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   14-DEC-2011, entry version 49.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   as a Th1 polarizing adjuvant.";
RL   Blood 103:1747-1754(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal gland;
RX   MEDLINE=20402571; 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.,
RA   Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA   Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA   Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT   axis 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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.,
RA   Liu S., Zhang M., Cao X.;
RT   "Hsp70-like protein 1 fusion protein enhances induction of
RT   carcinoembryonic antigen-specific CD8+ CTL response by dendritic cell
RT   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.,
RA   Rucknagel P., Stahl J., Rospert S.;
RT   "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-
RT   associated 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
RT   enhanced 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].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., 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   [13]
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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Component of the ribosome-associated complex (RAC), a
CC       complex involved in folding or maintaining nascent polypeptides in
CC       a folding-competent state. In the RAC complex, binds to the
CC       nascent polypeptide chain, while DNAJC2 stimulates its ATPase
CC       activity.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC), a
CC       heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and
CC       Hsp40/DnaJ-type chaperone DNAJC2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC   -!- MISCELLANEOUS: Acts as a potent immunoadjuvant, capable to
CC       interact with antigen-presenting cells and generating efficient
CC       CD8(+) T-cell responses. May be used as adjuvant to enhance effect
CC       of vaccine G1F/M2, a candidate vaccine against respiratory
CC       syncytial virus (RSV), a major respiratory pathogen in newborns
CC       (PubMed:18851947). May also be used as adjuvant to prepare
CC       antigenic fusion protein for the therapeutics of cancers
CC       (PubMed:15930317).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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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   IPI; IPI00292499; -.
DR   RefSeq; NP_057383.2; NM_016299.2.
DR   UniGene; Hs.534169; -.
DR   ProteinModelPortal; Q0VDF9; -.
DR   SMR; Q0VDF9; 1-508.
DR   STRING; Q0VDF9; -.
DR   PhosphoSite; Q0VDF9; -.
DR   DMDM; 121948121; -.
DR   PeptideAtlas; Q0VDF9; -.
DR   PRIDE; Q0VDF9; -.
DR   Ensembl; ENST00000378372; ENSP00000367623; ENSG00000187522.
DR   GeneID; 51182; -.
DR   KEGG; hsa:51182; -.
DR   NMPDR; fig|9606.3.peg.3580; -.
DR   UCSC; uc001inf.1; human.
DR   CTD; 51182; -.
DR   GeneCards; GC10P014790; -.
DR   H-InvDB; HIX0008667; -.
DR   HGNC; HGNC:29526; HSPA14.
DR   MIM; 610369; gene.
DR   neXtProt; NX_Q0VDF9; -.
DR   PharmGKB; PA134979057; -.
DR   GeneTree; ENSGT00600000084505; -.
DR   HOGENOM; HBG334976; -.
DR   HOVERGEN; HBG099873; -.
DR   InParanoid; Q0VDF9; -.
DR   OMA; FDFGEKQ; -.
DR   OrthoDB; EOG4S7JPV; -.
DR   PhylomeDB; Q0VDF9; -.
DR   NextBio; 54151; -.
DR   ArrayExpress; Q0VDF9; -.
DR   Bgee; Q0VDF9; -.
DR   CleanEx; HS_HSPA14; -.
DR   Genevestigator; Q0VDF9; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR   PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Polymorphism; Reference proteome.
FT   CHAIN         1    509       Heat shock 70 kDa protein 14.
FT                                /FTId=PRO_0000289946.
FT   VARIANT      85     85       A -> V (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036347.
FT   CONFLICT      6      6       V -> A (in Ref. 3; BAF85012).
FT   CONFLICT     15     15       V -> E (in Ref. 1; AAF66640).
FT   CONFLICT    282    282       L -> P (in Ref. 2; AAF17198).
FT   CONFLICT    312    312       I -> L (in Ref. 2; AAF17198).
FT   CONFLICT    350    350       D -> G (in Ref. 3; BAF85012).
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
//