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P54652

- HSP72_HUMAN

UniProt

P54652 - HSP72_HUMAN

Protein

Heat shock-related 70 kDa protein 2

Gene

HSPA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 164ATP
    Nucleotide bindingi205 – 2073ATP
    Nucleotide bindingi271 – 2788ATP
    Nucleotide bindingi342 – 3454ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: BHF-UCL
    3. glycolipid binding Source: Ensembl
    4. protein binding Source: IntAct
    5. unfolded protein binding Source: UniProt

    GO - Biological processi

    1. male meiosis Source: ProtInc
    2. male meiosis I Source: Ensembl
    3. negative regulation of inclusion body assembly Source: UniProt
    4. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle Source: Ensembl
    5. protein refolding Source: UniProt
    6. response to unfolded protein Source: ProtInc
    7. spermatid development Source: ProtInc
    8. synaptonemal complex disassembly Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_200624. Attenuation phase.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_75792. Meiotic synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock-related 70 kDa protein 2
    Short name:
    Heat shock 70 kDa protein 2
    Gene namesi
    Name:HSPA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:5235. HSPA2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. CatSper complex Source: UniProtKB
    3. cell surface Source: Ensembl
    4. cytosol Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. male germ cell nucleus Source: Ensembl
    7. membrane Source: UniProtKB
    8. mitochondrion Source: Ensembl
    9. nucleus Source: UniProt
    10. synaptonemal complex Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi564 – 5641K → A: Abolishes methylation by METTL21A. 1 Publication

    Organism-specific databases

    PharmGKBiPA29501.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 639639Heat shock-related 70 kDa protein 2PRO_0000078258Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei403 – 4031PhosphoserineBy similarity
    Modified residuei408 – 4081PhosphothreonineBy similarity
    Modified residuei414 – 4141PhosphothreonineBy similarity
    Modified residuei564 – 5641N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP54652.
    PaxDbiP54652.
    PeptideAtlasiP54652.
    PRIDEiP54652.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00007702.

    PTM databases

    PhosphoSiteiP54652.

    Expressioni

    Gene expression databases

    BgeeiP54652.
    CleanExiHS_HSPA2.
    GenevestigatoriP54652.

    Organism-specific databases

    HPAiHPA000798.

    Interactioni

    Subunit structurei

    Interacts with ZNF541. Component of the CatSper complex By similarity. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with FKBP6.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q96BE02EBI-356991,EBI-9356686
    BAG4O954292EBI-356991,EBI-2949658
    HSPBP1Q9NZL43EBI-356991,EBI-356763

    Protein-protein interaction databases

    BioGridi109538. 34 interactions.
    IntActiP54652. 25 interactions.
    MINTiMINT-1146083.
    STRINGi9606.ENSP00000247207.

    Structurei

    Secondary structure

    1
    639
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125
    Beta strandi14 – 2310
    Beta strandi26 – 294
    Beta strandi37 – 404
    Beta strandi43 – 453
    Beta strandi50 – 523
    Helixi54 – 585
    Turni59 – 624
    Helixi64 – 663
    Helixi71 – 733
    Turni74 – 763
    Helixi82 – 887
    Beta strandi92 – 987
    Beta strandi101 – 1088
    Beta strandi111 – 1155
    Helixi117 – 13620
    Beta strandi142 – 1476
    Helixi153 – 16614
    Beta strandi169 – 1757
    Helixi176 – 1838
    Turni184 – 1874
    Beta strandi191 – 1944
    Beta strandi197 – 2037
    Beta strandi208 – 2169
    Beta strandi219 – 22810
    Helixi233 – 25220
    Helixi260 – 27617
    Turni277 – 2793
    Beta strandi280 – 29112
    Beta strandi294 – 3018
    Helixi302 – 3087
    Helixi310 – 3156
    Helixi317 – 32711
    Helixi331 – 3333
    Beta strandi336 – 3416
    Helixi342 – 3454
    Helixi347 – 35610
    Turni357 – 3593
    Turni368 – 3703
    Helixi371 – 38313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I33X-ray1.30A6-386[»]
    4FSVX-ray1.80A2-387[»]
    ProteinModelPortaliP54652.
    SMRiP54652. Positions 3-613.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54652.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.
    InParanoidiP54652.
    KOiK03283.
    OMAiEAYLGCK.
    OrthoDBiEOG7PCJGF.
    PhylomeDBiP54652.
    TreeFamiTF105042.

    Family and domain databases

    Gene3Di1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    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. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEiPS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54652-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER    50
    LIGDAAKNQV AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG 100
    KPKVQVEYKG ETKTFFPEEI SSMVLTKMKE IAEAYLGGKV HSAVITVPAY 150
    FNDSQRQATK DAGTITGLNV LRIINEPTAA AIAYGLDKKG CAGGEKNVLI 200
    FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM VSHLAEEFKR 250
    KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI 300
    TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ 350
    KLLQDFFNGK ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT 400
    PLSLGIETAG GVMTPLIKRN TTIPTKQTQT FTTYSDNQSS VLVQVYEGER 450
    AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT FDIDANGILN VTAADKSTGK 500
    ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA AKNALESYTY 550
    NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK 600
    ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD 639
    Length:639
    Mass (Da):70,021
    Last modified:October 1, 1996 - v1
    Checksum:i3851755494E7B729
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141T → P in AAH36107. (PubMed:15489334)Curated
    Sequence conflicti54 – 541Missing in AAC50076. (PubMed:7849706)Curated
    Sequence conflicti80 – 801E → G in AAH36107. (PubMed:15489334)Curated
    Sequence conflicti266 – 2661L → S in AAD11466. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti191 – 1911C → S.1 Publication
    Corresponds to variant rs45456191 [ dbSNP | Ensembl ].
    VAR_032706
    Natural varianti496 – 4961K → E.1 Publication
    VAR_032707

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26336 Genomic DNA. Translation: AAA52698.1.
    U56725 mRNA. Translation: AAD11466.1.
    BT009815 mRNA. Translation: AAP88817.1.
    DQ489378 Genomic DNA. Translation: ABE96830.1.
    BC001752 mRNA. Translation: AAH01752.1.
    BC036107 mRNA. Translation: AAH36107.1.
    AH006615 Genomic DNA. Translation: AAC50076.1.
    CCDSiCCDS9766.1.
    PIRiA55719.
    I37564.
    RefSeqiNP_068814.2. NM_021979.3.
    UniGeneiHs.432648.

    Genome annotation databases

    EnsembliENST00000247207; ENSP00000247207; ENSG00000126803.
    ENST00000394709; ENSP00000378199; ENSG00000126803.
    GeneIDi3306.
    KEGGihsa:3306.
    UCSCiuc001xhj.3. human.

    Polymorphism databases

    DMDMi1708307.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26336 Genomic DNA. Translation: AAA52698.1 .
    U56725 mRNA. Translation: AAD11466.1 .
    BT009815 mRNA. Translation: AAP88817.1 .
    DQ489378 Genomic DNA. Translation: ABE96830.1 .
    BC001752 mRNA. Translation: AAH01752.1 .
    BC036107 mRNA. Translation: AAH36107.1 .
    AH006615 Genomic DNA. Translation: AAC50076.1 .
    CCDSi CCDS9766.1.
    PIRi A55719.
    I37564.
    RefSeqi NP_068814.2. NM_021979.3.
    UniGenei Hs.432648.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3I33 X-ray 1.30 A 6-386 [» ]
    4FSV X-ray 1.80 A 2-387 [» ]
    ProteinModelPortali P54652.
    SMRi P54652. Positions 3-613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109538. 34 interactions.
    IntActi P54652. 25 interactions.
    MINTi MINT-1146083.
    STRINGi 9606.ENSP00000247207.

    Chemistry

    ChEMBLi CHEMBL2062348.

    PTM databases

    PhosphoSitei P54652.

    Polymorphism databases

    DMDMi 1708307.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00007702.

    Proteomic databases

    MaxQBi P54652.
    PaxDbi P54652.
    PeptideAtlasi P54652.
    PRIDEi P54652.

    Protocols and materials databases

    DNASUi 3306.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247207 ; ENSP00000247207 ; ENSG00000126803 .
    ENST00000394709 ; ENSP00000378199 ; ENSG00000126803 .
    GeneIDi 3306.
    KEGGi hsa:3306.
    UCSCi uc001xhj.3. human.

    Organism-specific databases

    CTDi 3306.
    GeneCardsi GC14P065002.
    HGNCi HGNC:5235. HSPA2.
    HPAi HPA000798.
    MIMi 140560. gene.
    neXtProti NX_P54652.
    PharmGKBi PA29501.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0443.
    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.
    InParanoidi P54652.
    KOi K03283.
    OMAi EAYLGCK.
    OrthoDBi EOG7PCJGF.
    PhylomeDBi P54652.
    TreeFami TF105042.

    Enzyme and pathway databases

    Reactomei REACT_200624. Attenuation phase.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_75792. Meiotic synapsis.

    Miscellaneous databases

    ChiTaRSi HSPA2. human.
    EvolutionaryTracei P54652.
    GeneWikii HSPA2.
    GenomeRNAii 3306.
    NextBioi 13115.
    PROi P54652.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54652.
    CleanExi HS_HSPA2.
    Genevestigatori P54652.

    Family and domain databases

    Gene3Di 1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    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. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEi PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2)."
      Bonnycastle L.L.C., Yu C.-E., Hunt C.R., Trask B.J., Clancy K.P., Weber J.L., Patterson D., Schellenberg G.D.
      Genomics 23:85-93(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Goralski T.J., Krensky A.M.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. NIEHS SNPs program
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-191 AND GLU-496.
    5. "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 Eye.
    6. "A heat shock gene at 14q22: mapping and expression."
      Roux A.-F., Nguyen V.T.T., Squire J.A., Cox D.W.
      Hum. Mol. Genet. 3:1819-1822(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
    7. "FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes."
      Jarczowski F., Fischer G., Edlich F.
      Biochemistry 47:6946-6952(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FKBP6.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
      Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
      J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-564, MUTAGENESIS OF LYS-564.
    10. "Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
      Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
      PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 6-386 IN COMPLEX WITH ADP AND PHOSPHATE.

    Entry informationi

    Entry nameiHSP72_HUMAN
    AccessioniPrimary (citable) accession number: P54652
    Secondary accession number(s): Q15508, Q53XM3, Q9UE78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 138 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3