HS902_HUMAN
ID HS902_HUMAN Reviewed; 343 AA.
AC Q14568;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Heat shock protein HSP 90-alpha A2 {ECO:0000305};
DE AltName: Full=Heat shock 90 kDa protein 1 alpha-like 3 {ECO:0000305};
DE AltName: Full=Heat shock protein HSP 90-alpha A2 pseudogene {ECO:0000305};
GN Name=HSP90AA2P {ECO:0000312|HGNC:HGNC:5256};
GN Synonyms=HSP90AA2 {ECO:0000312|HGNC:HGNC:5256},
GN HSPCAL3 {ECO:0000312|HGNC:HGNC:5256};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311, AND VARIANT ALA-235.
RX PubMed=2591742; DOI=10.1016/0378-1119(89)90408-3;
RA Walter T., Drabent B., Krebs H., Tomalak M., Heiss S., Benecke B.J.J.;
RT "Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene.";
RL Gene 83:105-115(1989).
RN [3]
RP NOMENCLATURE.
RX PubMed=1740332; DOI=10.1016/0888-7543(92)90368-3;
RA Ozawa K., Murakami Y., Eki T., Soeda E., Yokoyama K.;
RT "Mapping of the gene family for human heat-shock protein 90 alpha to
RT chromosomes 1, 4, 11, and 14.";
RL Genomics 12:214-220(1992).
RN [4]
RP NOMENCLATURE.
RX PubMed=16269234; DOI=10.1016/j.ygeno.2005.08.012;
RA Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.;
RT "The HSP90 family of genes in the human genome: insights into their
RT divergence and evolution.";
RL Genomics 86:627-637(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [6]
RP HYDROXYBUTYRYLATION AT LYS-112.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
CC -!- FUNCTION: Putative molecular chaperone that may promote the maturation,
CC structural maintenance and proper regulation of specific target
CC proteins. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- CAUTION: Despite classification as a pseudogene, the existence of this
CC protein is supported by unambiguous mass spectrometry evidence.
CC {ECO:0000305}.
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DR EMBL; AC103796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M30627; AAA36024.1; -; mRNA.
DR PIR; JQ0129; JQ0129.
DR AlphaFoldDB; Q14568; -.
DR SMR; Q14568; -.
DR IntAct; Q14568; 18.
DR MINT; Q14568; -.
DR GlyGen; Q14568; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14568; -.
DR PhosphoSitePlus; Q14568; -.
DR SwissPalm; Q14568; -.
DR BioMuta; HGNC:5256; -.
DR DMDM; 172046850; -.
DR EPD; Q14568; -.
DR jPOST; Q14568; -.
DR MassIVE; Q14568; -.
DR MaxQB; Q14568; -.
DR PeptideAtlas; Q14568; -.
DR PRIDE; Q14568; -.
DR ProteomicsDB; 60048; -.
DR TopDownProteomics; Q14568; -.
DR GeneCards; HSP90AA2P; -.
DR HGNC; HGNC:5256; HSP90AA2P.
DR MIM; 140575; gene.
DR neXtProt; NX_Q14568; -.
DR InParanoid; Q14568; -.
DR PathwayCommons; Q14568; -.
DR SignaLink; Q14568; -.
DR ChiTaRS; HSP90AA2P; human.
DR Pharos; Q14568; Tdark.
DR PRO; PR:Q14568; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q14568; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Hydroxylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..343
FT /note="Heat shock protein HSP 90-alpha A2"
FT /id="PRO_0000324325"
FT REGION 227..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 112
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008"
FT VARIANT 235
FT /note="T -> A (in dbSNP:rs1826330)"
FT /evidence="ECO:0000269|PubMed:2591742"
FT /id="VAR_039732"
FT VARIANT 312
FT /note="C -> Y (in dbSNP:rs2726836)"
FT /id="VAR_039733"
FT CONFLICT 273
FT /note="D -> DK (in Ref. 2; AAA36024)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="Y -> I (in Ref. 2; AAA36024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 39365 MW; 2583C15C04090C65 CRC64;
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIW
YESLTDPSKL DSGKELHINL IPNKQDQTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
ALQAGADISM IGQFGVSFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGERM
GRGTKVILHL KEDQTEYLEE QRIKEIVKKH SQLIGYPITL FVEKECDKEV SDDETEEKED
KEEEKEKEEK ESKDKPEIED VGSDEEEEKK DGDKKKKKTK EKYIDQEELN KTKPIWTRNP
DDITNEEYGE FCKNLTNDWE DHLAVKHFSV EGQLEFRALL FVP
