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P63017

- HSP7C_MOUSE

UniProt

P63017 - HSP7C_MOUSE

Protein

Heat shock cognate 71 kDa protein

Gene

Hspa8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex By similarity. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154ATPBy similarity
    Nucleotide bindingi202 – 2043ATPBy similarity
    Nucleotide bindingi268 – 2758ATPBy similarity
    Nucleotide bindingi339 – 3424ATPBy similarity

    GO - Molecular functioni

    1. ATPase activity, coupled Source: MGI
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. unfolded protein binding Source: MGI

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chaperone mediated protein folding requiring cofactor Source: MGI
    3. clathrin coat disassembly Source: MGI
    4. mRNA processing Source: UniProtKB-KW
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. protein folding Source: MGI
    7. regulation of cell cycle Source: MGI
    8. response to stress Source: UniProtKB-KW
    9. RNA splicing Source: UniProtKB-KW
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_213550. HSF1-dependent transactivation.
    REACT_222185. Regulation of HSF1-mediated heat shock response.
    REACT_223784. Attenuation phase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock cognate 71 kDa protein
    Alternative name(s):
    Heat shock 70 kDa protein 8
    Gene namesi
    Name:Hspa8
    Synonyms:Hsc70, Hsc73
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:105384. Hspa8.

    Subcellular locationi

    Cytoplasm By similarity. Melanosome By similarity. Nucleusnucleolus By similarity. Cell membrane By similarity
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. extracellular vesicular exosome Source: MGI
    3. intracellular Source: MGI
    4. melanosome Source: UniProtKB-SubCell
    5. nucleolus Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: UniProtKB-SubCell
    8. Prp19 complex Source: UniProtKB
    9. ribonucleoprotein complex Source: UniProtKB
    10. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 646645Heat shock cognate 71 kDa proteinPRO_0000078271Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei108 – 1081N6-acetyllysine1 Publication
    Modified residuei153 – 1531PhosphoserineBy similarity
    Modified residuei246 – 2461N6-acetyllysine1 Publication
    Modified residuei319 – 3191N6-acetyllysine; alternate1 Publication
    Modified residuei319 – 3191N6-succinyllysine; alternate1 Publication
    Modified residuei328 – 3281N6-acetyllysine1 Publication
    Modified residuei362 – 3621PhosphoserineBy similarity
    Modified residuei512 – 5121N6-acetyllysine; alternate1 Publication
    Modified residuei512 – 5121N6-succinyllysine; alternate1 Publication
    Modified residuei524 – 5241N6-acetyllysine1 Publication
    Modified residuei561 – 5611N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A; alternateBy similarity
    Modified residuei589 – 5891N6-acetyllysineBy similarity
    Modified residuei597 – 5971N6-acetyllysineBy similarity
    Modified residuei601 – 6011N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylated.By similarity
    ISGylated.1 Publication
    Trimethylation at Lys-561 reduces fibrillar SNCA binding.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP63017.
    PaxDbiP63017.
    PRIDEiP63017.

    2D gel databases

    COMPLUYEAST-2DPAGEP63017.
    REPRODUCTION-2DPAGEIPI00323357.
    P63017.
    Q6NZD0.
    SWISS-2DPAGEP63017.
    UCD-2DPAGEP63017.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Inductioni

    Constitutively synthesized.

    Gene expression databases

    ArrayExpressiP63017.
    BgeeiP63017.
    CleanExiMM_HSPA8.
    GenevestigatoriP63017.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with DNAJC7 and DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with IRAK1BP1 and HSPH1/HSP105. Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity By similarity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1 By similarity. Interacts with PARK2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Klc1O884473EBI-433443,EBI-301550

    Protein-protein interaction databases

    BioGridi200428. 43 interactions.
    DIPiDIP-32353N.
    IntActiP63017. 34 interactions.
    MINTiMINT-189032.

    Structurei

    Secondary structure

    1
    646
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Beta strandi13 – 2210
    Beta strandi25 – 284
    Beta strandi36 – 394
    Beta strandi42 – 443
    Beta strandi49 – 513
    Helixi53 – 575
    Turni58 – 614
    Helixi63 – 653
    Helixi70 – 723
    Turni73 – 753
    Helixi81 – 866
    Turni87 – 893
    Beta strandi91 – 977
    Beta strandi100 – 1078
    Beta strandi110 – 1145
    Helixi116 – 13520
    Beta strandi141 – 1466
    Helixi152 – 16413
    Beta strandi168 – 1747
    Helixi175 – 1828
    Turni183 – 1864
    Beta strandi187 – 20014
    Beta strandi205 – 2139
    Beta strandi216 – 22510
    Helixi230 – 24920
    Helixi257 – 27317
    Turni274 – 2763
    Beta strandi278 – 28811
    Beta strandi291 – 2988
    Helixi299 – 31214
    Helixi314 – 32411
    Helixi328 – 3303
    Beta strandi333 – 3386
    Helixi339 – 3424
    Helixi344 – 35310
    Turni354 – 3563
    Turni365 – 3673
    Helixi368 – 38013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CQXX-ray2.30A/B1-381[»]
    ProteinModelPortaliP63017.
    SMRiP63017. Positions 1-621.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63017.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 377192Interaction with BAG1By similarityAdd
    BLAST

    Domaini

    The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain.By similarity

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    GeneTreeiENSGT00750000117237.
    HOVERGENiHBG051845.
    InParanoidiP63017.
    KOiK03283.
    OMAiGENKIFT.
    OrthoDBiEOG7PCJGF.
    PhylomeDBiP63017.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P63017-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL    50
    IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR 100
    PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF 150
    NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL 200
    GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK 250
    KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 300
    RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL 350
    QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS 400
    LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT 450
    KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK 500
    ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK 550
    ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE 600
    KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD 646
    Length:646
    Mass (Da):70,871
    Last modified:August 1, 1988 - v1
    Checksum:i03A27B30E6C076ED
    GO

    Sequence cautioni

    The sequence BAE31508.1 differs from that shown. Reason: Frameshift at positions 256 and 269.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91I → V in BAE28187. (PubMed:16141072)Curated
    Sequence conflicti35 – 351N → K in BAE30081. (PubMed:16141072)Curated
    Sequence conflicti35 – 351N → K in BAE30861. (PubMed:16141072)Curated
    Sequence conflicti35 – 351N → K in BAE30753. (PubMed:16141072)Curated
    Sequence conflicti268 – 2681E → G in BAE31432. (PubMed:16141072)Curated
    Sequence conflicti268 – 2681E → G in BAE31346. (PubMed:16141072)Curated
    Sequence conflicti269 – 2691R → G in BAE31508. (PubMed:16141072)Curated
    Sequence conflicti353 – 3531F → C in BAE31664. (PubMed:16141072)Curated
    Sequence conflicti428 – 4281F → L in AAA37869. (PubMed:3334718)Curated
    Sequence conflicti428 – 4281F → L in AAB18391. (PubMed:10095055)Curated
    Sequence conflicti432 – 4321S → Y in BAE30707. (PubMed:16141072)Curated
    Sequence conflicti589 – 5891K → E in AAH66191. (PubMed:15489334)Curated
    Sequence conflicti645 – 6451V → M in BAE30272. (PubMed:16141072)Curated
    Sequence conflicti645 – 6451V → M in BAE31427. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19141 mRNA. Translation: AAA37869.1.
    U27129 mRNA. Translation: AAC52836.1.
    U73744 Genomic DNA. Translation: AAB18391.1.
    AK035286 mRNA. Translation: BAC29016.1.
    AK075935 mRNA. Translation: BAC36065.1.
    AK145579 mRNA. Translation: BAE26523.1.
    AK146708 mRNA. Translation: BAE27374.1.
    AK146985 mRNA. Translation: BAE27588.1.
    AK147864 mRNA. Translation: BAE28187.1.
    AK150474 mRNA. Translation: BAE29591.1.
    AK150498 mRNA. Translation: BAE29612.1.
    AK150701 mRNA. Translation: BAE29780.1.
    AK150958 mRNA. Translation: BAE29990.1.
    AK151065 mRNA. Translation: BAE30081.1.
    AK151127 mRNA. Translation: BAE30135.1.
    AK151287 mRNA. Translation: BAE30272.1.
    AK151435 mRNA. Translation: BAE30398.1.
    AK151516 mRNA. Translation: BAE30465.1.
    AK151537 mRNA. Translation: BAE30484.1.
    AK151775 mRNA. Translation: BAE30681.1.
    AK151808 mRNA. Translation: BAE30707.1.
    AK151865 mRNA. Translation: BAE30753.1.
    AK151892 mRNA. Translation: BAE30776.1.
    AK151948 mRNA. Translation: BAE30822.1.
    AK151997 mRNA. Translation: BAE30861.1.
    AK152598 mRNA. Translation: BAE31346.1.
    AK152697 mRNA. Translation: BAE31427.1.
    AK152703 mRNA. Translation: BAE31432.1.
    AK152803 mRNA. Translation: BAE31508.1. Frameshift.
    AK153032 mRNA. Translation: BAE31664.1.
    AK153834 mRNA. Translation: BAE32204.1.
    AK159479 mRNA. Translation: BAE35116.1.
    AK164000 mRNA. Translation: BAE37581.1.
    AK166643 mRNA. Translation: BAE38912.1.
    AK166721 mRNA. Translation: BAE38970.1.
    AK166767 mRNA. Translation: BAE39005.1.
    AK166776 mRNA. Translation: BAE39012.1.
    AK166808 mRNA. Translation: BAE39036.1.
    AK166830 mRNA. Translation: BAE39053.1.
    AK166846 mRNA. Translation: BAE39065.1.
    AK166861 mRNA. Translation: BAE39076.1.
    AK166873 mRNA. Translation: BAE39084.1.
    AK166908 mRNA. Translation: BAE39109.1.
    AK166910 mRNA. Translation: BAE39111.1.
    AK166913 mRNA. Translation: BAE39113.1.
    AK166933 mRNA. Translation: BAE39127.1.
    AK167043 mRNA. Translation: BAE39211.1.
    AK167121 mRNA. Translation: BAE39269.1.
    AK167122 mRNA. Translation: BAE39270.1.
    AK167134 mRNA. Translation: BAE39280.1.
    AK167163 mRNA. Translation: BAE39304.1.
    AK167218 mRNA. Translation: BAE39344.1.
    AK167229 mRNA. Translation: BAE39353.1.
    AK167845 mRNA. Translation: BAE39865.1.
    AK167910 mRNA. Translation: BAE39917.1.
    AK168492 mRNA. Translation: BAE40379.1.
    AK168519 mRNA. Translation: BAE40398.1.
    AK168542 mRNA. Translation: BAE40419.1.
    AK168711 mRNA. Translation: BAE40553.1.
    AK168750 mRNA. Translation: BAE40590.1.
    AK168776 mRNA. Translation: BAE40612.1.
    AK168887 mRNA. Translation: BAE40704.1.
    AK168934 mRNA. Translation: BAE40745.1.
    AK169093 mRNA. Translation: BAE40876.1.
    AK169179 mRNA. Translation: BAE40957.1.
    AK169236 mRNA. Translation: BAE41004.1.
    AK169293 mRNA. Translation: BAE41049.1.
    BC006722 mRNA. Translation: AAH06722.1.
    BC066191 mRNA. Translation: AAH66191.1.
    BC085486 mRNA. Translation: AAH85486.1.
    BC089322 mRNA. Translation: AAH89322.1.
    BC089457 mRNA. Translation: AAH89457.1.
    BC106193 mRNA. Translation: AAI06194.1.
    X54401 Genomic DNA. Translation: CAA38267.1.
    X54402 Genomic DNA. Translation: CAA38268.1.
    X54403 Genomic DNA. Translation: CAA38269.1.
    CCDSiCCDS23083.1.
    PIRiA45935.
    JC4853.
    RefSeqiNP_112442.2. NM_031165.4.
    UniGeneiMm.290774.
    Mm.336743.
    Mm.351377.
    Mm.412745.
    Mm.485345.

    Genome annotation databases

    EnsembliENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
    GeneIDi15481.
    KEGGimmu:15481.
    UCSCiuc009ozx.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19141 mRNA. Translation: AAA37869.1 .
    U27129 mRNA. Translation: AAC52836.1 .
    U73744 Genomic DNA. Translation: AAB18391.1 .
    AK035286 mRNA. Translation: BAC29016.1 .
    AK075935 mRNA. Translation: BAC36065.1 .
    AK145579 mRNA. Translation: BAE26523.1 .
    AK146708 mRNA. Translation: BAE27374.1 .
    AK146985 mRNA. Translation: BAE27588.1 .
    AK147864 mRNA. Translation: BAE28187.1 .
    AK150474 mRNA. Translation: BAE29591.1 .
    AK150498 mRNA. Translation: BAE29612.1 .
    AK150701 mRNA. Translation: BAE29780.1 .
    AK150958 mRNA. Translation: BAE29990.1 .
    AK151065 mRNA. Translation: BAE30081.1 .
    AK151127 mRNA. Translation: BAE30135.1 .
    AK151287 mRNA. Translation: BAE30272.1 .
    AK151435 mRNA. Translation: BAE30398.1 .
    AK151516 mRNA. Translation: BAE30465.1 .
    AK151537 mRNA. Translation: BAE30484.1 .
    AK151775 mRNA. Translation: BAE30681.1 .
    AK151808 mRNA. Translation: BAE30707.1 .
    AK151865 mRNA. Translation: BAE30753.1 .
    AK151892 mRNA. Translation: BAE30776.1 .
    AK151948 mRNA. Translation: BAE30822.1 .
    AK151997 mRNA. Translation: BAE30861.1 .
    AK152598 mRNA. Translation: BAE31346.1 .
    AK152697 mRNA. Translation: BAE31427.1 .
    AK152703 mRNA. Translation: BAE31432.1 .
    AK152803 mRNA. Translation: BAE31508.1 . Frameshift.
    AK153032 mRNA. Translation: BAE31664.1 .
    AK153834 mRNA. Translation: BAE32204.1 .
    AK159479 mRNA. Translation: BAE35116.1 .
    AK164000 mRNA. Translation: BAE37581.1 .
    AK166643 mRNA. Translation: BAE38912.1 .
    AK166721 mRNA. Translation: BAE38970.1 .
    AK166767 mRNA. Translation: BAE39005.1 .
    AK166776 mRNA. Translation: BAE39012.1 .
    AK166808 mRNA. Translation: BAE39036.1 .
    AK166830 mRNA. Translation: BAE39053.1 .
    AK166846 mRNA. Translation: BAE39065.1 .
    AK166861 mRNA. Translation: BAE39076.1 .
    AK166873 mRNA. Translation: BAE39084.1 .
    AK166908 mRNA. Translation: BAE39109.1 .
    AK166910 mRNA. Translation: BAE39111.1 .
    AK166913 mRNA. Translation: BAE39113.1 .
    AK166933 mRNA. Translation: BAE39127.1 .
    AK167043 mRNA. Translation: BAE39211.1 .
    AK167121 mRNA. Translation: BAE39269.1 .
    AK167122 mRNA. Translation: BAE39270.1 .
    AK167134 mRNA. Translation: BAE39280.1 .
    AK167163 mRNA. Translation: BAE39304.1 .
    AK167218 mRNA. Translation: BAE39344.1 .
    AK167229 mRNA. Translation: BAE39353.1 .
    AK167845 mRNA. Translation: BAE39865.1 .
    AK167910 mRNA. Translation: BAE39917.1 .
    AK168492 mRNA. Translation: BAE40379.1 .
    AK168519 mRNA. Translation: BAE40398.1 .
    AK168542 mRNA. Translation: BAE40419.1 .
    AK168711 mRNA. Translation: BAE40553.1 .
    AK168750 mRNA. Translation: BAE40590.1 .
    AK168776 mRNA. Translation: BAE40612.1 .
    AK168887 mRNA. Translation: BAE40704.1 .
    AK168934 mRNA. Translation: BAE40745.1 .
    AK169093 mRNA. Translation: BAE40876.1 .
    AK169179 mRNA. Translation: BAE40957.1 .
    AK169236 mRNA. Translation: BAE41004.1 .
    AK169293 mRNA. Translation: BAE41049.1 .
    BC006722 mRNA. Translation: AAH06722.1 .
    BC066191 mRNA. Translation: AAH66191.1 .
    BC085486 mRNA. Translation: AAH85486.1 .
    BC089322 mRNA. Translation: AAH89322.1 .
    BC089457 mRNA. Translation: AAH89457.1 .
    BC106193 mRNA. Translation: AAI06194.1 .
    X54401 Genomic DNA. Translation: CAA38267.1 .
    X54402 Genomic DNA. Translation: CAA38268.1 .
    X54403 Genomic DNA. Translation: CAA38269.1 .
    CCDSi CCDS23083.1.
    PIRi A45935.
    JC4853.
    RefSeqi NP_112442.2. NM_031165.4.
    UniGenei Mm.290774.
    Mm.336743.
    Mm.351377.
    Mm.412745.
    Mm.485345.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CQX X-ray 2.30 A/B 1-381 [» ]
    ProteinModelPortali P63017.
    SMRi P63017. Positions 1-621.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200428. 43 interactions.
    DIPi DIP-32353N.
    IntActi P63017. 34 interactions.
    MINTi MINT-189032.

    2D gel databases

    COMPLUYEAST-2DPAGE P63017.
    REPRODUCTION-2DPAGE IPI00323357.
    P63017.
    Q6NZD0.
    SWISS-2DPAGE P63017.
    UCD-2DPAGE P63017.

    Proteomic databases

    MaxQBi P63017.
    PaxDbi P63017.
    PRIDEi P63017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015800 ; ENSMUSP00000015800 ; ENSMUSG00000015656 .
    GeneIDi 15481.
    KEGGi mmu:15481.
    UCSCi uc009ozx.3. mouse.

    Organism-specific databases

    CTDi 3312.
    MGIi MGI:105384. Hspa8.

    Phylogenomic databases

    eggNOGi COG0443.
    GeneTreei ENSGT00750000117237.
    HOVERGENi HBG051845.
    InParanoidi P63017.
    KOi K03283.
    OMAi GENKIFT.
    OrthoDBi EOG7PCJGF.
    PhylomeDBi P63017.
    TreeFami TF105042.

    Enzyme and pathway databases

    Reactomei REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_213550. HSF1-dependent transactivation.
    REACT_222185. Regulation of HSF1-mediated heat shock response.
    REACT_223784. Attenuation phase.

    Miscellaneous databases

    EvolutionaryTracei P63017.
    NextBioi 288328.
    PROi P63017.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63017.
    Bgeei P63017.
    CleanExi MM_HSPA8.
    Genevestigatori P63017.

    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. "Developmental regulation of a constitutively expressed mouse mRNA encoding a 72-kDa heat shock-like protein."
      Giebel L.B., Dworniczak B.P., Bautz E.K.F.
      Dev. Biol. 125:200-207(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Developmental regulation of murine integrin beta 1 subunit- and Hsc73-encoding genes in mammary gland: sequence of a new mouse Hsc73 cDNA."
      Soulier S., Vilotte J.-L., L'Huillier P.J., Mercier J.-C.
      Gene 172:285-289(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129.
      Tissue: Mammary gland.
    3. "Characterization and expression of the mouse Hsc70 gene."
      Hunt C.R., Parsian A.J., Goswami P.C., Kozak C.A.
      Biochim. Biophys. Acta 1444:315-325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and DBA/2.
      Tissue: Amnion, Bone marrow, Heart, Kidney, Liver, Stomach, Thymus and Urinary bladder.
    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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain, Embryo, Embryonic germ cell, Eye and Mammary gland.
    6. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-102; 113-155; 160-188; 221-246; 300-319; 326-342; 349-357; 362-384; 424-447; 540-550 AND 584-597, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "Mouse U14 snRNA is encoded in an intron of the mouse cognate hsc70 heat shock gene."
      Liu J., Maxwell E.S.
      Nucleic Acids Res. 18:6565-6571(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-383; 438-452 AND 580-587.
    8. "Association of HSP105 with HSC70 in high molecular mass complexes in mouse FM3A cells."
      Hatayama T., Yasuda K., Yasuda K.
      Biochem. Biophys. Res. Commun. 248:395-401(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPH1.
    9. "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity."
      Yamagishi N., Ishihara K., Hatayama T.
      J. Biol. Chem. 279:41727-41733(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPH1.
    10. Cited for: ISGYLATION.
    11. "The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family."
      Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.
      DNA Cell Biol. 25:704-714(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK1BP1, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "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-561.
    13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246; LYS-319; LYS-328; LYS-512; LYS-524 AND LYS-601, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-319 AND LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiHSP7C_MOUSE
    AccessioniPrimary (citable) accession number: P63017
    Secondary accession number(s): P08109
    , P12225, Q3U6R0, Q3U764, Q3U7D7, Q3U7E2, Q3U9B4, Q3U9G0, Q3UGM0, Q5FWJ6, Q62373, Q62374, Q62375, Q6NZD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3