ID   H90B2_HUMAN             Reviewed;         381 AA.
AC   Q58FF8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative heat shock protein HSP 90-beta 2;
DE   AltName: Full=Heat shock protein 90-beta b;
DE            Short=Heat shock protein 90Bb;
GN   Name=HSP90AB2P; Synonyms=HSP90BB;
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 [MRNA], AND 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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX38250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY956763; AAX38250.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q58FF8; -.
DR   SMR; Q58FF8; -.
DR   IntAct; Q58FF8; 37.
DR   MINT; Q58FF8; -.
DR   ChEMBL; CHEMBL4105858; -.
DR   GlyGen; Q58FF8; 1 site.
DR   iPTMnet; Q58FF8; -.
DR   PhosphoSitePlus; Q58FF8; -.
DR   SwissPalm; Q58FF8; -.
DR   BioMuta; HGNC:32537; -.
DR   DMDM; 190359598; -.
DR   EPD; Q58FF8; -.
DR   jPOST; Q58FF8; -.
DR   MassIVE; Q58FF8; -.
DR   MaxQB; Q58FF8; -.
DR   PeptideAtlas; Q58FF8; -.
DR   PRIDE; Q58FF8; -.
DR   ProteomicsDB; 62623; -.
DR   GeneCards; HSP90AB2P; -.
DR   HGNC; HGNC:32537; HSP90AB2P.
DR   neXtProt; NX_Q58FF8; -.
DR   InParanoid; Q58FF8; -.
DR   PhylomeDB; Q58FF8; -.
DR   PathwayCommons; Q58FF8; -.
DR   SignaLink; Q58FF8; -.
DR   ChiTaRS; HSP90AB2P; human.
DR   Pharos; Q58FF8; Tdark.
DR   PRO; PR:Q58FF8; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q58FF8; protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
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; 2.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..381
FT                   /note="Putative heat shock protein HSP 90-beta 2"
FT                   /id="PRO_0000340659"
FT   REGION          145..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          315..347
FT                   /evidence="ECO:0000255"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
SQ   SEQUENCE   381 AA;  44349 MW;  B8F6A86959E30905 CRC64;
     MPEEVHLGEK EVETFAFQAE IAQLMSLIIN TFYSNKEIFL WELISNASDA LDKIRYESLT
     DPSKLDSGKE LKIDIIPNTQ EHTLTLVDTG IGMTKADLIN NLGTIAKFQD QTEYLEEMQV
     KEVVEKHSQF LGYPITLYLE KEREKEISDG KAEEEKGEKE EENKDDEEKP KIEDVGSDEE
     DDSGKDKKKK TKKIKEKYID QEELNKTKPI WTRNTEDITQ EEYGEFYKSL TNDWKDHLAV
     RYFSVEEYVS RMKEIQKSIY YITGESKEQV ANSAFVEQVW KRDSRVVYMT EPIDGYQLKE
     FDGKSLVSVT KEGLELPEDG EEKKRMEERK AKFENLCKFM KETLDKKVEM VTVSNRLVSS
     SCCIVTSTYS WTANMEQIMK A