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P11142

- HSP7C_HUMAN

UniProt

P11142 - HSP7C_HUMAN

Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP.3 Publications

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. ATPase activity Source: BHF-UCL
    2. ATPase activity, coupled Source: UniProtKB
    3. ATP binding Source: BHF-UCL
    4. enzyme binding Source: BHF-UCL
    5. heat shock protein binding Source: BHF-UCL
    6. MHC class II protein complex binding Source: UniProt
    7. poly(A) RNA binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. unfolded protein binding Source: UniProt

    GO - Biological processi

    1. ATP catabolic process Source: BHF-UCL
    2. axon guidance Source: Reactome
    3. chaperone mediated protein folding requiring cofactor Source: Ensembl
    4. gene expression Source: Reactome
    5. membrane organization Source: Reactome
    6. mRNA metabolic process Source: Reactome
    7. mRNA processing Source: UniProtKB-KW
    8. negative regulation of fibril organization Source: BHF-UCL
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. neurotransmitter secretion Source: Reactome
    11. post-Golgi vesicle-mediated transport Source: Reactome
    12. protein folding Source: UniProtKB
    13. protein refolding Source: UniProt
    14. regulation of cell cycle Source: Ensembl
    15. response to unfolded protein Source: UniProtKB
    16. RNA metabolic process Source: Reactome
    17. RNA splicing Source: UniProtKB-KW
    18. synaptic transmission Source: Reactome
    19. transcription, DNA-templated Source: UniProtKB-KW
    20. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Repressor

    Keywords - Biological processi

    Host-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_200624. Attenuation phase.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_22292. CHL1 interactions.
    REACT_23947. GABA synthesis, release, reuptake and degradation.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock cognate 71 kDa protein
    Alternative name(s):
    Heat shock 70 kDa protein 8
    Lipopolysaccharide-associated protein 1
    Short name:
    LAP-1
    Short name:
    LPS-associated protein 1
    Gene namesi
    Name:HSPA8
    Synonyms:HSC70, HSP73, HSPA10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:5241. HSPA8.

    Subcellular locationi

    Cytoplasm. Melanosome. Nucleusnucleolus. Cell membrane
    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.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
    3. cytosol Source: UniProt
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProtKB
    6. intracellular Source: UniProtKB
    7. melanosome Source: UniProtKB-SubCell
    8. membrane Source: UniProtKB
    9. nucleolus Source: UniProtKB
    10. nucleus Source: UniProtKB
    11. plasma membrane Source: Reactome
    12. Prp19 complex Source: UniProtKB
    13. ribonucleoprotein complex Source: UniProtKB
    14. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi561 – 5611K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications

    Organism-specific databases

    PharmGKBiPA29507.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 646645Heat shock cognate 71 kDa proteinPRO_0000078270Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei108 – 1081N6-acetyllysineBy similarity
    Modified residuei153 – 1531Phosphoserine1 Publication
    Modified residuei246 – 2461N6-acetyllysine1 Publication
    Modified residuei319 – 3191N6-acetyllysine; alternate1 Publication
    Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-acetyllysineBy similarity
    Modified residuei362 – 3621Phosphoserine1 Publication
    Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
    Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
    Modified residuei524 – 5241N6-acetyllysineBy similarity
    Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A2 Publications
    Modified residuei589 – 5891N6-acetyllysine1 Publication
    Modified residuei597 – 5971N6-acetyllysine1 Publication
    Modified residuei601 – 6011N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylated.4 Publications
    ISGylated.2 Publications
    Trimethylation at Lys-561 reduces fibrillar SNCA binding.

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP11142.
    PaxDbiP11142.
    PeptideAtlasiP11142.
    PRIDEiP11142.

    2D gel databases

    DOSAC-COBS-2DPAGEP11142.
    OGPiP11142.
    REPRODUCTION-2DPAGEIPI00003865.
    SWISS-2DPAGEP11142.
    UCD-2DPAGEP11142.

    PTM databases

    PhosphoSiteiP11142.

    Miscellaneous databases

    PMAP-CutDBP11142.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    Constitutively synthesized.

    Gene expression databases

    ArrayExpressiP11142.
    BgeeiP11142.
    CleanExiHS_HSPA8.
    GenevestigatoriP11142.

    Organism-specific databases

    HPAiCAB002056.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. 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 SV40 VP1. Interacts with TRIM5. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PARK2.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB83EBI-351896,EBI-6927928From a different organism.
    ACTBP607092EBI-351896,EBI-353944
    AICDAQ9GZX72EBI-351896,EBI-3834328
    ARRB1P494074EBI-351896,EBI-743313
    ARRB2P321214EBI-351896,EBI-714559
    ATP13A2Q9NQ112EBI-351896,EBI-6308763
    BAG1Q9993310EBI-351896,EBI-1030678
    BAG2O958163EBI-351896,EBI-355275
    EBNA-LPQ8AZK73EBI-351896,EBI-1185167From a different organism.
    GAKO149765EBI-351896,EBI-714707
    LDHAP003384EBI-351896,EBI-372327
    LRRK2Q5S0075EBI-351896,EBI-5323863
    MP034854EBI-351896,EBI-2547543From a different organism.
    STUB1Q9UNE75EBI-351896,EBI-357085

    Protein-protein interaction databases

    BioGridi109544. 254 interactions.
    IntActiP11142. 91 interactions.
    MINTiMINT-4998609.
    STRINGi9606.ENSP00000227378.

    Structurei

    Secondary structure

    1
    646
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Beta strandi13 – 2210
    Beta strandi25 – 284
    Beta strandi36 – 405
    Beta strandi42 – 443
    Beta strandi49 – 524
    Helixi53 – 575
    Turni58 – 614
    Helixi63 – 653
    Helixi70 – 734
    Helixi81 – 866
    Helixi87 – 893
    Beta strandi91 – 977
    Beta strandi100 – 1078
    Beta strandi110 – 1145
    Helixi116 – 13520
    Beta strandi141 – 1466
    Helixi152 – 16413
    Beta strandi168 – 1747
    Helixi175 – 1828
    Helixi185 – 1873
    Beta strandi193 – 2008
    Beta strandi205 – 2139
    Beta strandi216 – 22510
    Helixi230 – 24920
    Helixi253 – 2553
    Helixi257 – 27418
    Beta strandi277 – 28812
    Beta strandi291 – 2988
    Helixi299 – 3057
    Helixi307 – 3126
    Helixi314 – 32310
    Helixi328 – 3303
    Beta strandi333 – 3386
    Helixi339 – 3424
    Helixi344 – 35310
    Turni354 – 3563
    Beta strandi357 – 3604
    Turni365 – 3673
    Helixi368 – 38013
    Beta strandi641 – 6444

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AGYX-ray1.85C/D/F639-646[»]
    3AGZX-ray2.51C/D/E/F639-646[»]
    3ESKX-ray2.05B635-646[»]
    3FZFX-ray2.20A4-381[»]
    3FZHX-ray2.00A4-381[»]
    3FZKX-ray2.10A4-381[»]
    3FZLX-ray2.20A4-381[»]
    3FZMX-ray2.30A4-381[»]
    3LDQX-ray1.90A4-381[»]
    3M3ZX-ray2.10A4-381[»]
    4H5NX-ray1.86A/B2-384[»]
    4H5RX-ray1.64A/B2-384[»]
    4H5TX-ray1.90A2-384[»]
    4H5VX-ray1.75A2-384[»]
    4H5WX-ray1.94A/B2-384[»]
    4HWIX-ray2.27A5-381[»]
    ProteinModelPortaliP11142.
    SMRiP11142. Positions 1-621.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11142.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 377192Interaction with BAG1Add
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.
    InParanoidiP11142.
    KOiK03283.
    OMAiGENKIFT.
    OrthoDBiEOG7PCJGF.
    PhylomeDBiP11142.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11142-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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 LDKCNEIINW LDKNQTAEKE EFEHQQKELE 600
    KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD 646
    Length:646
    Mass (Da):70,898
    Last modified:July 1, 1989 - v1
    Checksum:i9AA27B210730670C
    GO
    Isoform 2 (identifier: P11142-2) [UniParc]FASTAAdd to Basket

    Also known as: HSC54

    The sequence of this isoform differs from the canonical sequence as follows:
         464-616: Missing.

    Show »
    Length:493
    Mass (Da):53,518
    Checksum:iBA2CFBD68F17784E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321D → Y.
    Corresponds to variant rs11551602 [ dbSNP | Ensembl ].
    VAR_049619
    Natural varianti459 – 4591F → L.
    Corresponds to variant rs11551598 [ dbSNP | Ensembl ].
    VAR_049620

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei464 – 616153Missing in isoform 2. 1 PublicationVSP_002427Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00371 Genomic DNA. Translation: CAA68445.1.
    AB034951 mRNA. Translation: BAB18615.1.
    AF352832 mRNA. Translation: AAK17898.1.
    BC016179 mRNA. Translation: AAH16179.1.
    BC016660 mRNA. Translation: AAH16660.1.
    BC019816 mRNA. Translation: AAH19816.1.
    CCDSiCCDS44754.1. [P11142-2]
    CCDS8440.1. [P11142-1]
    PIRiA27077.
    RefSeqiNP_006588.1. NM_006597.5. [P11142-1]
    NP_694881.1. NM_153201.3. [P11142-2]
    XP_006718894.1. XM_006718831.1. [P11142-1]
    UniGeneiHs.180414.

    Genome annotation databases

    EnsembliENST00000227378; ENSP00000227378; ENSG00000109971. [P11142-1]
    ENST00000453788; ENSP00000404372; ENSG00000109971. [P11142-2]
    ENST00000532636; ENSP00000437125; ENSG00000109971. [P11142-1]
    ENST00000534624; ENSP00000432083; ENSG00000109971. [P11142-1]
    GeneIDi3312.
    KEGGihsa:3312.
    UCSCiuc001pyo.3. human. [P11142-1]
    uc001pyp.3. human. [P11142-2]

    Polymorphism databases

    DMDMi123648.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00371 Genomic DNA. Translation: CAA68445.1 .
    AB034951 mRNA. Translation: BAB18615.1 .
    AF352832 mRNA. Translation: AAK17898.1 .
    BC016179 mRNA. Translation: AAH16179.1 .
    BC016660 mRNA. Translation: AAH16660.1 .
    BC019816 mRNA. Translation: AAH19816.1 .
    CCDSi CCDS44754.1. [P11142-2 ]
    CCDS8440.1. [P11142-1 ]
    PIRi A27077.
    RefSeqi NP_006588.1. NM_006597.5. [P11142-1 ]
    NP_694881.1. NM_153201.3. [P11142-2 ]
    XP_006718894.1. XM_006718831.1. [P11142-1 ]
    UniGenei Hs.180414.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AGY X-ray 1.85 C/D/F 639-646 [» ]
    3AGZ X-ray 2.51 C/D/E/F 639-646 [» ]
    3ESK X-ray 2.05 B 635-646 [» ]
    3FZF X-ray 2.20 A 4-381 [» ]
    3FZH X-ray 2.00 A 4-381 [» ]
    3FZK X-ray 2.10 A 4-381 [» ]
    3FZL X-ray 2.20 A 4-381 [» ]
    3FZM X-ray 2.30 A 4-381 [» ]
    3LDQ X-ray 1.90 A 4-381 [» ]
    3M3Z X-ray 2.10 A 4-381 [» ]
    4H5N X-ray 1.86 A/B 2-384 [» ]
    4H5R X-ray 1.64 A/B 2-384 [» ]
    4H5T X-ray 1.90 A 2-384 [» ]
    4H5V X-ray 1.75 A 2-384 [» ]
    4H5W X-ray 1.94 A/B 2-384 [» ]
    4HWI X-ray 2.27 A 5-381 [» ]
    ProteinModelPortali P11142.
    SMRi P11142. Positions 1-621.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109544. 254 interactions.
    IntActi P11142. 91 interactions.
    MINTi MINT-4998609.
    STRINGi 9606.ENSP00000227378.

    Chemistry

    BindingDBi P11142.
    ChEMBLi CHEMBL1275223.

    PTM databases

    PhosphoSitei P11142.

    Polymorphism databases

    DMDMi 123648.

    2D gel databases

    DOSAC-COBS-2DPAGE P11142.
    OGPi P11142.
    REPRODUCTION-2DPAGE IPI00003865.
    SWISS-2DPAGE P11142.
    UCD-2DPAGE P11142.

    Proteomic databases

    MaxQBi P11142.
    PaxDbi P11142.
    PeptideAtlasi P11142.
    PRIDEi P11142.

    Protocols and materials databases

    DNASUi 3312.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227378 ; ENSP00000227378 ; ENSG00000109971 . [P11142-1 ]
    ENST00000453788 ; ENSP00000404372 ; ENSG00000109971 . [P11142-2 ]
    ENST00000532636 ; ENSP00000437125 ; ENSG00000109971 . [P11142-1 ]
    ENST00000534624 ; ENSP00000432083 ; ENSG00000109971 . [P11142-1 ]
    GeneIDi 3312.
    KEGGi hsa:3312.
    UCSCi uc001pyo.3. human. [P11142-1 ]
    uc001pyp.3. human. [P11142-2 ]

    Organism-specific databases

    CTDi 3312.
    GeneCardsi GC11M122969.
    H-InvDB HIX0033867.
    HGNCi HGNC:5241. HSPA8.
    HPAi CAB002056.
    MIMi 600816. gene.
    neXtProti NX_P11142.
    PharmGKBi PA29507.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0443.
    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.
    InParanoidi P11142.
    KOi K03283.
    OMAi GENKIFT.
    OrthoDBi EOG7PCJGF.
    PhylomeDBi P11142.
    TreeFami TF105042.

    Enzyme and pathway databases

    Reactomei REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_200624. Attenuation phase.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_22292. CHL1 interactions.
    REACT_23947. GABA synthesis, release, reuptake and degradation.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi HSPA8. human.
    EvolutionaryTracei P11142.
    GeneWikii HSPA8.
    GenomeRNAii 3312.
    NextBioi 13136.
    PMAP-CutDB P11142.
    PROi P11142.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11142.
    Bgeei P11142.
    CleanExi HS_HSPA8.
    Genevestigatori P11142.

    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. "Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein."
      Dworniczak B.P., Mirault M.-E.
      Nucleic Acids Res. 15:5181-5197(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "Molecular and functional characterization of HSC54, a novel variant of human heat shock cognate protein 70."
      Tsukahara F., Yoshioka T., Muraki T.
      Mol. Pharmacol. 58:1257-1263(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Complete coding sequence of human HSC70."
      Niswonger M.L., Berk L.R., Srivastava P.K.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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] (ISOFORM 1).
      Tissue: Placenta and Skin.
    5. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-49; 57-71; 77-102; 103-155; 160-188; 221-247; 273-311; 326-342; 349-416; 424-447; 452-493; 510-517; 540-550; 570-597 AND 602-646, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    6. Cited for: PROTEIN SEQUENCE OF 2-49; 57-72; 78-88; 113-188; 221-247; 300-319; 326-342; 349-357; 362-384; 424-447; 452-469; 510-517; 540-550 AND 584-609, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Ovarian carcinoma.
    7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-88; 113-126; 129-155; 160-187; 221-246; 300-311; 329-342; 362-384; 424-447; 540-550 AND 574-583, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 50-55; 103-107 AND 580-596.
    9. "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
      Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
      Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 77-86; 221-236 AND 302-311.
    10. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
      Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
      PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells."
      Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.
      Cell Struct. Funct. 17:77-86(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. Cited for: INTERACTION WITH BAG1, DOMAIN.
    13. "Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines."
      Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M., Reed J.C.
      Cancer Res. 58:3116-3131(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BAG1.
    14. "HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells."
      Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.
      Cell Stress Chaperones 5:132-138(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV40 VP1.
    15. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
      Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
      J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CITED1.
    16. Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSP90AA1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    17. "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
      Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
      J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PACRG.
    18. Cited for: ISGYLATION.
    19. Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
    20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    21. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
      Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HERC5, ISGYLATION.
    22. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
      Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
      J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; C11ORF30; MATR3; ZNF335; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
    26. "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.
    27. "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-246; LYS-319; LYS-589; LYS-597 AND LYS-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
      Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.
      J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM5.
    29. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR LOCATION.
    30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex."
      Smith M.C., Scaglione K.M., Assimon V.A., Patury S., Thompson A.D., Dickey C.A., Southworth D.R., Paulson H.L., Gestwicki J.E., Zuiderweg E.R.
      Biochemistry 52:5354-5364(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH CHIP.
    34. "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, MUTAGENESIS OF LYS-561, INTERACTION WITH METTL21A.
    35. "Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase."
      Matsumura Y., Sakai J., Skach W.R.
      J. Biol. Chem. 288:31069-31079(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ERAD, INTERACTION WITH CHIP.
    36. "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
      Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
      Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARK2.
    37. "Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering."
      Kajander T., Sachs J.N., Goldman A., Regan L.
      J. Biol. Chem. 284:25364-25374(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-634.
    38. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP AND ATP ANALOGS.
    39. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP ANALOGS.

    Entry informationi

    Entry nameiHSP7C_HUMAN
    AccessioniPrimary (citable) accession number: P11142
    Secondary accession number(s): Q9H3R6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 182 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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