 2002 |pmid= 11929840 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] ECE1

• INFO: Beginning work on ECE1... {November 18, 2007 2:46:33 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:47:31 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Endothelin converting enzyme 1
 | HGNCid = 3146
 | Symbol = ECE1
 | AltSymbols =; ECE
 | OMIM = 600423
 | ECnumber =  
 | Homologene = 1068
 | MGIid = 1101357
 | GeneAtlas_image1 = PBB_GE_ECE1_201750_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_ECE1_201749_at_tn.png
 | Function = {{GNF_GO|id=GO:0004245 |text = neprilysin activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016512 |text = endothelin-converting enzyme 1 activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1889
    | Hs_Ensembl = ENSG00000117298
    | Hs_RefseqProtein = NP_001388
    | Hs_RefseqmRNA = NM_001397
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 21417664
    | Hs_GenLoc_end = 21544584
    | Hs_Uniprot = P42892
    | Mm_EntrezGene = 230857
    | Mm_Ensembl = ENSMUSG00000057530
    | Mm_RefseqmRNA = XM_989734
    | Mm_RefseqProtein = XP_994828
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 137134373
    | Mm_GenLoc_end = 137237305
    | Mm_Uniprot = Q3TUZ3
  }}
}}
'''Endothelin converting enzyme 1''', also known as '''ECE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ECE1 endothelin converting enzyme 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1889| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Endothelin-converting enzyme-1 is involved in the proteolytic processing of endothelin-1 (EDN1; MIM 131240), -2 (EDN2; MIM 131241), and -3 (EDN3; MIM 131242) to biologically active peptides.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: ECE1 endothelin converting enzyme 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1889| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Yorimitsu K, Moroi K, Inagaki N, ''et al.'' |title=Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 2 |pages= 721-7 |year= 1995 |pmid= 7695628 |doi=  }}
*{{cite journal  | author=Schmidt M, Kröger B, Jacob E, ''et al.'' |title=Molecular characterization of human and bovine endothelin converting enzyme (ECE-1). |journal=FEBS Lett. |volume=356 |issue= 2-3 |pages= 238-43 |year= 1995 |pmid= 7805846 |doi=  }}
*{{cite journal  | author=Shimada K, Matsushita Y, Wakabayashi K, ''et al.'' |title=Cloning and functional expression of human endothelin-converting enzyme cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=207 |issue= 2 |pages= 807-12 |year= 1995 |pmid= 7864876 |doi= 10.1006/bbrc.1995.1258 }}
*{{cite journal  | author=Valdenaire O, Rohrbacher E, Mattei MG |title=Organization of the gene encoding the human endothelin-converting enzyme (ECE-1). |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29794-8 |year= 1996 |pmid= 8530372 |doi=  }}
*{{cite journal  | author=Matsuoka R, Sawamura T, Yamada K, ''et al.'' |title=Human endothelin converting enzyme gene (ECE1) mapped to chromosomal region 1p36.1. |journal=Cytogenet. Cell Genet. |volume=72 |issue= 4 |pages= 322-4 |year= 1996 |pmid= 8641140 |doi=  }}
*{{cite journal  | author=Orzechowski HD, Richter CM, Funke-Kaiser H, ''et al.'' |title=Evidence of alternative promoters directing isoform-specific expression of human endothelin-converting enzyme-1 mRNA in cultured endothelial cells. |journal=J. Mol. Med. |volume=75 |issue= 7 |pages= 512-21 |year= 1997 |pmid= 9253714 |doi=  }}
*{{cite journal  | author=Schweizer A, Valdenaire O, Nelböck P, ''et al.'' |title=Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations. |journal=Biochem. J. |volume=328 ( Pt 3) |issue=  |pages= 871-7 |year= 1998 |pmid= 9396733 |doi=  }}
*{{cite journal  | author=Kido T, Sawamura T, Masaki T |title=The processing pathway of endothelin-1 production. |journal=J. Cardiovasc. Pharmacol. |volume=31 Suppl 1 |issue=  |pages= S13-5 |year= 1998 |pmid= 9595387 |doi=  }}
*{{cite journal  | author=Hofstra RM, Valdenaire O, Arch E, ''et al.'' |title=A loss-of-function mutation in the endothelin-converting enzyme 1 (ECE-1) associated with Hirschsprung disease, cardiac defects, and autonomic dysfunction. |journal=Am. J. Hum. Genet. |volume=64 |issue= 1 |pages= 304-8 |year= 1999 |pmid= 9915973 |doi=  }}
*{{cite journal  | author=Lee S, Lin M, Mele A, ''et al.'' |title=Proteolytic processing of big endothelin-3 by the kell blood group protein. |journal=Blood |volume=94 |issue= 4 |pages= 1440-50 |year= 1999 |pmid= 10438732 |doi=  }}
*{{cite journal  | author=Valdenaire O, Lepailleur-Enouf D, Egidy G, ''et al.'' |title=A fourth isoform of endothelin-converting enzyme (ECE-1) is generated from an additional promoter molecular cloning and characterization. |journal=Eur. J. Biochem. |volume=264 |issue= 2 |pages= 341-9 |year= 1999 |pmid= 10491078 |doi=  }}
*{{cite journal  | author=Fahnoe DC, Johnson GD, Herman SB, Ahn K |title=Disulfide bonds in big ET-1 are essential for the specific cleavage at the Trp(21)-Val(22) bond by soluble endothelin converting enzyme-1 from baculovirus/insect cells. |journal=Arch. Biochem. Biophys. |volume=373 |issue= 2 |pages= 385-93 |year= 2000 |pmid= 10620363 |doi= 10.1006/abbi.1999.1586 }}
*{{cite journal  | author=López-Ongil S, Senchak V, Saura M, ''et al.'' |title=Superoxide regulation of endothelin-converting enzyme. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26423-7 |year= 2000 |pmid= 10833511 |doi= 10.1074/jbc.M000767200 }}
*{{cite journal  | author=Hachiya A, Kobayashi T, Takema Y, Imokawa G |title=Biochemical characterization of endothelin-converting enzyme-1alpha in cultured skin-derived cells and its postulated role in the stimulation of melanogenesis in human epidermis. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5395-403 |year= 2002 |pmid= 11723113 |doi= 10.1074/jbc.M105874200 }}
*{{cite journal  | author=Inguimbert N, Coric P, Poras H, ''et al.'' |title=Toward an optimal joint recognition of the S1' subsites of endothelin converting enzyme-1 (ECE-1), angiotensin converting enzyme (ACE), and neutral endopeptidase (NEP). |journal=J. Med. Chem. |volume=45 |issue= 7 |pages= 1477-86 |year= 2002 |pmid= 11906289 |doi=  }}
*{{cite journal  | author=MacLeod KJ, Husain RD, Gage DA, Ahn K |title=Constitutive phosphorylation of human endothelin-converting enzyme-1 isoforms. |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46355-63 |year= 2003 |pmid= 12244060 |doi= 10.1074/jbc.M207972200 }}
*{{cite journal  | author=Muller L, Barret A, Etienne E, ''et al.'' |title=Heterodimerization of endothelin-converting enzyme-1 isoforms regulates the subcellular distribution of this metalloprotease. |journal=J. Biol. Chem. |volume=278 |issue= 1 |pages= 545-55 |year= 2003 |pmid= 12393864 |doi= 10.1074/jbc.M208949200 }}
*{{cite journal  | author=Eckman EA, Watson M, Marlow L, ''et al.'' |title=Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2081-4 |year= 2003 |pmid= 12464614 |doi= 10.1074/jbc.C200642200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Masatsugu K, Itoh H, Chun TH, ''et al.'' |title=Shear stress attenuates endothelin and endothelin-converting enzyme expression through oxidative stress. |journal=Regul. Pept. |volume=111 |issue= 1-3 |pages= 13-9 |year= 2003 |pmid= 12609744 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] EEF1D

• INFO: Beginning work on EEF1D... {November 18, 2007 2:47:31 PM PST}
• SEARCH REDIRECT: Control Box Found: EEF1D {November 18, 2007 2:48:38 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:48:44 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:48:44 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:48:44 PM PST}
• UPDATED: Updated protein page: EEF1D {November 18, 2007 2:48:56 PM PST}

[edit] GABRA1

• INFO: Beginning work on GABRA1... {November 18, 2007 2:48:57 PM PST}
• SEARCH REDIRECT: Control Box Found: GABRA1 {November 18, 2007 2:49:53 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:50:01 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:50:01 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:50:01 PM PST}
• UPDATED: Updated protein page: GABRA1 {November 18, 2007 2:50:16 PM PST}

[edit] GAD1

• INFO: Beginning work on GAD1... {November 18, 2007 2:50:16 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:51:24 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_GAD1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2okj.
 | PDB = {{PDB2|2okj}}
 | Name = Glutamate decarboxylase 1 (brain, 67kDa)
 | HGNCid = 4092
 | Symbol = GAD1
 | AltSymbols =; FLJ45882; GAD; SCP
 | OMIM = 605363
 | ECnumber =  
 | Homologene = 635
 | MGIid = 95632
 | GeneAtlas_image1 = PBB_GE_GAD1_205278_at_tn.png
 | GeneAtlas_image2 = PBB_GE_GAD1_206670_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_GAD1_206669_at_tn.png
 | Function = {{GNF_GO|id=GO:0004351 |text = glutamate decarboxylase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0012506 |text = vesicle membrane}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0045202 |text = synapse}} 
 | Process = {{GNF_GO|id=GO:0006540 |text = glutamate decarboxylation to succinate}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0018352 |text = protein-pyridoxal-5-phosphate linkage}} {{GNF_GO|id=GO:0019752 |text = carboxylic acid metabolic process}} {{GNF_GO|id=GO:0042136 |text = neurotransmitter biosynthetic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2571
    | Hs_Ensembl = ENSG00000128683
    | Hs_RefseqProtein = NP_000808
    | Hs_RefseqmRNA = NM_000817
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 171381318
    | Hs_GenLoc_end = 171425907
    | Hs_Uniprot = Q99259
    | Mm_EntrezGene = 14415
    | Mm_Ensembl = ENSMUSG00000070880
    | Mm_RefseqmRNA = NM_008077
    | Mm_RefseqProtein = NP_032103
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 70363052
    | Mm_GenLoc_end = 70402856
    | Mm_Uniprot = Q3TQ56
  }}
}}
'''Glutamate decarboxylase 1 (brain, 67kDa)''', also known as '''GAD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAD1 glutamate decarboxylase 1 (brain, 67kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2571| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes one of several forms of glutamic acid decarboxylase, identified as a major autoantigen in insulin-dependent diabetes. The enzyme encoded is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for this enzyme has been identified in the human pancreas since it has been identified as an autoantigen and an autoreactive T cell target in insulin-dependent diabetes. This gene may also play a role in the stiff man syndrome. Deficiency in this enzyme has been shown to lead to pyridoxine dependency with seizures. Alternative splicing of this gene results in two products, the predominant 67-kD form and a less-frequent 25-kD form.<ref name="entrez">{{cite web | title = Entrez Gene: GAD1 glutamate decarboxylase 1 (brain, 67kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2571| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kelly CD, Edwards Y, Johnstone AP, ''et al.'' |title=Nucleotide sequence and chromosomal assignment of a cDNA encoding the large isoform of human glutamate decarboxylase. |journal=Ann. Hum. Genet. |volume=56 |issue= Pt 3 |pages= 255-65 |year= 1992 |pmid= 1339255 |doi=  }}
*{{cite journal  | author=Bu DF, Erlander MG, Hitz BC, ''et al.'' |title=Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 6 |pages= 2115-9 |year= 1992 |pmid= 1549570 |doi=  }}
*{{cite journal  | author=Giorda R, Peakman M, Tan KC, ''et al.'' |title=Glutamic acid decarboxylase expression in islets and brain. |journal=Lancet |volume=338 |issue= 8780 |pages= 1469-70 |year= 1991 |pmid= 1683463 |doi=  }}
*{{cite journal  | author=Persson H, Pelto-Huikko M, Metsis M, ''et al.'' |title=Expression of the neurotransmitter-synthesizing enzyme glutamic acid decarboxylase in male germ cells. |journal=Mol. Cell. Biol. |volume=10 |issue= 9 |pages= 4701-11 |year= 1990 |pmid= 1697032 |doi=  }}
*{{cite journal  | author=Cram DS, Barnett LD, Joseph JL, Harrison LC |title=Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1239-44 |year= 1991 |pmid= 2039509 |doi=  }}
*{{cite journal  | author=Dirkx R, Thomas A, Li L, ''et al.'' |title=Targeting of the 67-kDa isoform of glutamic acid decarboxylase to intracellular organelles is mediated by its interaction with the NH2-terminal region of the 65-kDa isoform of glutamic acid decarboxylase. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2241-6 |year= 1995 |pmid= 7836456 |doi=  }}
*{{cite journal  | author=Bu DF, Tobin AJ |title=The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. |journal=Genomics |volume=21 |issue= 1 |pages= 222-8 |year= 1994 |pmid= 8088791 |doi= 10.1006/geno.1994.1246 }}
*{{cite journal  | author=Yamashita K, Cram DS, Harrison LC |title=Molecular cloning of full-length glutamic acid decarboxylase 67 from human pancreas and islets. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 3 |pages= 1347-52 |year= 1993 |pmid= 8507202 |doi= 10.1006/bbrc.1993.1564 }}
*{{cite journal  | author=Kawasaki E, Moriuchi R, Watanabe M, ''et al.'' |title=Cloning and expression of large isoform of glutamic acid decarboxylase from human pancreatic islet. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 3 |pages= 1353-9 |year= 1993 |pmid= 8507203 |doi=  }}
*{{cite journal  | author=Asada H, Kawamura Y, Maruyama K, ''et al.'' |title=Mice lacking the 65 kDa isoform of glutamic acid decarboxylase (GAD65) maintain normal levels of GAD67 and GABA in their brains but are susceptible to seizures. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 3 |pages= 891-5 |year= 1997 |pmid= 8954991 |doi=  }}
*{{cite journal  | author=McHale DP, Mitchell S, Bundey S, ''et al.'' |title=A gene for autosomal recessive symmetrical spastic cerebral palsy maps to chromosome 2q24-25. |journal=Am. J. Hum. Genet. |volume=64 |issue= 2 |pages= 526-32 |year= 1999 |pmid= 9973289 |doi=  }}
*{{cite journal  | author=Chessler SD, Lernmark A |title=Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 5188-92 |year= 2000 |pmid= 10671565 |doi=  }}
*{{cite journal  | author=Luo J, Kaplitt MG, Fitzsimons HL, ''et al.'' |title=Subthalamic GAD gene therapy in a Parkinson's disease rat model. |journal=Science |volume=298 |issue= 5592 |pages= 425-9 |year= 2002 |pmid= 12376704 |doi= 10.1126/science.1074549 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Chessler SD, Hampe CS, Ortqvist E, ''et al.'' |title=Immune reactivity to GAD25 in type 1 diabetes mellitus. |journal=Autoimmunity |volume=35 |issue= 5 |pages= 335-41 |year= 2003 |pmid= 12515288 |doi=  }}
*{{cite journal  | author=Demakova EV, Korobov VP, Lemkina LM |title=[Determination of gamma-aminobutyric acid concentration and activity of glutamate decarboxylase in blood serum of patients with multiple sclerosis] |journal=Klin. Lab. Diagn. |volume= |issue= 4 |pages= 15-7 |year= 2003 |pmid= 12774663 |doi=  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Flace P, Benagiano V, Lorusso L, ''et al.'' |title=Glutamic acid decarboxylase immunoreactive large neuron types in the granular layer of the human cerebellar cortex. |journal=Anat. Embryol. |volume=208 |issue= 1 |pages= 55-64 |year= 2004 |pmid= 15014985 |doi= 10.1007/s00429-003-0374-x }}
*{{cite journal  | author=De Luca V, Muglia P, Masellis M, ''et al.'' |title=Polymorphisms in glutamate decarboxylase genes: analysis in schizophrenia. |journal=Psychiatr. Genet. |volume=14 |issue= 1 |pages= 39-42 |year= 2004 |pmid= 15091314 |doi=  }}
*{{cite journal  | author=Kanno K, Suzuki Y, Yamada A, ''et al.'' |title=Association between nonsyndromic cleft lip with or without cleft palate and the glutamic acid decarboxylase 67 gene in the Japanese population. |journal=Am. J. Med. Genet. A |volume=127 |issue= 1 |pages= 11-6 |year= 2004 |pmid= 15103710 |doi= 10.1002/ajmg.a.20649 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GAP43

• INFO: Beginning work on GAP43... {November 18, 2007 2:51:25 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:52:14 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Growth associated protein 43
 | HGNCid = 4140
 | Symbol = GAP43
 | AltSymbols =; B-50; PP46
 | OMIM = 162060
 | ECnumber =  
 | Homologene = 1545
 | MGIid = 95639
 | GeneAtlas_image1 = PBB_GE_GAP43_216963_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_GAP43_204471_at_tn.png
 | Function = {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0030424 |text = axon}} 
 | Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0010001 |text = glial cell differentiation}} {{GNF_GO|id=GO:0040008 |text = regulation of growth}} {{GNF_GO|id=GO:0045165 |text = cell fate commitment}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2596
    | Hs_Ensembl = ENSG00000172020
    | Hs_RefseqProtein = NP_002036
    | Hs_RefseqmRNA = NM_002045
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 116824861
    | Hs_GenLoc_end = 116922935
    | Hs_Uniprot = P17677
    | Mm_EntrezGene = 14432
    | Mm_Ensembl = ENSMUSG00000047261
    | Mm_RefseqmRNA = XM_994895
    | Mm_RefseqProtein = XP_999989
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 42167776
    | Mm_GenLoc_end = 42259983
    | Mm_Uniprot = P06837
  }}
}}
'''Growth associated protein 43''', also known as '''GAP43''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAP43 growth associated protein 43| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2596| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene has been termed a 'growth' or 'plasticity' protein because it is expressed at high levels in neuronal growth cones during development and axonal regeneration. This encoded protein is considered a crucial component of an effective regenerative response in the nervous system.<ref name="entrez">{{cite web | title = Entrez Gene: GAP43 growth associated protein 43| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2596| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Fantini F, Johansson O |title=Expression of growth-associated protein 43 and nerve growth factor receptor in human skin: a comparative immunohistochemical investigation. |journal=J. Invest. Dermatol. |volume=99 |issue= 6 |pages= 734-42 |year= 1993 |pmid= 1281863 |doi=  }}
*{{cite journal  | author=Mercken M, Lübke U, Vandermeeren M, ''et al.'' |title=Immunocytochemical detection of the growth-associated protein B-50 by newly characterized monoclonal antibodies in human brain and muscle. |journal=J. Neurobiol. |volume=23 |issue= 3 |pages= 309-21 |year= 1992 |pmid= 1385623 |doi= 10.1002/neu.480230310 }}
*{{cite journal  | author=Spencer SA, Schuh SM, Liu WS, Willard MB |title=GAP-43, a protein associated with axon growth, is phosphorylated at three sites in cultured neurons and rat brain. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9059-64 |year= 1992 |pmid= 1533624 |doi=  }}
*{{cite journal  | author=Apel ED, Litchfield DW, Clark RH, ''et al.'' |title=Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin. |journal=J. Biol. Chem. |volume=266 |issue= 16 |pages= 10544-51 |year= 1991 |pmid= 1828073 |doi=  }}
*{{cite journal  | author=Apel ED, Byford MF, Au D, ''et al.'' |title=Identification of the protein kinase C phosphorylation site in neuromodulin. |journal=Biochemistry |volume=29 |issue= 9 |pages= 2330-5 |year= 1990 |pmid= 2140056 |doi=  }}
*{{cite journal  | author=Kosik KS, Orecchio LD, Bruns GA, ''et al.'' |title=Human GAP-43: its deduced amino acid sequence and chromosomal localization in mouse and human. |journal=Neuron |volume=1 |issue= 2 |pages= 127-32 |year= 1990 |pmid= 3272162 |doi=  }}
*{{cite journal  | author=Ng SC, de la Monte SM, Conboy GL, ''et al.'' |title=Cloning of human GAP-43: growth association and ischemic resurgence. |journal=Neuron |volume=1 |issue= 2 |pages= 133-9 |year= 1990 |pmid= 3272163 |doi=  }}
*{{cite journal  | author=Nielander HB, De Groen PC, Eggen BJ, ''et al.'' |title=Structure of the human gene for the neural phosphoprotein B-50 (GAP-43). |journal=Brain Res. Mol. Brain Res. |volume=19 |issue= 4 |pages= 293-302 |year= 1993 |pmid= 8231732 |doi=  }}
*{{cite journal  | author=Oehrlein SA, Parker PJ, Herget T |title=Phosphorylation of GAP-43 (growth-associated protein of 43 kDa) by conventional, novel and atypical isotypes of the protein kinase C gene family: differences between oligopeptide and polypeptide phosphorylation. |journal=Biochem. J. |volume=317 ( Pt 1) |issue=  |pages= 219-24 |year= 1996 |pmid= 8694767 |doi=  }}
*{{cite journal  | author=Kanazir S, Ruzdijic S, Vukosavic S, ''et al.'' |title=GAP-43 mRNA expression in early development of human nervous system. |journal=Brain Res. Mol. Brain Res. |volume=38 |issue= 1 |pages= 145-55 |year= 1997 |pmid= 8737678 |doi=  }}
*{{cite journal  | author=de Groen PC, Eggen BJ, Gispen WH, ''et al.'' |title=Cloning and promoter analysis of the human B-50/GAP-43 gene. |journal=J. Mol. Neurosci. |volume=6 |issue= 2 |pages= 109-19 |year= 1996 |pmid= 8746449 |doi=  }}
*{{cite journal  | author=Chao S, Benowitz LI, Krainc D, Irwin N |title=Use of a two-hybrid system to investigate molecular interactions of GAP-43. |journal=Brain Res. Mol. Brain Res. |volume=40 |issue= 2 |pages= 195-202 |year= 1997 |pmid= 8872303 |doi=  }}
*{{cite journal  | author=Gamby C, Waage MC, Allen RG, Baizer L |title=Analysis of the role of calmodulin binding and sequestration in neuromodulin (GAP-43) function. |journal=J. Biol. Chem. |volume=271 |issue= 43 |pages= 26698-705 |year= 1996 |pmid= 8900147 |doi=  }}
*{{cite journal  | author=Heuss D, Schlötzer-Schrehardt U |title=Subcellular localization of phosphoprotein B-50 in regenerating muscle. An immuno-electron microscopic study. |journal=Neurol. Res. |volume=20 |issue= 4 |pages= 360-4 |year= 1998 |pmid= 9618702 |doi=  }}
*{{cite journal  | author=Neve RL, Coopersmith R, McPhie DL, ''et al.'' |title=The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis. |journal=J. Neurosci. |volume=18 |issue= 19 |pages= 7757-67 |year= 1998 |pmid= 9742146 |doi=  }}
*{{cite journal  | author=Arni S, Keilbaugh SA, Ostermeyer AG, Brown DA |title=Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues. |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 28478-85 |year= 1998 |pmid= 9774477 |doi=  }}
*{{cite journal  | author=Eastwood SL, Harrison PJ |title=Hippocampal and cortical growth-associated protein-43 messenger RNA in schizophrenia. |journal=Neuroscience |volume=86 |issue= 2 |pages= 437-48 |year= 1999 |pmid= 9881859 |doi=  }}
*{{cite journal  | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal  | author=Riederer BM, Routtenberg A |title=Can GAP-43 interact with brain spectrin? |journal=Brain Res. Mol. Brain Res. |volume=71 |issue= 2 |pages= 345-8 |year= 1999 |pmid= 10521589 |doi=  }}
*{{cite journal  | author=Vento P, Soinila S |title=Quantitative comparison of growth-associated protein GAP-43, neuron-specific enolase, and protein gene product 9.5 as neuronal markers in mature human intestine. |journal=J. Histochem. Cytochem. |volume=47 |issue= 11 |pages= 1405-16 |year= 1999 |pmid= 10544214 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GLI3

• INFO: Beginning work on GLI3... {November 18, 2007 2:52:14 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:53:21 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = GLI-Kruppel family member GLI3 (Greig cephalopolysyndactyly syndrome)
 | HGNCid = 4319
 | Symbol = GLI3
 | AltSymbols =; ACLS; GCPS; PAP-A; PAPA; PAPA1; PAPB; PHS; PPDIV
 | OMIM = 165240
 | ECnumber =  
 | Homologene = 139
 | MGIid = 95729
 | GeneAtlas_image1 = PBB_GE_GLI3_205201_at_tn.png
 | Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0017053 |text = transcriptional repressor complex}} 
 | Process = {{GNF_GO|id=GO:0000060 |text = protein import into nucleus, translocation}} {{GNF_GO|id=GO:0001656 |text = metanephros development}} {{GNF_GO|id=GO:0001658 |text = ureteric bud branching}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007224 |text = smoothened signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009953 |text = dorsal/ventral pattern formation}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0030326 |text = embryonic limb morphogenesis}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0045596 |text = negative regulation of cell differentiation}} {{GNF_GO|id=GO:0048558 |text = embryonic gut morphogenesis}} {{GNF_GO|id=GO:0048663 |text = neuron fate commitment}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2737
    | Hs_Ensembl = ENSG00000106571
    | Hs_RefseqProtein = NP_000159
    | Hs_RefseqmRNA = NM_000168
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 41970205
    | Hs_GenLoc_end = 42229420
    | Hs_Uniprot = P10071
    | Mm_EntrezGene = 14634
    | Mm_Ensembl = ENSMUSG00000021318
    | Mm_RefseqmRNA = NM_008130
    | Mm_RefseqProtein = NP_032156
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 15254867
    | Mm_GenLoc_end = 15517860
    | Mm_Uniprot = Q3TYX7
  }}
}}
'''GLI-Kruppel family member GLI3 (Greig cephalopolysyndactyly syndrome)''', also known as '''GLI3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GLI3 GLI-Kruppel family member GLI3 (Greig cephalopolysyndactyly syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2737| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a protein which belongs to the C2H2-type zinc finger proteins subclass of the Gli family. They are characterized as DNA-binding transcription factors and are mediators of Sonic hedgehog (Shh) signaling. The protein encoded by this gene localizes in the cytoplasm and activates patched Drosophila homolog (PTCH) gene expression. It is also thought to play a role during embryogenesis. Mutations in this gene have been associated with several diseases, including Greig cephalopolysyndactyly syndrome, Pallister-Hall syndrome, preaxial polydactyly type IV, and postaxial polydactyly types A1 and B.<ref name="entrez">{{cite web | title = Entrez Gene: GLI3 GLI-Kruppel family member GLI3 (Greig cephalopolysyndactyly syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2737| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Pettigrew AL, Greenberg F, Caskey CT, Ledbetter DH |title=Greig syndrome associated with an interstitial deletion of 7p: confirmation of the localization of Greig syndrome to 7p13. |journal=Hum. Genet. |volume=87 |issue= 4 |pages= 452-6 |year= 1991 |pmid= 1879832 |doi=  }}
*{{cite journal  | author=Ruppert JM, Vogelstein B, Arheden K, Kinzler KW |title=GLI3 encodes a 190-kilodalton protein with multiple regions of GLI similarity. |journal=Mol. Cell. Biol. |volume=10 |issue= 10 |pages= 5408-15 |year= 1990 |pmid= 2118997 |doi=  }}
*{{cite journal  | author=Ruppert JM, Kinzler KW, Wong AJ, ''et al.'' |title=The GLI-Kruppel family of human genes. |journal=Mol. Cell. Biol. |volume=8 |issue= 8 |pages= 3104-13 |year= 1989 |pmid= 2850480 |doi=  }}
*{{cite journal  | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi=  }}
*{{cite journal  | author=Pavletich NP, Pabo CO |title=Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. |journal=Science |volume=261 |issue= 5129 |pages= 1701-7 |year= 1993 |pmid= 8378770 |doi=  }}
*{{cite journal  | author=Kang S, Graham JM, Olney AH, Biesecker LG |title=GLI3 frameshift mutations cause autosomal dominant Pallister-Hall syndrome. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 266-8 |year= 1997 |pmid= 9054938 |doi= 10.1038/ng0397-266 }}
*{{cite journal  | author=Wild A, Kalff-Suske M, Vortkamp A, ''et al.'' |title=Point mutations in human GLI3 cause Greig syndrome. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1979-84 |year= 1998 |pmid= 9302279 |doi=  }}
*{{cite journal  | author=Radhakrishna U, Wild A, Grzeschik KH, Antonarakis SE |title=Mutation in GLI3 in postaxial polydactyly type A. |journal=Nat. Genet. |volume=17 |issue= 3 |pages= 269-71 |year= 1997 |pmid= 9354785 |doi= 10.1038/ng1197-269 }}
*{{cite journal  | author=Kang S, Rosenberg M, Ko VD, Biesecker LG |title=Gene structure and allelic expression assay of the human GLI3 gene. |journal=Hum. Genet. |volume=101 |issue= 2 |pages= 154-7 |year= 1998 |pmid= 9402960 |doi=  }}
*{{cite journal  | author=Liu F, Massagué J, Ruiz i Altaba A |title=Carboxy-terminally truncated Gli3 proteins associate with Smads. |journal=Nat. Genet. |volume=20 |issue= 4 |pages= 325-6 |year= 1998 |pmid= 9843199 |doi= 10.1038/3793 }}
*{{cite journal  | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi=  }}
*{{cite journal  | author=Dai P, Akimaru H, Tanaka Y, ''et al.'' |title=Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. |journal=J. Biol. Chem. |volume=274 |issue= 12 |pages= 8143-52 |year= 1999 |pmid= 10075717 |doi=  }}
*{{cite journal  | author=Shin SH, Kogerman P, Lindström E, ''et al.'' |title=GLI3 mutations in human disorders mimic Drosophila cubitus interruptus protein functions and localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 2880-4 |year= 1999 |pmid= 10077605 |doi=  }}
*{{cite journal  | author=Kalff-Suske M, Wild A, Topp J, ''et al.'' |title=Point mutations throughout the GLI3 gene cause Greig cephalopolysyndactyly syndrome. |journal=Hum. Mol. Genet. |volume=8 |issue= 9 |pages= 1769-77 |year= 2000 |pmid= 10441342 |doi=  }}
*{{cite journal  | author=Radhakrishna U, Bornholdt D, Scott HS, ''et al.'' |title=The phenotypic spectrum of GLI3 morphopathies includes autosomal dominant preaxial polydactyly type-IV and postaxial polydactyly type-A/B; No phenotype prediction from the position of GLI3 mutations. |journal=Am. J. Hum. Genet. |volume=65 |issue= 3 |pages= 645-55 |year= 1999 |pmid= 10441570 |doi=  }}
*{{cite journal  | author=Stone DM, Murone M, Luoh S, ''et al.'' |title=Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli. |journal=J. Cell. Sci. |volume=112 ( Pt 23) |issue=  |pages= 4437-48 |year= 2000 |pmid= 10564661 |doi=  }}
*{{cite journal  | author=Sobetzko D, Eich G, Kalff-Suske M, ''et al.'' |title=Boy with syndactylies, macrocephaly, and severe skeletal dysplasia: not a new syndrome, but two dominant mutations (GLI3 E543X and COL2A1 G973R) in the same individual. |journal=Am. J. Med. Genet. |volume=90 |issue= 3 |pages= 239-42 |year= 2000 |pmid= 10678662 |doi=  }}
*{{cite journal  | author=Murone M, Luoh SM, Stone D, ''et al.'' |title=Gli regulation by the opposing activities of fused and suppressor of fused. |journal=Nat. Cell Biol. |volume=2 |issue= 5 |pages= 310-2 |year= 2000 |pmid= 10806483 |doi= 10.1038/35010610 }}
*{{cite journal  | author=Koyabu Y, Nakata K, Mizugishi K, ''et al.'' |title=Physical and functional interactions between Zic and Gli proteins. |journal=J. Biol. Chem. |volume=276 |issue= 10 |pages= 6889-92 |year= 2001 |pmid= 11238441 |doi= 10.1074/jbc.C000773200 }}
*{{cite journal  | author=O'Rourke MP, Soo K, Behringer RR, ''et al.'' |title=Twist plays an essential role in FGF and SHH signal transduction during mouse limb development. |journal=Dev. Biol. |volume=248 |issue= 1 |pages= 143-56 |year= 2002 |pmid= 12142027 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GLRX

• INFO: Beginning work on GLRX... {November 18, 2007 2:53:21 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:54:14 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_GLRX_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b4q.
 | PDB = {{PDB2|1b4q}}, {{PDB2|1jhb}}
 | Name = Glutaredoxin (thioltransferase)
 | HGNCid = 4330
 | Symbol = GLRX
 | AltSymbols =; GRX; GRX1; MGC117407
 | OMIM = 600443
 | ECnumber =  
 | Homologene = 37566
 | MGIid = 2135625
 | GeneAtlas_image1 = PBB_GE_GLRX_206662_at_tn.png
 | GeneAtlas_image2 = PBB_GE_GLRX_209276_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0015035 |text = protein disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0015038 |text = glutathione disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0047485 |text = protein N-terminus binding}} 
 | Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} 
 | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0045454 |text = cell redox homeostasis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2745
    | Hs_Ensembl = ENSG00000173221
    | Hs_RefseqProtein = NP_002055
    | Hs_RefseqmRNA = NM_002064
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 95175309
    | Hs_GenLoc_end = 95184465
    | Hs_Uniprot = P35754
    | Mm_EntrezGene = 93692
    | Mm_Ensembl = ENSMUSG00000021591
    | Mm_RefseqmRNA = NM_053108
    | Mm_RefseqProtein = NP_444338
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 76305916
    | Mm_GenLoc_end = 76316153
    | Mm_Uniprot = Q3U6L3
  }}
}}
'''Glutaredoxin (thioltransferase)''', also known as '''GLRX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GLRX glutaredoxin (thioltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2745| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lou MF |title=Redox regulation in the lens. |journal=Progress in retinal and eye research |volume=22 |issue= 5 |pages= 657-82 |year= 2003 |pmid= 12892645 |doi=  }}
*{{cite journal  | author=Sykes MC, Mowbray AL, Jo H |title=Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death. |journal=Circ. Res. |volume=100 |issue= 2 |pages= 152-4 |year= 2007 |pmid= 17272816 |doi= 10.1161/01.RES.0000258171.08020.72 }}
*{{cite journal  | author=Padilla CA, Martínez-Galisteo E, Bárcena JA, ''et al.'' |title=Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. |journal=Eur. J. Biochem. |volume=227 |issue= 1-2 |pages= 27-34 |year= 1995 |pmid= 7851394 |doi=  }}
*{{cite journal  | author=Bandyopadhyay S, Gronostajski RM |title=Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins. |journal=J. Biol. Chem. |volume=269 |issue= 47 |pages= 29949-55 |year= 1994 |pmid= 7961993 |doi=  }}
*{{cite journal  | author=Fernando MR, Sumimoto H, Nanri H, ''et al.'' |title=Cloning and sequencing of the cDNA encoding human glutaredoxin. |journal=Biochim. Biophys. Acta |volume=1218 |issue= 2 |pages= 229-31 |year= 1994 |pmid= 8018729 |doi=  }}
*{{cite journal  | author=Papov VV, Gravina SA, Mieyal JJ, Biemann K |title=The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells. |journal=Protein Sci. |volume=3 |issue= 3 |pages= 428-34 |year= 1994 |pmid= 8019414 |doi=  }}
*{{cite journal  | author=Padilla CA, Spyrou G, Holmgren A |title=High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein. |journal=FEBS Lett. |volume=378 |issue= 1 |pages= 69-73 |year= 1996 |pmid= 8549805 |doi=  }}
*{{cite journal  | author=Park JB, Levine M |title=Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin. |journal=Biochem. J. |volume=315 ( Pt 3) |issue=  |pages= 931-8 |year= 1996 |pmid= 8645179 |doi=  }}
*{{cite journal  | author=Padilla CA, Bajalica S, Lagercrantz J, Holmgren A |title=The gene for human glutaredoxin (GLRX) is localized to human chromosome 5q14. |journal=Genomics |volume=32 |issue= 3 |pages= 455-7 |year= 1997 |pmid= 8838810 |doi= 10.1006/geno.1996.0141 }}
*{{cite journal  | author=Davis DA, Newcomb FM, Starke DW, ''et al.'' |title=Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. |journal=J. Biol. Chem. |volume=272 |issue= 41 |pages= 25935-40 |year= 1997 |pmid= 9325327 |doi=  }}
*{{cite journal  | author=Park JB, Levine M |title=The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis. |journal=Gene |volume=197 |issue= 1-2 |pages= 189-93 |year= 1997 |pmid= 9332366 |doi=  }}
*{{cite journal  | author=Bandyopadhyay S, Starke DW, Mieyal JJ, Gronostajski RM |title=Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. |journal=J. Biol. Chem. |volume=273 |issue= 1 |pages= 392-7 |year= 1998 |pmid= 9417094 |doi=  }}
*{{cite journal  | author=Sun C, Berardi MJ, Bushweller JH |title=The NMR solution structure of human glutaredoxin in the fully reduced form. |journal=J. Mol. Biol. |volume=280 |issue= 4 |pages= 687-701 |year= 1998 |pmid= 9677297 |doi= 10.1006/jmbi.1998.1913 }}
*{{cite journal  | author=Yang Y, Jao S, Nanduri S, ''et al.'' |title=Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. |journal=Biochemistry |volume=37 |issue= 49 |pages= 17145-56 |year= 1999 |pmid= 9860827 |doi= 10.1021/bi9806504 }}
*{{cite journal  | author=Balijepalli S, Tirumalai PS, Swamy KV, ''et al.'' |title=Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization. |journal=J. Neurochem. |volume=72 |issue= 3 |pages= 1170-8 |year= 1999 |pmid= 10037490 |doi=  }}
*{{cite journal  | author=Barrett WC, DeGnore JP, König S, ''et al.'' |title=Regulation of PTP1B via glutathionylation of the active site cysteine 215. |journal=Biochemistry |volume=38 |issue= 20 |pages= 6699-705 |year= 1999 |pmid= 10350489 |doi= 10.1021/bi990240v }}
*{{cite journal  | author=García-Pardo L, Granados MD, Gaytán F, ''et al.'' |title=Immunolocalization of glutaredoxin in the human corpus luteum. |journal=Mol. Hum. Reprod. |volume=5 |issue= 10 |pages= 914-9 |year= 1999 |pmid= 10508218 |doi=  }}
*{{cite journal  | author=Mallis RJ, Poland BW, Chatterjee TK, ''et al.'' |title=Crystal structure of S-glutathiolated carbonic anhydrase III. |journal=FEBS Lett. |volume=482 |issue= 3 |pages= 237-41 |year= 2000 |pmid= 11024467 |doi=  }}
*{{cite journal  | author=Balijepalli S, Boyd MR, Ravindranath V |title=Human brain thioltransferase: constitutive expression and localization by fluorescence in situ hybridization. |journal=Brain Res. Mol. Brain Res. |volume=85 |issue= 1-2 |pages= 123-32 |year= 2001 |pmid= 11146114 |doi=  }}
*{{cite journal  | author=Qiao F, Xing K, Liu A, ''et al.'' |title=Human lens thioltransferase: cloning, purification, and function. |journal=Invest. Ophthalmol. Vis. Sci. |volume=42 |issue= 3 |pages= 743-51 |year= 2001 |pmid= 11222536 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] HIST2H3C

• INFO: Beginning work on HIST2H3C... {November 18, 2007 3:18:41 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:19:23 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_HIST2H3C_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
 | PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1f66}}, {{PDB2|1hio}}, {{PDB2|1hq3}}, {{PDB2|1kx3}}, {{PDB2|1kx4}}, {{PDB2|1kx5}}, {{PDB2|1m18}}, {{PDB2|1m19}}, {{PDB2|1m1a}}, {{PDB2|1p34}}, {{PDB2|1p3a}}, {{PDB2|1p3b}}, {{PDB2|1p3f}}, {{PDB2|1p3g}}, {{PDB2|1p3i}}, {{PDB2|1p3k}}, {{PDB2|1p3l}}, {{PDB2|1p3m}}, {{PDB2|1p3o}}, {{PDB2|1p3p}}, {{PDB2|1s32}}, {{PDB2|1tzy}}, {{PDB2|1u35}}, {{PDB2|1zbb}}, {{PDB2|1zla}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2hue}}, {{PDB2|2io5}}, {{PDB2|2nzd}}
 | Name = Histone cluster 2, H3c
 | HGNCid = 20503
 | Symbol = HIST2H3C
 | AltSymbols =; H3; H3.2; H3/M; H3F2; H3FM; MGC9629; H3/n; H3/o
 | OMIM = 142780
 | ECnumber =  
 | Homologene = 79492
 | MGIid = 2448355
 | Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} 
 | Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}} 
 | Process = {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 126961
    | Hs_Ensembl =  
    | Hs_RefseqProtein = XP_001124743
    | Hs_RefseqmRNA = XM_001124743
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 15077
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = XM_886396
    | Mm_RefseqProtein = XP_891489
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Histone cluster 2, H3c''', also known as '''HIST2H3C''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3C histone cluster 2, H3c| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126961| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3C histone cluster 2, H3c| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126961| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Marashi F, Helms S, Shiels A, ''et al.'' |title=Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences. |journal=Biochem. Cell Biol. |volume=64 |issue= 4 |pages= 277-89 |year= 1986 |pmid= 3013246 |doi=  }}
*{{cite journal  | author=Green L, Van Antwerpen R, Stein J, ''et al.'' |title=A major human histone gene cluster on the long arm of chromosome 1. |journal=Science |volume=226 |issue= 4676 |pages= 838-40 |year= 1984 |pmid= 6494913 |doi=  }}
*{{cite journal  | author=Ohe Y, Iwai K |title=Human spleen histone H3. Isolation and amino acid sequence. |journal=J. Biochem. |volume=90 |issue= 4 |pages= 1205-11 |year= 1982 |pmid= 7309716 |doi=  }}
*{{cite journal  | author=Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M |title=Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay. |journal=Biochim. Biophys. Acta |volume=1296 |issue= 2 |pages= 219-27 |year= 1996 |pmid= 8814229 |doi=  }}
*{{cite journal  | author=Albig W, Doenecke D |title=The human histone gene cluster at the D6S105 locus. |journal=Hum. Genet. |volume=101 |issue= 3 |pages= 284-94 |year= 1998 |pmid= 9439656 |doi=  }}
*{{cite journal  | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535-44 |year= 1998 |pmid= 9566873 |doi=  }}
*{{cite journal  | author=Ahn J, Gruen JR |title=The genomic organization of the histone clusters on human 6p21.3. |journal=Mamm. Genome |volume=10 |issue= 7 |pages= 768-70 |year= 1999 |pmid= 10384058 |doi=  }}
*{{cite journal  | author=Goto H, Tomono Y, Ajiro K, ''et al.'' |title=Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25543-9 |year= 1999 |pmid= 10464286 |doi=  }}
*{{cite journal  | author=Deng L, de la Fuente C, Fu P, ''et al.'' |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278-95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 }}
*{{cite journal  | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116-20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
*{{cite journal  | author=Shankaranarayanan P, Chaitidis P, Kühn H, Nigam S |title=Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene. |journal=J. Biol. Chem. |volume=276 |issue= 46 |pages= 42753-60 |year= 2001 |pmid= 11509556 |doi= 10.1074/jbc.M102626200 }}
*{{cite journal  | author=Deng L, Wang D, de la Fuente C, ''et al.'' |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312-26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 }}
*{{cite journal  | author=Goto H, Yasui Y, Nigg EA, Inagaki M |title=Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. |journal=Genes Cells |volume=7 |issue= 1 |pages= 11-7 |year= 2002 |pmid= 11856369 |doi=  }}
*{{cite journal  | author=Marzluff WF, Gongidi P, Woods KR, ''et al.'' |title=The human and mouse replication-dependent histone genes. |journal=Genomics |volume=80 |issue= 5 |pages= 487-98 |year= 2003 |pmid= 12408966 |doi=  }}
*{{cite journal  | author=Ganesan S, Silver DP, Greenberg RA, ''et al.'' |title=BRCA1 supports XIST RNA concentration on the inactive X chromosome. |journal=Cell |volume=111 |issue= 3 |pages= 393-405 |year= 2002 |pmid= 12419249 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Goo YH, Sohn YC, Kim DH, ''et al.'' |title=Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 1 |pages= 140-9 |year= 2003 |pmid= 12482968 |doi=  }}
*{{cite journal  | author=Preuss U, Landsberg G, Scheidtmann KH |title=Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. |journal=Nucleic Acids Res. |volume=31 |issue= 3 |pages= 878-85 |year= 2003 |pmid= 12560483 |doi=  }}
*{{cite journal  | author=Yoon HG, Chan DW, Huang ZQ, ''et al.'' |title=Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. |journal=EMBO J. |volume=22 |issue= 6 |pages= 1336-46 |year= 2003 |pmid= 12628926 |doi= 10.1093/emboj/cdg120 }}
*{{cite journal  | author=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550-61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] HTR4

• INFO: Beginning work on HTR4... {November 18, 2007 2:56:08 PM PST}
• SEARCH REDIRECT: Control Box Found: HTR4 {November 18, 2007 2:57:59 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:58:13 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:58:13 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:58:13 PM PST}
• UPDATED: Updated protein page: HTR4 {November 18, 2007 2:58:29 PM PST}

[edit] ID3

• INFO: Beginning work on ID3... {November 18, 2007 2:58:30 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:59:43 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein
 | HGNCid = 5362
 | Symbol = ID3
 | AltSymbols =; HEIR-1
 | OMIM = 600277
 | ECnumber =  
 | Homologene = 1633
 | MGIid = 96398
 | GeneAtlas_image1 = PBB_GE_ID3_207826_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0019904 |text = protein domain specific binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0030855 |text = epithelial cell differentiation}} {{GNF_GO|id=GO:0043433 |text = negative regulation of transcription factor activity}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3399
    | Hs_Ensembl = ENSG00000117318
    | Hs_RefseqProtein = NP_002158
    | Hs_RefseqmRNA = NM_002167
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 23756996
    | Hs_GenLoc_end = 23758872
    | Hs_Uniprot = Q02535
    | Mm_EntrezGene = 15903
    | Mm_Ensembl = ENSMUSG00000007872
    | Mm_RefseqmRNA = NM_008321
    | Mm_RefseqProtein = NP_032347
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 135415900
    | Mm_GenLoc_end = 135417466
    | Mm_Uniprot = Q545W1
  }}
}}
'''Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein''', also known as '''ID3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3399| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Members of the ID family of helix-loop-helix (HLH) proteins lack a basic DNA-binding domain and inhibit transcription through formation of nonfunctional dimers that are incapable of binding to DNA.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3399| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Ellmeier W, Aguzzi A, Kleiner E, ''et al.'' |title=Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development. |journal=EMBO J. |volume=11 |issue= 7 |pages= 2563-71 |year= 1992 |pmid= 1628620 |doi=  }}
*{{cite journal  | author=White PS, Maris JM, Beltinger C, ''et al.'' |title=A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5520-4 |year= 1995 |pmid= 7777541 |doi=  }}
*{{cite journal  | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi=  }}
*{{cite journal  | author=Deed RW, Hirose T, Mitchell EL, ''et al.'' |title=Structural organisation and chromosomal mapping of the human Id-3 gene. |journal=Gene |volume=151 |issue= 1-2 |pages= 309-14 |year= 1995 |pmid= 7828896 |doi=  }}
*{{cite journal  | author=Deed RW, Bianchi SM, Atherton GT, ''et al.'' |title=An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types. |journal=Oncogene |volume=8 |issue= 3 |pages= 599-607 |year= 1993 |pmid= 8437843 |doi=  }}
*{{cite journal  | author=Ishiguro A, Spirin K, Shiohara M, ''et al.'' |title=Expression of Id2 and Id3 mRNA in human lymphocytes. |journal=Leuk. Res. |volume=19 |issue= 12 |pages= 989-96 |year= 1996 |pmid= 8632670 |doi=  }}
*{{cite journal  | author=Wibley J, Deed R, Jasiok M, ''et al.'' |title=A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions. |journal=Biochim. Biophys. Acta |volume=1294 |issue= 2 |pages= 138-46 |year= 1996 |pmid= 8645731 |doi=  }}
*{{cite journal  | author=Loveys DA, Streiff MB, Kato GJ |title=E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein. |journal=Nucleic Acids Res. |volume=24 |issue= 14 |pages= 2813-20 |year= 1996 |pmid= 8759016 |doi=  }}
*{{cite journal  | author=Deed RW, Armitage S, Norton JD |title=Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. |journal=J. Biol. Chem. |volume=271 |issue= 39 |pages= 23603-6 |year= 1996 |pmid= 8798572 |doi=  }}
*{{cite journal  | author=Deed RW, Jasiok M, Norton JD |title=Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. |journal=FEBS Lett. |volume=393 |issue= 1 |pages= 113-6 |year= 1996 |pmid= 8804437 |doi=  }}
*{{cite journal  | author=Chen B, Lim RW |title=Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2459-63 |year= 1997 |pmid= 8999959 |doi=  }}
*{{cite journal  | author=Langlands K, Yin X, Anand G, Prochownik EV |title=Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 19785-93 |year= 1997 |pmid= 9242638 |doi=  }}
*{{cite journal  | author=Deed RW, Hara E, Atherton GT, ''et al.'' |title=Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 6815-21 |year= 1997 |pmid= 9372912 |doi=  }}
*{{cite journal  | author=Deed RW, Jasiok M, Norton JD |title=Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells. |journal=J. Biol. Chem. |volume=273 |issue= 14 |pages= 8278-86 |year= 1998 |pmid= 9525934 |doi=  }}
*{{cite journal  | author=Asp J, Thornemo M, Inerot S, Lindahl A |title=The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes. |journal=FEBS Lett. |volume=438 |issue= 1-2 |pages= 85-90 |year= 1998 |pmid= 9821964 |doi=  }}
*{{cite journal  | author=Yates PR, Atherton GT, Deed RW, ''et al.'' |title=Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. |journal=EMBO J. |volume=18 |issue= 4 |pages= 968-76 |year= 1999 |pmid= 10022839 |doi= 10.1093/emboj/18.4.968 }}
*{{cite journal  | author=Moldes M, Boizard M, Liepvre XL, ''et al.'' |title=Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes. |journal=Biochem. J. |volume=344 Pt 3 |issue=  |pages= 873-80 |year= 2000 |pmid= 10585876 |doi=  }}
*{{cite journal  | author=Bounpheng MA, Dimas JJ, Dodds SG, Christy BA |title=Degradation of Id proteins by the ubiquitin-proteasome pathway. |journal=FASEB J. |volume=13 |issue= 15 |pages= 2257-64 |year= 2000 |pmid= 10593873 |doi=  }}
*{{cite journal  | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
*{{cite journal  | author=Jögi A, Persson P, Grynfeld A, ''et al.'' |title=Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9118-26 |year= 2002 |pmid= 11756408 |doi= 10.1074/jbc.M107713200 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] ITGAX

• INFO: Beginning work on ITGAX... {November 18, 2007 3:02:53 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:04:08 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_ITGAX_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n3y.
 | PDB = {{PDB2|1n3y}}
 | Name = Integrin, alpha X (complement component 3 receptor 4 subunit)
 | HGNCid = 6152
 | Symbol = ITGAX
 | AltSymbols =; CD11C
 | OMIM = 151510
 | ECnumber =  
 | Homologene = 55493
 | MGIid = 96609
 | GeneAtlas_image1 = PBB_GE_ITGAX_210184_at_tn.png
 | Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3687
    | Hs_Ensembl = ENSG00000140678
    | Hs_RefseqProtein = XP_001127869
    | Hs_RefseqmRNA = XM_001127869
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 31274010
    | Hs_GenLoc_end = 31301819
    | Hs_Uniprot = P20702
    | Mm_EntrezGene = 16411
    | Mm_Ensembl = ENSMUSG00000030789
    | Mm_RefseqmRNA = NM_021334
    | Mm_RefseqProtein = NP_067309
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 127920710
    | Mm_GenLoc_end = 127941804
    | Mm_Uniprot = Q3TD13
  }}
}}
'''Integrin, alpha X (complement component 3 receptor 4 subunit)''', also known as '''ITGAX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITGAX integrin, alpha X (complement component 3 receptor 4 subunit)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3687| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes the integrin alpha X chain protein. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as inactivated-C3b (iC3b) receptor 4 (CR4). The alpha X beta 2 complex seems to overlap the properties of the alpha M beta 2 integrin in the adherence of neutrophils and monocytes to stimulated endothelium cells, and in the phagocytosis of complement coated particles.<ref name="entrez">{{cite web | title = Entrez Gene: ITGAX integrin, alpha X (complement component 3 receptor 4 subunit)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3687| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Stewart M, Thiel M, Hogg N |title=Leukocyte integrins. |journal=Curr. Opin. Cell Biol. |volume=7 |issue= 5 |pages= 690-6 |year= 1996 |pmid= 8573344 |doi=  }}
*{{cite journal  | author=Steinman RM, Pack M, Inaba K |title=Dendritic cells in the T-cell areas of lymphoid organs. |journal=Immunol. Rev. |volume=156 |issue=  |pages= 25-37 |year= 1997 |pmid= 9176697 |doi=  }}
*{{cite journal  | author=Córbi AL, Lopéz-Rodríguez C |title=CD11c integrin gene promoter activity during myeloid differentiation. |journal=Leuk. Lymphoma |volume=25 |issue= 5-6 |pages= 415-25 |year= 1997 |pmid= 9250811 |doi=  }}
*{{cite journal  | author=Ugarova TP, Yakubenko VP |title=Recognition of fibrinogen by leukocyte integrins. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue=  |pages= 368-85 |year= 2001 |pmid= 11460493 |doi=  }}
*{{cite journal  | author=Valentin A, Lundin K, Patarroyo M, Asjö B |title=The leukocyte adhesion glycoprotein CD18 participates in HIV-1-induced syncytia formation in monocytoid and T cells. |journal=J. Immunol. |volume=144 |issue= 3 |pages= 934-7 |year= 1990 |pmid= 1967280 |doi=  }}
*{{cite journal  | author=Gaidano G, Bergui L, Schena M, ''et al.'' |title=Integrin distribution and cytoskeleton organization in normal and malignant monocytes. |journal=Leukemia |volume=4 |issue= 10 |pages= 682-7 |year= 1990 |pmid= 1976870 |doi=  }}
*{{cite journal  | author=Corbi AL, Garcia-Aguilar J, Springer TA |title=Genomic structure of an integrin alpha subunit, the leukocyte p150,95 molecule. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2782-8 |year= 1990 |pmid= 2303426 |doi=  }}
*{{cite journal  | author=Corbi AL, Larson RS, Kishimoto TK, ''et al.'' |title=Chromosomal location of the genes encoding the leukocyte adhesion receptors LFA-1, Mac-1 and p150,95. Identification of a gene cluster involved in cell adhesion. |journal=J. Exp. Med. |volume=167 |issue= 5 |pages= 1597-607 |year= 1988 |pmid= 3284962 |doi=  }}
*{{cite journal  | author=Corbi AL, Miller LJ, O'Connor K, ''et al.'' |title=cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p150,95. |journal=EMBO J. |volume=6 |issue= 13 |pages= 4023-8 |year= 1988 |pmid= 3327687 |doi=  }}
*{{cite journal  | author=Miller LJ, Wiebe M, Springer TA |title=Purification and alpha subunit N-terminal sequences of human Mac-1 and p150,95 leukocyte adhesion proteins. |journal=J. Immunol. |volume=138 |issue= 8 |pages= 2381-3 |year= 1987 |pmid= 3549901 |doi=  }}
*{{cite journal  | author=Bilsland CA, Diamond MS, Springer TA |title=The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous beta subunit and localization of a ligand recognition site to the I domain. |journal=J. Immunol. |volume=152 |issue= 9 |pages= 4582-9 |year= 1994 |pmid= 7512600 |doi=  }}
*{{cite journal  | author=Lecoanet-Henchoz S, Gauchat JF, Aubry JP, ''et al.'' |title=CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD11b-CD18 and CD11c-CD18. |journal=Immunity |volume=3 |issue= 1 |pages= 119-25 |year= 1995 |pmid= 7621072 |doi=  }}
*{{cite journal  | author=Garcìa-Barcina M, Winnock M, Bidaurrazaga I, ''et al.'' |title=Detection of cell-adhesion molecules on human liver-associated lymphocytes. |journal=Immunology |volume=82 |issue= 1 |pages= 95-8 |year= 1994 |pmid= 8045597 |doi=  }}
*{{cite journal  | author=Philippeaux MM, Vesin C, Tacchini-Cottier F, Piguet PF |title=Activated human platelets express beta2 integrin. |journal=Eur. J. Haematol. |volume=56 |issue= 3 |pages= 130-7 |year= 1996 |pmid= 8598231 |doi=  }}
*{{cite journal  | author=de Vree WJ, Fontijne-Dorsman AN, Koster JF, Sluiter W |title=Photodynamic treatment of human endothelial cells promotes the adherence of neutrophils in vitro. |journal=Br. J. Cancer |volume=73 |issue= 11 |pages= 1335-40 |year= 1996 |pmid= 8645576 |doi=  }}
*{{cite journal  | author=Bernstein CN, Sargent M, Gallatin WM |title=Beta2 integrin/ICAM expression in Crohn's disease. |journal=Clin. Immunol. Immunopathol. |volume=86 |issue= 2 |pages= 147-60 |year= 1998 |pmid= 9473377 |doi=  }}
*{{cite journal  | author=Shelley CS, Da Silva N, Georgakis A, ''et al.'' |title=Mapping of the human CD11c (ITGAX) and CD11d (ITGAD) genes demonstrates that they are arranged in tandem separated by no more than 11.5 kb. |journal=Genomics |volume=49 |issue= 2 |pages= 334-6 |year= 1998 |pmid= 9598326 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] KIR3DL1

• INFO: Beginning work on KIR3DL1... {November 18, 2007 3:04:09 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:05:58 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Killer cell immunoglobulin-like receptor, three domains, long cytoplasmic tail, 1
 | HGNCid = 6338
 | Symbol = KIR3DL1
 | AltSymbols =; KIR; AMB11; CD158E1; CD158E1/2; CD158E2; CL-11; CL-2; KIR-G1; KIR3DL1/2V; KIR3DS1; MGC119726; MGC119728; MGC126589; MGC126591; NKAT10; NKAT3; NKB1; NKB1B
 | OMIM = 604946
 | ECnumber =  
 | Homologene = 77448
 | MGIid = 3612791
 | GeneAtlas_image1 = PBB_GE_KIR3DL1_211389_x_at_tn.png
 | GeneAtlas_image2 = PBB_GE_KIR3DL1_207313_x_at_tn.png
 | GeneAtlas_image3 = PBB_GE_KIR3DL1_211687_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0030109 |text = HLA-B specific inhibitory MHC class I receptor activity}} {{GNF_GO|id=GO:0032393 |text = MHC class I receptor activity}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0030101 |text = natural killer cell activation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3811
    | Hs_Ensembl = ENSG00000167633
    | Hs_RefseqProtein = NP_037421
    | Hs_RefseqmRNA = NM_013289
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 60019741
    | Hs_GenLoc_end = 60034044
    | Hs_Uniprot = P43629
    | Mm_EntrezGene = 245615
    | Mm_Ensembl = ENSMUSG00000057439
    | Mm_RefseqmRNA = NM_177748
    | Mm_RefseqProtein = NP_808416
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 131795127
    | Mm_GenLoc_end = 131815400
    | Mm_Uniprot = Q673W3
  }}
}}
'''Killer cell immunoglobulin-like receptor, three domains, long cytoplasmic tail, 1''', also known as '''KIR3DL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KIR3DL1 killer cell immunoglobulin-like receptor, three domains, long cytoplasmic tail, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3811| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Killer cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. The KIR genes are polymorphic and highly homologous and they are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). The gene content of the KIR gene cluster varies among haplotypes, although several &quot;framework&quot; genes are found in all haplotypes (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response.<ref name="entrez">{{cite web | title = Entrez Gene: KIR3DL1 killer cell immunoglobulin-like receptor, three domains, long cytoplasmic tail, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3811| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Selvakumar A, Steffens U, Dupont B |title=Polymorphism and domain variability of human killer cell inhibitory receptors. |journal=Immunol. Rev. |volume=155 |issue=  |pages= 183-96 |year= 1997 |pmid= 9059894 |doi=  }}
*{{cite journal  | author=D'Andrea A, Chang C, Franz-Bacon K, ''et al.'' |title=Molecular cloning of NKB1. A natural killer cell receptor for HLA-B allotypes. |journal=J. Immunol. |volume=155 |issue= 5 |pages= 2306-10 |year= 1995 |pmid= 7650366 |doi=  }}
*{{cite journal  | author=Colonna M, Samaridis J |title=Cloning of immunoglobulin-superfamily members associated with HLA-C and HLA-B recognition by human natural killer cells. |journal=Science |volume=268 |issue= 5209 |pages= 405-8 |year= 1995 |pmid= 7716543 |doi=  }}
*{{cite journal  | author=Wagtmann N, Biassoni R, Cantoni C, ''et al.'' |title=Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related molecules with diversity in both the extra- and intracellular domains. |journal=Immunity |volume=2 |issue= 5 |pages= 439-49 |year= 1995 |pmid= 7749980 |doi=  }}
*{{cite journal  | author=Litwin V, Gumperz J, Parham P, ''et al.'' |title=NKB1: a natural killer cell receptor involved in the recognition of polymorphic HLA-B molecules. |journal=J. Exp. Med. |volume=180 |issue= 2 |pages= 537-43 |year= 1994 |pmid= 8046332 |doi=  }}
*{{cite journal  | author=Döhring C, Samaridis J, Colonna M |title=Alternatively spliced forms of human killer inhibitory receptors. |journal=Immunogenetics |volume=44 |issue= 3 |pages= 227-30 |year= 1996 |pmid= 8662091 |doi=  }}
*{{cite journal  | author=Pende D, Biassoni R, Cantoni C, ''et al.'' |title=The natural killer cell receptor specific for HLA-A allotypes: a novel member of the p58/p70 family of inhibitory receptors that is characterized by three immunoglobulin-like domains and is expressed as a 140-kD disulphide-linked dimer. |journal=J. Exp. Med. |volume=184 |issue= 2 |pages= 505-18 |year= 1996 |pmid= 8760804 |doi=  }}
*{{cite journal  | author=Wagtmann N, Rajagopalan S, Winter CC, ''et al.'' |title=Killer cell inhibitory receptors specific for HLA-C and HLA-B identified by direct binding and by functional transfer. |journal=Immunity |volume=3 |issue= 6 |pages= 801-9 |year= 1996 |pmid= 8777725 |doi=  }}
*{{cite journal  | author=Valiante NM, Uhrberg M, Shilling HG, ''et al.'' |title=Functionally and structurally distinct NK cell receptor repertoires in the peripheral blood of two human donors. |journal=Immunity |volume=7 |issue= 6 |pages= 739-51 |year= 1998 |pmid= 9430220 |doi=  }}
*{{cite journal  | author=Uhrberg M, Valiante NM, Shum BP, ''et al.'' |title=Human diversity in killer cell inhibitory receptor genes. |journal=Immunity |volume=7 |issue= 6 |pages= 753-63 |year= 1998 |pmid= 9430221 |doi=  }}
*{{cite journal  | author=Vyas Y, Selvakumar A, Steffens U, Dupont B |title=Multiple transcripts of the killer cell immunoglobulin-like receptor family, KIR3DL1 (NKB1), are expressed by natural killer cells of a single individual. |journal=Tissue Antigens |volume=52 |issue= 6 |pages= 510-9 |year= 1999 |pmid= 9894849 |doi=  }}
*{{cite journal  | author=Kwon D, Chwae YJ, Choi IH, ''et al.'' |title=Diversity of the p70 killer cell inhibitory receptor (KIR3DL) family members in a single individual. |journal=Mol. Cells |volume=10 |issue= 1 |pages= 54-60 |year= 2000 |pmid= 10774747 |doi=  }}
*{{cite journal  | author=Crum KA, Logue SE, Curran MD, Middleton D |title=Development of a PCR-SSOP approach capable of defining the natural killer cell inhibitory receptor (KIR) gene sequence repertoires. |journal=Tissue Antigens |volume=56 |issue= 4 |pages= 313-26 |year= 2001 |pmid= 11098931 |doi=  }}
*{{cite journal  | author=Gardiner CM, Guethlein LA, Shilling HG, ''et al.'' |title=Different NK cell surface phenotypes defined by the DX9 antibody are due to KIR3DL1 gene polymorphism. |journal=J. Immunol. |volume=166 |issue= 5 |pages= 2992-3001 |year= 2001 |pmid= 11207248 |doi=  }}
*{{cite journal  | author=Yamochi T, Semba K, Tsuji K, ''et al.'' |title=ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3). |journal=Eur. J. Biochem. |volume=268 |issue= 23 |pages= 6076-82 |year= 2002 |pmid= 11733001 |doi=  }}
*{{cite journal  | author=Shilling HG, Guethlein LA, Cheng NW, ''et al.'' |title=Allelic polymorphism synergizes with variable gene content to individualize human KIR genotype. |journal=J. Immunol. |volume=168 |issue= 5 |pages= 2307-15 |year= 2002 |pmid= 11859120 |doi=  }}
*{{cite journal  | author=Martin MP, Gao X, Lee JH, ''et al.'' |title=Epistatic interaction between KIR3DS1 and HLA-B delays the progression to AIDS. |journal=Nat. Genet. |volume=31 |issue= 4 |pages= 429-34 |year= 2002 |pmid= 12134147 |doi= 10.1038/ng934 }}
*{{cite journal  | author=Chwae YJ, Chang MJ, Park SM, ''et al.'' |title=Molecular mechanism of the activation-induced cell death inhibition mediated by a p70 inhibitory killer cell Ig-like receptor in Jurkat T cells. |journal=J. Immunol. |volume=169 |issue= 7 |pages= 3726-35 |year= 2002 |pmid= 12244166 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] KLK2

• INFO: Beginning work on KLK2... {November 18, 2007 3:05:59 PM PST}
• SEARCH REDIRECT: Control Box Found: KLK2 {November 18, 2007 3:07:25 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:07:34 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:07:34 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:07:34 PM PST}
• UPDATED: Updated protein page: KLK2 {November 18, 2007 3:07:47 PM PST}

[edit] LAMC1

• INFO: Beginning work on LAMC1... {November 18, 2007 3:07:47 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:08:36 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_LAMC1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1klo.
 | PDB = {{PDB2|1klo}}, {{PDB2|1npe}}, {{PDB2|1tle}}
 | Name = Laminin, gamma 1 (formerly LAMB2)
 | HGNCid = 6492
 | Symbol = LAMC1
 | AltSymbols =; LAMB2; MGC87297
 | OMIM = 150290
 | ECnumber =  
 | Homologene = 1724
 | MGIid = 99914
 | GeneAtlas_image1 = PBB_GE_LAMC1_200771_at_tn.png
 | GeneAtlas_image2 = PBB_GE_LAMC1_200770_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}} 
 | Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007492 |text = endoderm development}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3915
    | Hs_Ensembl = ENSG00000135862
    | Hs_RefseqProtein = NP_002284
    | Hs_RefseqmRNA = NM_002293
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 181259176
    | Hs_GenLoc_end = 181381350
    | Hs_Uniprot = P11047
    | Mm_EntrezGene = 226519
    | Mm_Ensembl = ENSMUSG00000026478
    | Mm_RefseqmRNA = NM_010683
    | Mm_RefseqProtein = NP_034813
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 154981138
    | Mm_GenLoc_end = 155095004
    | Mm_Uniprot = Q3TRH4
  }}
}}
'''Laminin, gamma 1 (formerly LAMB2)''', also known as '''LAMC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3915| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis.<ref name="entrez">{{cite web | title = Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3915| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Ljubimova JY, Fujita M, Khazenzon NM, ''et al.'' |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue=  |pages= 81-8 |year= 2006 |pmid= 16146715 |doi=  }}
*{{cite journal  | author=Santos CL, Sabbaga J, Brentani R |title=Differences in human laminin B2 sequences. |journal=DNA Seq. |volume=1 |issue= 4 |pages= 275-7 |year= 1992 |pmid= 1806043 |doi=  }}
*{{cite journal  | author=Kallunki T, Ikonen J, Chow LT, ''et al.'' |title=Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene. |journal=J. Biol. Chem. |volume=266 |issue= 1 |pages= 221-8 |year= 1991 |pmid= 1985895 |doi=  }}
*{{cite journal  | author=Hunter DD, Shah V, Merlie JP, Sanes JR |title=A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. |journal=Nature |volume=338 |issue= 6212 |pages= 229-34 |year= 1989 |pmid= 2922051 |doi= 10.1038/338229a0 }}
*{{cite journal  | author=Fukushima Y, Pikkarainen T, Kallunki T, ''et al.'' |title=Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25----q31. |journal=Cytogenet. Cell Genet. |volume=48 |issue= 3 |pages= 137-41 |year= 1989 |pmid= 3234037 |doi=  }}
*{{cite journal  | author=Pikkarainen T, Kallunki T, Tryggvason K |title=Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6751-8 |year= 1988 |pmid= 3360804 |doi=  }}
*{{cite journal  | author=Mattei MG, Weil D, Pribula-Conway D, ''et al.'' |title=cDNA cloning, expression and mapping of human laminin B2 gene to chromosome 1q31. |journal=Hum. Genet. |volume=79 |issue= 3 |pages= 235-41 |year= 1988 |pmid= 3402995 |doi=  }}
*{{cite journal  | author=Davis JM, Narachi MA, Alton NK, Arakawa T |title=Structure of human tumor necrosis factor alpha derived from recombinant DNA. |journal=Biochemistry |volume=26 |issue= 5 |pages= 1322-6 |year= 1987 |pmid= 3552045 |doi=  }}
*{{cite journal  | author=Wewer UM, Gerecke DR, Durkin ME, ''et al.'' |title=Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas. |journal=Genomics |volume=24 |issue= 2 |pages= 243-52 |year= 1995 |pmid= 7698745 |doi= 10.1006/geno.1994.1612 }}
*{{cite journal  | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675-84 |year= 1998 |pmid= 9647658 |doi=  }}
*{{cite journal  | author=Kohfeldt E, Sasaki T, Göhring W, Timpl R |title=Nidogen-2: a new basement membrane protein with diverse binding properties. |journal=J. Mol. Biol. |volume=282 |issue= 1 |pages= 99-109 |year= 1998 |pmid= 9733643 |doi= 10.1006/jmbi.1998.2004 }}
*{{cite journal  | author=Suzuki H, Denisenko ON, Suzuki Y, ''et al.'' |title=Inducible transcriptional activity of bcn-1 element from laminin gamma1-chain gene promoter in renal and nonrenal cells. |journal=Am. J. Physiol. |volume=275 |issue= 4 Pt 2 |pages= F518-26 |year= 1998 |pmid= 9755123 |doi=  }}
*{{cite journal  | author=Smyth N, Vatansever HS, Murray P, ''et al.'' |title=Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. |journal=J. Cell Biol. |volume=144 |issue= 1 |pages= 151-60 |year= 1999 |pmid= 9885251 |doi=  }}
*{{cite journal  | author=Kikkawa Y, Sanzen N, Fujiwara H, ''et al.'' |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue=  |pages= 869-76 |year= 2000 |pmid= 10671376 |doi=  }}
*{{cite journal  | author=Champliaud MF, Virtanen I, Tiger CF, ''et al.'' |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326-35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal  | author=Pedraza C, Geberhiwot T, Ingerpuu S, ''et al.'' |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831-8 |year= 2000 |pmid= 11067943 |doi=  }}
*{{cite journal  | author=Parsons SF, Lee G, Spring FA, ''et al.'' |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312-20 |year= 2001 |pmid= 11133776 |doi=  }}
*{{cite journal  | author=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545-55 |year= 2001 |pmid= 11311202 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] MAP3K11

• INFO: Beginning work on MAP3K11... {November 18, 2007 3:10:05 PM PST}
• SEARCH REDIRECT: Control Box Found: MAP3K11 {November 18, 2007 3:11:15 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:11:27 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:11:27 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:11:27 PM PST}
• UPDATED: Updated protein page: MAP3K11 {November 18, 2007 3:11:42 PM PST}

[edit] MSX1

• INFO: Beginning work on MSX1... {November 18, 2007 3:11:42 PM PST}
• SEARCH REDIRECT: Control Box Found: MSX1 {November 18, 2007 3:12:51 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:12:52 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:12:52 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:12:52 PM PST}
• UPDATED: Updated protein page: MSX1 {November 18, 2007 3:13:08 PM PST}

[edit] MSX2

• INFO: Beginning work on MSX2... {November 18, 2007 3:13:08 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:14:39 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_MSX2_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ig7.
 | PDB = {{PDB2|1ig7}}
 | Name = Msh homeobox 2
 | HGNCid = 7392
 | Symbol = MSX2
 | AltSymbols =; CRS2; FPP; HOX8; MSH; PFM; PFM1
 | OMIM = 123101
 | ECnumber =  
 | Homologene = 1837
 | MGIid = 97169
 | GeneAtlas_image1 = PBB_GE_MSX2_205555_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_MSX2_210319_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030326 |text = embryonic limb morphogenesis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4488
    | Hs_Ensembl = ENSG00000120149
    | Hs_RefseqProtein = NP_002440
    | Hs_RefseqmRNA = NM_002449
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 174084208
    | Hs_GenLoc_end = 174090507
    | Hs_Uniprot = P35548
    | Mm_EntrezGene = 17702
    | Mm_Ensembl = ENSMUSG00000021469
    | Mm_RefseqmRNA = NM_013601
    | Mm_RefseqProtein = NP_038629
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 53475420
    | Mm_GenLoc_end = 53480608
    | Mm_Uniprot = Q3UZH5
  }}
}}
'''Msh homeobox 2''', also known as '''MSX2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MSX2 msh homeobox 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4488| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a member of the muscle segment homeobox gene family. The encoded protein is a transcriptional repressor whose normal activity may establish a balance between survival and apoptosis of neural crest-derived cells required for proper craniofacial morphogenesis. The encoded protein may also have a role in promoting cell growth under certain conditions and may be an important target for the RAS signaling pathways. Mutations in this gene are associated with parietal foramina 1 and craniosynostosis type 2.<ref name="entrez">{{cite web | title = Entrez Gene: MSX2 msh homeobox 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4488| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Suzuki M, Tanaka M, Iwase T, ''et al.'' |title=Over-expression of HOX-8, the human homologue of the mouse Hox-8 homeobox gene, in human tumors. |journal=Biochem. Biophys. Res. Commun. |volume=194 |issue= 1 |pages= 187-93 |year= 1993 |pmid= 7687426 |doi= 10.1006/bbrc.1993.1802 }}
*{{cite journal  | author=Semenza GL, Wang GL, Kundu R |title=DNA binding and transcriptional properties of wild-type and mutant forms of the homeodomain protein Msx2. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 1 |pages= 257-62 |year= 1995 |pmid= 7726844 |doi= 10.1006/bbrc.1995.1497 }}
*{{cite journal  | author=Iimura T |title=[Molecular cloning and expression of homeobox-containing genes during hard tissue development] |journal=Kokubyo Gakkai Zasshi |volume=61 |issue= 4 |pages= 590-604 |year= 1995 |pmid= 7897272 |doi=  }}
*{{cite journal  | author=Hodgkinson JE, Davidson CL, Beresford J, Sharpe PT |title=Expression of a human homeobox-containing gene is regulated by 1,25(OH)2D3 in bone cells. |journal=Biochim. Biophys. Acta |volume=1174 |issue= 1 |pages= 11-6 |year= 1993 |pmid= 8101453 |doi=  }}
*{{cite journal  | author=Jabs EW, Müller U, Li X, ''et al.'' |title=A mutation in the homeodomain of the human MSX2 gene in a family affected with autosomal dominant craniosynostosis. |journal=Cell |volume=75 |issue= 3 |pages= 443-50 |year= 1993 |pmid= 8106171 |doi=  }}
*{{cite journal  | author=Takahashi C, Akiyama N, Matsuzaki T, ''et al.'' |title=Characterization of a human MSX-2 cDNA and its fragment isolated as a transformation suppressor gene against v-Ki-ras oncogene. |journal=Oncogene |volume=12 |issue= 10 |pages= 2137-46 |year= 1996 |pmid= 8668339 |doi=  }}
*{{cite journal  | author=Kostrzewa M, Grady DL, Moyzis RK, ''et al.'' |title=Integration of four genes, a pseudogene, thirty-one STSs, and a highly polymorphic STRP into the 7-10 Mb YAC contig of 5q34-q35. |journal=Hum. Genet. |volume=97 |issue= 3 |pages= 399-403 |year= 1996 |pmid= 8786091 |doi=  }}
*{{cite journal  | author=Ma L, Golden S, Wu L, Maxson R |title=The molecular basis of Boston-type craniosynostosis: the Pro148-->His mutation in the N-terminal arm of the MSX2 homeodomain stabilizes DNA binding without altering nucleotide sequence preferences. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 1915-20 |year= 1997 |pmid= 8968743 |doi=  }}
*{{cite journal  | author=Quinn LM, Johnson BV, Nicholl J, ''et al.'' |title=Isolation and identification of homeobox genes from the human placenta including a novel member of the Distal-less family, DLX4. |journal=Gene |volume=187 |issue= 1 |pages= 55-61 |year= 1997 |pmid= 9073066 |doi=  }}
*{{cite journal  | author=Zhang H, Hu G, Wang H, ''et al.'' |title=Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism. |journal=Mol. Cell. Biol. |volume=17 |issue= 5 |pages= 2920-32 |year= 1997 |pmid= 9111364 |doi=  }}
*{{cite journal  | author=Wu L, Wu H, Ma L, ''et al.'' |title=Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA. |journal=Mech. Dev. |volume=65 |issue= 1-2 |pages= 3-17 |year= 1997 |pmid= 9256341 |doi=  }}
*{{cite journal  | author=Newberry EP, Latifi T, Battaile JT, Towler DA |title=Structure-function analysis of Msx2-mediated transcriptional suppression. |journal=Biochemistry |volume=36 |issue= 34 |pages= 10451-62 |year= 1997 |pmid= 9265625 |doi= 10.1021/bi971008x }}
*{{cite journal  | author=Stelnicki EJ, Kömüves LG, Holmes D, ''et al.'' |title=The human homeobox genes MSX-1, MSX-2, and MOX-1 are differentially expressed in the dermis and epidermis in fetal and adult skin. |journal=Differentiation |volume=62 |issue= 1 |pages= 33-41 |year= 1997 |pmid= 9373945 |doi=  }}
*{{cite journal  | author=Iimura T, Takeda K, Goseki M, ''et al.'' |title=Characterization of two length cDNA for human MSX-2 from dental pulp-derived cells. |journal=DNA Seq. |volume=8 |issue= 1-2 |pages= 87-92 |year= 1998 |pmid= 9522127 |doi=  }}
*{{cite journal  | author=Newberry EP, Latifi T, Towler DA |title=The RRM domain of MINT, a novel Msx2 binding protein, recognizes and regulates the rat osteocalcin promoter. |journal=Biochemistry |volume=38 |issue= 33 |pages= 10678-90 |year= 1999 |pmid= 10451362 |doi= 10.1021/bi990967j }}
*{{cite journal  | author=Wilkie AO, Tang Z, Elanko N, ''et al.'' |title=Functional haploinsufficiency of the human homeobox gene MSX2 causes defects in skull ossification. |journal=Nat. Genet. |volume=24 |issue= 4 |pages= 387-90 |year= 2000 |pmid= 10742103 |doi= 10.1038/74224 }}
*{{cite journal  | author=Wuyts W, Reardon W, Preis S, ''et al.'' |title=Identification of mutations in the MSX2 homeobox gene in families affected with foramina parietalia permagna. |journal=Hum. Mol. Genet. |volume=9 |issue= 8 |pages= 1251-5 |year= 2000 |pmid= 10767351 |doi=  }}
*{{cite journal  | author=Quinn LM, Latham SE, Kalionis B |title=The homeobox genes MSX2 and MOX2 are candidates for regulating epithelial-mesenchymal cell interactions in the human placenta. |journal=Placenta |volume=21 Suppl A |issue=  |pages= S50-4 |year= 2000 |pmid= 10831122 |doi=  }}
*{{cite journal  | author=Masuda Y, Sasaki A, Shibuya H, ''et al.'' |title=Dlxin-1, a novel protein that binds Dlx5 and regulates its transcriptional function. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 5331-8 |year= 2001 |pmid= 11084035 |doi= 10.1074/jbc.M008590200 }}
*{{cite journal  | author=Shirakabe K, Terasawa K, Miyama K, ''et al.'' |title=Regulation of the activity of the transcription factor Runx2 by two homeobox proteins, Msx2 and Dlx5. |journal=Genes Cells |volume=6 |issue= 10 |pages= 851-6 |year= 2002 |pmid= 11683913 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] MT2A

• INFO: Beginning work on MT2A... {November 18, 2007 3:14:39 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:15:23 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_MT2A_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mhu.
 | PDB = {{PDB2|1mhu}}, {{PDB2|1mrb}}, {{PDB2|1mrt}}, {{PDB2|2mhu}}
 | Name = Metallothionein 2A
 | HGNCid = 7406
 | Symbol = MT2A
 | AltSymbols =; MT2
 | OMIM = 156360
 | ECnumber =  
 | Homologene = 48388
 | MGIid = 97172
 | GeneAtlas_image1 = PBB_GE_MT2A_212185_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006878 |text = cellular copper ion homeostasis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4502
    | Hs_Ensembl = ENSG00000125148
    | Hs_RefseqProtein = NP_005944
    | Hs_RefseqmRNA = NM_005953
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 55199997
    | Hs_GenLoc_end = 55200909
    | Hs_Uniprot = P02795
    | Mm_EntrezGene = 17750
    | Mm_Ensembl = ENSMUSG00000031762
    | Mm_RefseqmRNA = NM_008630
    | Mm_RefseqProtein = NP_032656
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 97061913
    | Mm_GenLoc_end = 97062691
    | Mm_Uniprot = P02798
  }}
}}
'''Metallothionein 2A''', also known as '''MT2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MT2A metallothionein 2A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4502| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kissling MM, Kägi HR |title=Primary structure of human hepatic metallothionein. |journal=FEBS Lett. |volume=82 |issue= 2 |pages= 247-50 |year= 1977 |pmid= 913597 |doi=  }}
*{{cite journal  | author=Yamazaki S, Nakanishi M, Hamamoto T, ''et al.'' |title=Expression of human metallothionein-II fusion protein in Escherichia coli. |journal=Biochem. Int. |volume=28 |issue= 3 |pages= 451-60 |year= 1993 |pmid= 1339282 |doi=  }}
*{{cite journal  | author=Messerle BA, Schäffer A, Vasák M, ''et al.'' |title=Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy. |journal=J. Mol. Biol. |volume=225 |issue= 2 |pages= 433-43 |year= 1992 |pmid= 1593628 |doi=  }}
*{{cite journal  | author=Zafarullah M, Martel-Pelletier J, Cloutier JM, ''et al.'' |title=Expression of c-fos, c-jun, jun-B, metallothionein and metalloproteinase genes in human chondrocyte. |journal=FEBS Lett. |volume=306 |issue= 2-3 |pages= 169-72 |year= 1992 |pmid= 1633872 |doi=  }}
*{{cite journal  | author=Messerle BA, Schäffer A, Vasák M, ''et al.'' |title=Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy. |journal=J. Mol. Biol. |volume=214 |issue= 3 |pages= 765-79 |year= 1990 |pmid= 2388267 |doi=  }}
*{{cite journal  | author=Duguid JR, Bohmont CW, Liu NG, Tourtellotte WW |title=Changes in brain gene expression shared by scrapie and Alzheimer disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 18 |pages= 7260-4 |year= 1989 |pmid= 2780570 |doi=  }}
*{{cite journal  | author=Karin M, Haslinger A, Heguy A, ''et al.'' |title=Metal-responsive elements act as positive modulators of human metallothionein-IIA enhancer activity. |journal=Mol. Cell. Biol. |volume=7 |issue= 2 |pages= 606-13 |year= 1987 |pmid= 3821726 |doi=  }}
*{{cite journal  | author=Karin M, Haslinger A, Holtgreve H, ''et al.'' |title=Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene. |journal=Nature |volume=308 |issue= 5959 |pages= 513-9 |year= 1984 |pmid= 6323998 |doi=  }}
*{{cite journal  | author=Schmidt CJ, Hamer DH, McBride OW |title=Chromosomal location of human metallothionein genes: implications for Menkes' disease. |journal=Science |volume=224 |issue= 4653 |pages= 1104-6 |year= 1984 |pmid= 6719135 |doi=  }}
*{{cite journal  | author=Karin M, Richards RI |title=Human metallothionein genes: molecular cloning and sequence analysis of the mRNA. |journal=Nucleic Acids Res. |volume=10 |issue= 10 |pages= 3165-73 |year= 1982 |pmid= 6896577 |doi=  }}
*{{cite journal  | author=Karin M, Richards RI |title=Human metallothionein genes--primary structure of the metallothionein-II gene and a related processed gene. |journal=Nature |volume=299 |issue= 5886 |pages= 797-802 |year= 1982 |pmid= 7133118 |doi=  }}
*{{cite journal  | author=Lambert E, Kille P, Swaminathan R |title=Cloning and sequencing a novel metallothionein I isoform expressed in human reticulocytes. |journal=FEBS Lett. |volume=389 |issue= 2 |pages= 210-2 |year= 1996 |pmid= 8766831 |doi=  }}
*{{cite journal  | author=Woo ES, Dellapiazza D, Wang AS, Lazo JS |title=Energy-dependent nuclear binding dictates metallothionein localization. |journal=J. Cell. Physiol. |volume=182 |issue= 1 |pages= 69-76 |year= 1999 |pmid= 10567918 |doi= 10.1002/(SICI)1097-4652(200001)182:1<69::AID-JCP8>3.0.CO;2-9 }}
*{{cite journal  | author=Jiang LJ, Vasák M, Vallee BL, Maret W |title=Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole molecule. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2503-8 |year= 2000 |pmid= 10716985 |doi=  }}
*{{cite journal  | author=Garrett SH, Sens MA, Shukla D, ''et al.'' |title=Metallothionein isoform 1 and 2 gene expression in the human prostate: downregulation of MT-1X in advanced prostate cancer. |journal=Prostate |volume=43 |issue= 2 |pages= 125-35 |year= 2000 |pmid= 10754528 |doi=  }}
*{{cite journal  | author=Ebert MP, Günther T, Hoffmann J, ''et al.'' |title=Expression of metallothionein II in intestinal metaplasia, dysplasia, and gastric cancer. |journal=Cancer Res. |volume=60 |issue= 7 |pages= 1995-2001 |year= 2000 |pmid= 10766190 |doi=  }}
*{{cite journal  | author=Toyama M, Yamashita M, Hirayama N, Murooka Y |title=Interactions of arsenic with human metallothionein-2. |journal=J. Biochem. |volume=132 |issue= 2 |pages= 217-21 |year= 2003 |pmid= 12153718 |doi=  }}
*{{cite journal  | author=Sun X, Kang YJ |title=Prior increase in metallothionein levels is required to prevent doxorubicin cardiotoxicity. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 8 |pages= 652-7 |year= 2002 |pmid= 12192109 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Izmailova E, Bertley FM, Huang Q, ''et al.'' |title=HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages. |journal=Nat. Med. |volume=9 |issue= 2 |pages= 191-7 |year= 2003 |pmid= 12539042 |doi= 10.1038/nm822 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] OAS1

• INFO: Beginning work on OAS1... {November 18, 2007 3:15:24 PM PST}
• SEARCH REDIRECT: Control Box Found: OAS1 {November 18, 2007 3:16:17 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:16:23 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:16:23 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:16:23 PM PST}
• UPDATED: Updated protein page: OAS1 {November 18, 2007 3:16:34 PM PST}

[edit] RAPGEF1

• INFO: Beginning work on RAPGEF1... {November 18, 2007 2:54:14 PM PST}
• SEARCH REDIRECT: Control Box Found: RAPGEF1 {November 18, 2007 2:55:46 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:55:53 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:55:53 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:55:53 PM PST}
• UPDATED: Updated protein page: RAPGEF1 {November 18, 2007 2:56:07 PM PST}

[edit] TACSTD1

• INFO: Beginning work on TACSTD1... {November 18, 2007 3:08:36 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:10:05 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Tumor-associated calcium signal transducer 1
 | HGNCid = 11529
 | Symbol = TACSTD1
 | AltSymbols =; CD326; CO17-1A; EGP; EGP40; Ep-CAM; GA733-2; KSA; M4S1; MIC18; MK-1; TROP1; hEGP-2
 | OMIM = 185535
 | ECnumber =  
 | Homologene = 1764
 | MGIid = 106653
 | GeneAtlas_image1 = PBB_GE_TACSTD1_201839_s_at_tn.png
 | Function = 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4072
    | Hs_Ensembl = ENSG00000119888
    | Hs_RefseqProtein = NP_002345
    | Hs_RefseqmRNA = NM_002354
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 47449954
    | Hs_GenLoc_end = 47467661
    | Hs_Uniprot = P16422
    | Mm_EntrezGene = 17075
    | Mm_Ensembl = ENSMUSG00000045394
    | Mm_RefseqmRNA = NM_008532
    | Mm_RefseqProtein = NP_032558
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 87545024
    | Mm_GenLoc_end = 87559453
    | Mm_Uniprot =  
  }}
}}
'''Tumor-associated calcium signal transducer 1''', also known as '''TACSTD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TACSTD1 tumor-associated calcium signal transducer 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4072| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This 9-exon gene encodes a carcinoma-associated antigen and is a member of a family that includes at least two type I membrane proteins. This antigen is expressed on most normal epithelial cells and gastrointestinal carcinomas and functions as a homotypic calcium-independent cell adhesion molecule. The antigen is being used as a target for immunotherapy treatment of human carcinomas.<ref name="entrez">{{cite web | title = Entrez Gene: TACSTD1 tumor-associated calcium signal transducer 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4072| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Bergsagel PL, Victor-Kobrin C, Timblin CR, ''et al.'' |title=A murine cDNA encodes a pan-epithelial glycoprotein that is also expressed on plasma cells. |journal=J. Immunol. |volume=148 |issue= 2 |pages= 590-6 |year= 1992 |pmid= 1729376 |doi=  }}
*{{cite journal  | author=Simon B, Podolsky DK, Moldenhauer G, ''et al.'' |title=Epithelial glycoprotein is a member of a family of epithelial cell surface antigens homologous to nidogen, a matrix adhesion protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 7 |pages= 2755-9 |year= 1990 |pmid= 2108441 |doi=  }}
*{{cite journal  | author=Szala S, Froehlich M, Scollon M, ''et al.'' |title=Molecular cloning of cDNA for the carcinoma-associated antigen GA733-2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 9 |pages= 3542-6 |year= 1990 |pmid= 2333300 |doi=  }}
*{{cite journal  | author=Strnad J, Hamilton AE, Beavers LS, ''et al.'' |title=Molecular cloning and characterization of a human adenocarcinoma/epithelial cell surface antigen complementary DNA. |journal=Cancer Res. |volume=49 |issue= 2 |pages= 314-7 |year= 1989 |pmid= 2463074 |doi=  }}
*{{cite journal  | author=Perez MS, Walker LE |title=Isolation and characterization of a cDNA encoding the KS1/4 epithelial carcinoma marker. |journal=J. Immunol. |volume=142 |issue= 10 |pages= 3662-7 |year= 1989 |pmid= 2469722 |doi=  }}
*{{cite journal  | author=Linnenbach AJ, Wojcierowski J, Wu SA, ''et al.'' |title=Sequence investigation of the major gastrointestinal tumor-associated antigen gene family, GA733. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 1 |pages= 27-31 |year= 1989 |pmid= 2911574 |doi=  }}
*{{cite journal  | author=Spurr NK, Durbin H, Sheer D, ''et al.'' |title=Characterization and chromosomal assignment of a human cell surface antigen defined by the monoclonal antibody AUAI. |journal=Int. J. Cancer |volume=38 |issue= 5 |pages= 631-6 |year= 1986 |pmid= 3770992 |doi=  }}
*{{cite journal  | author=Björk P, Jönsson U, Svedberg H, ''et al.'' |title=Isolation, partial characterization, and molecular cloning of a human colon adenocarcinoma cell-surface glycoprotein recognized by the C215 mouse monoclonal antibody. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 24232-41 |year= 1993 |pmid= 7693697 |doi=  }}
*{{cite journal  | author=Linnenbach AJ, Seng BA, Wu S, ''et al.'' |title=Retroposition in a family of carcinoma-associated antigen genes. |journal=Mol. Cell. Biol. |volume=13 |issue= 3 |pages= 1507-15 |year= 1993 |pmid= 8382772 |doi=  }}
*{{cite journal  | author=Zhong XY, Kaul S, Eichler A, Bastert G |title=Evaluating GA733-2 mRNA as a marker for the detection of micrometastatic breast cancer in peripheral blood and bone marrow. |journal=Arch. Gynecol. Obstet. |volume=263 |issue= 1-2 |pages= 2-6 |year= 2000 |pmid= 10728619 |doi=  }}
*{{cite journal  | author=Tomita Y, Arakawa F, Yamamoto T, ''et al.'' |title=Molecular identification of a human carcinoma-associated glycoprotein antigen recognized by mouse monoclonal antibody FU-MK-1. |journal=Jpn. J. Cancer Res. |volume=91 |issue= 2 |pages= 231-8 |year= 2000 |pmid= 10761711 |doi=  }}
*{{cite journal  | author=Trebak M, Begg GE, Chong JM, ''et al.'' |title=Oligomeric state of the colon carcinoma-associated glycoprotein GA733-2 (Ep-CAM/EGP40) and its role in GA733-mediated homotypic cell-cell adhesion. |journal=J. Biol. Chem. |volume=276 |issue= 3 |pages= 2299-309 |year= 2001 |pmid= 11058587 |doi= 10.1074/jbc.M004770200 }}
*{{cite journal  | author=Chong JM, Speicher DW |title=Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM). |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5804-13 |year= 2001 |pmid= 11080501 |doi= 10.1074/jbc.M008839200 }}
*{{cite journal  | author=Calabrese G, Crescenzi C, Morizio E, ''et al.'' |title=Assignment of TACSTD1 (alias TROP1, M4S1) to human chromosome 2p21 and refinement of mapping of TACSTD2 (alias TROP2, M1S1) to human chromosome 1p32 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=92 |issue= 1-2 |pages= 164-5 |year= 2001 |pmid= 11306819 |doi=  }}
*{{cite journal  | author=Meyaard L, van der Vuurst de Vries AR, de Ruiter T, ''et al.'' |title=The epithelial cellular adhesion molecule (Ep-CAM) is a ligand for the leukocyte-associated immunoglobulin-like receptor (LAIR). |journal=J. Exp. Med. |volume=194 |issue= 1 |pages= 107-12 |year= 2001 |pmid= 11435477 |doi=  }}
*{{cite journal  | author=Lammers R, Giesert C, Grünebach F, ''et al.'' |title=Monoclonal antibody 9C4 recognizes epithelial cellular adhesion molecule, a cell surface antigen expressed in early steps of erythropoiesis. |journal=Exp. Hematol. |volume=30 |issue= 6 |pages= 537-45 |year= 2002 |pmid= 12063020 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Spizzo G, Gastl G, Wolf D, ''et al.'' |title=Correlation of COX-2 and Ep-CAM overexpression in human invasive breast cancer and its impact on survival. |journal=Br. J. Cancer |volume=88 |issue= 4 |pages= 574-8 |year= 2003 |pmid= 12592372 |doi= 10.1038/sj.bjc.6600741 }}
*{{cite journal  | author=Nasr AF, Nutini M, Palombo B, ''et al.'' |title=Mutations of TP53 induce loss of DNA methylation and amplification of the TROP1 gene. |journal=Oncogene |volume=22 |issue= 11 |pages= 1668-77 |year= 2003 |pmid= 12642870 |doi= 10.1038/sj.onc.1206248 }}
*{{cite journal  | author=Gires O, Eskofier S, Lang S, ''et al.'' |title=Cloning and characterisation of a 1.1 kb fragment of the carcinoma-associated epithelial cell adhesion molecule promoter. |journal=Anticancer Res. |volume=23 |issue= 4 |pages= 3255-61 |year= 2003 |pmid= 12926061 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] TBK1

• INFO: Beginning work on TBK1... {November 18, 2007 3:17:36 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:18:41 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = TANK-binding kinase 1
 | HGNCid = 11584
 | Symbol = TBK1
 | AltSymbols =; FLJ11330; NAK; T2K
 | OMIM = 604834
 | ECnumber =  
 | Homologene = 22742
 | MGIid = 1929658
 | GeneAtlas_image1 = PBB_GE_TBK1_218520_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007249 |text = I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045087 |text = innate immune response}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 29110
    | Hs_Ensembl = ENSG00000183735
    | Hs_RefseqProtein = NP_037386
    | Hs_RefseqmRNA = NM_013254
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 63132167
    | Hs_GenLoc_end = 63182153
    | Hs_Uniprot = Q9UHD2
    | Mm_EntrezGene = 56480
    | Mm_Ensembl = ENSMUSG00000020115
    | Mm_RefseqmRNA = NM_019786
    | Mm_RefseqProtein = NP_062760
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 120949520
    | Mm_GenLoc_end = 120989807
    | Mm_Uniprot = Q3THP3
  }}
}}
'''TANK-binding kinase 1''', also known as '''TBK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TBK1 TANK-binding kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29110| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The NF-kappa-B (NFKB) complex of proteins is inhibited by I-kappa-B (IKB) proteins, which inactivate NFKB by trapping it in the cytoplasm. Phosphorylation of serine residues on the IKB proteins by IKB kinases marks them for destruction via the ubiquitination pathway, thereby allowing activation and nuclear translocation of the NFKB complex. The protein encoded by this gene is similar to IKB kinases and can mediate NFKB activation in response to certain growth factors. For example, the protein can form a complex with the IKB protein TANK and TRAF2 and release the NFKB inhibition caused by TANK.<ref name="entrez">{{cite web | title = Entrez Gene: TBK1 TANK-binding kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29110| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Chou MM, Hanafusa H |title=A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7359-64 |year= 1995 |pmid= 7706279 |doi=  }}
*{{cite journal  | author=Chen ZJ, Parent L, Maniatis T |title=Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. |journal=Cell |volume=84 |issue= 6 |pages= 853-62 |year= 1996 |pmid= 8601309 |doi=  }}
*{{cite journal  | author=Zandi E, Chen Y, Karin M |title=Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate. |journal=Science |volume=281 |issue= 5381 |pages= 1360-3 |year= 1998 |pmid= 9721103 |doi=  }}
*{{cite journal  | author=Pomerantz JL, Baltimore D |title=NF-kappaB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase. |journal=EMBO J. |volume=18 |issue= 23 |pages= 6694-704 |year= 2000 |pmid= 10581243 |doi= 10.1093/emboj/18.23.6694 }}
*{{cite journal  | author=Tojima Y, Fujimoto A, Delhase M, ''et al.'' |title=NAK is an IkappaB kinase-activating kinase. |journal=Nature |volume=404 |issue= 6779 |pages= 778-82 |year= 2000 |pmid= 10783893 |doi= 10.1038/35008109 }}
*{{cite journal  | author=Bonnard M, Mirtsos C, Suzuki S, ''et al.'' |title=Deficiency of T2K leads to apoptotic liver degeneration and impaired NF-kappaB-dependent gene transcription. |journal=EMBO J. |volume=19 |issue= 18 |pages= 4976-85 |year= 2000 |pmid= 10990461 |doi= 10.1093/emboj/19.18.4976 }}
*{{cite journal  | author=Kishore N, Huynh QK, Mathialagan S, ''et al.'' |title=IKK-i and TBK-1 are enzymatically distinct from the homologous enzyme IKK-2: comparative analysis of recombinant human IKK-i, TBK-1, and IKK-2. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13840-7 |year= 2002 |pmid= 11839743 |doi= 10.1074/jbc.M110474200 }}
*{{cite journal  | author=Chariot A, Leonardi A, Muller J, ''et al.'' |title=Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37029-36 |year= 2002 |pmid= 12133833 |doi= 10.1074/jbc.M205069200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Li SF, Fujita F, Hirai M, ''et al.'' |title=Genomic structure and characterization of the promoter region of the human NAK gene. |journal=Gene |volume=304 |issue=  |pages= 57-64 |year= 2003 |pmid= 12568715 |doi=  }}
*{{cite journal  | author=Fitzgerald KA, McWhirter SM, Faia KL, ''et al.'' |title=IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. |journal=Nat. Immunol. |volume=4 |issue= 5 |pages= 491-6 |year= 2003 |pmid= 12692549 |doi= 10.1038/ni921 }}
*{{cite journal  | author=Sharma S, tenOever BR, Grandvaux N, ''et al.'' |title=Triggering the interferon antiviral response through an IKK-related pathway. |journal=Science |volume=300 |issue= 5622 |pages= 1148-51 |year= 2003 |pmid= 12702806 |doi= 10.1126/science.1081315 }}
*{{cite journal  | author=Matsuda A, Suzuki Y, Honda G, ''et al.'' |title=Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. |journal=Oncogene |volume=22 |issue= 21 |pages= 3307-18 |year= 2003 |pmid= 12761501 |doi= 10.1038/sj.onc.1206406 }}
*{{cite journal  | author=Sato S, Sugiyama M, Yamamoto M, ''et al.'' |title=Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-kappa B and IFN-regulatory factor-3, in the Toll-like receptor signaling. |journal=J. Immunol. |volume=171 |issue= 8 |pages= 4304-10 |year= 2004 |pmid= 14530355 |doi=  }}
*{{cite journal  | author=Fujita F, Taniguchi Y, Kato T, ''et al.'' |title=Identification of NAP1, a regulatory subunit of IkappaB kinase-related kinases that potentiates NF-kappaB signaling. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7780-93 |year= 2003 |pmid= 14560022 |doi=  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  | author=tenOever BR, Sharma S, Zou W, ''et al.'' |title=Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus infection and the role of viral ribonucleoprotein in the development of interferon antiviral immunity. |journal=J. Virol. |volume=78 |issue= 19 |pages= 10636-49 |year= 2004 |pmid= 15367631 |doi= 10.1128/JVI.78.19.10636-10649.2004 }}
*{{cite journal  | author=Kuai J, Wooters J, Hall JP, ''et al.'' |title=NAK is recruited to the TNFR1 complex in a TNFalpha-dependent manner and mediates the production of RANTES: identification of endogenous TNFR-interacting proteins by a proteomic approach. |journal=J. Biol. Chem. |volume=279 |issue= 51 |pages= 53266-71 |year= 2005 |pmid= 15485837 |doi= 10.1074/jbc.M411037200 }}
*{{cite journal  | author=Buss H, Dörrie A, Schmitz ML, ''et al.'' |title=Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription. |journal=J. Biol. Chem. |volume=279 |issue= 53 |pages= 55633-43 |year= 2005 |pmid= 15489227 |doi= 10.1074/jbc.M409825200 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] TNFRSF9

• INFO: Beginning work on TNFRSF9... {November 18, 2007 2:59:44 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:02:52 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Tumor necrosis factor receptor superfamily, member 9
 | HGNCid = 11924
 | Symbol = TNFRSF9
 | AltSymbols =; 4-1BB; CD137; CDw137; ILA; MGC2172
 | OMIM = 602250
 | ECnumber =  
 | Homologene = 1199
 | MGIid = 1101059
 | GeneAtlas_image1 = PBB_GE_TNFRSF9_207536_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_TNFRSF9_211786_at_tn.png
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3604
    | Hs_Ensembl = ENSG00000049249
    | Hs_RefseqProtein = NP_001552
    | Hs_RefseqmRNA = NM_001561
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 7902494
    | Hs_GenLoc_end = 7923513
    | Hs_Uniprot = Q07011
    | Mm_EntrezGene = 21942
    | Mm_Ensembl = ENSMUSG00000028965
    | Mm_RefseqmRNA = NM_001077508
    | Mm_RefseqProtein = NP_001070976
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 149763990
    | Mm_GenLoc_end = 149789893
    | Mm_Uniprot = Q3U3R1
  }}
}}
'''Tumor necrosis factor receptor superfamily, member 9''', also known as '''TNFRSF9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNFRSF9 tumor necrosis factor receptor superfamily, member 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3604| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.<ref name="entrez">{{cite web | title = Entrez Gene: TNFRSF9 tumor necrosis factor receptor superfamily, member 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3604| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Sica G, Chen L |title=Biochemical and immunological characteristics of 4-1BB (CD137) receptor and ligand and potential applications in cancer therapy. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=47 |issue= 5 |pages= 275-9 |year= 2000 |pmid= 10604232 |doi=  }}
*{{cite journal  | author=Schwarz H |title=Biological activities of reverse signal transduction through CD137 ligand. |journal=J. Leukoc. Biol. |volume=77 |issue= 3 |pages= 281-6 |year= 2005 |pmid= 15618293 |doi= 10.1189/jlb.0904558 }}
*{{cite journal  | author=Kwon BS, Weissman SM |title=cDNA sequences of two inducible T-cell genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 6 |pages= 1963-7 |year= 1989 |pmid= 2784565 |doi=  }}
*{{cite journal  | author=Zhou Z, Kim S, Hurtado J, ''et al.'' |title=Characterization of human homologue of 4-1BB and its ligand. |journal=Immunol. Lett. |volume=45 |issue= 1-2 |pages= 67-73 |year= 1995 |pmid= 7622190 |doi=  }}
*{{cite journal  | author=Alderson MR, Smith CA, Tough TW, ''et al.'' |title=Molecular and biological characterization of human 4-1BB and its ligand. |journal=Eur. J. Immunol. |volume=24 |issue= 9 |pages= 2219-27 |year= 1994 |pmid= 8088337 |doi=  }}
*{{cite journal  | author=Schwarz H, Tuckwell J, Lotz M |title=A receptor induced by lymphocyte activation (ILA): a new member of the human nerve-growth-factor/tumor-necrosis-factor receptor family. |journal=Gene |volume=134 |issue= 2 |pages= 295-8 |year= 1994 |pmid= 8262389 |doi=  }}
*{{cite journal  | author=Schwarz H, Blanco FJ, von Kempis J, ''et al.'' |title=ILA, a member of the human nerve growth factor/tumor necrosis factor receptor family, regulates T-lymphocyte proliferation and survival. |journal=Blood |volume=87 |issue= 7 |pages= 2839-45 |year= 1996 |pmid= 8639902 |doi=  }}
*{{cite journal  | author=Loo DT, Chalupny NJ, Bajorath J, ''et al.'' |title=Analysis of 4-1BBL and laminin binding to murine 4-1BB, a member of the tumor necrosis factor receptor superfamily, and comparison with human 4-1BB. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6448-56 |year= 1997 |pmid= 9045669 |doi=  }}
*{{cite journal  | author=Schwarz H, Arden K, Lotz M |title=CD137, a member of the tumor necrosis factor receptor family, is located on chromosome 1p36, in a cluster of related genes, and colocalizes with several malignancies. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 699-703 |year= 1997 |pmid= 9207223 |doi= 10.1006/bbrc.1997.6870 }}
*{{cite journal  | author=Arch RH, Thompson CB |title=4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB. |journal=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 558-65 |year= 1998 |pmid= 9418902 |doi=  }}
*{{cite journal  | author=Jang IK, Lee ZH, Kim YJ, ''et al.'' |title=Human 4-1BB (CD137) signals are mediated by TRAF2 and activate nuclear factor-kappa B. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 3 |pages= 613-20 |year= 1998 |pmid= 9464265 |doi= 10.1006/bbrc.1997.8016 }}
*{{cite journal  | author=Kim YJ, Kim SH, Mantel P, Kwon BS |title=Human 4-1BB regulates CD28 co-stimulation to promote Th1 cell responses. |journal=Eur. J. Immunol. |volume=28 |issue= 3 |pages= 881-90 |year= 1998 |pmid= 9541583 |doi=  }}
*{{cite journal  | author=Saoulli K, Lee SY, Cannons JL, ''et al.'' |title=CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand. |journal=J. Exp. Med. |volume=187 |issue= 11 |pages= 1849-62 |year= 1998 |pmid= 9607925 |doi=  }}
*{{cite journal  | author=Langstein J, Michel J, Schwarz H |title=CD137 induces proliferation and endomitosis in monocytes. |journal=Blood |volume=94 |issue= 9 |pages= 3161-8 |year= 1999 |pmid= 10556203 |doi=  }}
*{{cite journal  | author=Jang LK, Lee ZH, Kim HH, ''et al.'' |title=A novel leucine-rich repeat protein (LRR-1): potential involvement in 4-1BB-mediated signal transduction. |journal=Mol. Cells |volume=12 |issue= 3 |pages= 304-12 |year= 2002 |pmid= 11804328 |doi=  }}
*{{cite journal  | author=Cooper D, Bansal-Pakala P, Croft M |title=4-1BB (CD137) controls the clonal expansion and survival of CD8 T cells in vivo but does not contribute to the development of cytotoxicity. |journal=Eur. J. Immunol. |volume=32 |issue= 2 |pages= 521-9 |year= 2002 |pmid= 11828369 |doi=  }}
*{{cite journal  | author=Wilcox RA, Chapoval AI, Gorski KS, ''et al.'' |title=Cutting edge: Expression of functional CD137 receptor by dendritic cells. |journal=J. Immunol. |volume=168 |issue= 9 |pages= 4262-7 |year= 2002 |pmid= 11970964 |doi=  }}
*{{cite journal  | author=Shulzhenko N, Morgun A, Chinellato AP, ''et al.'' |title=CD27 but not CD70 and 4-1BB intragraft gene expression is a risk factor for acute cardiac allograft rejection in humans. |journal=Transplant. Proc. |volume=34 |issue= 2 |pages= 474-5 |year= 2002 |pmid= 12009595 |doi=  }}
*{{cite journal  | author=Pauly S, Broll K, Wittmann M, ''et al.'' |title=CD137 is expressed by follicular dendritic cells and costimulates B lymphocyte activation in germinal centers. |journal=J. Leukoc. Biol. |volume=72 |issue= 1 |pages= 35-42 |year= 2002 |pmid= 12101260 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

end log.