ID   H90B4_HUMAN             Reviewed;         505 AA.
AC   Q58FF6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Putative heat shock protein HSP 90-beta 4;
GN   Name=HSP90AB4P;
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   -!- 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; AY956765; AAX38252.1; -; mRNA.
DR   AlphaFoldDB; Q58FF6; -.
DR   SMR; Q58FF6; -.
DR   IntAct; Q58FF6; 47.
DR   GlyGen; Q58FF6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q58FF6; -.
DR   PhosphoSitePlus; Q58FF6; -.
DR   BioMuta; HGNC:32538; -.
DR   DMDM; 74722491; -.
DR   EPD; Q58FF6; -.
DR   jPOST; Q58FF6; -.
DR   MassIVE; Q58FF6; -.
DR   MaxQB; Q58FF6; -.
DR   PeptideAtlas; Q58FF6; -.
DR   PRIDE; Q58FF6; -.
DR   ProteomicsDB; 62621; -.
DR   GeneCards; HSP90AB4P; -.
DR   HGNC; HGNC:32538; HSP90AB4P.
DR   neXtProt; NX_Q58FF6; -.
DR   InParanoid; Q58FF6; -.
DR   PhylomeDB; Q58FF6; -.
DR   PathwayCommons; Q58FF6; -.
DR   SignaLink; Q58FF6; -.
DR   Pharos; Q58FF6; Tdark.
DR   PRO; PR:Q58FF6; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q58FF6; protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; -; 1.
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; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   5: Uncertain;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..505
FT                   /note="Putative heat shock protein HSP 90-beta 4"
FT                   /id="PRO_0000349174"
FT   REGION          197..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   505 AA;  58264 MW;  69C72AB3F4086E0C CRC64;
     MSLIINTFYS NKEIFLQELI SNASDALDKI RYESLTDPSK LDGGKELKID IIPNPRECIL
     TLVNTGIGMT KADLINNLGA IAKSGTEAFM EAFQSCAEIS MIGQFGVGFY SAYLVAEKVA
     ITKHNDEEQY SWVSSAGSSF TLHVDHGEPI DRDTKVILHL KEDQTEYLEE RWVKEVVKKH
     PQFIGCLIAV YLEKEPEKEI SDDEEEKGEK EEEDKDDKEK PKTEDVGSDE EDDTDKNNKK
     KTKKIKEKYT DREELNQTKP IWTRNPDDIT QEECGEFYKS LTSAWEDHLA VKQFPVEEQE
     ENEQLCVHHV WIMDSFDDLM PEYVGFVRED KENNKKLDEV FSKISWLGIH EDSINWRHLS
     ELLWSHTFQS GDEMTSLSEY VSCMKEAQKS ICDIIGECKE QVANSAFVEQ EWKKGFEVIY
     MSEPIDEYCV QQLKEFDGKS LLSVTKEGLE LPEDEEEKKI MEESNVKFEN LCRLMKEILD
     KKVERVTISS RLVSSPCRIV TSTYS