Heat shock protein 90kDa alpha (cytosolic), member A1

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

PDB rendering based on 1byq.

Available structures

1BYQ, 1OSF, 1UY6, 1UY7, 1UY8, 1UY9, 1UYC, 1UYD, 1UYE, 1UYF, 1UYG, 1UYH, 1UYI, 1UYK, 1UYL, 1YC1, 1YC3, 1YC4, 1YER, 1YES, 1YET, 2BSM, 2BT0, 2BUG, 2BYH, 2BYI, 2BZ5, 2C2L, 2CCS, 2CCT, 2CCU, 2CDD, 2FWY, 2FWZ, 2H55, 2JJC, 2K5B, 2QF6, 2QFO, 2QG0, 2QG2, 2UWD, 2VCI, 2VCJ, 2WI1, 2WI2, 2WI3, 2WI4, 2WI5, 2WI6, 2WI7, 2XAB, 2XDK, 2XDL, 2XDS, 2XDU, 2XDX, 2XHR, 2XHT, 2XHX, 2XJG, 2XJJ, 2XJX, 2XK2, 3BM9, 3BMY, 3D0B, 3EKO, 3EKR, 3FT5, 3FT8, 3HEK, 3HHU, 3HYY, 3HYZ, 3HZ1, 3HZ5, 3INW, 3INX, 3K97, 3K98, 3K99, 3MNR

Identifiers

Symbols

HSP90AA1; FLJ31884; HSP86; HSP89A; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; Hsp89; Hsp90; LAP2

External IDs

OMIM: 140571 MGI: 96250 HomoloGene: 68464 GeneCards: HSP90AA1 Gene

Gene Ontology
Molecular function	• nucleotide binding • protein binding • ATP binding • ATPase activity • nitric-oxide synthase regulator activity • TPR domain binding • TPR domain binding • protein homodimerization activity • unfolded protein binding
Cellular component	• intracellular • cytoplasm • cytosol • cytosol • cytosol • plasma membrane • plasma membrane • melanosome
Biological process	• G2/M transition of mitotic cell cycle • mitotic cell cycle • ATP catabolic process • mitochondrial transport • response to unfolded protein • signal transduction • axon guidance • cellular chaperone-mediated protein complex assembly • protein refolding • protein import into mitochondrial outer membrane • positive regulation of nitric oxide biosynthetic process • nitric oxide metabolic process • regulation of nitric-oxide synthase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
102.55 – 102.61 Mb

Chr 12:
111.93 – 111.94 Mb

PubMed search

[1]

[2]

Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene.^[1]^[2]

Interactions

Heat shock protein 90kDa alpha (cytosolic), member A1 has been shown to interact with TGF beta receptor 2,^[3] FKBP5,^[4] TGF beta receptor 1,^[3] Glucocorticoid receptor,^[5]^[6]^[7]^[8]^[9]^[10]^[11] AKT1,^[12]^[13]^[14] Hop,^[15]^[16] Peroxisome proliferator-activated receptor alpha,^[17] AHSA1,^[18] HSF1,^[19]^[20] STK11,^[21] C-Raf,^[22]^[23] ERN1,^[24] PIM1,^[25] GNA12,^[26] Endothelial NOS,^[27]^[28]^[29] Androgen receptor,^[30]^[31] CDC37,^[32]^[33] DAP3,^[6] SMYD3,^[34] Telomerase reverse transcriptase,^[12]^[13] HER2/neu,^[35]^[36] EPRS,^[37] P53,^[38]^[39]^[40] Estrogen receptor alpha^[20]^[41] and GUCY1B3.^[27]

References

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Csermely P, Schnaider T, Soti C, et al. (1998). "The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review.". Pharmacol. Ther. 79 (2): 129–68. doi:10.1016/S0163-7258(98)00013-8. PMID 9749880.
Young JC, Moarefi I, Hartl FU (2001). "Hsp90: a specialized but essential protein-folding tool.". J. Cell Biol. 154 (2): 267–73. doi:10.1083/jcb.200104079. PMC 2150759. PMID 11470816. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2150759.
Hamblin AD, Hamblin TJ (2006). "Functional and prognostic role of ZAP-70 in chronic lymphocytic leukaemia.". Expert Opin. Ther. Targets 9 (6): 1165–78. doi:10.1517/14728222.9.6.1165. PMID 16300468.
Lattouf JB, Srinivasan R, Pinto PA, et al. (2007). "Mechanisms of disease: the role of heat-shock protein 90 in genitourinary malignancy.". Nature clinical practice. Urology 3 (11): 590–601. doi:10.1038/ncpuro0604. PMID 17088927.

PDB gallery

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

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

1uy6: HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE

1uy7: HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(4-METHOXY-BENZYL)-9H-PURIN-6-YLAMINE

1uy8: HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(3-TRIMETHOXY-BENZYL)-9H-PURIN-6YLAMINE

1uy9: HUMAN HSP90-ALPHA WITH 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-9H-PURIN-6-YLAMINE

1uyc: HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2,5-DIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE

1uyd: HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE

1uye: HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL) -9-PENT-4-YLNYL-9H-PURIN-6-YLAMINE

1uyf: HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL) -2-FLUORO-9-PENT-4-YLNYL-9H-PURIN-6-YLAMINE

1uyg: HUMAN HSP90-ALPHA WITH 8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9H-PURIN-6-YLAMINE

1uyh: HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9H-PURIN-6-YLAMINE

1uyi: HUMAN HSP90-ALPHA WITH 8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9-PENT-9H-PURIN-6-YLAMINE

1uyk: HUMAN HSP90-ALPHA WITH 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUT YL-2-FLUORO-9H-PURIN-6-YLAMINE

1uyl: STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED INHIBITOR BINDING TO HSP90 ISOFORMS

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

2ccs: HUMAN HSP90 WITH 4-CHLORO-6-(4-PIPERAZIN-1-YL-1H-PYRAZOL-3-YL)-BENZENE-1,2-DIOL

2cct: HUMAN HSP90 WITH 5-(5-CHLORO-2,4-DIHYDROXY-PHENYL)-4-PIPERAZIN-1-YL-2H-PYRAZOLE-3-CARBOXYLIC ACID ETHYLAMIDE

2ccu: HUMAN HSP90 WITH 4-CHLORO-6-(4-(4-(4-METHANESULPHONYL-BENZYL)-PIERAZIN-1-YL)-1H-PYRAZOL-3-YL)-BENZENE-1,3-DIOL

2cdd: HUMAN HSP90 WITH 4-(4-(2,3-DIHYDRO-BENZOL(1,4)DIOXIN-6-YL)-5-METHYL-1H-PYRAZOL-3-YL)-6-ETHYL-BENZENE-1,3-DIOL

2fwy: Structure of human Hsp90-alpha bound to the potent water soluble inhibitor PU-H64

2fwz: Structure of human Hsp90-alpha bound to the potent water soluble inhibitor PU-H71

2h55: Structure of human Hsp90-alpha bound to the potent water soluble inhibitor PU-DZ8

2uwd: INHIBITION OF THE HSP90 MOLECULAR CHAPERONE IN VITRO AND IN VIVO BY NOVEL, SYNTHETIC, POTENT RESORCINYLIC PYRAZOLE, ISOXAZOLE AMIDE ANALOGS

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

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)

Deubiquitinating enzyme: Ataxin 3 • USP6 • CYLD

ATG3 • BIRC6 • UFC1

Other

SUMO protein

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°)

Heat shock protein 90kDa alpha (cytosolic), member A1

Interactions

References

Further reading