Full text data of HSPA14
HSPA14
(HSP60, HSP70L1)
[Confidence: low (only semi-automatic identification from reviews)]
Heat shock 70 kDa protein 14 (HSP70-like protein 1; Heat shock protein HSP60)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heat shock 70 kDa protein 14 (HSP70-like protein 1; Heat shock protein HSP60)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q0VDF9
ID HSP7E_HUMAN Reviewed; 509 AA.
AC Q0VDF9; A8K8F8; B0YIY9; Q9P0X2; Q9UI07;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-SEP-2006, sequence version 1.
DT 22-JAN-2014, entry version 65.
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 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].
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.,
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 [14]
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 RefSeq; NP_057383.2; NM_016299.3.
DR UniGene; Hs.534169; -.
DR UniGene; Hs.736996; -.
DR ProteinModelPortal; Q0VDF9; -.
DR SMR; Q0VDF9; 3-505.
DR IntAct; Q0VDF9; 1.
DR STRING; 9606.ENSP00000367623; -.
DR PhosphoSite; Q0VDF9; -.
DR DMDM; 121948121; -.
DR PaxDb; Q0VDF9; -.
DR PeptideAtlas; Q0VDF9; -.
DR PRIDE; Q0VDF9; -.
DR Ensembl; ENST00000378372; ENSP00000367623; ENSG00000187522.
DR GeneID; 51182; -.
DR KEGG; hsa:51182; -.
DR UCSC; uc001inf.4; human.
DR CTD; 51182; -.
DR GeneCards; GC10P014790; -.
DR H-InvDB; HIX0008667; -.
DR HGNC; HGNC:29526; HSPA14.
DR HPA; HPA046180; -.
DR MIM; 610369; gene.
DR neXtProt; NX_Q0VDF9; -.
DR PharmGKB; PA134979057; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG099873; -.
DR InParanoid; Q0VDF9; -.
DR OMA; SLMIECS; -.
DR OrthoDB; EOG73804J; -.
DR PhylomeDB; Q0VDF9; -.
DR ChiTaRS; HSPA14; human.
DR GeneWiki; HSPA14; -.
DR GenomeRNAi; 51182; -.
DR NextBio; 54151; -.
DR PRO; PR:Q0VDF9; -.
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:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
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
//
ID HSP7E_HUMAN Reviewed; 509 AA.
AC Q0VDF9; A8K8F8; B0YIY9; Q9P0X2; Q9UI07;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-SEP-2006, sequence version 1.
DT 22-JAN-2014, entry version 65.
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 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].
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.,
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 [14]
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 RefSeq; NP_057383.2; NM_016299.3.
DR UniGene; Hs.534169; -.
DR UniGene; Hs.736996; -.
DR ProteinModelPortal; Q0VDF9; -.
DR SMR; Q0VDF9; 3-505.
DR IntAct; Q0VDF9; 1.
DR STRING; 9606.ENSP00000367623; -.
DR PhosphoSite; Q0VDF9; -.
DR DMDM; 121948121; -.
DR PaxDb; Q0VDF9; -.
DR PeptideAtlas; Q0VDF9; -.
DR PRIDE; Q0VDF9; -.
DR Ensembl; ENST00000378372; ENSP00000367623; ENSG00000187522.
DR GeneID; 51182; -.
DR KEGG; hsa:51182; -.
DR UCSC; uc001inf.4; human.
DR CTD; 51182; -.
DR GeneCards; GC10P014790; -.
DR H-InvDB; HIX0008667; -.
DR HGNC; HGNC:29526; HSPA14.
DR HPA; HPA046180; -.
DR MIM; 610369; gene.
DR neXtProt; NX_Q0VDF9; -.
DR PharmGKB; PA134979057; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG099873; -.
DR InParanoid; Q0VDF9; -.
DR OMA; SLMIECS; -.
DR OrthoDB; EOG73804J; -.
DR PhylomeDB; Q0VDF9; -.
DR ChiTaRS; HSPA14; human.
DR GeneWiki; HSPA14; -.
DR GenomeRNAi; 51182; -.
DR NextBio; 54151; -.
DR PRO; PR:Q0VDF9; -.
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:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
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
//
MIM
610369
*RECORD*
*FIELD* NO
610369
*FIELD* TI
*610369 HEAT-SHOCK 70-KD PROTEIN 14; HSPA14
;;HSP70-LIKE 1; HSP70L1
*FIELD* TX
CLONING
read more
By sequencing a human dendritic cell cDNA library, Wan et al. (2004)
obtained a full-length cDNA encoding HSPA14, which they called HSP70L1.
The deduced 509-amino acid protein has a calculated molecular mass of
54.8 kD. It has an N-terminal ATPase domain and 2 potential
N-glycosylation sites. Northern blot analysis detected a 2.1-kb
transcript in all tissues examined, with highest levels in testis,
spleen, and thymus. RT-PCR detected HSP70L1 expression in various cell
lines, with highest levels in immune cells.
GENE FUNCTION
Wan et al. (2004) transfected HeLa cells with HSP70L1 and found that
HSP70L1 expression was upregulated by heat stress, TNF-alpha (191160),
and phorbol esters. HSP70L1 interacted with human dendritic cells (DCs),
resulting in DC maturation and activation. Although HSP70L1 shared
common cell surface receptors with HSP70 (HSPA1A; 140550), including
TLR2 (603028) and TLR4 (603030), there were functional differences
between the 2 proteins. HSP70L1 and HSP70 stimulated DC secretion of the
proinflammatory cytokines IL1B (147720) and TNF-alpha at comparable
levels, but HSP70L1 was a more potent stimulator of IL12p70 (see
161560). HSP70L1 induced secretion of the chemokines MIP1A (CCL3;
182283), MIP1B (CCL4; 182284), and RANTES (CCL5; 187011) and expression
of the chemokine receptors CCR7 (600242) and CXCR4 (162643) more
potently than HSP70. In addition, HSP70L1, but not HSP70, could induce
IP10 (CXCL10; 147310) secretion.
Otto et al. (2005) found that MPP11 and HSP70L1 formed a complex in HeLa
cells, rat liver, and rabbit reticulate lysate. The 2 proteins coeluted
on cation and anion exchange columns, and sucrose density gradients
showed that they comigrated with polysomes and ribosomes. The 200-kD
dimeric ribosome-associated complex (RAC) formed by MPP11 and HSP70L1
was sensitive to salt treatment and could rescue growth defects in yeast
strains lacking functional RAC.
MAPPING
By genomic sequence analysis, Wan et al. (2004) mapped the HSPA14 gene
to chromosome 10p12.33.
*FIELD* RF
1. Otto, H.; Conz, C.; Maier, P.; Wolfle, T.; Suzuki, C. K.; Jeno,
P.; Rucknagel, P.; Stahl, J.; Rospert, S.: The chaperones MPP11 and
Hsp70L1 form the mammalian ribosome-associated complex. Proc. Nat.
Acad. Sci. 102: 10064-10069, 2005.
2. Wan, T.; Zhou, X.; Chen, G.; An, H.; Chen, T.; Zhang, W.; Liu,
S.; Jiang, Y.; Yang, F.; Wu, Y.; Cao, X.: Novel heat shock protein
Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant. Blood 103:
1747-1754, 2004.
*FIELD* CD
Patricia A. Hartz: 9/1/2006
*FIELD* ED
mgross: 09/01/2006
mgross: 9/1/2006
*RECORD*
*FIELD* NO
610369
*FIELD* TI
*610369 HEAT-SHOCK 70-KD PROTEIN 14; HSPA14
;;HSP70-LIKE 1; HSP70L1
*FIELD* TX
CLONING
read more
By sequencing a human dendritic cell cDNA library, Wan et al. (2004)
obtained a full-length cDNA encoding HSPA14, which they called HSP70L1.
The deduced 509-amino acid protein has a calculated molecular mass of
54.8 kD. It has an N-terminal ATPase domain and 2 potential
N-glycosylation sites. Northern blot analysis detected a 2.1-kb
transcript in all tissues examined, with highest levels in testis,
spleen, and thymus. RT-PCR detected HSP70L1 expression in various cell
lines, with highest levels in immune cells.
GENE FUNCTION
Wan et al. (2004) transfected HeLa cells with HSP70L1 and found that
HSP70L1 expression was upregulated by heat stress, TNF-alpha (191160),
and phorbol esters. HSP70L1 interacted with human dendritic cells (DCs),
resulting in DC maturation and activation. Although HSP70L1 shared
common cell surface receptors with HSP70 (HSPA1A; 140550), including
TLR2 (603028) and TLR4 (603030), there were functional differences
between the 2 proteins. HSP70L1 and HSP70 stimulated DC secretion of the
proinflammatory cytokines IL1B (147720) and TNF-alpha at comparable
levels, but HSP70L1 was a more potent stimulator of IL12p70 (see
161560). HSP70L1 induced secretion of the chemokines MIP1A (CCL3;
182283), MIP1B (CCL4; 182284), and RANTES (CCL5; 187011) and expression
of the chemokine receptors CCR7 (600242) and CXCR4 (162643) more
potently than HSP70. In addition, HSP70L1, but not HSP70, could induce
IP10 (CXCL10; 147310) secretion.
Otto et al. (2005) found that MPP11 and HSP70L1 formed a complex in HeLa
cells, rat liver, and rabbit reticulate lysate. The 2 proteins coeluted
on cation and anion exchange columns, and sucrose density gradients
showed that they comigrated with polysomes and ribosomes. The 200-kD
dimeric ribosome-associated complex (RAC) formed by MPP11 and HSP70L1
was sensitive to salt treatment and could rescue growth defects in yeast
strains lacking functional RAC.
MAPPING
By genomic sequence analysis, Wan et al. (2004) mapped the HSPA14 gene
to chromosome 10p12.33.
*FIELD* RF
1. Otto, H.; Conz, C.; Maier, P.; Wolfle, T.; Suzuki, C. K.; Jeno,
P.; Rucknagel, P.; Stahl, J.; Rospert, S.: The chaperones MPP11 and
Hsp70L1 form the mammalian ribosome-associated complex. Proc. Nat.
Acad. Sci. 102: 10064-10069, 2005.
2. Wan, T.; Zhou, X.; Chen, G.; An, H.; Chen, T.; Zhang, W.; Liu,
S.; Jiang, Y.; Yang, F.; Wu, Y.; Cao, X.: Novel heat shock protein
Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant. Blood 103:
1747-1754, 2004.
*FIELD* CD
Patricia A. Hartz: 9/1/2006
*FIELD* ED
mgross: 09/01/2006
mgross: 9/1/2006