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Q0VDF9

- HSP7E_HUMAN

UniProt

Q0VDF9 - HSP7E_HUMAN

Protein

Heat shock 70 kDa protein 14

Gene

HSPA14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. 'de novo' cotranslational protein folding Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock 70 kDa protein 14
    Alternative name(s):
    HSP70-like protein 1
    Heat shock protein HSP60
    Gene namesi
    Name:HSPA14
    Synonyms:HSP60, HSP70L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:29526. HSPA14.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134979057.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 509509Heat shock 70 kDa protein 14PRO_0000289946Add
    BLAST

    Proteomic databases

    MaxQBiQ0VDF9.
    PaxDbiQ0VDF9.
    PeptideAtlasiQ0VDF9.
    PRIDEiQ0VDF9.

    PTM databases

    PhosphoSiteiQ0VDF9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ0VDF9.
    BgeeiQ0VDF9.
    CleanExiHS_HSPA14.
    GenevestigatoriQ0VDF9.

    Organism-specific databases

    HPAiHPA046180.

    Interactioni

    Subunit structurei

    Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2.1 Publication

    Protein-protein interaction databases

    BioGridi119358. 7 interactions.
    IntActiQ0VDF9. 1 interaction.
    STRINGi9606.ENSP00000367623.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0VDF9.
    SMRiQ0VDF9. Positions 3-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOGENOMiHOG000228135.
    HOVERGENiHBG099873.
    InParanoidiQ0VDF9.
    OMAiSLMIECS.
    OrthoDBiEOG73804J.
    PhylomeDBiQ0VDF9.
    TreeFamiTF105045.

    Family and domain databases

    Gene3Di2.60.34.10. 1 hit.
    InterProiIPR018181. Heat_shock_70_CS.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view]
    PfamiPF00012. HSP70. 1 hit.
    [Graphical view]
    PRINTSiPR00301. HEATSHOCK70.
    SUPFAMiSSF100920. SSF100920. 1 hit.
    PROSITEiPS01036. HSP70_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q0VDF9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL    50
    AAKQSRIRNI SNTVMKVKQI LGRSSSDPQA QKYIAESKCL VIEKNGKLRY 100
    EIDTGEETKF VNPEDVARLI FSKMKETAHS VLGSDANDVV ITVPFDFGEK 150
    QKNALGEAAR AAGFNVLRLI HEPSAALLAY GIGQDSPTGK SNILVFKLGG 200
    TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA SEFQRSFKHD 250
    VRGNARAMMK LTNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF 300
    ELLCSPLFNK CIEAIRGLLD QNGFTADDIN KVVLCGGSSR IPKLQQLIKD 350
    LFPAVELLNS IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL 400
    VKGVDESGAS RFTVLFPSGT PLPARRQHTL QAPGSISSVC LELYESDGKN 450
    SAKEETKFAQ VVLQDLDKKE NGLRDILAVL TMKRDGSLHV TCTDQETGKC 500
    EAISIEIAS 509
    Length:509
    Mass (Da):54,794
    Last modified:September 5, 2006 - v1
    Checksum:iC3B685C7192B95C3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61V → A in BAF85012. (PubMed:14702039)Curated
    Sequence conflicti15 – 151V → E in AAF66640. (PubMed:14592822)Curated
    Sequence conflicti282 – 2821L → P in AAF17198. (PubMed:10931946)Curated
    Sequence conflicti312 – 3121I → L in AAF17198. (PubMed:10931946)Curated
    Sequence conflicti350 – 3501D → G in BAF85012. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851A → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036347

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS7103.1.
    RefSeqiNP_057383.2. NM_016299.3.
    UniGeneiHs.534169.
    Hs.736996.

    Genome annotation databases

    EnsembliENST00000378372; ENSP00000367623; ENSG00000187522.
    GeneIDi51182.
    KEGGihsa:51182.
    UCSCiuc001inf.4. human.

    Polymorphism databases

    DMDMi121948121.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS7103.1.
    RefSeqi NP_057383.2. NM_016299.3.
    UniGenei Hs.534169.
    Hs.736996.

    3D structure databases

    ProteinModelPortali Q0VDF9.
    SMRi Q0VDF9. Positions 3-505.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119358. 7 interactions.
    IntActi Q0VDF9. 1 interaction.
    STRINGi 9606.ENSP00000367623.

    PTM databases

    PhosphoSitei Q0VDF9.

    Polymorphism databases

    DMDMi 121948121.

    Proteomic databases

    MaxQBi Q0VDF9.
    PaxDbi Q0VDF9.
    PeptideAtlasi Q0VDF9.
    PRIDEi Q0VDF9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378372 ; ENSP00000367623 ; ENSG00000187522 .
    GeneIDi 51182.
    KEGGi hsa:51182.
    UCSCi uc001inf.4. human.

    Organism-specific databases

    CTDi 51182.
    GeneCardsi GC10P014790.
    H-InvDB HIX0008667.
    HGNCi HGNC:29526. HSPA14.
    HPAi HPA046180.
    MIMi 610369. gene.
    neXtProti NX_Q0VDF9.
    PharmGKBi PA134979057.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0443.
    HOGENOMi HOG000228135.
    HOVERGENi HBG099873.
    InParanoidi Q0VDF9.
    OMAi SLMIECS.
    OrthoDBi EOG73804J.
    PhylomeDBi Q0VDF9.
    TreeFami TF105045.

    Miscellaneous databases

    ChiTaRSi HSPA14. human.
    GeneWikii HSPA14.
    GenomeRNAii 51182.
    NextBioi 54151.
    PROi Q0VDF9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q0VDF9.
    Bgeei Q0VDF9.
    CleanExi HS_HSPA14.
    Genevestigatori Q0VDF9.

    Family and domain databases

    Gene3Di 2.60.34.10. 1 hit.
    InterProi IPR018181. Heat_shock_70_CS.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view ]
    Pfami PF00012. HSP70. 1 hit.
    [Graphical view ]
    PRINTSi PR00301. HEATSHOCK70.
    SUPFAMi SSF100920. SSF100920. 1 hit.
    PROSITEi PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-85.

    Entry informationi

    Entry nameiHSP7E_HUMAN
    AccessioniPrimary (citable) accession number: Q0VDF9
    Secondary accession number(s): A8K8F8
    , B0YIY9, Q9P0X2, Q9UI07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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 (PubMed:18851947). May also be used as adjuvant to prepare antigenic fusion protein for the therapeutics of cancers (PubMed:15930317).2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3