HSP90AB1

From Wikipedia, the free encyclopedia

Heat shock protein 90kDa alpha (cytosolic), class B member 1

PDB rendering based on 1byq.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1QZ2, 1UYM, 3FWV, 3NMQ, 3PRY

Identifiers

Symbols

HSP90AB1; D6S182; HSP84; HSP90B; HSPC2; HSPCB

External IDs

OMIM: 140572 MGI: 96247 HomoloGene: 74306 ChEMBL: 4303 GeneCards: HSP90AB1 Gene

Gene Ontology
Molecular function	• UTP binding • CTP binding • protein binding • ATP binding • GTP binding • sulfonylurea receptor binding • protein kinase binding • nitric-oxide synthase regulator activity • TPR domain binding • dATP binding • ion channel binding • unfolded protein binding
Cellular component	• cytoplasm • mitochondrion • cytosol • signalosome • cell surface • inclusion body • basolateral plasma membrane • apical plasma membrane • brush border membrane • melanosome
Biological process	• placenta development • protein folding • response to unfolded protein • axon guidance • response to salt stress • positive regulation of protein binding • negative regulation of proteasomal ubiquitin-dependent protein catabolic process • positive regulation of protein import into nucleus, translocation • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • Fc-gamma receptor signaling pathway involved in phagocytosis • negative regulation of neuron apoptotic process • innate immune response • positive regulation of nitric oxide biosynthetic process • positive regulation of cell size • regulation of interferon-gamma-mediated signaling pathway • regulation of type I interferon-mediated signaling pathway • cellular response to organic cyclic compound • positive regulation of protein serine/threonine kinase activity
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
44.21 – 44.22 Mb

Chr 17:
45.57 – 45.57 Mb

PubMed search

Heat shock protein HSP 90-beta is a protein that in humans is encoded by the HSP90AB1 gene.^[1]^[2]^[3]

References

↑ Rebbe NF, Hickman WS, Ley TJ, Stafford DW, Hickman S (Oct 1989). "Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene". J Biol Chem 264 (25): 15006–11. PMID 2768249.
↑ Chen B, Piel WH, Gui L, Bruford E, Monteiro A (Dec 2005). "The HSP90 family of genes in the human genome: insights into their divergence and evolution". Genomics 86 (6): 627–37. doi:10.1016/j.ygeno.2005.08.012. PMID 16269234.
↑ "Entrez Gene: HSP90AB1 Heat shock protein 90kDa alpha (cytosolic), class B member 1".

Hoffmann T, Hovemann B (1989). "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens.". Gene 74 (2): 491–501. doi:10.1016/0378-1119(88)90182-5. PMID 2469626.
Lees-Miller SP, Anderson CW (1989). "Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II.". J. Biol. Chem. 264 (5): 2431–7. PMID 2492519.
Rebbe NF, Ware J, Bertina RM, et al. (1987). "Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family.". Gene 53 (2–3): 235–45. doi:10.1016/0378-1119(87)90012-6. PMID 3301534.
Tang PZ, Gannon MJ, Andrew A, Miller D (1995). "Evidence for oestrogenic regulation of heat shock protein expression in human endometrium and steroid-responsive cell lines". Eur. J. Endocrinol. 133 (5): 598–605. doi:10.1530/eje.0.1330598. PMID 7581991.
Nemoto T, Ohara-Nemoto Y, Ota M, et al. (1995). "Mechanism of dimer formation of the 90-kDa heat-shock protein". Eur. J. Biochem. 233 (1): 1–8. doi:10.1111/j.1432-1033.1995.001_1.x. PMID 7588731.
Takahashi I, Tanuma R, Hirata M, Hashimoto K (1994). "A cosmid clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa heat shock protein beta gene (HSP90 beta)". Mamm. Genome 5 (2): 121–2. doi:10.1007/BF00292342. PMID 8180474.
Ji H, Reid GE, Moritz RL, et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948.
Yano M, Naito Z, Yokoyama M, et al. (1999). "Expression of hsp90 and cyclin D1 in human breast cancer". Cancer Lett. 137 (1): 45–51. doi:10.1016/S0304-3835(98)00338-3. PMID 10376793.
Sato S, Fujita N, Tsuruo T (2000). "Modulation of Akt kinase activity by binding to Hsp90". Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10832–7. doi:10.1073/pnas.170276797. PMC 27109. PMID 10995457.
Gisler SM, Stagljar I, Traebert M, et al. (2001). "Interaction of the type IIa Na/Pi cotransporter with PDZ proteins". J. Biol. Chem. 276 (12): 9206–13. doi:10.1074/jbc.M008745200. PMID 11099500.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
King FW, Wawrzynow A, Höhfeld J, Zylicz M (2002). "Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53". EMBO J. 20 (22): 6297–305. doi:10.1093/emboj/20.22.6297. PMC 125724. PMID 11707401.
Bouhouche-Chatelier L, Chadli A, Catelli MG (2002). "The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor". Cell Stress Chaperones 6 (4): 297–305. doi:10.1379/1466-1268(2001)006<0297:TNTATB>2.0.CO;2. PMC 434412. PMID 11795466.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Sato N, Yamamoto T, Sekine Y, et al. (2003). "Involvement of heat-shock protein 90 in the interleukin-6-mediated signaling pathway through STAT3". Biochem. Biophys. Res. Commun. 300 (4): 847–52. doi:10.1016/S0006-291X(02)02941-8. PMID 12559950.
Wu JM, Xiao L, Cheng XK, et al. (2004). "PKC epsilon is a unique regulator for hsp90 beta gene in heat shock response". J. Biol. Chem. 278 (51): 51143–9. doi:10.1074/jbc.M305537200. PMID 14532285.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Nagaraja GM, Kandpal RP (2004). "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins". Biochem. Biophys. Res. Commun. 313 (3): 654–65. doi:10.1016/j.bbrc.2003.12.001. PMID 14697242.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.

PDB gallery

1byq: HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG

1osf: Human Hsp90 in complex with 17-desmethoxy-17-N,N-Dimethylaminoethylamino-Geldanamycin

1uym: HUMAN HSP90-BETA WITH PU3 (9-BUTYL-8(3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE)

1yc1: Crystal Structures of human HSP90alpha complexed with dihydroxyphenylpyrazoles

1yc3: Crystal Structure of human HSP90alpha complexed with dihydroxyphenylpyrazoles

1yc4: Crystal structure of human HSP90alpha complexed with dihydroxyphenylpyrazoles

1yer: HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, ""CLOSED"" CONFORMATION

1yes: HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, ""OPEN"" CONFORMATION

1yet: GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN

2bsm: NOVEL, POTENT SMALL MOLECULE INHIBITORS OF THE MOLECULAR CHAPERONE HSP90 DISCOVERED THROUGH STRUCTURE-BASED DESIGN

2bt0: NOVEL, POTENT SMALL MOLECULE INHIBITORS OF THE MOLECULAR CHAPERONE HSP90 DISCOVERED THROUGH STRUCTURE-BASED DESIGN

2byh: 3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-PYRAZOLE-4-CARBOXAMIDES AS INHIBITORS OF THE HSP90 MOLECULAR CHAPERONE

2byi: 3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-PYRAZOLE-4-CARBOXAMIDES AS INHIBITORS OF THE HSP90 MOLECULAR CHAPERONE

2bz5: STRUCTURE-BASED DISCOVERY OF A NEW CLASS OF HSP90 INHIBITORS

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Early pregnancy factor Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α₁ α₂ β ER TRAP1

Other	Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2

Protein targeting

Signal peptide Mitochondrial targeting signal

Ubiquitin

E1 Ubiquitin-activating enzyme
- UBA1
- UBA2
- UBA3
- UBA5
- UBA6
- UBA7
- ATG7
- NAE1
- SAE1

E2 Ubiquitin-conjugating enzyme
- A
- B
- C
- D1
- D2
- D3
- E1
- E2
- E3
- G1
- G2
- H
- I
- J1
- J2
- K
- L1
- L2
- L3
- L4
- L6
- M
- N
- O
- Q1
- Q2
- R1 (CDC34)
- R2
- S
- V1
- V2
- Z

E3 Ubiquitin ligase
- VHL
- Cullin
- CBL
- MDM2
- FANCL
- UBR1

ATG3
BIRC6
UFC1

Other

Ubiquitin-like modifiers
- SUMO protein
- ISG15
- URM1
- NEDD8
- FAT10
- ATG8
- ATG12
- FUB1
- MUB
- UFM1
- UBL5

See also: posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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HSP90AB1

References

Further reading