ID   HSP13_HUMAN             Reviewed;         471 AA.
AC   P48723; B2R616; Q8NE40;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   28-JAN-2026, entry version 199.
DE   RecName: Full=Heat shock 70 kDa protein 13;
DE   AltName: Full=Heat shock protein family A member 13;
DE   AltName: Full=Microsomal stress-70 protein ATPase core;
DE   AltName: Full=Stress-70 protein chaperone microsome-associated 60 kDa protein;
DE   Flags: Precursor;
GN   Name=HSPA13; Synonyms=STCH;
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=8131751; DOI=10.1002/j.1460-2075.1994.tb06371.x;
RA   Otterson G.A., Flynn G.C., Kratzke R.A., Coxon A., Johnston P.G.,
RA   Kaye F.J.;
RT   "Stch encodes the 'ATPase core' of a microsomal stress 70 protein.";
RL   EMBO J. 13:1216-1225(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Blechschmidt K., Nordsiek G., Groet J., Nizetic D., Hildmann T.,
RA   Drescher B., Weber J., Menzel U., Schattevoy R., Yaspo M.-L., Rosenthal A.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH UBQLN2.
RX   PubMed=10675567; DOI=10.1016/s0014-5793(00)01135-2;
RA   Kaye F.J., Modi S., Ivanovska I., Koonin E.V., Thress K., Kubo A.,
RA   Kornbluth S., Rose M.D.;
RT   "A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like
RT   Stch.";
RL   FEBS Lett. 467:348-355(2000).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Has peptide-independent ATPase activity.
CC   -!- SUBUNIT: Binds UBQLN2.
CC   -!- INTERACTION:
CC       P48723; O43286: B4GALT5; NbExp=2; IntAct=EBI-750892, EBI-21511746;
CC       P48723; Q24JT5: CRYGA; NbExp=3; IntAct=EBI-750892, EBI-10239205;
CC       P48723; O43765: SGTA; NbExp=8; IntAct=EBI-750892, EBI-347996;
CC       P48723; Q96EQ0: SGTB; NbExp=6; IntAct=EBI-750892, EBI-744081;
CC       P48723; Q9UMX0: UBQLN1; NbExp=8; IntAct=EBI-750892, EBI-741480;
CC       P48723; Q9UMX0-2: UBQLN1; NbExp=4; IntAct=EBI-750892, EBI-10173939;
CC       P48723; Q9UHD9: UBQLN2; NbExp=6; IntAct=EBI-750892, EBI-947187;
CC       P48723; Q9NRR5: UBQLN4; NbExp=3; IntAct=EBI-750892, EBI-711226;
CC   -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in all tissues.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U04735; AAA16954.1; -; mRNA.
DR   EMBL; AF130249; AAD21091.1; -; Genomic_DNA.
DR   EMBL; AK312396; BAG35313.1; -; mRNA.
DR   EMBL; AL163206; CAB90390.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX10056.1; -; Genomic_DNA.
DR   EMBL; BC036370; AAH36370.1; -; mRNA.
DR   CCDS; CCDS13567.1; -.
DR   PIR; S42631; S42631.
DR   RefSeq; NP_008879.3; NM_006948.4.
DR   AlphaFoldDB; P48723; -.
DR   SMR; P48723; -.
DR   BioGRID; 112659; 166.
DR   FunCoup; P48723; 2853.
DR   IntAct; P48723; 95.
DR   MINT; P48723; -.
DR   STRING; 9606.ENSP00000285667; -.
DR   DrugBank; DB09130; Copper.
DR   GlyConnect; 1294; 5 N-Linked glycans (2 sites).
DR   GlyCosmos; P48723; 2 sites, 4 glycans.
DR   GlyGen; P48723; 5 sites, 9 N-linked glycans (3 sites), 2 O-linked glycans (2 sites).
DR   iPTMnet; P48723; -.
DR   PhosphoSitePlus; P48723; -.
DR   BioMuta; HSPA13; -.
DR   DMDM; 1351125; -.
DR   REPRODUCTION-2DPAGE; IPI00299299; -.
DR   jPOST; P48723; -.
DR   MassIVE; P48723; -.
DR   PaxDb; 9606-ENSP00000285667; -.
DR   PeptideAtlas; P48723; -.
DR   ProteomicsDB; 55924; -.
DR   Pumba; P48723; -.
DR   TopDownProteomics; P48723; -.
DR   Antibodypedia; 2522; 193 antibodies from 29 providers.
DR   DNASU; 6782; -.
DR   Ensembl; ENST00000285667.4; ENSP00000285667.3; ENSG00000155304.7.
DR   GeneID; 6782; -.
DR   KEGG; hsa:6782; -.
DR   MANE-Select; ENST00000285667.4; ENSP00000285667.3; NM_006948.5; NP_008879.3.
DR   UCSC; uc002yjt.4; human.
DR   AGR; HGNC:11375; -.
DR   ClinPGx; PA162391697; -.
DR   CTD; 6782; -.
DR   DisGeNET; 6782; -.
DR   GeneCards; HSPA13; -.
DR   HGNC; HGNC:11375; HSPA13.
DR   HPA; ENSG00000155304; Low tissue specificity.
DR   MIM; 601100; gene.
DR   OpenTargets; ENSG00000155304; -.
DR   VEuPathDB; HostDB:ENSG00000155304; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00890000139503; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; P48723; -.
DR   OMA; GGMFITR; -.
DR   OrthoDB; 2401965at2759; -.
DR   PAN-GO; P48723; 11 GO annotations based on evolutionary models.
DR   PhylomeDB; P48723; -.
DR   PathwayCommons; P48723; -.
DR   Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR   SignaLink; P48723; -.
DR   Agora; ENSG00000155304; -.
DR   BioGRID-ORCS; 6782; 117 hits in 1162 CRISPR screens.
DR   ChiTaRS; HSPA13; human.
DR   GeneWiki; STCH; -.
DR   GenomeRNAi; 6782; -.
DR   Pharos; P48723; Tbio.
DR   PRO; PR:P48723; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P48723; protein.
DR   Bgee; ENSG00000155304; Expressed in ventricular zone and 208 other cell types or tissues.
DR   ExpressionAtlas; P48723; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd10237; ASKHA_NBD_HSP70_HSPA13; 1.
DR   FunFam; 3.30.30.30:FF:000007; Heat shock 70 kDa protein 13; 1.
DR   FunFam; 3.30.420.40:FF:000099; Heat shock 70 kDa protein 13; 1.
DR   FunFam; 3.30.420.40:FF:000103; Heat shock 70 kDa protein 13; 1.
DR   FunFam; 3.90.640.10:FF:000037; Heat shock 70 kDa protein 13; 1.
DR   FunFam; 3.90.640.10:FF:000022; heat shock 70 kDa protein 13; 1.
DR   FunFam; 3.30.420.40:FF:000110; heat shock 70 kDa protein 13 isoform X1; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 4.
DR   Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR042048; HSPA13.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endoplasmic reticulum; Microsome; Nucleotide-binding;
KW   Proteomics identification; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..471
FT                   /note="Heat shock 70 kDa protein 13"
FT                   /id="PRO_0000013558"
FT   REGION          315..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        450
FT                   /note="S -> F (in Ref. 6; AAH36370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   471 AA;  51927 MW;  C78028E7CB0D03F3 CRC64;
     MAREMTILGS AVLTLLLAGY LAQQYLPLPT PKVIGIDLGT TYCSVGVFFP GTGKVKVIPD
     ENGHISIPSM VSFTDNDVYV GYESVELADS NPQNTIYDAK RFIGKIFTAE ELEAEIGRYP
     FKVLNKNGMV EFSVTSNETI TVSPEYVGSR LLLKLKEMAE AYLGMPVANA VISVPAEFDL
     KQRNSTIEAA NLAGLKILRV INEPTAAAMA YGLHKADVFH VLVIDLGGGT LDVSLLNKQG
     GMFLTRAMSG NNKLGGQDFN QRLLQYLYKQ IYQTYGFVPS RKEEIHRLRQ AVEMVKLNLT
     LHQSAQLSVL LTVEEQDRKE PHSSDTELPK DKLSSADDHR VNSGFGRGLS DKKSGESQVL
     FETEISRKLF DTLNEDLFQK ILVPIQQVLK EGHLEKTEID EVVLVGGSTR IPRIRQVIQE
     FFGKDPNTSV DPDLAVVTGV AIQAGIDGGS WPLQVSALEI PNKHLQKTNF N
//