User:ProteinBoxBot/PBB Log Wiki 11-9-2007-A2-11

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Contents 1 Log file for Protein Box Bot 2 Protein Status Quick Log - Date: 18:49, 19 November 2007 (UTC) 2.1 Proteins without matches (7) 2.2 Proteins with a High Potential Match (10) 2.3 Redirected Proteins (8) 2.4 Manual Inspection (Page not found) (17) 2.5 Updated (8) 3 Protein Status Grid - Date: 18:49, 19 November 2007 (UTC) 4 Vebose Log - Date: 18:49, 19 November 2007 (UTC) 4.1 ADRA1A 4.2 AMACR 4.3 AMPD1 4.4 AP1G1 4.5 APBA1 4.6 ATN1 4.7 ATP2C1 4.8 CYP27A1 4.9 DICER1 4.10 DLG2 4.11 EPHA4 4.12 F13B 4.13 FAH 4.14 FCGRT 4.15 FLNC 4.16 GALNS 4.17 GAS6 4.18 GP1BB 4.19 GPR30 4.20 GTF2A1 4.21 HK1 4.22 HRG 4.23 HSD3B1 4.24 HSPE1 4.25 MS4A2

[edit] Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

[edit] Protein Status Quick Log - Date: 18:49, 19 November 2007 (UTC)

[edit] Proteins without matches (7)

HRG	GALNS	EPHA4	ATP2C1	FLNC
MS4A2	AMPD1

[edit] Proteins with a High Potential Match (10)

GTF2A1	FAH	CYP27A1	GPR30	HSPE1
AMACR	APBA1	ATN1	DICER1	GP1BB

[edit] Redirected Proteins (8)

HSD3B1	AP1G1	DLG2	HK1	F13B
FCGRT	GAS6	ADRA1A

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

GTF2A1	HRG	GALNS	FAH	EPHA4
CYP27A1	GPR30	ATP2C1	HSPE1	AMACR
FLNC	APBA1	ATN1	MS4A2	DICER1
GP1BB	AMPD1

[edit] Updated (8)

HSD3B1	AP1G1	DLG2	HK1	F13B
FCGRT	GAS6	ADRA1A

[edit] Protein Status Grid - Date: 18:49, 19 November 2007 (UTC)

HUGO Symbol	Action Summary	Target page(s)	WP Symbol Search
GTF2A1	Manual Inspection (Page not found)	Other Pages: General transcription factor IIA (No Data); GTF2A1 (No Data); MGC129969 (No Data); Mgc129969 (No Data); MGC129970 (No Data); Mgc129970 (No Data); TF2A1 (No Data); Tf2a1 (No Data); TFIIA (Protein Template); Tfiia (No Data);	[1]
HSD3B1	Updated	Other Pages: Hydroxy-delta-5-steroid dehydrogenase (No Data); HSD3B1 (Good Codes + Entrez Match); HSD3B (No Data); Hsd3b (No Data); HSDB3 (No Data); Hsdb3 (No Data);	[2]
HRG	Manual Inspection (Page not found)	Other Pages: Histidine-rich glycoprotein (No Data); HRG (Unknown Data); DKFZp779H1622 (No Data); Dkfzp779h1622 (No Data); HPRG (No Data); Hprg (No Data); HRGP (No Data); Hrgp (No Data);	[3]
AP1G1	Updated	Other Pages: Adaptor-related protein complex 1 (No Data); AP1G1 (Good Codes + Entrez Match); ADTG (No Data); Adtg (No Data); CLAPG1 (No Data); Clapg1 (No Data); MGC18255 (No Data); Mgc18255 (No Data);	[4]
DLG2	Updated	Other Pages: Discs (Redirect -> DLG4); DLG2 (Good Codes + Entrez Match); DKFZp781D1854 (No Data); Dkfzp781d1854 (No Data); DKFZp781E0954 (No Data); Dkfzp781e0954 (No Data); FLJ37266 (No Data); Flj37266 (No Data); MGC131811 (No Data); Mgc131811 (No Data); PSD-93 (No Data); Psd-93 (No Data); DLG4 (Codes Found, but no match[skip]);	[5]
HK1	Updated	Other Pages: Hexokinase 1 (No Data); HK1 (Good Codes + Entrez Match); HK1-ta (No Data); Hk1-ta (No Data); HK1-tb (No Data); Hk1-tb (No Data); HK1-tc (No Data); Hk1-tc (No Data); HKI (No Data); Hki (No Data); HXK1 (No Data); Hxk1 (No Data);	[6]
GALNS	Manual Inspection (Page not found)	Other Pages: Galactosamine (Unknown Data); GALNS (No Data); GAS (Redirect -> Gas (disambiguation)); Gas (Unknown Data); GALNAC6S (No Data); Galnac6s (No Data); MPS4A (No Data); Mps4a (No Data); Gas (disambiguation) (DisAmbig);	[7]
FAH	Manual Inspection (Page not found)	Other Pages: Fumarylacetoacetate hydrolase (Protein Template); FAH (DisAmbig);	[8]
EPHA4	Manual Inspection (Page not found)	Other Pages: EPH receptor A4 (No Data); EPHA4 (No Data); HEK8 (No Data); Hek8 (No Data); SEK (DisAmbig); Sek (No Data); TYRO1 (No Data); Tyro1 (No Data);	[9]
CYP27A1	Manual Inspection (Page not found)	Other Pages: Cytochrome P450 (Unknown Data); CYP27A1 (Protein Template); CP27 (No Data); Cp27 (No Data); CTX (DisAmbig); Ctx (No Data); CYP27 (No Data); Cyp27 (No Data);	[10]
GPR30	Manual Inspection (Page not found)	Other Pages: G protein-coupled receptor 30 (No Data); GPR30 (Protein Template); CMKRL2 (No Data); Cmkrl2 (No Data); DRY12 (No Data); Dry12 (No Data); FEG-1 (No Data); Feg-1 (No Data); GPCR-Br (No Data); Gpcr-br (No Data); LERGU (No Data); Lergu (No Data); LERGU2 (No Data); Lergu2 (No Data); LyGPR (No Data); Lygpr (No Data); MGC99678 (No Data); Mgc99678 (No Data);	[11]
ATP2C1	Manual Inspection (Page not found)	Other Pages: ATPase (Unknown Data); ATP2C1 (No Data); ATP2C1A (No Data); Atp2c1a (No Data); BCPM (No Data); Bcpm (No Data); HHD (Redirect -> Hybrid drive); Hhd (No Data); KIAA1347 (No Data); Kiaa1347 (No Data); PMR1 (No Data); Pmr1 (No Data); SPCA1 (No Data); Spca1 (No Data); HSPCA1 (No Data); Hspca1 (No Data); Hybrid drive (Unknown Data);	[12]
HSPE1	Manual Inspection (Page not found)	Other Pages: Heat shock 10kDa protein 1 (No Data); HSPE1 (No Data); CPN10 (No Data); Cpn10 (No Data); GROES (No Data); Groes (No Data); HSP10 (No Data); Hsp10 (Redirect -> GroES); GroES (Protein Template);	[13]
F13B	Updated	Other Pages: Coagulation factor XIII (No Data); F13B (Good Codes + Entrez Match); FXIIIB (No Data); Fxiiib (No Data);	[14]
FCGRT	Updated	Other Pages: Fc fragment of IgG (No Data); FCGRT (Good Codes + Entrez Match); FCRN (No Data); Fcrn (No Data); Alpha-chain (No Data);	[15]
AMACR	Manual Inspection (Page not found)	Other Pages: Alpha-methylacyl-CoA racemase (Unknown Data); AMACR (Protein Template); RACE (DisAmbig); Race (DisAmbig);	[16]
FLNC	Manual Inspection (Page not found)	Other Pages: Filamin C (No Data); FLNC (Redirect -> National Front for the Liberation of Corsica); ABP-280 (No Data); Abp-280 (No Data); ABP280A (No Data); Abp280a (No Data); ABPA (Redirect -> Allergic bronchopulmonary aspergillosis); Abpa (No Data); ABPL (No Data); Abpl (No Data); FLJ10186 (No Data); Flj10186 (No Data); FLN2 (No Data); Fln2 (No Data); National Front for the Liberation of Corsica (Unknown Data); Allergic bronchopulmonary aspergillosis (Unknown Data);	[17]
APBA1	Manual Inspection (Page not found)	Other Pages: Amyloid beta (Protein Template); APBA1 (No Data); D9S411E (No Data); D9s411e (No Data); MINT1 (No Data); Mint1 (No Data); X11 (Redirect -> X Window System); X11A (No Data); X11a (No Data); X11ALPHA (No Data); X11alpha (No Data); X Window System (Unknown Data);	[18]
GAS6	Updated	Other Pages: Growth arrest-specific 6 (No Data); GAS6 (Good Codes + Entrez Match); AXLLG (No Data); Axllg (No Data); AXSF (No Data); Axsf (No Data); DKFZp666G247 (No Data); Dkfzp666g247 (No Data); FLJ34709 (No Data); Flj34709 (No Data);	[19]
ATN1	Manual Inspection (Page not found)	Other Pages: Atrophin 1 (No Data); ATN1 (Protein Template); B37 (No Data); D12S755E (No Data); D12s755e (No Data); DRPLA (No Data); Drpla (No Data); NOD (DisAmbig); Nod (Redirect -> NOD);	[20]
MS4A2	Manual Inspection (Page not found)	Other Pages: Membrane-spanning 4-domains (No Data); MS4A2 (No Data); MS4A1 (No Data); Ms4a1 (No Data); APY (DisAmbig); Apy (No Data); ATOPY (No Data); Atopy (Unknown Data); FCER1B (No Data); Fcer1b (No Data); FCERI (No Data); Fceri (No Data); IGEL (No Data); Igel (Unknown Data); IGER (Redirect -> Institute of Grassland and Environmental Research); Iger (No Data); IGHER (No Data); Igher (No Data); Institute of Grassland and Environmental Research (Unknown Data);	[21]
ADRA1A	Updated	Other Pages: Adrenergic (DisAmbig); ADRA1A (Good Codes + Entrez Match); ADRA1C (No Data); Adra1c (No Data); ADRA1L1 (No Data); Adra1l1 (No Data); ALPHA1AAR (No Data); Alpha1aar (No Data);	[22]
DICER1	Manual Inspection (Page not found)	Other Pages: Dicer1 (No Data); DICER1 (No Data); Dicer (Protein Template); HERNA (No Data); Herna (No Data); KIAA0928 (No Data); Kiaa0928 (No Data);	[23]
GP1BB	Manual Inspection (Page not found)	Other Pages: Glycoprotein Ib (Protein Template); GP1BB (No Data); CD42c (No Data); Cd42c (No Data);	[24]
AMPD1	Manual Inspection (Page not found)	Other Pages: Adenosine monophosphate deaminase 1 (No Data); AMPD1 (No Data); MAD (DisAmbig); Mad (Redirect -> MAD); MADA (No Data); Mada (Redirect -> Assyria (Persian province)); Assyria (Persian province) (Unknown Data);	[25]

[edit] Vebose Log - Date: 18:49, 19 November 2007 (UTC)

[edit] ADRA1A

• INFO: Beginning work on ADRA1A... {November 19, 2007 12:47:42 AM PST}
• SEARCH REDIRECT: Control Box Found: ADRA1A {November 19, 2007 12:48:21 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:48:24 AM PST}
• SKIP SUMMARY: SKIPPING Summary, No Errors. {November 19, 2007 12:48:24 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:48:24 AM PST}
• UPDATED: Updated protein page: ADRA1A {November 19, 2007 12:48:31 AM PST}

[edit] AMACR

• INFO: Beginning work on AMACR... {November 19, 2007 10:40:42 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:41:07 AM 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 = Alpha-methylacyl-CoA racemase
 | HGNCid = 451
 | Symbol = AMACR
 | AltSymbols =; RACE
 | OMIM = 604489
 | ECnumber =  
 | Homologene = 7410
 | MGIid = 1098273
 | Function = {{GNF_GO|id=GO:0008111 |text = alpha-methylacyl-CoA racemase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}} 
 | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}} 
 | Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23600
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_055139
    | Hs_RefseqmRNA = NM_014324
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 17117
    | Mm_Ensembl = ENSMUSG00000022244
    | Mm_RefseqmRNA = NM_008537
    | Mm_RefseqProtein = NP_032563
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 10926481
    | Mm_GenLoc_end = 10941349
    | Mm_Uniprot = Q3TUS8
  }}
}}
'''Alpha-methylacyl-CoA racemase''', also known as '''AMACR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMACR alpha-methylacyl-CoA racemase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23600| 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=Jiang Z, Woda BA, Wu CL, Yang XJ |title=Discovery and clinical application of a novel prostate cancer marker: alpha-methylacyl CoA racemase (P504S). |journal=Am. J. Clin. Pathol. |volume=122 |issue= 2 |pages= 275-89 |year= 2004 |pmid= 15323145 |doi= 10.1309/EJUY-UQPE-X1MG-68MK }}
*{{cite journal  | author=Bautch S |title=Wisconsin doctor selected as national symbol of physicians' sacrifices. |journal=Wis. Med. J. |volume=90 |issue= 8 |pages= 485-7 |year= 1991 |pmid= 1926890 |doi=  }}
*{{cite journal  | author=Schmitz W, Albers C, Fingerhut R, Conzelmann E |title=Purification and characterization of an alpha-methylacyl-CoA racemase from human liver. |journal=Eur. J. Biochem. |volume=231 |issue= 3 |pages= 815-22 |year= 1995 |pmid= 7649182 |doi=  }}
*{{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=Schmitz W, Helander HM, Hiltunen JK, Conzelmann E |title=Molecular cloning of cDNA species for rat and mouse liver alpha-methylacyl-CoA racemases. |journal=Biochem. J. |volume=326 ( Pt 3) |issue=  |pages= 883-9 |year= 1997 |pmid= 9307041 |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=Ferdinandusse S, Denis S, Clayton PT, ''et al.'' |title=Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA racemase cause adult-onset sensory motor neuropathy. |journal=Nat. Genet. |volume=24 |issue= 2 |pages= 188-91 |year= 2000 |pmid= 10655068 |doi= 10.1038/72861 }}
*{{cite journal  | author=Kotti TJ, Savolainen K, Helander HM, ''et al.'' |title=In mouse alpha -methylacyl-CoA racemase, the same gene product is simultaneously located in mitochondria and peroxisomes. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20887-95 |year= 2000 |pmid= 10770938 |doi= 10.1074/jbc.M002067200 }}
*{{cite journal  | author=Amery L, Fransen M, De Nys K, ''et al.'' |title=Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans. |journal=J. Lipid Res. |volume=41 |issue= 11 |pages= 1752-9 |year= 2001 |pmid= 11060344 |doi=  }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | author=Rubin MA, Zhou M, Dhanasekaran SM, ''et al.'' |title=alpha-Methylacyl coenzyme A racemase as a tissue biomarker for prostate cancer. |journal=JAMA |volume=287 |issue= 13 |pages= 1662-70 |year= 2002 |pmid= 11926890 |doi=  }}
*{{cite journal  | author=Luo J, Zha S, Gage WR, ''et al.'' |title=Alpha-methylacyl-CoA racemase: a new molecular marker for prostate cancer. |journal=Cancer Res. |volume=62 |issue= 8 |pages= 2220-6 |year= 2002 |pmid= 11956072 |doi=  }}
*{{cite journal  | author=Zhou M, Chinnaiyan AM, Kleer CG, ''et al.'' |title=Alpha-Methylacyl-CoA racemase: a novel tumor marker over-expressed in several human cancers and their precursor lesions. |journal=Am. J. Surg. Pathol. |volume=26 |issue= 7 |pages= 926-31 |year= 2002 |pmid= 12131161 |doi=  }}
*{{cite journal  | author=Kuefer R, Varambally S, Zhou M, ''et al.'' |title=alpha-Methylacyl-CoA racemase: expression levels of this novel cancer biomarker depend on tumor differentiation. |journal=Am. J. Pathol. |volume=161 |issue= 3 |pages= 841-8 |year= 2002 |pmid= 12213712 |doi=  }}
*{{cite journal  | author=Varambally S, Dhanasekaran SM, Zhou M, ''et al.'' |title=The polycomb group protein EZH2 is involved in progression of prostate cancer. |journal=Nature |volume=419 |issue= 6907 |pages= 624-9 |year= 2002 |pmid= 12374981 |doi= 10.1038/nature01075 }}
*{{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=Leav I, McNeal JE, Ho SM, Jiang Z |title=Alpha-methylacyl-CoA racemase (P504S) expression in evolving carcinomas within benign prostatic hyperplasia and in cancers of the transition zone. |journal=Hum. Pathol. |volume=34 |issue= 3 |pages= 228-33 |year= 2003 |pmid= 12673556 |doi= 10.1053/hupa.2003.42 }}
*{{cite journal  | author=Shen-Ong GL, Feng Y, Troyer DA |title=Expression profiling identifies a novel alpha-methylacyl-CoA racemase exon with fumarate hydratase homology. |journal=Cancer Res. |volume=63 |issue= 12 |pages= 3296-301 |year= 2003 |pmid= 12810662 |doi=  }}
*{{cite journal  | author=Zha S, Ferdinandusse S, Denis S, ''et al.'' |title=Alpha-methylacyl-CoA racemase as an androgen-independent growth modifier in prostate cancer. |journal=Cancer Res. |volume=63 |issue= 21 |pages= 7365-76 |year= 2004 |pmid= 14612535 |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 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] AMPD1

• INFO: Beginning work on AMPD1... {November 19, 2007 12:49:14 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:49:37 AM 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 = Adenosine monophosphate deaminase 1 (isoform M)
 | HGNCid = 468
 | Symbol = AMPD1
 | AltSymbols =; MAD; MADA
 | OMIM = 102770
 | ECnumber =  
 | Homologene = 20
 | MGIid = 88015
 | GeneAtlas_image1 = PBB_GE_AMPD1_206121_at_tn.png
 | Function = {{GNF_GO|id=GO:0003876 |text = AMP deaminase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0009117 |text = nucleotide metabolic process}} {{GNF_GO|id=GO:0009168 |text = purine ribonucleoside monophosphate biosynthetic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 270
    | Hs_Ensembl = ENSG00000116748
    | Hs_RefseqProtein = NP_000027
    | Hs_RefseqmRNA = NM_000036
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 115017245
    | Hs_GenLoc_end = 115039762
    | Hs_Uniprot = P23109
    | Mm_EntrezGene = 229665
    | Mm_Ensembl = ENSMUSG00000070385
    | Mm_RefseqmRNA = NM_001033303
    | Mm_RefseqProtein = NP_001028475
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 103203157
    | Mm_GenLoc_end = 103228775
    | Mm_Uniprot = Q3V1D3
  }}
}}
'''Adenosine monophosphate deaminase 1 (isoform M)''', also known as '''AMPD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMPD1 adenosine monophosphate deaminase 1 (isoform M)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=270| 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 = Adenosine monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle. Two other genes have been identified, AMPD2 and AMPD3, for the liver- and erythocyte-specific isoforms, respectively. Deficiency of the muscle-specific enzyme is apparently a common cause of exercise-induced myopathy and probably the most common cause of metabolic myopathy in the human.<ref name="entrez">{{cite web | title = Entrez Gene: AMPD1 adenosine monophosphate deaminase 1 (isoform M)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=270| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Fishbein WN, Armbrustmacher VW, Griffin JL |title=Myoadenylate deaminase deficiency: a new disease of muscle. |journal=Science |volume=200 |issue= 4341 |pages= 545-8 |year= 1978 |pmid= 644316 |doi=  }}
*{{cite journal  | author=Sabina RL, Fishbein WN, Pezeshkpour G, ''et al.'' |title=Molecular analysis of the myoadenylate deaminase deficiencies. |journal=Neurology |volume=42 |issue= 1 |pages= 170-9 |year= 1992 |pmid= 1370861 |doi=  }}
*{{cite journal  | author=Mahnke-Zizelman DK, Sabina RL |title=Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. |journal=J. Biol. Chem. |volume=267 |issue= 29 |pages= 20866-77 |year= 1992 |pmid= 1400401 |doi=  }}
*{{cite journal  | author=Morisaki T, Gross M, Morisaki H, ''et al.'' |title=Molecular basis of AMP deaminase deficiency in skeletal muscle. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 14 |pages= 6457-61 |year= 1992 |pmid= 1631143 |doi=  }}
*{{cite journal  | author=Sabina RL, Morisaki T, Clarke P, ''et al.'' |title=Characterization of the human and rat myoadenylate deaminase genes. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 9423-33 |year= 1990 |pmid= 2345176 |doi=  }}
*{{cite journal  | author=Dale GL |title=Radioisotopic assay for erythrocyte adenosine 5'-monophosphate deaminase. |journal=Clin. Chim. Acta |volume=182 |issue= 1 |pages= 1-7 |year= 1989 |pmid= 2502331 |doi=  }}
*{{cite journal  | author=Mercelis R, Martin JJ, Dehaene I, ''et al.'' |title=Myoadenylate deaminase deficiency in a patient with facial and limb girdle myopathy. |journal=J. Neurol. |volume=225 |issue= 3 |pages= 157-66 |year= 1981 |pmid= 6167680 |doi=  }}
*{{cite journal  | author=van Laarhoven JP, de Gast GC, Spierenburg GT, de Bruyn CH |title=Enzymological studies in chronic lymphocytic leukemia. |journal=Leuk. Res. |volume=7 |issue= 2 |pages= 261-7 |year= 1983 |pmid= 6406772 |doi=  }}
*{{cite journal  | author=Kelemen J, Rice DR, Bradley WG, ''et al.'' |title=Familial myoadenylate deaminase deficiency and exertional myalgia. |journal=Neurology |volume=32 |issue= 8 |pages= 857-63 |year= 1982 |pmid= 7201581 |doi=  }}
*{{cite journal  | author=Baumeister FA, Gross M, Wagner DR, ''et al.'' |title=Myoadenylate deaminase deficiency with severe rhabdomyolysis. |journal=Eur. J. Pediatr. |volume=152 |issue= 6 |pages= 513-5 |year= 1993 |pmid= 8335021 |doi=  }}
*{{cite journal  | author=Morisaki T, Holmes EW |title=Functionally distinct elements are required for expression of the AMPD1 gene in myocytes. |journal=Mol. Cell. Biol. |volume=13 |issue= 9 |pages= 5854-60 |year= 1993 |pmid= 8355716 |doi=  }}
*{{cite journal  | author=Bruno C, Minetti C, Shanske S, ''et al.'' |title=Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria. |journal=Neurology |volume=50 |issue= 1 |pages= 296-8 |year= 1998 |pmid= 9443500 |doi=  }}
*{{cite journal  | author=Hisatome I, Morisaki T, Kamma H, ''et al.'' |title=Control of AMP deaminase 1 binding to myosin heavy chain. |journal=Am. J. Physiol. |volume=275 |issue= 3 Pt 1 |pages= C870-81 |year= 1998 |pmid= 9730972 |doi=  }}
*{{cite journal  | author=Sims B, Powers RE, Sabina RL, Theibert AB |title=Elevated adenosine monophosphate deaminase activity in Alzheimer's disease brain. |journal=Neurobiol. Aging |volume=19 |issue= 5 |pages= 385-91 |year= 1999 |pmid= 9880040 |doi=  }}
*{{cite journal  | author=Loh E, Rebbeck TR, Mahoney PD, ''et al.'' |title=Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure. |journal=Circulation |volume=99 |issue= 11 |pages= 1422-5 |year= 1999 |pmid= 10086964 |doi=  }}
*{{cite journal  | author=Abe M, Higuchi I, Morisaki H, ''et al.'' |title=Myoadenylate deaminase deficiency with progressive muscle weakness and atrophy caused by new missense mutations in AMPD1 gene: case report in a Japanese patient. |journal=Neuromuscul. Disord. |volume=10 |issue= 7 |pages= 472-7 |year= 2000 |pmid= 10996775 |doi=  }}
*{{cite journal  | author=Morisaki H, Higuchi I, Abe M, ''et al.'' |title=First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient. |journal=Hum. Mutat. |volume=16 |issue= 6 |pages= 467-72 |year= 2001 |pmid= 11102975 |doi= 10.1002/1098-1004(200012)16:6<467::AID-HUMU3>3.0.CO;2-V }}
*{{cite journal  | author=Gross M, Rötzer E, Kölle P, ''et al.'' |title=A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population. |journal=Neuromuscul. Disord. |volume=12 |issue= 6 |pages= 558-65 |year= 2002 |pmid= 12117480 |doi=  }}
*{{cite journal  | author=Mahnke-Zizelman DK, Sabina RL |title=N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42654-62 |year= 2003 |pmid= 12213808 |doi= 10.1074/jbc.M203473200 }}
*{{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] AP1G1

• INFO: Beginning work on AP1G1... {November 19, 2007 12:48:31 AM PST}
• SEARCH REDIRECT: Control Box Found: AP1G1 {November 19, 2007 12:49:07 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:49:08 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:49:08 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:49:08 AM PST}
• UPDATED: Updated protein page: AP1G1 {November 19, 2007 12:49:14 AM PST}

[edit] APBA1

• INFO: Beginning work on APBA1... {November 19, 2007 12:49:37 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:50:08 AM 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_APBA1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aqc.
 | PDB = {{PDB2|1aqc}}, {{PDB2|1u37}}, {{PDB2|1u38}}, {{PDB2|1u39}}, {{PDB2|1u3b}}, {{PDB2|1x11}}, {{PDB2|1x45}}, {{PDB2|1y7n}}
 | Name = Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)
 | HGNCid = 578
 | Symbol = APBA1
 | AltSymbols =; D9S411E; MINT1; X11; X11A; X11ALPHA
 | OMIM = 602414
 | ECnumber =  
 | Homologene = 897
 | MGIid = 1860297
 | GeneAtlas_image1 = PBB_GE_APBA1_206679_at_tn.png
 | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} 
 | Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008088 |text = axon cargo transport}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 320
    | Hs_Ensembl = ENSG00000107282
    | Hs_RefseqProtein = NP_001154
    | Hs_RefseqmRNA = NM_001163
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 71235022
    | Hs_GenLoc_end = 71477042
    | Hs_Uniprot = Q02410
    | Mm_EntrezGene = 319924
    | Mm_Ensembl = ENSMUSG00000024897
    | Mm_RefseqmRNA = NM_177034
    | Mm_RefseqProtein = NP_796008
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 23825973
    | Mm_GenLoc_end = 24016694
    | Mm_Uniprot =  
  }}
}}
'''Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)''', also known as '''APBA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320| 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 X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.<ref name="entrez">{{cite web | title = Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=van der Geer P, Pawson T |title=The PTB domain: a new protein module implicated in signal transduction. |journal=Trends Biochem. Sci. |volume=20 |issue= 7 |pages= 277-80 |year= 1995 |pmid= 7545337 |doi=  }}
*{{cite journal  | author=Chen WJ, Goldstein JL, Brown MS |title=NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. |journal=J. Biol. Chem. |volume=265 |issue= 6 |pages= 3116-23 |year= 1990 |pmid= 1968060 |doi=  }}
*{{cite journal  | author=Duclos F, Boschert U, Sirugo G, ''et al.'' |title=Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 1 |pages= 109-13 |year= 1993 |pmid= 7678331 |doi=  }}
*{{cite journal  | author=Duclos F, Koenig M |title=Comparison of primary structure of a neuron-specific protein, X11, between human and mouse. |journal=Mamm. Genome |volume=6 |issue= 1 |pages= 57-8 |year= 1995 |pmid= 7719031 |doi=  }}
*{{cite journal  | author=Borg JP, Ooi J, Levy E, Margolis B |title=The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6229-41 |year= 1996 |pmid= 8887653 |doi=  }}
*{{cite journal  | author=Zhang Z, Lee CH, Mandiyan V, ''et al.'' |title=Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. |journal=EMBO J. |volume=16 |issue= 20 |pages= 6141-50 |year= 1997 |pmid= 9321393 |doi= 10.1093/emboj/16.20.6141 }}
*{{cite journal  | author=Okamoto M, Südhof TC |title=Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. |journal=J. Biol. Chem. |volume=272 |issue= 50 |pages= 31459-64 |year= 1998 |pmid= 9395480 |doi=  }}
*{{cite journal  | author=Blanco G, Irving NG, Brown SD, ''et al.'' |title=Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein. |journal=Mamm. Genome |volume=9 |issue= 6 |pages= 473-5 |year= 1998 |pmid= 9585438 |doi=  }}
*{{cite journal  | author=Borg JP, Yang Y, De Taddéo-Borg M, ''et al.'' |title=The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. |journal=J. Biol. Chem. |volume=273 |issue= 24 |pages= 14761-6 |year= 1998 |pmid= 9614075 |doi=  }}
*{{cite journal  | author=Butz S, Okamoto M, Südhof TC |title=A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. |journal=Cell |volume=94 |issue= 6 |pages= 773-82 |year= 1998 |pmid= 9753324 |doi=  }}
*{{cite journal  | author=Borg JP, Straight SW, Kaech SM, ''et al.'' |title=Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31633-6 |year= 1998 |pmid= 9822620 |doi=  }}
*{{cite journal  | author=Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, ''et al.'' |title=Molecular analysis of the X11-mLin-2/CASK complex in brain. |journal=J. Neurosci. |volume=19 |issue= 4 |pages= 1307-16 |year= 1999 |pmid= 9952408 |doi=  }}
*{{cite journal  | author=Maximov A, Südhof TC, Bezprozvanny I |title=Association of neuronal calcium channels with modular adaptor proteins. |journal=J. Biol. Chem. |volume=274 |issue= 35 |pages= 24453-6 |year= 1999 |pmid= 10455105 |doi=  }}
*{{cite journal  | author=Mueller HT, Borg JP, Margolis B, Turner RS |title=Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains. |journal=J. Biol. Chem. |volume=275 |issue= 50 |pages= 39302-6 |year= 2001 |pmid= 11010978 |doi= 10.1074/jbc.M008453200 }}
*{{cite journal  | author=Biederer T, Südhof TC |title=Mints as adaptors. Direct binding to neurexins and recruitment of munc18. |journal=J. Biol. Chem. |volume=275 |issue= 51 |pages= 39803-6 |year= 2001 |pmid= 11036064 |doi= 10.1074/jbc.C000656200 }}
*{{cite journal  | author=Lau KF, McLoughlin DM, Standen C, Miller CC |title=X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains. |journal=Mol. Cell. Neurosci. |volume=16 |issue= 5 |pages= 557-65 |year= 2001 |pmid= 11083918 |doi= 10.1006/mcne.2000.0898 }}
*{{cite journal  | author=McLoughlin DM, Standen CL, Lau KF, ''et al.'' |title=The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9303-7 |year= 2001 |pmid= 11115513 |doi= 10.1074/jbc.M010023200 }}
*{{cite journal  | author=Bécamel C, Alonso G, Galéotti N, ''et al.'' |title=Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach. |journal=EMBO J. |volume=21 |issue= 10 |pages= 2332-42 |year= 2002 |pmid= 12006486 |doi= 10.1093/emboj/21.10.2332 }}
*{{cite journal  | author=Ho CS, Marinescu V, Steinhilb ML, ''et al.'' |title=Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27021-8 |year= 2002 |pmid= 12016213 |doi= 10.1074/jbc.M201823200 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] ATN1

• INFO: Beginning work on ATN1... {November 19, 2007 12:51:13 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:51:49 AM 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 = Atrophin 1
 | HGNCid = 3033
 | Symbol = ATN1
 | AltSymbols =; B37; D12S755E; DRPLA; NOD
 | OMIM = 607462
 | ECnumber =  
 | Homologene = 1461
 | MGIid = 104725
 | GeneAtlas_image1 = PBB_GE_ATN1_40489_at_tn.png
 | GeneAtlas_image2 = PBB_GE_ATN1_208871_at_tn.png
 | GeneAtlas_image3 = PBB_GE_ATN1_211076_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0050827 |text = toxin receptor binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0008219 |text = cell death}} {{GNF_GO|id=GO:0009404 |text = toxin metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1822
    | Hs_Ensembl = ENSG00000111676
    | Hs_RefseqProtein = NP_001007027
    | Hs_RefseqmRNA = NM_001007026
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 6903887
    | Hs_GenLoc_end = 6921743
    | Hs_Uniprot = P54259
    | Mm_EntrezGene = 13498
    | Mm_Ensembl = ENSMUSG00000004263
    | Mm_RefseqmRNA = XM_981322
    | Mm_RefseqProtein = XP_986416
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 124708161
    | Mm_GenLoc_end = 124722106
    | Mm_Uniprot =  
  }}
}}
'''Atrophin 1''', also known as '''ATN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATN1 atrophin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1822| 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 = Dentatorubral pallidoluysian atrophy is a rare neurodegenerative disorder characterized by cerebellar ataxia, myoclonic epilepsy, choreoathetosis, and dementia. The disorder is related to the expansion of a trinucleotide repeat within this gene. The encoded protein includes a serine repeat and a region of alternating acidic and basic amino acids, as well as the variable glutamine repeat. Alternative splicing results in two transcripts variants that encode the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: ATN1 atrophin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1822| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Onodera O, Oyake M, Takano H, ''et al.'' |title=Molecular cloning of a full-length cDNA for dentatorubral-pallidoluysian atrophy and regional expressions of the expanded alleles in the CNS. |journal=Am. J. Hum. Genet. |volume=57 |issue= 5 |pages= 1050-60 |year= 1995 |pmid= 7485154 |doi=  }}
*{{cite journal  | author=Yazawa I, Nukina N, Hashida H, ''et al.'' |title=Abnormal gene product identified in hereditary dentatorubral-pallidoluysian atrophy (DRPLA) brain. |journal=Nat. Genet. |volume=10 |issue= 1 |pages= 99-103 |year= 1995 |pmid= 7647802 |doi= 10.1038/ng0595-99 }}
*{{cite journal  | author=Nagafuchi S, Yanagisawa H, Ohsaki E, ''et al.'' |title=Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA). |journal=Nat. Genet. |volume=8 |issue= 2 |pages= 177-82 |year= 1995 |pmid= 7842016 |doi= 10.1038/ng1094-177 }}
*{{cite journal  | author=Burke JR, Wingfield MS, Lewis KE, ''et al.'' |title=The Haw River syndrome: dentatorubropallidoluysian atrophy (DRPLA) in an African-American family. |journal=Nat. Genet. |volume=7 |issue= 4 |pages= 521-4 |year= 1994 |pmid= 7951323 |doi= 10.1038/ng0894-521 }}
*{{cite journal  | author=Nagafuchi S, Yanagisawa H, Sato K, ''et al.'' |title=Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p. |journal=Nat. Genet. |volume=6 |issue= 1 |pages= 14-8 |year= 1994 |pmid= 8136826 |doi= 10.1038/ng0194-14 }}
*{{cite journal  | author=Koide R, Ikeuchi T, Onodera O, ''et al.'' |title=Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA). |journal=Nat. Genet. |volume=6 |issue= 1 |pages= 9-13 |year= 1994 |pmid= 8136840 |doi= 10.1038/ng0194-9 }}
*{{cite journal  | author=Li SH, McInnis MG, Margolis RL, ''et al.'' |title=Novel triplet repeat containing genes in human brain: cloning, expression, and length polymorphisms. |journal=Genomics |volume=16 |issue= 3 |pages= 572-9 |year= 1993 |pmid= 8325628 |doi= 10.1006/geno.1993.1232 }}
*{{cite journal  | author=Ansari-Lari MA, Muzny DM, Lu J, ''et al.'' |title=A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. |journal=Genome Res. |volume=6 |issue= 4 |pages= 314-26 |year= 1996 |pmid= 8723724 |doi=  }}
*{{cite journal  | author=Takano T, Yamanouchi Y, Nagafuchi S, Yamada M |title=Assignment of the dentatorubral and pallidoluysian atrophy (DRPLA) gene to 12p 13.31 by fluorescence in situ hybridization. |journal=Genomics |volume=32 |issue= 1 |pages= 171-2 |year= 1996 |pmid= 8786114 |doi= 10.1006/geno.1996.0100 }}
*{{cite journal  | author=Yanagisawa H, Fujii K, Nagafuchi S, ''et al.'' |title=A unique origin and multistep process for the generation of expanded DRPLA triplet repeats. |journal=Hum. Mol. Genet. |volume=5 |issue= 3 |pages= 373-9 |year= 1997 |pmid= 8852663 |doi=  }}
*{{cite journal  | author=Margolis RL, Li SH, Young WS, ''et al.'' |title=DRPLA gene (atrophin-1) sequence and mRNA expression in human brain. |journal=Brain Res. Mol. Brain Res. |volume=36 |issue= 2 |pages= 219-26 |year= 1996 |pmid= 8965642 |doi=  }}
*{{cite journal  | author=Ansari-Lari MA, Shen Y, Muzny DM, ''et al.'' |title=Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. |journal=Genome Res. |volume=7 |issue= 3 |pages= 268-80 |year= 1997 |pmid= 9074930 |doi=  }}
*{{cite journal  | author=Miyashita T, Okamura-Oho Y, Mito Y, ''et al.'' |title=Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29238-42 |year= 1997 |pmid= 9361003 |doi=  }}
*{{cite journal  | author=Wellington CL, Ellerby LM, Hackam AS, ''et al.'' |title=Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 9158-67 |year= 1998 |pmid= 9535906 |doi=  }}
*{{cite journal  | author=Wood JD, Yuan J, Margolis RL, ''et al.'' |title=Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins. |journal=Mol. Cell. Neurosci. |volume=11 |issue= 3 |pages= 149-60 |year= 1998 |pmid= 9647693 |doi= 10.1006/mcne.1998.0677 }}
*{{cite journal  | author=Hayashi Y, Kakita A, Yamada M, ''et al.'' |title=Hereditary dentatorubral-pallidoluysian atrophy: detection of widespread ubiquitinated neuronal and glial intranuclear inclusions in the brain. |journal=Acta Neuropathol. |volume=96 |issue= 6 |pages= 547-52 |year= 1999 |pmid= 9845282 |doi=  }}
*{{cite journal  | author=Takiyama Y, Sakoe K, Amaike M, ''et al.'' |title=Single sperm analysis of the CAG repeats in the gene for dentatorubral-pallidoluysian atrophy (DRPLA): the instability of the CAG repeats in the DRPLA gene is prominent among the CAG repeat diseases. |journal=Hum. Mol. Genet. |volume=8 |issue= 3 |pages= 453-7 |year= 1999 |pmid= 9949204 |doi=  }}
*{{cite journal  | author=Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M |title=Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate. |journal=Hum. Mol. Genet. |volume=8 |issue= 6 |pages= 947-57 |year= 1999 |pmid= 10332026 |doi=  }}
*{{cite journal  | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi=  }}
*{{cite journal  | author=Yanagisawa H, Bundo M, Miyashita T, ''et al.'' |title=Protein binding of a DRPLA family through arginine-glutamic acid dipeptide repeats is enhanced by extended polyglutamine. |journal=Hum. Mol. Genet. |volume=9 |issue= 9 |pages= 1433-42 |year= 2000 |pmid= 10814707 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] ATP2C1

• INFO: Beginning work on ATP2C1... {November 19, 2007 10:41:07 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:42:00 AM 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 = ATPase, Ca++ transporting, type 2C, member 1
 | HGNCid = 13211
 | Symbol = ATP2C1
 | AltSymbols =; ATP2C1A; BCPM; HHD; KIAA1347; PMR1; SPCA1; hSPCA1
 | OMIM = 604384
 | ECnumber =  
 | Homologene = 56672
 | MGIid = 1889008
 | GeneAtlas_image1 = PBB_GE_ATP2C1_209934_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_ATP2C1_209935_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005388 |text = calcium-transporting ATPase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}} 
 | Component = {{GNF_GO|id=GO:0000139 |text = Golgi membrane}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005802 |text = trans-Golgi network}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0016339 |text = calcium-dependent cell-cell adhesion}} {{GNF_GO|id=GO:0031532 |text = actin cytoskeleton reorganization}} {{GNF_GO|id=GO:0032468 |text = Golgi calcium ion homeostasis}} {{GNF_GO|id=GO:0032472 |text = Golgi calcium ion transport}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 27032
    | Hs_Ensembl = ENSG00000017260
    | Hs_RefseqProtein = NP_001001485
    | Hs_RefseqmRNA = NM_001001485
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 132095712
    | Hs_GenLoc_end = 132218243
    | Hs_Uniprot = P98194
    | Mm_EntrezGene = 235574
    | Mm_Ensembl = ENSMUSG00000032570
    | Mm_RefseqmRNA = XM_981296
    | Mm_RefseqProtein = XP_986390
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 105269458
    | Mm_GenLoc_end = 105379247
    | Mm_Uniprot = Q3UWW0
  }}
}}
'''ATPase, Ca++ transporting, type 2C, member 1''', also known as '''ATP2C1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP2C1 ATPase, Ca++ transporting, type 2C, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27032| 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 belongs to the family of P-type cation transport ATPases. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in this gene cause Hailey-Hailey disease, an autosomal dominant disorder. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ATP2C1 ATPase, Ca++ transporting, type 2C, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27032| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Missiaen L, Raeymaekers L, Dode L, ''et al.'' |title=SPCA1 pumps and Hailey-Hailey disease. |journal=Biochem. Biophys. Res. Commun. |volume=322 |issue= 4 |pages= 1204-13 |year= 2004 |pmid= 15336968 |doi= 10.1016/j.bbrc.2004.07.128 }}
*{{cite journal  | author=Ikeda S, Welsh EA, Peluso AM, ''et al.'' |title=Localization of the gene whose mutations underlie Hailey-Hailey disease to chromosome 3q. |journal=Hum. Mol. Genet. |volume=3 |issue= 7 |pages= 1147-50 |year= 1995 |pmid= 7981684 |doi=  }}
*{{cite journal  | author=Hu Z, Bonifas JM, Beech J, ''et al.'' |title=Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. |journal=Nat. Genet. |volume=24 |issue= 1 |pages= 61-5 |year= 2000 |pmid= 10615129 |doi= 10.1038/71701 }}
*{{cite journal  | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi=  }}
*{{cite journal  | author=Sudbrak R, Brown J, Dobson-Stone C, ''et al.'' |title=Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump. |journal=Hum. Mol. Genet. |volume=9 |issue= 7 |pages= 1131-40 |year= 2000 |pmid= 10767338 |doi=  }}
*{{cite journal  | author=Stanchi F, Bertocco E, Toppo S, ''et al.'' |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69-80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H }}
*{{cite journal  | author=Ton VK, Mandal D, Vahadji C, Rao R |title=Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 6422-7 |year= 2002 |pmid= 11741891 |doi= 10.1074/jbc.M110612200 }}
*{{cite journal  | author=Dobson-Stone C, Fairclough R, Dunne E, ''et al.'' |title=Hailey-Hailey disease: molecular and clinical characterization of novel mutations in the ATP2C1 gene. |journal=J. Invest. Dermatol. |volume=118 |issue= 2 |pages= 338-43 |year= 2002 |pmid= 11841554 |doi= 10.1046/j.0022-202x.2001.01675.x }}
*{{cite journal  | author=Yokota K, Yasukawa K, Shimizu H |title=Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease. |journal=J. Invest. Dermatol. |volume=118 |issue= 3 |pages= 550-1 |year= 2002 |pmid= 11874499 |doi= 10.1046/j.0022-202x.2001.01686.x }}
*{{cite journal  | author=Chao SC, Tsai YM, Yang MH |title=Mutation analysis of ATP2C1 gene in Taiwanese patients with Hailey-Hailey disease. |journal=Br. J. Dermatol. |volume=146 |issue= 4 |pages= 595-600 |year= 2002 |pmid= 11966689 |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=Fairclough RJ, Dode L, Vanoevelen J, ''et al.'' |title=Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1). |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 24721-30 |year= 2003 |pmid= 12707275 |doi= 10.1074/jbc.M300509200 }}
*{{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=Van Baelen K, Vanoevelen J, Callewaert G, ''et al.'' |title=The contribution of the SPCA1 Ca2+ pump to the Ca2+ accumulation in the Golgi apparatus of HeLa cells assessed via RNA-mediated interference. |journal=Biochem. Biophys. Res. Commun. |volume=306 |issue= 2 |pages= 430-6 |year= 2003 |pmid= 12804581 |doi=  }}
*{{cite journal  | author=Callewaert G, Parys JB, De Smedt H, ''et al.'' |title=Similar Ca(2+)-signaling properties in keratinocytes and in COS-1 cells overexpressing the secretory-pathway Ca(2+)-ATPase SPCA1. |journal=Cell Calcium |volume=34 |issue= 2 |pages= 157-62 |year= 2004 |pmid= 12810057 |doi=  }}
*{{cite journal  | author=Aronchik I, Behne MJ, Leypoldt L, ''et al.'' |title=Actin reorganization is abnormal and cellular ATP is decreased in Hailey-Hailey keratinocytes. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 681-7 |year= 2003 |pmid= 14632182 |doi= 10.1046/j.1523-1747.2003.12472.x }}
*{{cite journal  | author=Behne MJ, Tu CL, Aronchik I, ''et al.'' |title=Human keratinocyte ATP2C1 localizes to the Golgi and controls Golgi Ca2+ stores. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 688-94 |year= 2003 |pmid= 14632183 |doi= 10.1046/j.1523-1747.2003.12528.x }}
*{{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=Mitchell KJ, Tsuboi T, Rutter GA |title=Role for plasma membrane-related Ca2+-ATPase-1 (ATP2C1) in pancreatic beta-cell Ca2+ homeostasis revealed by RNA silencing. |journal=Diabetes |volume=53 |issue= 2 |pages= 393-400 |year= 2004 |pmid= 14747290 |doi=  }}
*{{cite journal  | author=Fairclough RJ, Lonie L, Van Baelen K, ''et al.'' |title=Hailey-Hailey disease: identification of novel mutations in ATP2C1 and effect of missense mutation A528P on protein expression levels. |journal=J. Invest. Dermatol. |volume=123 |issue= 1 |pages= 67-71 |year= 2004 |pmid= 15191544 |doi= 10.1111/j.0022-202X.2004.22713.x }}
}}
{{refend}}

{{protein-stub}}
 

[edit] CYP27A1

• INFO: Beginning work on CYP27A1... {November 19, 2007 12:50:09 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:50:34 AM 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 = Cytochrome P450, family 27, subfamily A, polypeptide 1
 | HGNCid = 2605
 | Symbol = CYP27A1
 | AltSymbols =; CP27; CTX; CYP27
 | OMIM = 606530
 | ECnumber =  
 | Homologene = 36040
 | MGIid = 88594
 | GeneAtlas_image1 = PBB_GE_CYP27A1_203979_at_tn.png
 | Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008395 |text = steroid hydroxylase activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0047749 |text = cholestanetriol 26-monooxygenase activity}} 
 | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1593
    | Hs_Ensembl = ENSG00000135929
    | Hs_RefseqProtein = NP_000775
    | Hs_RefseqmRNA = NM_000784
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 219354745
    | Hs_GenLoc_end = 219388254
    | Hs_Uniprot = Q02318
    | Mm_EntrezGene = 104086
    | Mm_Ensembl = ENSMUSG00000026170
    | Mm_RefseqmRNA = NM_024264
    | Mm_RefseqProtein = NP_077226
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 74646781
    | Mm_GenLoc_end = 74671097
    | Mm_Uniprot = Q99LX3
  }}
}}
'''Cytochrome P450, family 27, subfamily A, polypeptide 1''', also known as '''CYP27A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP27A1 cytochrome P450, family 27, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1593| 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 cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This mitochondrial protein oxidizes cholesterol intermediates as part of the bile synthesis pathway. Since the conversion of cholesterol to bile acids is the major route for removing cholesterol from the body, this protein is important for overall cholesterol homeostasis. Mutations in this gene cause cerebrotendinous xanthomatosis, a rare autosomal recessive lipid storage disease.<ref name="entrez">{{cite web | title = Entrez Gene: CYP27A1 cytochrome P450, family 27, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1593| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Cali JJ, Russell DW |title=Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. |journal=J. Biol. Chem. |volume=266 |issue= 12 |pages= 7774-8 |year= 1991 |pmid= 1708392 |doi=  }}
*{{cite journal  | author=Cali JJ, Hsieh CL, Francke U, Russell DW |title=Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis. |journal=J. Biol. Chem. |volume=266 |issue= 12 |pages= 7779-83 |year= 1991 |pmid= 2019602 |doi=  }}
*{{cite journal  | author=Guo YD, Strugnell S, Back DW, Jones G |title=Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 18 |pages= 8668-72 |year= 1993 |pmid= 7690968 |doi=  }}
*{{cite journal  | author=Kim KS, Kubota S, Kuriyama M, ''et al.'' |title=Identification of new mutations in sterol 27-hydroxylase gene in Japanese patients with cerebrotendinous xanthomatosis (CTX). |journal=J. Lipid Res. |volume=35 |issue= 6 |pages= 1031-9 |year= 1994 |pmid= 7915755 |doi=  }}
*{{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=Leitersdorf E, Reshef A, Meiner V, ''et al.'' |title=Frameshift and splice-junction mutations in the sterol 27-hydroxylase gene cause cerebrotendinous xanthomatosis in Jews or Moroccan origin. |journal=J. Clin. Invest. |volume=91 |issue= 6 |pages= 2488-96 |year= 1993 |pmid= 8514861 |doi=  }}
*{{cite journal  | author=Chen W, Kubota S, Kim KS, ''et al.'' |title=Novel homozygous and compound heterozygous mutations of sterol 27-hydroxylase gene (CYP27) cause cerebrotendinous xanthomatosis in three Japanese patients from two unrelated families. |journal=J. Lipid Res. |volume=38 |issue= 5 |pages= 870-9 |year= 1997 |pmid= 9186905 |doi=  }}
*{{cite journal  | author=Reiss AB, Martin KO, Rojer DE, ''et al.'' |title=Sterol 27-hydroxylase: expression in human arterial endothelium. |journal=J. Lipid Res. |volume=38 |issue= 6 |pages= 1254-60 |year= 1997 |pmid= 9215552 |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=Chen W, Kubota S, Ujike H, ''et al.'' |title=A novel Arg362Ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity. |journal=Biochemistry |volume=37 |issue= 43 |pages= 15050-6 |year= 1998 |pmid= 9790667 |doi= 10.1021/bi9807660 }}
*{{cite journal  | author=Shiga K, Fukuyama R, Kimura S, ''et al.'' |title=Mutation of the sterol 27-hydroxylase gene (CYP27) results in truncation of mRNA expressed in leucocytes in a Japanese family with cerebrotendinous xanthomatosis. |journal=J. Neurol. Neurosurg. Psychiatr. |volume=67 |issue= 5 |pages= 675-7 |year= 1999 |pmid= 10519880 |doi=  }}
*{{cite journal  | author=Gascon-Barré M, Demers C, Ghrab O, ''et al.'' |title=Expression of CYP27A, a gene encoding a vitamin D-25 hydroxylase in human liver and kidney. |journal=Clin. Endocrinol. (Oxf) |volume=54 |issue= 1 |pages= 107-15 |year= 2001 |pmid= 11167933 |doi=  }}
*{{cite journal  | author=Johnston TP, Nguyen LB, Chu WA, Shefer S |title=Potency of select statin drugs in a new mouse model of hyperlipidemia and atherosclerosis. |journal=International journal of pharmaceutics |volume=229 |issue= 1-2 |pages= 75-86 |year= 2001 |pmid= 11604260 |doi=  }}
*{{cite journal  | author=Toba H, Fukuyama R, Sasaki M, ''et al.'' |title=A Japanese patient with cerebrotendinous xanthomatosis has different mutations within two functional domains of CYP27. |journal=Clin. Genet. |volume=61 |issue= 1 |pages= 77-8 |year= 2002 |pmid= 11903362 |doi=  }}
*{{cite journal  | author=Lamon-Fava S, Schaefer EJ, Garuti R, ''et al.'' |title=Two novel mutations in the sterol 27-hydroxylase gene causing cerebrotendinous xanthomatosis. |journal=Clin. Genet. |volume=61 |issue= 3 |pages= 185-91 |year= 2002 |pmid= 12000359 |doi=  }}
*{{cite journal  | author=Björkhem I, Araya Z, Rudling M, ''et al.'' |title=Differences in the regulation of the classical and the alternative pathway for bile acid synthesis in human liver. No coordinate regulation of CYP7A1 and CYP27A1. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 26804-7 |year= 2002 |pmid= 12011083 |doi= 10.1074/jbc.M202343200 }}
*{{cite journal  | author=von Bahr S, Movin T, Papadogiannakis N, ''et al.'' |title=Mechanism of accumulation of cholesterol and cholestanol in tendons and the role of sterol 27-hydroxylase (CYP27A1). |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 7 |pages= 1129-35 |year= 2002 |pmid= 12117727 |doi=  }}
*{{cite journal  | author=Meir K, Kitsberg D, Alkalay I, ''et al.'' |title=Human sterol 27-hydroxylase (CYP27) overexpressor transgenic mouse model. Evidence against 27-hydroxycholesterol as a critical regulator of cholesterol homeostasis. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34036-41 |year= 2002 |pmid= 12119285 |doi= 10.1074/jbc.M201122200 }}
*{{cite journal  | author=Lee MJ, Huang YC, Sweeney MG, ''et al.'' |title=Mutation of the sterol 27-hydroxylase gene ( CYP27A1) in a Taiwanese family with cerebrotendinous xanthomatosis. |journal=J. Neurol. |volume=249 |issue= 9 |pages= 1311-2 |year= 2002 |pmid= 12242561 |doi= 10.1007/s00415-002-0762-9 }}
*{{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] DICER1

• INFO: Beginning work on DICER1... {November 19, 2007 10:40:18 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:40:42 AM 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 = Dicer1, Dcr-1 homolog (Drosophila)
 | HGNCid = 17098
 | Symbol = DICER1
 | AltSymbols =; Dicer; HERNA; KIAA0928
 | OMIM = 606241
 | ECnumber =  
 | Homologene = 13251
 | MGIid = 2177178
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003725 |text = double-stranded RNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004525 |text = ribonuclease III activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008026 |text = ATP-dependent helicase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} 
 | Process = {{GNF_GO|id=GO:0006396 |text = RNA processing}} {{GNF_GO|id=GO:0019827 |text = stem cell maintenance}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0030422 |text = RNA interference, production of siRNA}} {{GNF_GO|id=GO:0030423 |text = RNA interference, targeting of mRNA for destruction}} {{GNF_GO|id=GO:0035116 |text = embryonic hindlimb morphogenesis}} {{GNF_GO|id=GO:0035196 |text = miRNA-mediated gene silencing, production of miRNAs}} {{GNF_GO|id=GO:0048754 |text = branching morphogenesis of a tube}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23405
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_085124
    | Hs_RefseqmRNA = NM_030621
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 192119
    | Mm_Ensembl = ENSMUSG00000041415
    | Mm_RefseqmRNA = NM_148948
    | Mm_RefseqProtein = NP_683750
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 105092486
    | Mm_GenLoc_end = 105152987
    | Mm_Uniprot = Q3UUV8
  }}
}}
'''Dicer1, Dcr-1 homolog (Drosophila)''', also known as '''DICER1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DICER1 Dicer1, Dcr-1 homolog (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23405| 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 possessing an RNA helicase motif containing a DEXH box in its amino terminus and an RNA motif in the carboxy terminus. The encoded protein functions as a ribonuclease and is required by the RNA interference and small temporal RNA (stRNA) pathways to produce the active small RNA component that represses gene expression. Two transcript variants encoding the same protein have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: DICER1 Dicer1, Dcr-1 homolog (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23405| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi=  }}
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
*{{cite journal  | author=Provost P, Samuelsson B, Rådmark O |title=Interaction of 5-lipoxygenase with cellular proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 1881-5 |year= 1999 |pmid= 10051563 |doi=  }}
*{{cite journal  | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 1 |pages= 63-70 |year= 1999 |pmid= 10231032 |doi=  }}
*{{cite journal  | author=Suk K, Kim S, Kim YH, ''et al.'' |title=Identification of a novel human member of the DEAD box protein family. |journal=Biochim. Biophys. Acta |volume=1501 |issue= 1 |pages= 63-9 |year= 2000 |pmid= 10727850 |doi=  }}
*{{cite journal  | author=Matsuda S, Ichigotani Y, Okuda T, ''et al.'' |title=Molecular cloning and characterization of a novel human gene (HERNA) which encodes a putative RNA-helicase. |journal=Biochim. Biophys. Acta |volume=1490 |issue= 1-2 |pages= 163-9 |year= 2000 |pmid= 10786632 |doi=  }}
*{{cite journal  | author=Tabara H, Yigit E, Siomi H, Mello CC |title=The dsRNA binding protein RDE-4 interacts with RDE-1, DCR-1, and a DExH-box helicase to direct RNAi in C. elegans. |journal=Cell |volume=109 |issue= 7 |pages= 861-71 |year= 2002 |pmid= 12110183 |doi=  }}
*{{cite journal  | author=Provost P, Dishart D, Doucet J, ''et al.'' |title=Ribonuclease activity and RNA binding of recombinant human Dicer. |journal=EMBO J. |volume=21 |issue= 21 |pages= 5864-74 |year= 2002 |pmid= 12411504 |doi=  }}
*{{cite journal  | author=Zhang H, Kolb FA, Brondani V, ''et al.'' |title=Human Dicer preferentially cleaves dsRNAs at their termini without a requirement for ATP. |journal=EMBO J. |volume=21 |issue= 21 |pages= 5875-85 |year= 2002 |pmid= 12411505 |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=Doi N, Zenno S, Ueda R, ''et al.'' |title=Short-interfering-RNA-mediated gene silencing in mammalian cells requires Dicer and eIF2C translation initiation factors. |journal=Curr. Biol. |volume=13 |issue= 1 |pages= 41-6 |year= 2003 |pmid= 12526743 |doi=  }}
*{{cite journal  | author=Kawasaki H, Taira K |title=Short hairpin type of dsRNAs that are controlled by tRNA(Val) promoter significantly induce RNAi-mediated gene silencing in the cytoplasm of human cells. |journal=Nucleic Acids Res. |volume=31 |issue= 2 |pages= 700-7 |year= 2003 |pmid= 12527779 |doi=  }}
*{{cite journal  | author=Kawasaki H, Suyama E, Iyo M, Taira K |title=siRNAs generated by recombinant human Dicer induce specific and significant but target site-independent gene silencing in human cells. |journal=Nucleic Acids Res. |volume=31 |issue= 3 |pages= 981-7 |year= 2003 |pmid= 12560494 |doi=  }}
*{{cite journal  | author=Sasaki T, Shiohama A, Minoshima S, Shimizu N |title=Identification of eight members of the Argonaute family in the human genome small star, filled. |journal=Genomics |volume=82 |issue= 3 |pages= 323-30 |year= 2004 |pmid= 12906857 |doi=  }}
*{{cite journal  | author=Handa V, Saha T, Usdin K |title=The fragile X syndrome repeats form RNA hairpins that do not activate the interferon-inducible protein kinase, PKR, but are cut by Dicer. |journal=Nucleic Acids Res. |volume=31 |issue= 21 |pages= 6243-8 |year= 2003 |pmid= 14576312 |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=Tahbaz N, Kolb FA, Zhang H, ''et al.'' |title=Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer. |journal=EMBO Rep. |volume=5 |issue= 2 |pages= 189-94 |year= 2004 |pmid= 14749716 |doi= 10.1038/sj.embor.7400070 }}
*{{cite journal  | author=Zhang H, Kolb FA, Jaskiewicz L, ''et al.'' |title=Single processing center models for human Dicer and bacterial RNase III. |journal=Cell |volume=118 |issue= 1 |pages= 57-68 |year= 2004 |pmid= 15242644 |doi= 10.1016/j.cell.2004.06.017 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] DLG2

• INFO: Beginning work on DLG2... {November 19, 2007 12:50:34 AM PST}
• SEARCH REDIRECT: Control Box Found: DLG2 {November 19, 2007 12:51:06 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:51:07 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:51:07 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:51:07 AM PST}
• UPDATED: Updated protein page: DLG2 {November 19, 2007 12:51:13 AM PST}

[edit] EPHA4

• INFO: Beginning work on EPHA4... {November 19, 2007 12:51:49 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:52:39 AM 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_EPHA4_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b0x.
 | PDB = {{PDB2|1b0x}}, {{PDB2|2hel}}
 | Name = EPH receptor A4
 | HGNCid = 3388
 | Symbol = EPHA4
 | AltSymbols =; HEK8; SEK; TYRO1
 | OMIM = 602188
 | ECnumber =  
 | Homologene = 20933
 | MGIid = 98277
 | GeneAtlas_image1 = PBB_GE_EPHA4_206114_at_tn.png
 | GeneAtlas_image2 = PBB_GE_EPHA4_gnf1h07687_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005003 |text = ephrin receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007628 |text = adult walking behavior}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2043
    | Hs_Ensembl = ENSG00000116106
    | Hs_RefseqProtein = NP_004429
    | Hs_RefseqmRNA = NM_004438
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 221990993
    | Hs_GenLoc_end = 222145254
    | Hs_Uniprot = P54764
    | Mm_EntrezGene = 13838
    | Mm_Ensembl = ENSMUSG00000026235
    | Mm_RefseqmRNA = NM_007936
    | Mm_RefseqProtein = NP_031962
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 77250333
    | Mm_GenLoc_end = 77398236
    | Mm_Uniprot = Q3V1W9
  }}
}}
'''EPH receptor A4''', also known as '''EPHA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPHA4 EPH receptor A4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2043| 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 belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.<ref name="entrez">{{cite web | title = Entrez Gene: EPHA4 EPH receptor A4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2043| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development. |journal=Annu. Rev. Neurosci. |volume=21 |issue=  |pages= 309-45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
*{{cite journal  | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151-81 |year= 1998 |pmid= 9576626 |doi=  }}
*{{cite journal  | author=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033-44 |year= 1999 |pmid= 10207129 |doi=  }}
*{{cite journal  | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue=  |pages= 177-244 |year= 2000 |pmid= 10730216 |doi=  }}
*{{cite journal  | author=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=355 |issue= 1399 |pages= 993-1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635 }}
*{{cite journal  | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155-64 |year= 2001 |pmid= 11256076 |doi=  }}
*{{cite journal  | author=Fox GM, Holst PL, Chute HT, ''et al.'' |title=cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases. |journal=Oncogene |volume=10 |issue= 5 |pages= 897-905 |year= 1995 |pmid= 7898931 |doi=  }}
*{{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=Ellis C, Kasmi F, Ganju P, ''et al.'' |title=A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn. |journal=Oncogene |volume=12 |issue= 8 |pages= 1727-36 |year= 1996 |pmid= 8622893 |doi=  }}
*{{cite journal  | author=Gale NW, Holland SJ, Valenzuela DM, ''et al.'' |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9-19 |year= 1996 |pmid= 8755474 |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= |title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403-4 |year= 1997 |pmid= 9267020 |doi=  }}
*{{cite journal  | author=Aasheim HC, Terstappen LW, Logtenberg T |title=Regulated expression of the Eph-related receptor tyrosine kinase Hek11 in early human B lymphopoiesis. |journal=Blood |volume=90 |issue= 9 |pages= 3613-22 |year= 1997 |pmid= 9345045 |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=Bergemann AD, Zhang L, Chiang MK, ''et al.'' |title=Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. |journal=Oncogene |volume=16 |issue= 4 |pages= 471-80 |year= 1998 |pmid= 9484836 |doi= 10.1038/sj.onc.1201557 }}
*{{cite journal  | author=Janis LS, Cassidy RM, Kromer LF |title=Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum. |journal=J. Neurosci. |volume=19 |issue= 12 |pages= 4962-71 |year= 1999 |pmid= 10366629 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] F13B

• INFO: Beginning work on F13B... {November 19, 2007 12:52:39 AM PST}
• SEARCH REDIRECT: Control Box Found: F13B {November 19, 2007 12:52:58 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:53:01 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:53:01 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:53:01 AM PST}
• UPDATED: Updated protein page: F13B {November 19, 2007 12:53:06 AM PST}

[edit] FAH

• INFO: Beginning work on FAH... {November 19, 2007 12:53:07 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:53:34 AM 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 = Fumarylacetoacetate hydrolase (fumarylacetoacetase)
 | HGNCid = 3579
 | Symbol = FAH
 | AltSymbols =; 
 | OMIM = 276700
 | ECnumber =  
 | Homologene = 110
 | MGIid = 95482
 | GeneAtlas_image1 = PBB_GE_FAH_202862_at_tn.png
 | Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004334 |text = fumarylacetoacetase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006527 |text = arginine catabolic process}} {{GNF_GO|id=GO:0006559 |text = L-phenylalanine catabolic process}} {{GNF_GO|id=GO:0006572 |text = tyrosine catabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009072 |text = aromatic amino acid family metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2184
    | Hs_Ensembl = ENSG00000103876
    | Hs_RefseqProtein = NP_000128
    | Hs_RefseqmRNA = NM_000137
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 78232191
    | Hs_GenLoc_end = 78265740
    | Hs_Uniprot = P16930
    | Mm_EntrezGene = 14085
    | Mm_Ensembl = ENSMUSG00000030630
    | Mm_RefseqmRNA = NM_010176
    | Mm_RefseqProtein = NP_034306
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 84461344
    | Mm_GenLoc_end = 84481937
    | Mm_Uniprot = Q3TY87
  }}
}}
'''Fumarylacetoacetate hydrolase (fumarylacetoacetase)''', also known as '''FAH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FAH fumarylacetoacetate hydrolase (fumarylacetoacetase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2184| 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 last enzyme in the tyrosine catabolism pathway. FAH deficiency is associated with Type 1 hereditary tyrosinemia (HT).<ref name="entrez">{{cite web | title = Entrez Gene: FAH fumarylacetoacetate hydrolase (fumarylacetoacetase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2184| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=St-Louis M, Tanguay RM |title=Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview. |journal=Hum. Mutat. |volume=9 |issue= 4 |pages= 291-9 |year= 1997 |pmid= 9101289 |doi= 10.1002/(SICI)1098-1004(1997)9:4<291::AID-HUMU1>3.0.CO;2-9 }}
*{{cite journal  | author=Phaneuf D, Lambert M, Laframboise R, ''et al.'' |title=Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient. |journal=J. Clin. Invest. |volume=90 |issue= 4 |pages= 1185-92 |year= 1992 |pmid= 1401056 |doi=  }}
*{{cite journal  | author=Phaneuf D, Labelle Y, Bérubé D, ''et al.'' |title=Cloning and expression of the cDNA encoding human fumarylacetoacetate hydrolase, the enzyme deficient in hereditary tyrosinemia: assignment of the gene to chromosome 15. |journal=Am. J. Hum. Genet. |volume=48 |issue= 3 |pages= 525-35 |year= 1991 |pmid= 1998338 |doi=  }}
*{{cite journal  | author=Agsteribbe E, van Faassen H, Hartog MV, ''et al.'' |title=Nucleotide sequence of cDNA encoding human fumarylacetoacetase. |journal=Nucleic Acids Res. |volume=18 |issue= 7 |pages= 1887 |year= 1990 |pmid= 2336361 |doi=  }}
*{{cite journal  | author=Tanguay RM, Valet JP, Lescault A, ''et al.'' |title=Different molecular basis for fumarylacetoacetate hydrolase deficiency in the two clinical forms of hereditary tyrosinemia (type I). |journal=Am. J. Hum. Genet. |volume=47 |issue= 2 |pages= 308-16 |year= 1990 |pmid= 2378356 |doi=  }}
*{{cite journal  | author=Laberge C, Grenier A, Valet JP, Morissette J |title=Fumarylacetoacetase measurement as a mass-screening procedure for hereditary tyrosinemia type I. |journal=Am. J. Hum. Genet. |volume=47 |issue= 2 |pages= 325-8 |year= 1990 |pmid= 2378358 |doi=  }}
*{{cite journal  | author=Kvittingen EA, Halvorsen S, Jellum E |title=Deficient fumarylacetoacetate fumarylhydrolase activity in lymphocytes and fibroblasts from patients with hereditary tyrosinemia. |journal=Pediatr. Res. |volume=17 |issue= 7 |pages= 541-4 |year= 1983 |pmid= 6622096 |doi=  }}
*{{cite journal  | author=Kvittingen EA, Jellum E, Stokke O |title=Assay of fumarylacetoacetate fumarylhydrolase in human liver-deficient activity in a case of hereditary tyrosinemia. |journal=Clin. Chim. Acta |volume=115 |issue= 3 |pages= 311-9 |year= 1982 |pmid= 7296877 |doi=  }}
*{{cite journal  | author=Hahn SH, Krasnewich D, Brantly M, ''et al.'' |title=Heterozygosity for an exon 12 splicing mutation and a W234G missense mutation in an American child with chronic tyrosinemia type 1. |journal=Hum. Mutat. |volume=6 |issue= 1 |pages= 66-73 |year= 1995 |pmid= 7550234 |doi= 10.1002/humu.1380060113 }}
*{{cite journal  | author=St-Louis M, Poudrier J, Phaneuf D, ''et al.'' |title=Two novel mutations involved in hereditary tyrosinemia type I. |journal=Hum. Mol. Genet. |volume=4 |issue= 2 |pages= 319-20 |year= 1995 |pmid= 7757089 |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=Rootwelt H, Berger R, Gray G, ''et al.'' |title=Novel splice, missense, and nonsense mutations in the fumarylacetoacetase gene causing tyrosinemia type 1. |journal=Am. J. Hum. Genet. |volume=55 |issue= 4 |pages= 653-8 |year= 1994 |pmid= 7942842 |doi=  }}
*{{cite journal  | author=Rootwelt H, Brodtkorb E, Kvittingen EA |title=Identification of a frequent pseudodeficiency mutation in the fumarylacetoacetase gene, with implications for diagnosis of tyrosinemia type I. |journal=Am. J. Hum. Genet. |volume=55 |issue= 6 |pages= 1122-7 |year= 1994 |pmid= 7977370 |doi=  }}
*{{cite journal  | author=Rootwelt H, Chou J, Gahl WA, ''et al.'' |title=Two missense mutations causing tyrosinemia type 1 with presence and absence of immunoreactive fumarylacetoacetase. |journal=Hum. Genet. |volume=93 |issue= 6 |pages= 615-9 |year= 1994 |pmid= 8005583 |doi=  }}
*{{cite journal  | author=Grompe M, St-Louis M, Demers SI, ''et al.'' |title=A single mutation of the fumarylacetoacetate hydrolase gene in French Canadians with hereditary tyrosinemia type I. |journal=N. Engl. J. Med. |volume=331 |issue= 6 |pages= 353-7 |year= 1994 |pmid= 8028615 |doi=  }}
*{{cite journal  | author=St-Louis M, Leclerc B, Laine J, ''et al.'' |title=Identification of a stop mutation in five Finnish patients suffering from hereditary tyrosinemia type I. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 69-72 |year= 1994 |pmid= 8162054 |doi=  }}
*{{cite journal  | author=Grompe M, al-Dhalimy M |title=Mutations of the fumarylacetoacetate hydrolase gene in four patients with tyrosinemia, type I. |journal=Hum. Mutat. |volume=2 |issue= 2 |pages= 85-93 |year= 1993 |pmid= 8318997 |doi= 10.1002/humu.1380020205 }}
*{{cite journal  | author=Labelle Y, Phaneuf D, Leclerc B, Tanguay RM |title=Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity. |journal=Hum. Mol. Genet. |volume=2 |issue= 7 |pages= 941-6 |year= 1993 |pmid= 8364576 |doi=  }}
*{{cite journal  | author=Labelle Y, Puymirat J, Tanguay RM |title=Localization of cells in the rat brain expressing fumarylacetoacetate hydrolase, the deficient enzyme in hereditary tyrosinemia type 1. |journal=Biochim. Biophys. Acta |volume=1180 |issue= 3 |pages= 250-6 |year= 1993 |pmid= 8422430 |doi=  }}
*{{cite journal  | author=Ploos van Amstel JK, Bergman AJ, van Beurden EA, ''et al.'' |title=Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship. |journal=Hum. Genet. |volume=97 |issue= 1 |pages= 51-9 |year= 1996 |pmid= 8557261 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] FCGRT

• INFO: Beginning work on FCGRT... {November 19, 2007 12:54:17 AM PST}
• SEARCH REDIRECT: Control Box Found: FCGRT {November 19, 2007 12:54:42 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:54:44 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:54:44 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:54:44 AM PST}
• UPDATED: Updated protein page: FCGRT {November 19, 2007 12:54:49 AM PST}

[edit] FLNC

• INFO: Beginning work on FLNC... {November 19, 2007 12:54:49 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:33:46 AM 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_FLNC_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1v05.
 | PDB = {{PDB2|1v05}}, {{PDB2|2brq}}, {{PDB2|2d7m}}, {{PDB2|2d7n}}, {{PDB2|2d7o}}, {{PDB2|2d7p}}, {{PDB2|2d7q}}
 | Name = Filamin C, gamma (actin binding protein 280)
 | HGNCid = 3756
 | Symbol = FLNC
 | AltSymbols =; ABP-280; ABP280A; ABPA; ABPL; FLJ10186; FLN2
 | OMIM = 102565
 | ECnumber =  
 | Homologene = 37481
 | MGIid = 95557
 | GeneAtlas_image1 = PBB_GE_FLNC_207876_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} 
 | Process = 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2318
    | Hs_Ensembl = ENSG00000128591
    | Hs_RefseqProtein = NP_001449
    | Hs_RefseqmRNA = NM_001458
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 128257719
    | Hs_GenLoc_end = 128286568
    | Hs_Uniprot = Q14315
    | Mm_EntrezGene = 68794
    | Mm_Ensembl = ENSMUSG00000068699
    | Mm_RefseqmRNA = XM_284175
    | Mm_RefseqProtein = XP_284175
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 29383469
    | Mm_GenLoc_end = 29411891
    | Mm_Uniprot = Q8VHX6
  }}
}}
'''Filamin C, gamma (actin binding protein 280)''', also known as '''FLNC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FLNC filamin C, gamma (actin binding protein 280)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2318| 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 three related filamin genes, specifically gamma filamin. These filamin proteins crosslink actin filaments into orthogonal networks in cortical cytoplasm and participate in the anchoring of membrane proteins for the actin cytoskeleton. Three functional domains exist in filamin: an N-terminal filamentous actin-binding domain, a C-terminal self-association domain, and a membrane glycoprotein-binding domain.<ref name="entrez">{{cite web | title = Entrez Gene: FLNC filamin C, gamma (actin binding protein 280)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2318| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Stossel TP, Condeelis J, Cooley L, ''et al.'' |title=Filamins as integrators of cell mechanics and signalling. |journal=Nat. Rev. Mol. Cell Biol. |volume=2 |issue= 2 |pages= 138-45 |year= 2001 |pmid= 11252955 |doi= 10.1038/35052082 }}
*{{cite journal  | author=Maestrini E, Patrosso C, Mancini M, ''et al.'' |title=Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7. |journal=Hum. Mol. Genet. |volume=2 |issue= 6 |pages= 761-6 |year= 1993 |pmid= 7689010 |doi=  }}
*{{cite journal  | author=Gariboldi M, Maestrini E, Canzian F, ''et al.'' |title=Comparative mapping of the actin-binding protein 280 genes in human and mouse. |journal=Genomics |volume=21 |issue= 2 |pages= 428-30 |year= 1994 |pmid= 8088838 |doi=  }}
*{{cite journal  | author=Lanfranchi G, Muraro T, Caldara F, ''et al.'' |title=Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization. |journal=Genome Res. |volume=6 |issue= 1 |pages= 35-42 |year= 1996 |pmid= 8681137 |doi=  }}
*{{cite journal  | author=Marti A, Luo Z, Cunningham C, ''et al.'' |title=Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2620-8 |year= 1997 |pmid= 9006895 |doi=  }}
*{{cite journal  | author=Liu G, Thomas L, Warren RA, ''et al.'' |title=Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway. |journal=J. Cell Biol. |volume=139 |issue= 7 |pages= 1719-33 |year= 1998 |pmid= 9412467 |doi=  }}
*{{cite journal  | author=Xu W, Xie Z, Chung DW, Davie EW |title=A novel human actin-binding protein homologue that binds to platelet glycoprotein Ibalpha. |journal=Blood |volume=92 |issue= 4 |pages= 1268-76 |year= 1998 |pmid= 9694715 |doi=  }}
*{{cite journal  | author=Xie Z, Xu W, Davie EW, Chung DW |title=Molecular cloning of human ABPL, an actin-binding protein homologue. |journal=Biochem. Biophys. Res. Commun. |volume=251 |issue= 3 |pages= 914-9 |year= 1998 |pmid= 9791010 |doi=  }}
*{{cite journal  | author=Thompson TG, Chan YM, Hack AA, ''et al.'' |title=Filamin 2 (FLN2): A muscle-specific sarcoglycan interacting protein. |journal=J. Cell Biol. |volume=148 |issue= 1 |pages= 115-26 |year= 2000 |pmid= 10629222 |doi=  }}
*{{cite journal  | author=van der Ven PF, Obermann WM, Lemke B, ''et al.'' |title=Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation. |journal=Cell Motil. Cytoskeleton |volume=45 |issue= 2 |pages= 149-62 |year= 2000 |pmid= 10658210 |doi= 10.1002/(SICI)1097-0169(200002)45:2<149::AID-CM6>3.0.CO;2-G }}
*{{cite journal  | author=Faulkner G, Pallavicini A, Comelli A, ''et al.'' |title=FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41234-42 |year= 2001 |pmid= 10984498 |doi= 10.1074/jbc.M007493200 }}
*{{cite journal  | author=van der Ven PF, Wiesner S, Salmikangas P, ''et al.'' |title=Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin. |journal=J. Cell Biol. |volume=151 |issue= 2 |pages= 235-48 |year= 2000 |pmid= 11038172 |doi=  }}
*{{cite journal  | author=Petrecca K, Miller DM, Shrier A |title=Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin. |journal=J. Neurosci. |volume=20 |issue= 23 |pages= 8736-44 |year= 2001 |pmid= 11102480 |doi=  }}
*{{cite journal  | author=Chakarova C, Wehnert MS, Uhl K, ''et al.'' |title=Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family. |journal=Hum. Genet. |volume=107 |issue= 6 |pages= 597-611 |year= 2001 |pmid= 11153914 |doi=  }}
*{{cite journal  | author=Takada F, Vander Woude DL, Tong HQ, ''et al.'' |title=Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 4 |pages= 1595-600 |year= 2001 |pmid= 11171996 |doi= 10.1073/pnas.041609698 }}
*{{cite journal  | author=Dyson JM, O'Malley CJ, Becanovic J, ''et al.'' |title=The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. |journal=J. Cell Biol. |volume=155 |issue= 6 |pages= 1065-79 |year= 2002 |pmid= 11739414 |doi= 10.1083/jcb.200104005 }}
*{{cite journal  | author=Frey N, Olson EN |title=Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13998-4004 |year= 2002 |pmid= 11842093 |doi= 10.1074/jbc.M200712200 }}
*{{cite journal  | author=Donaldson JC, Dise RS, Ritchie MD, Hanks SK |title=Nephrocystin-conserved domains involved in targeting to epithelial cell-cell junctions, interaction with filamins, and establishing cell polarity. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 29028-35 |year= 2002 |pmid= 12006559 |doi= 10.1074/jbc.M111697200 }}
*{{cite journal  | author=Shoeman RL, Hartig R, Hauses C, Traub P |title=Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. |journal=Cell Biol. Int. |volume=26 |issue= 6 |pages= 529-39 |year= 2003 |pmid= 12119179 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GALNS

• INFO: Beginning work on GALNS... {November 19, 2007 10:33:46 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:35:02 AM 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 = Galactosamine (N-acetyl)-6-sulfate sulfatase (Morquio syndrome, mucopolysaccharidosis type IVA)
 | HGNCid = 4122
 | Symbol = GALNS
 | AltSymbols =; GAS; GALNAC6S; MPS4A
 | OMIM = 253000
 | ECnumber =  
 | Homologene = 55468
 | MGIid = 1355303
 | GeneAtlas_image1 = PBB_GE_GALNS_206335_at_tn.png
 | Function = {{GNF_GO|id=GO:0003943 |text = N-acetylgalactosamine-4-sulfatase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008484 |text = sulfuric ester hydrolase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} 
 | Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0030203 |text = glycosaminoglycan metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2588
    | Hs_Ensembl = ENSG00000141012
    | Hs_RefseqProtein = NP_000503
    | Hs_RefseqmRNA = NM_000512
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 87407644
    | Hs_GenLoc_end = 87450885
    | Hs_Uniprot = P34059
    | Mm_EntrezGene = 50917
    | Mm_Ensembl = ENSMUSG00000015027
    | Mm_RefseqmRNA = NM_016722
    | Mm_RefseqProtein = NP_057931
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 125464328
    | Mm_GenLoc_end = 125497494
    | Mm_Uniprot = Q571E4
  }}
}}
'''Galactosamine (N-acetyl)-6-sulfate sulfatase (Morquio syndrome, mucopolysaccharidosis type IVA)''', also known as '''GALNS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GALNS galactosamine (N-acetyl)-6-sulfate sulfatase (Morquio syndrome, mucopolysaccharidosis type IVA)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2588| 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 N-acetylgalactosamine-6-sulfatase which is a lysosomal exohydrolase required for the degradation of the glycosaminoglycans, keratan sulfate, and chondroitin 6-sulfate. Sequence alterations including point, missense and nonsense mutations, as well as those that affect splicing, result in a deficiency of this enzyme. Deficiencies of this enzyme lead to Morquio A syndrome, a lysosomal storage disorder.<ref name="entrez">{{cite web | title = Entrez Gene: GALNS galactosamine (N-acetyl)-6-sulfate sulfatase (Morquio syndrome, mucopolysaccharidosis type IVA)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2588| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Fukuda S, Tomatsu S, Masue M, ''et al.'' |title=Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases. |journal=J. Clin. Invest. |volume=90 |issue= 3 |pages= 1049-53 |year= 1992 |pmid= 1522213 |doi=  }}
*{{cite journal  | author=Tomatsu S, Fukuda S, Masue M, ''et al.'' |title=Morquio disease: isolation, characterization and expression of full-length cDNA for human N-acetylgalactosamine-6-sulfate sulfatase. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 2 |pages= 677-83 |year= 1992 |pmid= 1755850 |doi=  }}
*{{cite journal  | author=Masue M, Sukegawa K, Orii T, Hashimoto T |title=N-acetylgalactosamine-6-sulfate sulfatase in human placenta: purification and characteristics. |journal=J. Biochem. |volume=110 |issue= 6 |pages= 965-70 |year= 1992 |pmid= 1794986 |doi=  }}
*{{cite journal  | author=Bielicki J, Hopwood JJ |title=Human liver N-acetylgalactosamine 6-sulphatase. Purification and characterization. |journal=Biochem. J. |volume=279 ( Pt 2) |issue=  |pages= 515-20 |year= 1991 |pmid= 1953646 |doi=  }}
*{{cite journal  | author=Matalon R, Arbogast B, Justice P, ''et al.'' |title=Morquio's syndrome: deficiency of a chondroitin sulfate N-acetylhexosamine sulfate sulfatase. |journal=Biochem. Biophys. Res. Commun. |volume=61 |issue= 2 |pages= 759-65 |year= 1975 |pmid= 4218100 |doi=  }}
*{{cite journal  | author=Fujimoto A, Horwitz AL |title=Biochemical defect of non-keratan-sulfate-excreting Morquio syndrome. |journal=Am. J. Med. Genet. |volume=15 |issue= 2 |pages= 265-73 |year= 1983 |pmid= 6224421 |doi= 10.1002/ajmg.1320150210 }}
*{{cite journal  | author=Bielicki J, Fuller M, Guo XH, ''et al.'' |title=Expression, purification and characterization of recombinant human N-acetylgalactosamine-6-sulphatase. |journal=Biochem. J. |volume=311 ( Pt 1) |issue=  |pages= 333-9 |year= 1995 |pmid= 7575473 |doi=  }}
*{{cite journal  | author=Tomatsu S, Fukuda S, Cooper A, ''et al.'' |title=Two new mutations, Q473X and N487S, in a Caucasian patient with mucopolysaccharidosis IVA (Morquio disease). |journal=Hum. Mutat. |volume=6 |issue= 2 |pages= 195-6 |year= 1995 |pmid= 7581409 |doi= 10.1002/humu.1380060218 }}
*{{cite journal  | author=Tomatsu S, Fukuda S, Cooper A, ''et al.'' |title=Mucopolysaccharidosis type IVA: identification of six novel mutations among non-Japanese patients. |journal=Hum. Mol. Genet. |volume=4 |issue= 4 |pages= 741-3 |year= 1995 |pmid= 7633425 |doi=  }}
*{{cite journal  | author=Tomatsu S, Fukuda S, Cooper A, ''et al.'' |title=Mucopolysaccharidosis IVA: identification of a common missense mutation I113F in the N-Acetylgalactosamine-6-sulfate sulfatase gene. |journal=Am. J. Hum. Genet. |volume=57 |issue= 3 |pages= 556-63 |year= 1995 |pmid= 7668283 |doi=  }}
*{{cite journal  | author=Ogawa T, Tomatsu S, Fukuda S, ''et al.'' |title=Mucopolysaccharidosis IVA: screening and identification of mutations of the N-acetylgalactosamine-6-sulfate sulfatase gene. |journal=Hum. Mol. Genet. |volume=4 |issue= 3 |pages= 341-9 |year= 1995 |pmid= 7795586 |doi=  }}
*{{cite journal  | author=Morris CP, Guo XH, Apostolou S, ''et al.'' |title=Morquio A syndrome: cloning, sequence, and structure of the human N-acetylgalactosamine 6-sulfatase (GALNS) gene. |journal=Genomics |volume=22 |issue= 3 |pages= 652-4 |year= 1995 |pmid= 8001980 |doi= 10.1006/geno.1994.1443 }}
*{{cite journal  | author=Nakashima Y, Tomatsu S, Hori T, ''et al.'' |title=Mucopolysaccharidosis IV A: molecular cloning of the human N-acetylgalactosamine-6-sulfatase gene (GALNS) and analysis of the 5'-flanking region. |journal=Genomics |volume=20 |issue= 1 |pages= 99-104 |year= 1994 |pmid= 8020961 |doi= 10.1006/geno.1994.1132 }}
*{{cite journal  | author=Masuno M, Tomatsu S, Nakashima Y, ''et al.'' |title=Mucopolysaccharidosis IV A: assignment of the human N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene to chromosome 16q24. |journal=Genomics |volume=16 |issue= 3 |pages= 777-8 |year= 1993 |pmid= 8325655 |doi= 10.1006/geno.1993.1266 }}
*{{cite journal  | author=Baker E, Guo XH, Orsborn AM, ''et al.'' |title=The morquio A syndrome (mucopolysaccharidosis IVA) gene maps to 16q24.3. |journal=Am. J. Hum. Genet. |volume=52 |issue= 1 |pages= 96-8 |year= 1993 |pmid= 8434612 |doi=  }}
*{{cite journal  | author=Tomatsu S, Fukuda S, Yamagishi A, ''et al.'' |title=Mucopolysaccharidosis IVA: four new exonic mutations in patients with N-acetylgalactosamine-6-sulfate sulfatase deficiency. |journal=Am. J. Hum. Genet. |volume=58 |issue= 5 |pages= 950-62 |year= 1996 |pmid= 8651279 |doi=  }}
*{{cite journal  | author=Cole DE, Fukuda S, Gordon BA, ''et al.'' |title=Heteroallelic missense mutations of the galactosamine-6-sulfate sulfatase (GALNS) gene in a mild form of Morquio disease (MPS IVA). |journal=Am. J. Med. Genet. |volume=63 |issue= 4 |pages= 558-65 |year= 1997 |pmid= 8826435 |doi= 10.1002/(SICI)1096-8628(19960628)63:4<558::AID-AJMG9>3.0.CO;2-K }}
*{{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=Pshezhetsky AV, Potier M |title=Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate. |journal=J. Biol. Chem. |volume=271 |issue= 45 |pages= 28359-65 |year= 1996 |pmid= 8910459 |doi=  }}
*{{cite journal  | author=Bunge S, Kleijer WJ, Tylki-Szymanska A, ''et al.'' |title=Identification of 31 novel mutations in the N-acetylgalactosamine-6-sulfatase gene reveals excessive allelic heterogeneity among patients with Morquio A syndrome. |journal=Hum. Mutat. |volume=10 |issue= 3 |pages= 223-32 |year= 1997 |pmid= 9298823 |doi= 10.1002/(SICI)1098-1004(1997)10:3<223::AID-HUMU8>3.0.CO;2-J }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GAS6

• INFO: Beginning work on GAS6... {November 19, 2007 10:35:02 AM PST}
• SEARCH REDIRECT: Control Box Found: GAS6 {November 19, 2007 10:35:57 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:35:58 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:35:58 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:35:58 AM PST}
• UPDATED: Updated protein page: GAS6 {November 19, 2007 10:36:06 AM PST}

[edit] GP1BB

• INFO: Beginning work on GP1BB... {November 19, 2007 10:36:06 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:36:29 AM 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 = Glycoprotein Ib (platelet), beta polypeptide
 | HGNCid = 4440
 | Symbol = GP1BB
 | AltSymbols =; CD42c
 | OMIM = 138720
 | ECnumber =  
 | Homologene = 30972
 | MGIid = 107852
 | Function = {{GNF_GO|id=GO:0004888 |text = transmembrane 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:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2812
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_000398
    | Hs_RefseqmRNA = NM_000407
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 14724
    | Mm_Ensembl = ENSMUSG00000050761
    | Mm_RefseqmRNA = NM_001001999
    | Mm_RefseqProtein = NP_001001999
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 18534285
    | Mm_GenLoc_end = 18534929
    | Mm_Uniprot = P56400
  }}
}}
'''Glycoprotein Ib (platelet), beta polypeptide''', also known as '''GP1BB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GP1BB glycoprotein Ib (platelet), beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2812| 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 = Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. It is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor (VWF), and mediates platelet adhesion in the arterial circulation. GPIb alpha chain provides the VWF binding site, and GPIb beta contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain. Mutations in the GPIb beta subunit have been associated with Bernard-Soulier syndrome, velocardiofacial syndrome and giant platelet disorder. The 206 amino acid precursor of GPIb beta is synthesized from a 1.0 kb mRNA expressed in plateletes and megakaryocytes. A 411 amino acid protein arising from a longer, unspliced transcript in endothelial cells has been described; however, the authenticity of this product has been questioned. Yet another less abundant GPIb beta mRNA species of 3.5 kb, expressed in nonhematopoietic tissues such as endothelium, brain and heart, was shown to result from inefficient usage of a non-consensus polyA signal within a separate gene (septin 5) located upstream of this gene. In the absence of polyadenylation from its own imperfect site, the septin 5 gene uses the consensus polyA signal of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: GP1BB glycoprotein Ib (platelet), beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2812| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kunishima S, Kamiya T, Saito H |title=Genetic abnormalities of Bernard-Soulier syndrome. |journal=Int. J. Hematol. |volume=76 |issue= 4 |pages= 319-27 |year= 2003 |pmid= 12463594 |doi=  }}
*{{cite journal  | author=Clemetson KJ |title=A short history of platelet glycoprotein Ib complex. |journal=Thromb. Haemost. |volume=98 |issue= 1 |pages= 63-8 |year= 2007 |pmid= 17597992 |doi=  }}
*{{cite journal  | author=Wardell MR, Reynolds CC, Berndt MC, ''et al.'' |title=Platelet glycoprotein Ib beta is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=264 |issue= 26 |pages= 15656-61 |year= 1989 |pmid= 2504723 |doi=  }}
*{{cite journal  | author=Andrews RK, Booth WJ, Gorman JJ, ''et al.'' |title=Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex. |journal=Biochemistry |volume=28 |issue= 21 |pages= 8317-26 |year= 1990 |pmid= 2557900 |doi=  }}
*{{cite journal  | author=Berndt MC, Gregory C, Kabral A, ''et al.'' |title=Purification and preliminary characterization of the glycoprotein Ib complex in the human platelet membrane. |journal=Eur. J. Biochem. |volume=151 |issue= 3 |pages= 637-49 |year= 1985 |pmid= 3161731 |doi=  }}
*{{cite journal  | author=Lopez JA, Chung DW, Fujikawa K, ''et al.'' |title=The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 7 |pages= 2135-9 |year= 1988 |pmid= 3353370 |doi=  }}
*{{cite journal  | author=Canfield VA, Ozols J, Nugent D, Roth GJ |title=Isolation and characterization of the alpha and beta chains of human platelet glycoprotein Ib. |journal=Biochem. Biophys. Res. Commun. |volume=147 |issue= 2 |pages= 526-34 |year= 1987 |pmid= 3632685 |doi=  }}
*{{cite journal  | author=Hickey MJ, Hagen FS, Yagi M, Roth GJ |title=Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 18 |pages= 8327-31 |year= 1993 |pmid= 7690959 |doi=  }}
*{{cite journal  | author=Meyer SC, Fox JE |title=Interaction of platelet glycoprotein V with glycoprotein Ib-IX regulates expression of the glycoproteins and binding of von Willebrand factor to glycoprotein Ib-IX in transfected cells. |journal=J. Biol. Chem. |volume=270 |issue= 24 |pages= 14693-9 |year= 1995 |pmid= 7782333 |doi=  }}
*{{cite journal  | author=Yagi M, Edelhoff S, Disteche CM, Roth GJ |title=Structural characterization and chromosomal location of the gene encoding human platelet glycoprotein Ib beta. |journal=J. Biol. Chem. |volume=269 |issue= 26 |pages= 17424-7 |year= 1994 |pmid= 8021244 |doi=  }}
*{{cite journal  | author=Du X, Harris SJ, Tetaz TJ, ''et al.'' |title=Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex. |journal=J. Biol. Chem. |volume=269 |issue= 28 |pages= 18287-90 |year= 1994 |pmid= 8034572 |doi=  }}
*{{cite journal  | author=Kelly MD, Essex DW, Shapiro SS, ''et al.'' |title=Complementary DNA cloning of the alternatively expressed endothelial cell glycoprotein Ib beta (GPIb beta) and localization of the GPIb beta gene to chromosome 22. |journal=J. Clin. Invest. |volume=93 |issue= 6 |pages= 2417-24 |year= 1994 |pmid= 8200976 |doi=  }}
*{{cite journal  | author=Ludlow LB, Schick BP, Budarf ML, ''et al.'' |title=Identification of a mutation in a GATA binding site of the platelet glycoprotein Ibbeta promoter resulting in the Bernard-Soulier syndrome. |journal=J. Biol. Chem. |volume=271 |issue= 36 |pages= 22076-80 |year= 1996 |pmid= 8703016 |doi=  }}
*{{cite journal  | author=Zieger B, Hashimoto Y, Ware J |title=Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence. |journal=J. Clin. Invest. |volume=99 |issue= 3 |pages= 520-5 |year= 1997 |pmid= 9022087 |doi=  }}
*{{cite journal  | author=Kunishima S, Lopez JA, Kobayashi S, ''et al.'' |title=Missense mutations of the glycoprotein (GP) Ib beta gene impairing the GPIb alpha/beta disulfide linkage in a family with giant platelet disorder. |journal=Blood |volume=89 |issue= 7 |pages= 2404-12 |year= 1997 |pmid= 9116284 |doi=  }}
*{{cite journal  | author=Andrews RK, Harris SJ, McNally T, Berndt MC |title=Binding of purified 14-3-3 zeta signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. |journal=Biochemistry |volume=37 |issue= 2 |pages= 638-47 |year= 1998 |pmid= 9425086 |doi= 10.1021/bi970893g }}
*{{cite journal  | author=Longhurst CM, White MM, Wilkinson DA, Jennings LK |title=A CD9, alphaIIbbeta3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by alphaIIbbeta3 conformational states. |journal=Eur. J. Biochem. |volume=263 |issue= 1 |pages= 104-11 |year= 1999 |pmid= 10429193 |doi=  }}
*{{cite journal  | author=Feng S, Christodoulides N, Reséndiz JC, ''et al.'' |title=Cytoplasmic domains of GpIbalpha and GpIbbeta regulate 14-3-3zeta binding to GpIb/IX/V. |journal=Blood |volume=95 |issue= 2 |pages= 551-7 |year= 2000 |pmid= 10627461 |doi=  }}
*{{cite journal  | author=Moran N, Morateck PA, Deering A, ''et al.'' |title=Surface expression of glycoprotein ib alpha is dependent on glycoprotein ib beta: evidence from a novel mutation causing Bernard-Soulier syndrome. |journal=Blood |volume=96 |issue= 2 |pages= 532-9 |year= 2000 |pmid= 10887115 |doi=  }}
*{{cite journal  | author=Kasirer-Friede A, Ware J, Leng L, ''et al.'' |title=Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11949-56 |year= 2002 |pmid= 11812775 |doi= 10.1074/jbc.M108727200 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GPR30

• INFO: Beginning work on GPR30... {November 19, 2007 10:36:29 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:37:16 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| 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 = G protein-coupled receptor 30
 | HGNCid = 4485
 | Symbol = GPR30
 | AltSymbols =; CMKRL2; DRY12; FEG-1; GPCR-Br; LERGU; LERGU2; LyGPR; MGC99678
 | OMIM = 601805
 | ECnumber =  
 | Homologene = 15855
 | MGIid = 1924104
 | GeneAtlas_image1 = PBB_GE_GPR30_210640_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_GPR30_211829_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0045028 |text = purinergic nucleotide receptor activity, G-protein coupled}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2852
    | Hs_Ensembl = ENSG00000164850
    | Hs_RefseqProtein = NP_001035055
    | Hs_RefseqmRNA = NM_001039966
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 1093038
    | Hs_GenLoc_end = 1099977
    | Hs_Uniprot = Q99527
    | Mm_EntrezGene = 76854
    | Mm_Ensembl = ENSMUSG00000053647
    | Mm_RefseqmRNA = NM_029771
    | Mm_RefseqProtein = NP_084047
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 139676821
    | Mm_GenLoc_end = 139681430
    | Mm_Uniprot = Q8BMP4
  }}
}}
'''G protein-coupled receptor 30''', also known as '''GPR30''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GPR30 G protein-coupled receptor 30| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2852| 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 is a member of the G-protein coupled receptor 1 family and encodes a multi-pass membrane protein that localizes to the endoplasmic reticulum. The protein binds estrogen, resulting in intracellular calcium mobilization and synthesis of phosphatidylinositol 3,4,5-trisphosphate in the nucleus. This protein therefore plays a role in the rapid nongenomic signaling events widely observed following stimulation of cells and tissues with estrogen. Alternate transcriptional splice variants which encode the same protein have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: GPR30 G protein-coupled receptor 30| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2852| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Filardo EJ |title=Epidermal growth factor receptor (EGFR) transactivation by estrogen via the G-protein-coupled receptor, GPR30: a novel signaling pathway with potential significance for breast cancer. |journal=J. Steroid Biochem. Mol. Biol. |volume=80 |issue= 2 |pages= 231-8 |year= 2002 |pmid= 11897506 |doi=  }}
*{{cite journal  | author=Filardo EJ, Thomas P |title=GPR30: a seven-transmembrane-spanning estrogen receptor that triggers EGF release. |journal=Trends Endocrinol. Metab. |volume=16 |issue= 8 |pages= 362-7 |year= 2005 |pmid= 16125968 |doi= 10.1016/j.tem.2005.08.005 }}
*{{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=Owman C, Blay P, Nilsson C, Lolait SJ |title=Cloning of human cDNA encoding a novel heptahelix receptor expressed in Burkitt's lymphoma and widely distributed in brain and peripheral tissues. |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 2 |pages= 285-92 |year= 1996 |pmid= 8920907 |doi= 10.1006/bbrc.1996.1654 }}
*{{cite journal  | author=Feng Y, Gregor P |title=Cloning of a novel member of the G protein-coupled receptor family related to peptide receptors. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 3 |pages= 651-4 |year= 1997 |pmid= 9070864 |doi= 10.1006/bbrc.1997.6161 }}
*{{cite journal  | author=Kvingedal AM, Smeland EB |title=A novel putative G-protein-coupled receptor expressed in lung, heart and lymphoid tissue. |journal=FEBS Lett. |volume=407 |issue= 1 |pages= 59-62 |year= 1997 |pmid= 9141481 |doi=  }}
*{{cite journal  | author=Carmeci C, Thompson DA, Ring HZ, ''et al.'' |title=Identification of a gene (GPR30) with homology to the G-protein-coupled receptor superfamily associated with estrogen receptor expression in breast cancer. |journal=Genomics |volume=45 |issue= 3 |pages= 607-17 |year= 1998 |pmid= 9367686 |doi= 10.1006/geno.1997.4972 }}
*{{cite journal  | author=Takada Y, Kato C, Kondo S, ''et al.'' |title=Cloning of cDNAs encoding G protein-coupled receptor expressed in human endothelial cells exposed to fluid shear stress. |journal=Biochem. Biophys. Res. Commun. |volume=240 |issue= 3 |pages= 737-41 |year= 1998 |pmid= 9398636 |doi= 10.1006/bbrc.1997.7734 }}
*{{cite journal  | author=O'Dowd BF, Nguyen T, Marchese A, ''et al.'' |title=Discovery of three novel G-protein-coupled receptor genes. |journal=Genomics |volume=47 |issue= 2 |pages= 310-3 |year= 1998 |pmid= 9479505 |doi= 10.1006/geno.1998.5095 }}
*{{cite journal  | author=Filardo EJ, Quinn JA, Bland KI, Frackelton AR |title=Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF. |journal=Mol. Endocrinol. |volume=14 |issue= 10 |pages= 1649-60 |year= 2001 |pmid= 11043579 |doi=  }}
*{{cite journal  | author=Filardo EJ, Quinn JA, Frackelton AR, Bland KI |title=Estrogen action via the G protein-coupled receptor, GPR30: stimulation of adenylyl cyclase and cAMP-mediated attenuation of the epidermal growth factor receptor-to-MAPK signaling axis. |journal=Mol. Endocrinol. |volume=16 |issue= 1 |pages= 70-84 |year= 2002 |pmid= 11773440 |doi=  }}
*{{cite journal  | author=Ahola TM, Purmonen S, Pennanen P, ''et al.'' |title=Progestin upregulates G-protein-coupled receptor 30 in breast cancer cells. |journal=Eur. J. Biochem. |volume=269 |issue= 10 |pages= 2485-90 |year= 2002 |pmid= 12027886 |doi=  }}
*{{cite journal  | author=Ahola TM, Manninen T, Alkio N, Ylikomi T |title=G protein-coupled receptor 30 is critical for a progestin-induced growth inhibition in MCF-7 breast cancer cells. |journal=Endocrinology |volume=143 |issue= 9 |pages= 3376-84 |year= 2002 |pmid= 12193550 |doi=  }}
*{{cite journal  | author=Ahola TM, Alkio N, Manninen T, Ylikomi T |title=Progestin and G protein-coupled receptor 30 inhibit mitogen-activated protein kinase activity in MCF-7 breast cancer cells. |journal=Endocrinology |volume=143 |issue= 12 |pages= 4620-6 |year= 2002 |pmid= 12446589 |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=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
*{{cite journal  | author=Hamza A, Sarma MH, Sarma RH |title=Plausible interaction of an alpha-fetoprotein cyclopeptide with the G-protein-coupled receptor model GPR30: docking study by molecular dynamics simulated annealing. |journal=J. Biomol. Struct. Dyn. |volume=20 |issue= 6 |pages= 751-8 |year= 2004 |pmid= 12744705 |doi=  }}
*{{cite journal  | author=Kanda N, Watanabe S |title=17Beta-estradiol enhances the production of nerve growth factor in THP-1-derived macrophages or peripheral blood monocyte-derived macrophages. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 771-80 |year= 2003 |pmid= 14632195 |doi= 10.1046/j.1523-1747.2003.12487.x }}
*{{cite journal  | author=Kanda N, Watanabe S |title=17beta-estradiol inhibits oxidative stress-induced apoptosis in keratinocytes by promoting Bcl-2 expression. |journal=J. Invest. Dermatol. |volume=121 |issue= 6 |pages= 1500-9 |year= 2004 |pmid= 14675202 |doi= 10.1111/j.1523-1747.2003.12617.x }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GTF2A1

• INFO: Beginning work on GTF2A1... {November 19, 2007 10:37:16 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:37:55 AM 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_GTF2A1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nvp.
 | PDB = {{PDB2|1nvp}}
 | Name = General transcription factor IIA, 1, 19/37kDa
 | HGNCid = 4646
 | Symbol = GTF2A1
 | AltSymbols =; MGC129969; MGC129970; TF2A1; TFIIA
 | OMIM = 600520
 | ECnumber =  
 | Homologene = 56331
 | MGIid = 1933277
 | GeneAtlas_image1 = PBB_GE_GTF2A1_206521_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016986 |text = transcription initiation factor activity}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005672 |text = transcription factor TFIIA complex}} 
 | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2957
    | Hs_Ensembl = ENSG00000165417
    | Hs_RefseqProtein = NP_056943
    | Hs_RefseqmRNA = NM_015859
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 80716147
    | Hs_GenLoc_end = 80757328
    | Hs_Uniprot = P52655
    | Mm_EntrezGene = 83602
    | Mm_Ensembl = ENSMUSG00000020962
    | Mm_RefseqmRNA = NM_031391
    | Mm_RefseqProtein = NP_113568
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 91964245
    | Mm_GenLoc_end = 91995136
    | Mm_Uniprot = Q0VGZ0
  }}
}}
'''General transcription factor IIA, 1, 19/37kDa''', also known as '''GTF2A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2A1 general transcription factor IIA, 1, 19/37kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2957| 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=Ha I, Lane WS, Reinberg D |title=Cloning of a human gene encoding the general transcription initiation factor IIB. |journal=Nature |volume=352 |issue= 6337 |pages= 689-95 |year= 1991 |pmid= 1876184 |doi= 10.1038/352689a0 }}
*{{cite journal  | author=DeJong J, Bernstein R, Roeder RG |title=Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3313-7 |year= 1995 |pmid= 7724559 |doi=  }}
*{{cite journal  | author=Ozer J, Moore PA, Bolden AH, ''et al.'' |title=Molecular cloning of the small (gamma) subunit of human TFIIA reveals functions critical for activated transcription. |journal=Genes Dev. |volume=8 |issue= 19 |pages= 2324-35 |year= 1994 |pmid= 7958899 |doi=  }}
*{{cite journal  | author=Sun X, Ma D, Sheldon M, ''et al.'' |title=Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription. |journal=Genes Dev. |volume=8 |issue= 19 |pages= 2336-48 |year= 1994 |pmid= 7958900 |doi=  }}
*{{cite journal  | author=Ge H, Roeder RG |title=The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. |journal=J. Biol. Chem. |volume=269 |issue= 25 |pages= 17136-40 |year= 1994 |pmid= 8006019 |doi=  }}
*{{cite journal  | author=DeJong J, Roeder RG |title=A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of human TFIIA. |journal=Genes Dev. |volume=7 |issue= 11 |pages= 2220-34 |year= 1993 |pmid= 8224848 |doi=  }}
*{{cite journal  | author=Ma D, Watanabe H, Mermelstein F, ''et al.'' |title=Isolation of a cDNA encoding the largest subunit of TFIIA reveals functions important for activated transcription. |journal=Genes Dev. |volume=7 |issue= 11 |pages= 2246-57 |year= 1993 |pmid= 8224850 |doi=  }}
*{{cite journal  | author=Tang H, Sun X, Reinberg D, Ebright RH |title=Protein-protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 3 |pages= 1119-24 |year= 1996 |pmid= 8577725 |doi=  }}
*{{cite journal  | author=Kashanchi F, Khleif SN, Duvall JF, ''et al.'' |title=Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5503-10 |year= 1996 |pmid= 8764062 |doi=  }}
*{{cite journal  | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |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=Ozer J, Mitsouras K, Zerby D, ''et al.'' |title=Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding. |journal=J. Biol. Chem. |volume=273 |issue= 23 |pages= 14293-300 |year= 1998 |pmid= 9603936 |doi=  }}
*{{cite journal  | author=Yokomori K, Verrijzer CP, Tjian R |title=An interplay between TATA box-binding protein and transcription factors IIE and IIA modulates DNA binding and transcription. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 12 |pages= 6722-7 |year= 1998 |pmid= 9618479 |doi=  }}
*{{cite journal  | author=Na SY, Choi HS, Kim JW, ''et al.'' |title=Bcl3, an IkappaB protein, as a novel transcription coactivator of the retinoid X receptor. |journal=J. Biol. Chem. |volume=273 |issue= 47 |pages= 30933-8 |year= 1998 |pmid= 9812988 |doi=  }}
*{{cite journal  | author=Upadhyaya AB, Lee SH, DeJong J |title=Identification of a general transcription factor TFIIAalpha/beta homolog selectively expressed in testis. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 18040-8 |year= 1999 |pmid= 10364255 |doi=  }}
*{{cite journal  | author=Kim HJ, Yi JY, Sung HS, ''et al.'' |title=Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation. |journal=Mol. Cell. Biol. |volume=19 |issue= 9 |pages= 6323-32 |year= 1999 |pmid= 10454579 |doi=  }}
*{{cite journal  | author=Lee SK, Anzick SL, Choi JE, ''et al.'' |title=A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34283-93 |year= 1999 |pmid= 10567404 |doi=  }}
*{{cite journal  | author=Teichmann M, Wang Z, Martinez E, ''et al.'' |title=Human TATA-binding protein-related factor-2 (hTRF2) stably associates with hTFIIA in HeLa cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 24 |pages= 13720-5 |year= 2000 |pmid= 10570139 |doi=  }}
*{{cite journal  | author=Solow S, Salunek M, Ryan R, Lieberman PM |title=Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 15886-92 |year= 2001 |pmid= 11278496 |doi= 10.1074/jbc.M009385200 }}
*{{cite journal  | author=Xing J, Sheppard HM, Corneillie SI, Liu X |title=p53 Stimulates TFIID-TFIIA-promoter complex assembly, and p53-T antigen complex inhibits TATA binding protein-TATA interaction. |journal=Mol. Cell. Biol. |volume=21 |issue= 11 |pages= 3652-61 |year= 2001 |pmid= 11340159 |doi= 10.1128/MCB.21.11.3652-3661.2001 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] HK1

• INFO: Beginning work on HK1... {November 19, 2007 10:37:55 AM PST}
• SEARCH REDIRECT: Control Box Found: HK1 {November 19, 2007 10:38:32 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:38:33 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:38:33 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:38:33 AM PST}
• UPDATED: Updated protein page: HK1 {November 19, 2007 10:38:39 AM PST}

[edit] HRG

• INFO: Beginning work on HRG... {November 19, 2007 10:38:39 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:39:09 AM 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 = Histidine-rich glycoprotein
 | HGNCid = 5181
 | Symbol = HRG
 | AltSymbols =; DKFZp779H1622; HPRG; HRGP
 | OMIM = 142640
 | ECnumber =  
 | Homologene = 30973
 | MGIid = 2146636
 | GeneAtlas_image1 = PBB_GE_HRG_31835_at_tn.png
 | GeneAtlas_image2 = PBB_GE_HRG_206226_at_tn.png
 | Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} 
 | Process = 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3273
    | Hs_Ensembl = ENSG00000113905
    | Hs_RefseqProtein = NP_000403
    | Hs_RefseqmRNA = NM_000412
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 187866487
    | Hs_GenLoc_end = 187878718
    | Hs_Uniprot = P04196
    | Mm_EntrezGene = 94175
    | Mm_Ensembl = ENSMUSG00000022877
    | Mm_RefseqmRNA = NM_053176
    | Mm_RefseqProtein = NP_444406
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 22866448
    | Mm_GenLoc_end = 22876990
    | Mm_Uniprot =  
  }}
}}
'''Histidine-rich glycoprotein''', also known as '''HRG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HRG histidine-rich glycoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3273| 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 histidine-rich glycoprotein contains two cystatin-like domains and is located in plasma and platelets. The physiological function has not been determined but it is known that the protein binds heme, dyes and divalent metal ions. It can inhibit rosette formation and interacts with heparin, thrombospondin and plasminogen. Two of the protein's effects, the inhibition of fibrinolysis and the reduction of inhibition of coagulation, indicate a potential prothrombotic effect. Mutations in this gene lead to thrombophilia due to abnormal histidine-rich glycoprotein levels.<ref name="entrez">{{cite web | title = Entrez Gene: HRG histidine-rich glycoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3273| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Hughes GJ, Frutiger S, Paquet N, ''et al.'' |title=Plasma protein map: an update by microsequencing. |journal=Electrophoresis |volume=13 |issue= 9-10 |pages= 707-14 |year= 1993 |pmid= 1459097 |doi=  }}
*{{cite journal  | author=Hutchens TW, Yip TT, Morgan WT |title=Identification of histidine-rich glycoprotein in human colostrum and milk. |journal=Pediatr. Res. |volume=31 |issue= 3 |pages= 239-46 |year= 1992 |pmid= 1561009 |doi=  }}
*{{cite journal  | author=Hennis BC, Kluft C |title=KpnI RFLP in the human histidine-rich glycoprotein gene. |journal=Nucleic Acids Res. |volume=19 |issue= 15 |pages= 4311 |year= 1991 |pmid= 1678514 |doi=  }}
*{{cite journal  | author=van den Berg EA, le Clercq E, Kluft C, ''et al.'' |title=Assignment of the human gene for histidine-rich glycoprotein to chromosome 3. |journal=Genomics |volume=7 |issue= 2 |pages= 276-9 |year= 1990 |pmid= 2347592 |doi=  }}
*{{cite journal  | author=Shatsky M, Saigo K, Burdach S, ''et al.'' |title=Histidine-rich glycoprotein blocks T cell rosette formation and modulates both T cell activation and immunoregulation. |journal=J. Biol. Chem. |volume=264 |issue= 14 |pages= 8254-9 |year= 1989 |pmid= 2524479 |doi=  }}
*{{cite journal  | author=Saigo K, Shatsky M, Levitt LJ, Leung LK |title=Interaction of histidine-rich glycoprotein with human T lymphocytes. |journal=J. Biol. Chem. |volume=264 |issue= 14 |pages= 8249-53 |year= 1989 |pmid= 2566603 |doi=  }}
*{{cite journal  | author=Koide T, Foster D, Yoshitake S, Davie EW |title=Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide sequence of its cDNA. |journal=Biochemistry |volume=25 |issue= 8 |pages= 2220-5 |year= 1986 |pmid= 3011081 |doi=  }}
*{{cite journal  | author=Hajjar DP, Boyd DB, Harpel PC, Nachman RL |title=Histidine-rich glycoprotein inhibits the antiproliferative effect of heparin on smooth muscle cells. |journal=J. Exp. Med. |volume=165 |issue= 3 |pages= 908-13 |year= 1987 |pmid= 3819648 |doi=  }}
*{{cite journal  | author=Leung LL |title=Interaction of histidine-rich glycoprotein with fibrinogen and fibrin. |journal=J. Clin. Invest. |volume=77 |issue= 4 |pages= 1305-11 |year= 1986 |pmid= 3958188 |doi=  }}
*{{cite journal  | author=Heimburger N, Haupt H, Kranz T, Baudner S |title=[Human serum proteins with high affinity to carboxymethylcellulose. II. Physico-chemical and immunological characterization of a histidine-rich 3,8S-  2 -glycoportein (CM-protein I)] |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=353 |issue= 7 |pages= 1133-40 |year= 1972 |pmid= 4116337 |doi=  }}
*{{cite journal  | author=Silverstein RL, Leung LL, Harpel PC, Nachman RL |title=Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator. |journal=J. Clin. Invest. |volume=74 |issue= 5 |pages= 1625-33 |year= 1984 |pmid= 6438154 |doi=  }}
*{{cite journal  | author=Hennis BC, Frants RR, Bakker E, ''et al.'' |title=Evidence for the absence of intron H of the histidine-rich glycoprotein (HRG) gene: genetic mapping and in situ localization of HRG to chromosome 3q28-q29. |journal=Genomics |volume=19 |issue= 1 |pages= 195-7 |year= 1994 |pmid= 8188234 |doi= 10.1006/geno.1994.1046 }}
*{{cite journal  | author=Sørensen CB, Krogh-Pedersen H, Petersen TE |title=Determination of the disulphide bridge arrangement of bovine histidine-rich glycoprotein. |journal=FEBS Lett. |volume=328 |issue= 3 |pages= 285-90 |year= 1993 |pmid= 8348977 |doi=  }}
*{{cite journal  | author=Leung L |title=Histidine-rich glycoprotein: an abundant plasma protein in search of a function. |journal=J. Lab. Clin. Med. |volume=121 |issue= 5 |pages= 630-1 |year= 1993 |pmid= 8478589 |doi=  }}
*{{cite journal  | author=Angles-Cano E, Gris JC, Loyau S, Schved JF |title=Familial association of high levels of histidine-rich glycoprotein and plasminogen activator inhibitor-1 with venous thromboembolism. |journal=J. Lab. Clin. Med. |volume=121 |issue= 5 |pages= 646-53 |year= 1993 |pmid= 8478593 |doi=  }}
*{{cite journal  | author=Gorgani NN, Parish CR, Easterbrook Smith SB, Altin JG |title=Histidine-rich glycoprotein binds to human IgG and C1q and inhibits the formation of insoluble immune complexes. |journal=Biochemistry |volume=36 |issue= 22 |pages= 6653-62 |year= 1997 |pmid= 9184145 |doi= 10.1021/bi962573n }}
*{{cite journal  | author=Schinke T, Koide T, Jahnen-Dechent W |title=Human histidine-rich glycoprotein expressed in SF9 insect cells inhibits apatite formation. |journal=FEBS Lett. |volume=412 |issue= 3 |pages= 559-62 |year= 1997 |pmid= 9276466 |doi=  }}
*{{cite journal  | author=Shigekiyo T, Yoshida H, Matsumoto K, ''et al.'' |title=HRG Tokushima: molecular and cellular characterization of histidine-rich glycoprotein (HRG) deficiency. |journal=Blood |volume=91 |issue= 1 |pages= 128-33 |year= 1998 |pmid= 9414276 |doi=  }}
*{{cite journal  | author=Wakabayashi S, Takahashi K, Koide T |title=Structural characterization of the gene for human histidine-rich glycoprotein, reinvestigation of the 5'-terminal region of cDNA and a search for the liver specific promoter in the gene. |journal=J. Biochem. |volume=125 |issue= 3 |pages= 522-30 |year= 1999 |pmid= 10050040 |doi=  }}
*{{cite journal  | author=Gorgani NN, Altin JG, Parish CR |title=Histidine-rich glycoprotein regulates the binding of monomeric IgG and immune complexes to monocytes. |journal=Int. Immunol. |volume=11 |issue= 8 |pages= 1275-82 |year= 1999 |pmid= 10421785 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] HSD3B1

• INFO: Beginning work on HSD3B1... {November 19, 2007 10:39:09 AM PST}
• SEARCH REDIRECT: Control Box Found: HSD3B1 {November 19, 2007 10:39:33 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:39:36 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:39:36 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:39:36 AM PST}
• UPDATED: Updated protein page: HSD3B1 {November 19, 2007 10:39:44 AM PST}

[edit] HSPE1

• INFO: Beginning work on HSPE1... {November 19, 2007 10:39:44 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:40:18 AM 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 = Heat shock 10kDa protein 1 (chaperonin 10)
 | HGNCid = 5269
 | Symbol = HSPE1
 | AltSymbols =; CPN10; GROES; HSP10
 | OMIM = 600141
 | ECnumber =  
 | Homologene = 20500
 | MGIid = 104680
 | GeneAtlas_image1 = PBB_GE_HSPE1_205133_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}} {{GNF_GO|id=GO:0051087 |text = chaperone binding}} 
 | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} 
 | Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3336
    | Hs_Ensembl = ENSG00000115541
    | Hs_RefseqProtein = NP_002148
    | Hs_RefseqmRNA = NM_002157
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 198073292
    | Hs_GenLoc_end = 198076349
    | Hs_Uniprot = P61604
    | Mm_EntrezGene = 15528
    | Mm_Ensembl = ENSMUSG00000073676
    | Mm_RefseqmRNA = NM_008303
    | Mm_RefseqProtein = NP_032329
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 55033596
    | Mm_GenLoc_end = 55035665
    | Mm_Uniprot = Q4KL76
  }}
}}
'''Heat shock 10kDa protein 1 (chaperonin 10)''', also known as '''HSPE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPE1 heat shock 10kDa protein 1 (chaperonin 10)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3336| 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=Czarnecka AM, Campanella C, Zummo G, Cappello F |title=Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis? |journal=Cell Stress Chaperones |volume=11 |issue= 4 |pages= 287-94 |year= 2007 |pmid= 17278877 |doi=  }}
*{{cite journal  | author=Legname G, Fossati G, Gromo G, ''et al.'' |title=Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10. |journal=FEBS Lett. |volume=361 |issue= 2-3 |pages= 211-4 |year= 1995 |pmid= 7698325 |doi=  }}
*{{cite journal  | author=Cavanagh AC, Morton H |title=The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10. |journal=Eur. J. Biochem. |volume=222 |issue= 2 |pages= 551-60 |year= 1994 |pmid= 7912672 |doi=  }}
*{{cite journal  | author=Monzini N, Legname G, Marcucci F, ''et al.'' |title=Identification and cloning of human chaperonin 10 homologue. |journal=Biochim. Biophys. Acta |volume=1218 |issue= 3 |pages= 478-80 |year= 1994 |pmid= 7914093 |doi=  }}
*{{cite journal  | author=Chen JJ, McNealy DJ, Dalal S, Androphy EJ |title=Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 1 |pages= 189-90 |year= 1994 |pmid= 7916212 |doi=  }}
*{{cite journal  | author=Samali A, Cai J, Zhivotovsky B, ''et al.'' |title=Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. |journal=EMBO J. |volume=18 |issue= 8 |pages= 2040-8 |year= 1999 |pmid= 10205158 |doi= 10.1093/emboj/18.8.2040 }}
*{{cite journal  | author=Summers KM, Fletcher BH, Macaranas DD, ''et al.'' |title=Mapping and characterization of the eukaryotic early pregnancy factor/chaperonin 10 gene family. |journal=Somat. Cell Mol. Genet. |volume=24 |issue= 6 |pages= 315-26 |year= 2000 |pmid= 10763410 |doi=  }}
*{{cite journal  | author=Richardson A, Schwager F, Landry SJ, Georgopoulos C |title=The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4981-7 |year= 2001 |pmid= 11050098 |doi= 10.1074/jbc.M008628200 }}
*{{cite journal  | author=Fletcher BH, Cassady AI, Summers KM, Cavanagh AC |title=The murine chaperonin 10 gene family contains an intronless, putative gene for early pregnancy factor, Cpn10-rs1. |journal=Mamm. Genome |volume=12 |issue= 2 |pages= 133-40 |year= 2001 |pmid= 11210183 |doi=  }}
*{{cite journal  | author=Parissi V, Calmels C, De Soultrait VR, ''et al.'' |title=Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60. |journal=J. Virol. |volume=75 |issue= 23 |pages= 11344-53 |year= 2001 |pmid= 11689615 |doi= 10.1128/JVI.75.23.11344-11353.2001 }}
*{{cite journal  | author=Hansen JJ, Dürr A, Cournu-Rebeix I, ''et al.'' |title=Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. |journal=Am. J. Hum. Genet. |volume=70 |issue= 5 |pages= 1328-32 |year= 2002 |pmid= 11898127 |doi=  }}
*{{cite journal  | author=Guidry JJ, Wittung-Stafshede P |title=Low stability for monomeric human chaperonin protein 10: interprotein interactions contribute majority of oligomer stability. |journal=Arch. Biochem. Biophys. |volume=405 |issue= 2 |pages= 280-2 |year= 2002 |pmid= 12220543 |doi=  }}
*{{cite journal  | author=Lee KH, Kim HS, Jeong HS, Lee YS |title=Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 2 |pages= 216-24 |year= 2002 |pmid= 12387818 |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=Hansen JJ, Bross P, Westergaard M, ''et al.'' |title=Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. |journal=Hum. Genet. |volume=112 |issue= 1 |pages= 71-7 |year= 2003 |pmid= 12483302 |doi= 10.1007/s00439-002-0837-9 }}
*{{cite journal  | author=Mansell JP, Yarram SJ, Brown NL, Sandy JR |title=Type I collagen synthesis by human osteoblasts in response to placental lactogen and chaperonin 10, a homolog of early-pregnancy factor. |journal=In Vitro Cell. Dev. Biol. Anim. |volume=38 |issue= 9 |pages= 518-22 |year= 2004 |pmid= 12703979 |doi=  }}
*{{cite journal  | author=Cappello F, Bellafiore M, David S, ''et al.'' |title=Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix. |journal=Cancer Lett. |volume=196 |issue= 1 |pages= 35-41 |year= 2003 |pmid= 12860287 |doi=  }}
*{{cite journal  | author=Shan YX, Liu TJ, Su HF, ''et al.'' |title=Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells. |journal=J. Mol. Cell. Cardiol. |volume=35 |issue= 9 |pages= 1135-43 |year= 2004 |pmid= 12967636 |doi=  }}
*{{cite journal  | author=Shan YX, Yang TL, Mestril R, Wang PH |title=Hsp10 and Hsp60 suppress ubiquitination of insulin-like growth factor-1 receptor and augment insulin-like growth factor-1 receptor signaling in cardiac muscle: implications on decreased myocardial protection in diabetic cardiomyopathy. |journal=J. Biol. Chem. |volume=278 |issue= 46 |pages= 45492-8 |year= 2003 |pmid= 12970367 |doi= 10.1074/jbc.M304498200 }}
*{{cite journal  | author=Guidry JJ, Shewmaker F, Maskos K, ''et al.'' |title=Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified. |journal=BMC Biochem. |volume=4 |issue=  |pages= 14 |year= 2004 |pmid= 14525625 |doi= 10.1186/1471-2091-4-14 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] MS4A2

• INFO: Beginning work on MS4A2... {November 19, 2007 12:53:34 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:54:17 AM 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 = Membrane-spanning 4-domains, subfamily A, member 2 (Fc fragment of IgE, high affinity I, receptor for; beta polypeptide)
 | HGNCid = 7316
 | Symbol = MS4A2
 | AltSymbols =; MS4A1; APY; ATOPY; FCER1B; FCERI; IGEL; IGER; IGHER
 | OMIM = 147138
 | ECnumber =  
 | Homologene = 112
 | MGIid = 95495
 | GeneAtlas_image1 = PBB_GE_MS4A2_207497_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_MS4A2_207496_at_tn.png
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005262 |text = calcium channel activity}} {{GNF_GO|id=GO:0019863 |text = IgE binding}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2206
    | Hs_Ensembl = ENSG00000149534
    | Hs_RefseqProtein = NP_000130
    | Hs_RefseqmRNA = NM_000139
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 59612713
    | Hs_GenLoc_end = 59622593
    | Hs_Uniprot = Q01362
    | Mm_EntrezGene = 14126
    | Mm_Ensembl = ENSMUSG00000024680
    | Mm_RefseqmRNA = NM_013516
    | Mm_RefseqProtein = NP_038544
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 11684238
    | Mm_GenLoc_end = 11690688
    | Mm_Uniprot = P20490
  }}
}}
'''Membrane-spanning 4-domains, subfamily A, member 2 (Fc fragment of IgE, high affinity I, receptor for; beta polypeptide)''', also known as '''MS4A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MS4A2 membrane-spanning 4-domains, subfamily A, member 2 (Fc fragment of IgE, high affinity I, receptor for; beta polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2206| 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 allergic response involves the binding of allergen to receptor-bound IgE followed by cell activation and the release of mediators responsible for the manifestations of allergy. The IgE-receptor, a tetramer composed of an alpha, beta, and 2 disulfide-linked gamma chains, is found on the surface of mast cells and basophils. This gene encodes the beta subunit of the high affinity IgE receptor which is a member of the membrane-spanning 4A gene family. Members of this nascent protein family are characterized by common structural features and similar intron/exon splice boundaries and display unique expression patterns among hematopoietic cells and nonlymphoid tissues. This family member is localized to 11q12, among a cluster of family members.<ref name="entrez">{{cite web | title = Entrez Gene: MS4A2 membrane-spanning 4-domains, subfamily A, member 2 (Fc fragment of IgE, high affinity I, receptor for; beta polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2206| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Jouvin MH, Numerof RP, Kinet JP |title=Signal transduction through the conserved motifs of the high affinity IgE receptor Fc epsilon RI. |journal=Semin. Immunol. |volume=7 |issue= 1 |pages= 29-35 |year= 1995 |pmid= 7612892 |doi=  }}
*{{cite journal  | author=Wilson BS, Pfeiffer JR, Oliver JM |title=FcepsilonRI signaling observed from the inside of the mast cell membrane. |journal=Mol. Immunol. |volume=38 |issue= 16-18 |pages= 1259-68 |year= 2003 |pmid= 12217393 |doi=  }}
*{{cite journal  | author=Kraft S, Rana S, Jouvin MH, Kinet JP |title=The role of the FcepsilonRI beta-chain in allergic diseases. |journal=Int. Arch. Allergy Immunol. |volume=135 |issue= 1 |pages= 62-72 |year= 2004 |pmid= 15316148 |doi= 10.1159/000080231 }}
*{{cite journal  | author=Maekawa K, Imagawa N, Tanaka Y, Harada S |title=Determination of the sequence coding for the beta subunit of the human high-affinity IgE receptor. |journal=FEBS Lett. |volume=302 |issue= 2 |pages= 161-5 |year= 1992 |pmid= 1386024 |doi=  }}
*{{cite journal  | author=Bieber T, de la Salle H, Wollenberg A, ''et al.'' |title=Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI). |journal=J. Exp. Med. |volume=175 |issue= 5 |pages= 1285-90 |year= 1992 |pmid= 1533242 |doi=  }}
*{{cite journal  | author=Küster H, Zhang L, Brini AT, ''et al.'' |title=The gene and cDNA for the human high affinity immunoglobulin E receptor beta chain and expression of the complete human receptor. |journal=J. Biol. Chem. |volume=267 |issue= 18 |pages= 12782-7 |year= 1992 |pmid= 1535625 |doi=  }}
*{{cite journal  | author=Le Coniat M, Kinet JP, Berger R |title=The human genes for the alpha and gamma subunits of the mast cell receptor for immunoglobulin E are located on human chromosome band 1q23. |journal=Immunogenetics |volume=32 |issue= 3 |pages= 183-6 |year= 1990 |pmid= 2146219 |doi=  }}
*{{cite journal  | author=Tedder TF, Streuli M, Schlossman SF, Saito H |title=Isolation and structure of a cDNA encoding the B1 (CD20) cell-surface antigen of human B lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 1 |pages= 208-12 |year= 1988 |pmid= 2448768 |doi=  }}
*{{cite journal  | author=Paolini R, Renard V, Vivier E, ''et al.'' |title=Different roles for the Fc epsilon RI gamma chain as a function of the receptor context. |journal=J. Exp. Med. |volume=181 |issue= 1 |pages= 247-55 |year= 1995 |pmid= 7528770 |doi=  }}
*{{cite journal  | author=Shirakawa T, Li A, Dubowitz M, ''et al.'' |title=Association between atopy and variants of the beta subunit of the high-affinity immunoglobulin E receptor. |journal=Nat. Genet. |volume=7 |issue= 2 |pages= 125-9 |year= 1994 |pmid= 7920628 |doi= 10.1038/ng0694-125 }}
*{{cite journal  | author=Kihara H, Siraganian RP |title=Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor. |journal=J. Biol. Chem. |volume=269 |issue= 35 |pages= 22427-32 |year= 1994 |pmid= 8071371 |doi=  }}
*{{cite journal  | author=Sandford AJ, Shirakawa T, Moffatt MF, ''et al.'' |title=Localisation of atopy and beta subunit of high-affinity IgE receptor (Fc epsilon RI) on chromosome 11q. |journal=Lancet |volume=341 |issue= 8841 |pages= 332-4 |year= 1993 |pmid= 8094113 |doi=  }}
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}}
{{refend}}

{{protein-stub}}
 

end log.