H90B3_HUMAN
ID H90B3_HUMAN Reviewed; 597 AA.
AC Q58FF7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative heat shock protein HSP 90-beta-3;
DE AltName: Full=Heat shock protein 90-beta c;
DE Short=Heat shock protein 90Bc;
GN Name=HSP90AB3P; Synonyms=HSP90BC;
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].
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).
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 -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AY956764; AAX38251.1; -; mRNA.
DR AlphaFoldDB; Q58FF7; -.
DR SMR; Q58FF7; -.
DR IntAct; Q58FF7; 60.
DR MINT; Q58FF7; -.
DR GlyConnect; 1697; 2 N-Linked glycans (2 sites).
DR GlyGen; Q58FF7; 4 sites, 2 N-linked glycans (2 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; Q58FF7; -.
DR PhosphoSitePlus; Q58FF7; -.
DR SwissPalm; Q58FF7; -.
DR BioMuta; HGNC:5259; -.
DR DMDM; 74722492; -.
DR EPD; Q58FF7; -.
DR jPOST; Q58FF7; -.
DR MassIVE; Q58FF7; -.
DR MaxQB; Q58FF7; -.
DR PeptideAtlas; Q58FF7; -.
DR PRIDE; Q58FF7; -.
DR ProteomicsDB; 62622; -.
DR TopDownProteomics; Q58FF7; -.
DR GeneCards; HSP90AB3P; -.
DR HGNC; HGNC:5259; HSP90AB3P.
DR neXtProt; NX_Q58FF7; -.
DR InParanoid; Q58FF7; -.
DR PhylomeDB; Q58FF7; -.
DR PathwayCommons; Q58FF7; -.
DR SignaLink; Q58FF7; -.
DR ChiTaRS; HSP90AB3P; human.
DR Pharos; Q58FF7; Tdark.
DR PRO; PR:Q58FF7; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q58FF7; 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; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 3.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 5: Uncertain;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..597
FT /note="Putative heat shock protein HSP 90-beta-3"
FT /id="PRO_0000336047"
FT REGION 201..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..446
FT /evidence="ECO:0000255"
FT MOTIF 593..597
FT /note="TPR repeat-binding"
FT COMPBIAS 203..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 597 AA; 68325 MW; 9DA27E4F47CA6949 CRC64;
MPEEVHHGEE EVETFAFQAE IAQLISLIIN TFYSNEEIFL QELISNASDA LDKIRYESLT
DPSKLDSGKE LKIDIIPNPQ ERTLALVDTG IGMTKADLIN NLRTIAKSGT KACMEALQAE
KLVVITKHND DEQYAWESSA GGSFTVHADH GEPIGRGTKV ILHLKEDQTE YLEERRVKEV
VKKHSQFIGY PITLYLEKEQ DKEISDDEAE EEKGEKEEED KDDEEKPKIK DVGSDEEDDS
KEYGEFYKSL TSDWEDHLAV KHFSVEGQLE FRALLFSPRR APFDLFENKK KKNNIKLYVR
RVFIMDSCDE LIPEYLNFIH GVVDSEDLPL NISREMLQQS KILKYVSHMK ETQKSTYYIT
GESKEQVANS AFVERVRKQG FEVVYMTEPI DEYCVQQLKE FDGKSLVSVT KEGLELPEDE
EEKKKMEESK EKFENLCKLM KEILDKKVEK VTISNRLVSS PCCIVTSTYG WTANMEQIMK
AQALRDNSTM GYMMAKKHLE INPDHPIMET LRQKAEADKN DKAVKDLVVL LFETALLSSG
FSLEDPQTHS NHIYHMIKLG LGTDEDEVAA EEPSDAVPDE IPPLEGDEDA SRMEEVD
