ID   HS905_HUMAN             Reviewed;         334 AA.
AC   Q58FG0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Putative heat shock protein HSP 90-alpha A5;
DE   AltName: Full=Heat shock protein 90-alpha E;
DE            Short=Heat shock protein 90Ae;
GN   Name=HSP90AA5P; Synonyms=HSP90AE;
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).
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: 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; AY956761; AAX38248.1; -; mRNA.
DR   AlphaFoldDB; Q58FG0; -.
DR   SMR; Q58FG0; -.
DR   IntAct; Q58FG0; 49.
DR   MINT; Q58FG0; -.
DR   iPTMnet; Q58FG0; -.
DR   PhosphoSitePlus; Q58FG0; -.
DR   BioMuta; HGNC:32535; -.
DR   EPD; Q58FG0; -.
DR   jPOST; Q58FG0; -.
DR   MassIVE; Q58FG0; -.
DR   MaxQB; Q58FG0; -.
DR   PeptideAtlas; Q58FG0; -.
DR   PRIDE; Q58FG0; -.
DR   ProteomicsDB; 62624; -.
DR   GeneCards; HSP90AA5P; -.
DR   HGNC; HGNC:32535; HSP90AA5P.
DR   neXtProt; NX_Q58FG0; -.
DR   PhylomeDB; Q58FG0; -.
DR   PathwayCommons; Q58FG0; -.
DR   SignaLink; Q58FG0; -.
DR   Pharos; Q58FG0; Tdark.
DR   PRO; PR:Q58FG0; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q58FG0; protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 3.
DR   Pfam; PF00183; HSP90; 2.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..334
FT                   /note="Putative heat shock protein HSP 90-alpha A5"
FT                   /id="PRO_0000340660"
FT   REGION          55..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..267
FT                   /evidence="ECO:0000255"
FT   MOTIF           327..331
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        55..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q58FF8"
SQ   SEQUENCE   334 AA;  38738 MW;  2B7C73A0BD9DBAFB CRC64;
     MGFHHVGQAG LELLTSGHPA LERRPEYLEE RRIKEIVKKH SQFIGYPITL FVEKKRNKQV
     SDAEAEKKED KRKKKKESND KPEIEDVGSD EEEEKKDADK KKKKSKEKYI DQELNKTKPI
     WTRNPDAITN EEYGEFHQSL TNNWEDHLAV KHFSVEGQLE ELKDSRRVMK ANQKHIYYIT
     GETKDQVANS AFVECLQKHG LEVIYMIELI DKYCVQQLKE LESKTVVSVA KEGLELPEDE
     EEKKKQEEKK TKFENLCKIM KDMLEKKVKK VVVSNCMEDP QRHTNKIYRM IKLGLGVDEY
     DPTANDINAA ITKEMPPLRG GDDTSRMEEV GGSG