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Q0VDF9 (HSP7E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock 70 kDa protein 14
Alternative name(s):
HSP70-like protein 1
Heat shock protein HSP60
Gene names
Name:HSPA14
Synonyms:HSP60, HSP70L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. Ref.9

Subunit structure

Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2. Ref.9

Subcellular location

Cytoplasmcytosol Ref.9.

Miscellaneous

Acts as a potent immunoadjuvant, capable to interact with antigen-presenting cells and generating efficient CD8+ T-cell responses. May be used as adjuvant to enhance effect of vaccine G1F/M2, a candidate vaccine against respiratory syncytial virus (RSV), a major respiratory pathogen in newborns (Ref.11). May also be used as adjuvant to prepare antigenic fusion protein for the therapeutics of cancers (Ref.8).

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' cotranslational protein folding

Traceable author statement Ref.9. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Heat shock 70 kDa protein 14
PRO_0000289946

Natural variations

Natural variant851A → V in a breast cancer sample; somatic mutation. Ref.14
VAR_036347

Experimental info

Sequence conflict61V → A in BAF85012. Ref.3
Sequence conflict151V → E in AAF66640. Ref.1
Sequence conflict2821L → P in AAF17198. Ref.2
Sequence conflict3121I → L in AAF17198. Ref.2
Sequence conflict3501D → G in BAF85012. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q0VDF9 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: C3B685C7192B95C3

FASTA50954,794
        10         20         30         40         50         60 
MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI 

        70         80         90        100        110        120 
SNTVMKVKQI LGRSSSDPQA QKYIAESKCL VIEKNGKLRY EIDTGEETKF VNPEDVARLI 

       130        140        150        160        170        180 
FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY 

       190        200        210        220        230        240 
GIGQDSPTGK SNILVFKLGG TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA 

       250        260        270        280        290        300 
SEFQRSFKHD VRGNARAMMK LTNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF 

       310        320        330        340        350        360 
ELLCSPLFNK CIEAIRGLLD QNGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVELLNS 

       370        380        390        400        410        420 
IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT 

       430        440        450        460        470        480 
PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL 

       490        500 
TMKRDGSLHV TCTDQETGKC EAISIEIAS 

« Hide

References

« Hide 'large scale' references
[1]"Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant."
Wan T., Zhou X., Chen G., An H., Chen T., Zhang W., Liu S., Jiang Y., Yang F., Wu Y., Cao X.
Blood 103:1747-1754(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Hsp70-like protein 1 fusion protein enhances induction of carcinoembryonic antigen-specific CD8+ CTL response by dendritic cell vaccine."
Wu Y., Wan T., Zhou X., Wang B., Yang F., Li N., Chen G., Dai S., Liu S., Zhang M., Cao X.
Cancer Res. 65:4947-4954(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IMMUNOADJUVANT ABILITY.
[9]"The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex."
Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P., Rucknagel P., Stahl J., Rospert S.
Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, INTERACTION WITH DNAJC2.
[10]"Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous."
Hundley H.A., Walter W., Bairstow S., Craig E.A.
Science 308:1032-1034(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[11]"Protective effect of a RSV subunit vaccine candidate G1F/M2 was enhanced by a HSP70-Like protein in mice."
Zeng R., Zhang Z., Mei X., Gong W., Wei L.
Biochem. Biophys. Res. Commun. 377:495-499(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IMMUNOADJUVANT ABILITY.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-85.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF143723 mRNA. Translation: AAF66640.1.
AF112210 mRNA. Translation: AAF17198.1.
AK292323 mRNA. Translation: BAF85012.1.
EF444968 Genomic DNA. Translation: ACA05969.1.
EF444968 Genomic DNA. Translation: ACA05970.1.
AC069544 Genomic DNA. No translation available.
CH471072 Genomic DNA. Translation: EAW86258.1.
BC119690 mRNA. Translation: AAI19691.1.
RefSeqNP_057383.2. NM_016299.3.
UniGeneHs.534169.
Hs.736996.

3D structure databases

ProteinModelPortalQ0VDF9.
SMRQ0VDF9. Positions 3-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119358. 7 interactions.
IntActQ0VDF9. 1 interaction.
STRING9606.ENSP00000367623.

PTM databases

PhosphoSiteQ0VDF9.

Polymorphism databases

DMDM121948121.

Proteomic databases

PaxDbQ0VDF9.
PeptideAtlasQ0VDF9.
PRIDEQ0VDF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378372; ENSP00000367623; ENSG00000187522.
GeneID51182.
KEGGhsa:51182.
UCSCuc001inf.4. human.

Organism-specific databases

CTD51182.
GeneCardsGC10P014790.
H-InvDBHIX0008667.
HGNCHGNC:29526. HSPA14.
HPAHPA046180.
MIM610369. gene.
neXtProtNX_Q0VDF9.
PharmGKBPA134979057.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
HOVERGENHBG099873.
InParanoidQ0VDF9.
OMASLMIECS.
OrthoDBEOG73804J.
PhylomeDBQ0VDF9.
TreeFamTF105045.

Gene expression databases

ArrayExpressQ0VDF9.
BgeeQ0VDF9.
CleanExHS_HSPA14.
GenevestigatorQ0VDF9.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA14. human.
GeneWikiHSPA14.
GenomeRNAi51182.
NextBio54151.
PROQ0VDF9.
SOURCESearch...

Entry information

Entry nameHSP7E_HUMAN
AccessionPrimary (citable) accession number: Q0VDF9
Secondary accession number(s): A8K8F8 expand/collapse secondary AC list , B0YIY9, Q9P0X2, Q9UI07
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM