HSP13_HUMAN
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 03-AUG-2022, entry version 182.
DE RecName: Full=Heat shock 70 kDa protein 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; 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=5; IntAct=EBI-750892, EBI-744081;
CC P48723; Q9UMX0: UBQLN1; NbExp=8; IntAct=EBI-750892, EBI-741480;
CC P48723; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-750892, EBI-10173939;
CC P48723; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-750892, EBI-947187;
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}.
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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; 126.
DR IntAct; P48723; 18.
DR MINT; P48723; -.
DR STRING; 9606.ENSP00000285667; -.
DR DrugBank; DB09130; Copper.
DR GlyConnect; 1294; 5 N-Linked glycans (2 sites).
DR GlyGen; P48723; 2 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; P48723; -.
DR PhosphoSitePlus; P48723; -.
DR BioMuta; HSPA13; -.
DR DMDM; 1351125; -.
DR REPRODUCTION-2DPAGE; IPI00299299; -.
DR EPD; P48723; -.
DR jPOST; P48723; -.
DR MassIVE; P48723; -.
DR MaxQB; P48723; -.
DR PaxDb; P48723; -.
DR PeptideAtlas; P48723; -.
DR PRIDE; P48723; -.
DR ProteomicsDB; 55924; -.
DR TopDownProteomics; P48723; -.
DR Antibodypedia; 2522; 197 antibodies from 30 providers.
DR DNASU; 6782; -.
DR Ensembl; ENST00000285667.4; ENSP00000285667.3; ENSG00000155304.6.
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 CTD; 6782; -.
DR DisGeNET; 6782; -.
DR GeneCards; HSPA13; -.
DR HGNC; HGNC:11375; HSPA13.
DR HPA; ENSG00000155304; Low tissue specificity.
DR MIM; 601100; gene.
DR neXtProt; NX_P48723; -.
DR OpenTargets; ENSG00000155304; -.
DR PharmGKB; PA162391697; -.
DR VEuPathDB; HostDB:ENSG00000155304; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00890000139503; -.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; P48723; -.
DR OMA; LRKTNFN; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P48723; -.
DR TreeFam; TF105047; -.
DR PathwayCommons; P48723; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; P48723; -.
DR BioGRID-ORCS; 6782; 116 hits in 1082 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 206 other tissues.
DR ExpressionAtlas; P48723; baseline and differential.
DR Genevisible; P48723; HS.
DR GO; GO:0005737; C:cytoplasm; 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:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10237; HSPA13-like_NBD; 1.
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; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF53067; SSF53067; 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 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..338
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
