HSP7E_HUMAN
ID HSP7E_HUMAN Reviewed; 509 AA.
AC Q0VDF9; A8K8F8; B0YIY9; Q9P0X2; Q9UI07;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Heat shock 70 kDa protein 14;
DE AltName: Full=HSP70-like protein 1;
DE AltName: Full=Heat shock protein HSP60;
GN Name=HSPA14; Synonyms=HSP60, HSP70L1;
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=14592822; DOI=10.1182/blood-2003-08-2828;
RA Wan T., Zhou X., Chen G., An H., Chen T., Zhang W., Liu S., Jiang Y.,
RA Yang F., Wu Y., Cao X.;
RT "Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a
RT Th1 polarizing adjuvant.";
RL Blood 103:1747-1754(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP IMMUNOADJUVANT ABILITY.
RX PubMed=15930317; DOI=10.1158/0008-5472.can-04-3912;
RA Wu Y., Wan T., Zhou X., Wang B., Yang F., Li N., Chen G., Dai S., Liu S.,
RA Zhang M., Cao X.;
RT "Hsp70-like protein 1 fusion protein enhances induction of carcinoembryonic
RT antigen-specific CD8+ CTL response by dendritic cell vaccine.";
RL Cancer Res. 65:4947-4954(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, AND
RP INTERACTION WITH DNAJC2.
RX PubMed=16002468; DOI=10.1073/pnas.0504400102;
RA Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P., Rucknagel P.,
RA Stahl J., Rospert S.;
RT "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005).
RN [10]
RP IDENTIFICATION.
RX PubMed=15802566; DOI=10.1126/science.1109247;
RA Hundley H.A., Walter W., Bairstow S., Craig E.A.;
RT "Human Mpp11 J protein: ribosome-tethered molecular chaperones are
RT ubiquitous.";
RL Science 308:1032-1034(2005).
RN [11]
RP IMMUNOADJUVANT ABILITY.
RX PubMed=18851947; DOI=10.1016/j.bbrc.2008.10.002;
RA Zeng R., Zhang Z., Mei X., Gong W., Wei L.;
RT "Protective effect of a RSV subunit vaccine candidate G1F/M2 was enhanced
RT by a HSP70-Like protein in mice.";
RL Biochem. Biophys. Res. Commun. 377:495-499(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-85.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the ribosome-associated complex (RAC), a complex
CC involved in folding or maintaining nascent polypeptides in a folding-
CC competent state. In the RAC complex, binds to the nascent polypeptide
CC chain, while DNAJC2 stimulates its ATPase activity.
CC {ECO:0000269|PubMed:16002468}.
CC -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer
CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC chaperone DNAJC2. {ECO:0000269|PubMed:16002468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16002468}.
CC -!- MISCELLANEOUS: Acts as a potent immunoadjuvant, capable to interact
CC with antigen-presenting cells and generating efficient CD8(+) T-cell
CC responses. May be used as adjuvant to enhance effect of vaccine G1F/M2,
CC a candidate vaccine against respiratory syncytial virus (RSV), a major
CC respiratory pathogen in newborns (PubMed:18851947). May also be used as
CC adjuvant to prepare antigenic fusion protein for the therapeutics of
CC cancers (PubMed:15930317). {ECO:0000305|PubMed:15930317,
CC ECO:0000305|PubMed:18851947}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF143723; AAF66640.1; -; mRNA.
DR EMBL; AF112210; AAF17198.1; -; mRNA.
DR EMBL; AK292323; BAF85012.1; -; mRNA.
DR EMBL; EF444968; ACA05969.1; -; Genomic_DNA.
DR EMBL; EF444968; ACA05970.1; -; Genomic_DNA.
DR EMBL; AC069544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86258.1; -; Genomic_DNA.
DR EMBL; BC119690; AAI19691.1; -; mRNA.
DR CCDS; CCDS7103.1; -.
DR RefSeq; NP_057383.2; NM_016299.3.
DR AlphaFoldDB; Q0VDF9; -.
DR SMR; Q0VDF9; -.
DR BioGRID; 119358; 102.
DR DIP; DIP-62114N; -.
DR IntAct; Q0VDF9; 24.
DR MINT; Q0VDF9; -.
DR STRING; 9606.ENSP00000367623; -.
DR GlyGen; Q0VDF9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q0VDF9; -.
DR PhosphoSitePlus; Q0VDF9; -.
DR SwissPalm; Q0VDF9; -.
DR BioMuta; HSPA14; -.
DR DMDM; 121948121; -.
DR EPD; Q0VDF9; -.
DR jPOST; Q0VDF9; -.
DR MassIVE; Q0VDF9; -.
DR MaxQB; Q0VDF9; -.
DR PaxDb; Q0VDF9; -.
DR PeptideAtlas; Q0VDF9; -.
DR PRIDE; Q0VDF9; -.
DR ProteomicsDB; 58825; -.
DR Antibodypedia; 37843; 146 antibodies from 28 providers.
DR DNASU; 51182; -.
DR Ensembl; ENST00000378372.8; ENSP00000367623.3; ENSG00000187522.16.
DR GeneID; 51182; -.
DR KEGG; hsa:51182; -.
DR MANE-Select; ENST00000378372.8; ENSP00000367623.3; NM_016299.4; NP_057383.2.
DR UCSC; uc001inf.5; human.
DR CTD; 51182; -.
DR DisGeNET; 51182; -.
DR GeneCards; HSPA14; -.
DR HGNC; HGNC:29526; HSPA14.
DR HPA; ENSG00000187522; Low tissue specificity.
DR MIM; 610369; gene.
DR neXtProt; NX_Q0VDF9; -.
DR OpenTargets; ENSG00000187522; -.
DR PharmGKB; PA134979057; -.
DR VEuPathDB; HostDB:ENSG00000187522; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000156380; -.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; Q0VDF9; -.
DR OMA; YIKESKC; -.
DR OrthoDB; 646813at2759; -.
DR PhylomeDB; Q0VDF9; -.
DR TreeFam; TF105045; -.
DR PathwayCommons; Q0VDF9; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; Q0VDF9; -.
DR BioGRID-ORCS; 51182; 282 hits in 1089 CRISPR screens.
DR ChiTaRS; HSPA14; human.
DR GeneWiki; HSPA14; -.
DR GenomeRNAi; 51182; -.
DR Pharos; Q0VDF9; Tbio.
DR PRO; PR:Q0VDF9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q0VDF9; protein.
DR Bgee; ENSG00000187522; Expressed in secondary oocyte and 192 other tissues.
DR ExpressionAtlas; Q0VDF9; baseline and differential.
DR Genevisible; Q0VDF9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; 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:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
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 GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd10238; HSPA14-like_NBD; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR042049; HSPA14_NBD.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..509
FT /note="Heat shock 70 kDa protein 14"
FT /id="PRO_0000289946"
FT VARIANT 85
FT /note="A -> V (in a breast cancer sample; somatic mutation;
FT dbSNP:rs374837716)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036347"
FT CONFLICT 6
FT /note="V -> A (in Ref. 3; BAF85012)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="V -> E (in Ref. 1; AAF66640)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="L -> P (in Ref. 2; AAF17198)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="I -> L (in Ref. 2; AAF17198)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="D -> G (in Ref. 3; BAF85012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 54794 MW; C3B685C7192B95C3 CRC64;
MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI
SNTVMKVKQI LGRSSSDPQA QKYIAESKCL VIEKNGKLRY EIDTGEETKF VNPEDVARLI
FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY
GIGQDSPTGK SNILVFKLGG TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA
SEFQRSFKHD VRGNARAMMK LTNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF
ELLCSPLFNK CIEAIRGLLD QNGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVELLNS
IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT
PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL
TMKRDGSLHV TCTDQETGKC EAISIEIAS
