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P34932

- HSP74_HUMAN

UniProt

P34932 - HSP74_HUMAN

Protein

Heat shock 70 kDa protein 4

Gene

HSPA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB

    GO - Biological processi

    1. chaperone-mediated protein complex assembly Source: BHF-UCL
    2. protein import into mitochondrial outer membrane Source: BHF-UCL
    3. response to unfolded protein Source: UniProtKB

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock 70 kDa protein 4
    Alternative name(s):
    HSP70RY
    Heat shock 70-related protein APG-2
    Gene namesi
    Name:HSPA4
    Synonyms:APG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:5237. HSPA4.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: UniProt
    2. extracellular vesicular exosome Source: UniProtKB
    3. mitochondrion Source: GOC

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29503.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 840840Heat shock 70 kDa protein 4PRO_0000078262Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-acetyllysineBy similarity
    Modified residuei76 – 761Phosphoserine2 Publications
    Modified residuei89 – 891Phosphotyrosine1 Publication
    Modified residuei336 – 3361Phosphotyrosine2 Publications
    Modified residuei430 – 4301N6-acetyllysine1 Publication
    Modified residuei538 – 5381Phosphothreonine1 Publication
    Modified residuei546 – 5461Phosphoserine1 Publication
    Modified residuei660 – 6601PhosphotyrosineBy similarity
    Modified residuei679 – 6791N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP34932.
    PaxDbiP34932.
    PRIDEiP34932.

    2D gel databases

    DOSAC-COBS-2DPAGEP34932.
    REPRODUCTION-2DPAGEIPI00002966.
    P34932.

    PTM databases

    PhosphoSiteiP34932.

    Expressioni

    Gene expression databases

    ArrayExpressiP34932.
    BgeeiP34932.
    CleanExiHS_HSPA4.
    GenevestigatoriP34932.

    Organism-specific databases

    HPAiCAB025529.
    HPA010023.

    Interactioni

    Subunit structurei

    Interacts with TJP1/ZO-1.By similarity

    Protein-protein interaction databases

    BioGridi109540. 277 interactions.
    DIPiDIP-460N.
    IntActiP34932. 25 interactions.
    MINTiMINT-1159519.
    STRINGi9606.ENSP00000302961.

    Structurei

    3D structure databases

    ProteinModelPortaliP34932.
    SMRiP34932. Positions 5-697.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOGENOMiHOG000228138.
    HOVERGENiHBG047955.
    InParanoidiP34932.
    KOiK09489.
    OMAiKVKYMEE.
    OrthoDBiEOG77M8N0.
    PhylomeDBiP34932.
    TreeFamiTF105043.

    Family and domain databases

    Gene3Di1.20.1270.10. 2 hits.
    2.60.34.10. 2 hits.
    InterProiIPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view]
    PfamiPF00012. HSP70. 1 hit.
    [Graphical view]
    PRINTSiPR00301. HEATSHOCK70.
    SUPFAMiSSF100920. SSF100920. 2 hits.
    SSF100934. SSF100934. 2 hits.
    PROSITEiPS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P34932-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA    50
    AAKSQVISNA KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG 100
    IKVTYMEEER NFTTEQVTAM LLSKLKETAE SVLKKPVVDC VVSVPCFYTD 150
    AERRSVMDAT QIAGLNCLRL MNETTAVALA YGIYKQDLPA LEEKPRNVVF 200
    VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL VNHFCEEFGK 250
    KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT 300
    MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV 350
    KEKISKFFGK ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY 400
    PISLRWNSPA EEGSSDCEVF SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ 450
    DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV KVRVNVHGIF SVSSASLVEV 500
    HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA ENKAESEEME 550
    TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN 600
    EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL 650
    KLEDTENWLY EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE 700
    ELGKQIQQYM KIISSFKNKE DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN 750
    LQNKQSLTMD PVVKSKEIEA KIKELTSTCS PIISKPKPKV EPPKEEQKNA 800
    EQNGPVDGQG DNPGPQAAEQ GTDTAVPSDS DKKLPEMDID 840
    Length:840
    Mass (Da):94,331
    Last modified:September 23, 2008 - v4
    Checksum:i8B690A52A0729C2A
    GO

    Sequence cautioni

    The sequence AAA02807.1 differs from that shown. Reason: Frameshift at positions 567, 586, 697, 715 and 722.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941L → W in AAA02807. (PubMed:8335910)Curated
    Sequence conflicti190 – 1901A → R in AAA02807. (PubMed:8335910)Curated
    Sequence conflicti583 – 5864NQLL → ESAI in AAA02807. (PubMed:8335910)Curated
    Sequence conflicti622 – 6221E → R in BAA75062. 1 PublicationCurated
    Sequence conflicti644 – 6441D → G in BAA75062. 1 PublicationCurated
    Sequence conflicti746 – 7494NNKL → EVTP in AAA02807. (PubMed:8335910)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023420 mRNA. Translation: BAA75062.1.
    AC113410 Genomic DNA. No translation available.
    BC110861 mRNA. Translation: AAI10862.1.
    BC126122 mRNA. Translation: AAI26123.1.
    BC126124 mRNA. Translation: AAI26125.1.
    L12723 mRNA. Translation: AAA02807.1. Frameshift.
    CCDSiCCDS4166.1.
    PIRiI56208.
    RefSeqiNP_002145.3. NM_002154.3.
    UniGeneiHs.90093.

    Genome annotation databases

    EnsembliENST00000304858; ENSP00000302961; ENSG00000170606.
    GeneIDi3308.
    KEGGihsa:3308.
    UCSCiuc003kyj.3. human.

    Polymorphism databases

    DMDMi206729934.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023420 mRNA. Translation: BAA75062.1 .
    AC113410 Genomic DNA. No translation available.
    BC110861 mRNA. Translation: AAI10862.1 .
    BC126122 mRNA. Translation: AAI26123.1 .
    BC126124 mRNA. Translation: AAI26125.1 .
    L12723 mRNA. Translation: AAA02807.1 . Frameshift.
    CCDSi CCDS4166.1.
    PIRi I56208.
    RefSeqi NP_002145.3. NM_002154.3.
    UniGenei Hs.90093.

    3D structure databases

    ProteinModelPortali P34932.
    SMRi P34932. Positions 5-697.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109540. 277 interactions.
    DIPi DIP-460N.
    IntActi P34932. 25 interactions.
    MINTi MINT-1159519.
    STRINGi 9606.ENSP00000302961.

    PTM databases

    PhosphoSitei P34932.

    Polymorphism databases

    DMDMi 206729934.

    2D gel databases

    DOSAC-COBS-2DPAGE P34932.
    REPRODUCTION-2DPAGE IPI00002966.
    P34932.

    Proteomic databases

    MaxQBi P34932.
    PaxDbi P34932.
    PRIDEi P34932.

    Protocols and materials databases

    DNASUi 3308.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304858 ; ENSP00000302961 ; ENSG00000170606 .
    GeneIDi 3308.
    KEGGi hsa:3308.
    UCSCi uc003kyj.3. human.

    Organism-specific databases

    CTDi 3308.
    GeneCardsi GC05P132415.
    HGNCi HGNC:5237. HSPA4.
    HPAi CAB025529.
    HPA010023.
    MIMi 601113. gene.
    neXtProti NX_P34932.
    PharmGKBi PA29503.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0443.
    HOGENOMi HOG000228138.
    HOVERGENi HBG047955.
    InParanoidi P34932.
    KOi K09489.
    OMAi KVKYMEE.
    OrthoDBi EOG77M8N0.
    PhylomeDBi P34932.
    TreeFami TF105043.

    Miscellaneous databases

    ChiTaRSi HSPA4. human.
    GeneWikii HSPA4.
    GenomeRNAii 3308.
    NextBioi 13119.
    PROi P34932.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P34932.
    Bgeei P34932.
    CleanExi HS_HSPA4.
    Genevestigatori P34932.

    Family and domain databases

    Gene3Di 1.20.1270.10. 2 hits.
    2.60.34.10. 2 hits.
    InterProi IPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view ]
    Pfami PF00012. HSP70. 1 hit.
    [Graphical view ]
    PRINTSi PR00301. HEATSHOCK70.
    SUPFAMi SSF100920. SSF100920. 2 hits.
    SSF100934. SSF100934. 2 hits.
    PROSITEi PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of human apg-1 and apg-2, members of the hsp110 family, cDNAs and chromosomal assignment of the genes."
      Nonoguchi K., Fujita J.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Brain and Skin.
    4. "Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5."
      Fathallah D.M., Cherif D., Dellagi K., Arnaout M.A.
      J. Immunol. 151:810-813(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-749.
      Tissue: Lymphocyte.
    5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 20-33; 111-124; 170-185; 222-234; 333-346; 361-374 AND 391-422, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND TYR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430 AND LYS-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHSP74_HUMAN
    AccessioniPrimary (citable) accession number: P34932
    Secondary accession number(s): O95756, Q2TAL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3