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UniProtKB/Swiss-Prot entry P11142


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HSP7C_HUMAN
Primary accession number P11142
Secondary accession number Q9H3R6
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 123)
Name and origin of the protein
Protein name Heat shock cognate 71 kDa protein
Synonym Heat shock 70 kDa protein 8
Gene name
Name: HSPA8
Synonyms: HSC70, HSP73, HSPA10
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
DOI=10.1093/nar/15.13.5181; PubMed=3037489 [NCBI, ExPASy, EBI, Israel, Japan]
Dworniczak B.P., Mirault M.-E.;
"Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein.";
Nucleic Acids Res. 15:5181-5197(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11093761 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukahara F., Yoshioka T., Muraki T.;
"Molecular and functional characterization of HSC54, a novel variant of human heat shock cognate protein 70.";
Mol. Pharmacol. 58:1257-1263(2000).
[3]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Niswonger M.L., Berk L.R., Srivastava P.K.;
"Complete coding sequence of human HSC70.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
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, AND MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[6]
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, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 4-49; 57-71; 78-88; 113-155; 160-188; 221-246; 300-319; 329-342; 349-357; 362-384; 459-469; 510-517; 540-550; 584-597 AND 602-609, AND MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 50-55; 103-107 AND 580-596.
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
PROTEIN SEQUENCE OF 77-86; 221-236 AND 302-311.
DOI=10.1006/bbrc.1996.1082; PubMed=8713105 [NCBI, ExPASy, EBI, Israel, Japan]
Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.;
"Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes.";
Biochem. Biophys. Res. Commun. 224:666-674(1996).
[10]
SUBCELLULAR LOCATION.
PubMed=1586970 [NCBI, ExPASy, EBI, Israel, Japan]
Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.;
"Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.";
Cell Struct. Funct. 17:77-86(1992).
[11]
INTERACTION WITH SV40 VP1.
PubMed=11147964 [NCBI, ExPASy, EBI, Israel, Japan]
Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.;
"HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells.";
Cell Stress Chaperones 5:132-138(2000).
[12]
INTERACTION WITH PACRG.
DOI=10.1074/jbc.M309655200; PubMed=14532270 [NCBI, ExPASy, EBI, Israel, Japan]
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.";
J. Biol. Chem. 278:51901-51910(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-477, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[14]
INTERACTION WITH TSC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1016/j.bbrc.2005.05.175; PubMed=15963462 [NCBI, ExPASy, EBI, Israel, Japan]
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.;
"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.";
Biochem. Biophys. Res. Commun. 333:818-826(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[16]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41 AND TYR-107, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; TYR-115; SER-120 AND SER-121, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00371; CAA68445.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB034951; BAB18615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF352832; AAK17898.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016179; AAH16179.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016660; AAH16660.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019816; AAH19816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00003865; -.
IPI00037070; -.
PIR A27077; A27077.
RefSeq NP_006588.1; -.
NP_694881.1; -.
UniGene Hs.702021
3D structure databases
PDB
3FZF; X-ray; 2.20 A; A=4-381.[ExPASy / RCSB / EBI]
3FZH; X-ray; 2.00 A; A=4-381.[ExPASy / RCSB / EBI]
3FZK; X-ray; 2.10 A; A=4-381.[ExPASy / RCSB / EBI]
3FZL; X-ray; 2.20 A; A=4-381.[ExPASy / RCSB / EBI]
3FZM; X-ray; 2.30 A; A=4-381.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 3FZF; -.
3FZH; -.
3FZK; -.
3FZL; -.
3FZM; -.
SMR P11142; 1-554.
ModBase P11142.
Protein-protein interaction databases
IntAct P11142; 58.
PTM databases
PhosphoSite P11142; -.
Enzyme and pathway databases
Pathway_Interaction_DB smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
Reactome REACT_11123; Membrane Trafficking.
2D gel databases
SWISS-2DPAGE P11142; -.
Aarhus/Ghent-2DPAGE 6504; IEF.
Cornea-2DPAGE P11142; -.
DOSAC-COBS-2DPAGE P11142; -.
HSC-2DPAGE P11142; -.
OGP P11142; -.
PHCI-2DPAGE P11142; -.
REPRODUCTION-2DPAGE IPI00003865; -.
Organism-specific databases
GeneCards GC11M122460; -.
H-InvDB HIX0010213; -.
HGNC HGNC:5241; HSPA8.
GenAtlas HSPA8.
HPA CAB002056; -.
MIM 600816; gene. [NCBI / EBI]
PharmGKB PA29507; -.
Gene expression databases
ArrayExpress P11142; -.
Bgee P11142; -.
CleanEx HS_HSPA8; -.
GermOnline ENSG00000109971; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042623; Molecular function: ATPase activity, coupled (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006457; Biological process: protein folding (non-traceable author statement from UniProtKB).
GO:0006986; Biological process: response to unfolded protein (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR018181; Heat_shock_70_CS.
IPR001023; Hsp70.
IPR013126; Hsp_70.
Graphical view of domain structure.
PANTHER PTHR19375; Hsp70; 1.
Pfam PF00012; HSP70; 1.
Pfam graphical view of domain structure.
PRINTS PR00301; HEATSHOCK70.
ProDom PD000089; Hsp70; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00297; HSP70_1; 1.
PS00329; HSP70_2; 1.
PS01036; HSP70_3; 1.
Proteomic databases
PeptideAtlas P11142; -.
PRIDE P11142; -.
Genome annotation databases
Ensembl ENSG00000109971; Homo sapiens. [Contig view]
GeneID 3312; -.
KEGG hsa:3312; -.
Phylogenomic databases
HOGENOM P11142; -.
HOVERGEN P11142; -.
OMA P11142; QDYFNGK.
Other
NextBio 13136; -.
PMAP-CutDB P11142; -.
SOURCE HSPA8; Homo sapiens.
ProtoNet P11142.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleotide-binding; Phosphoprotein; Polymorphism; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   646  645     Heat shock cognate 71 kDa protein. PRO_0000078270
MOD_RES   2     2        N-acetylserine. 
MOD_RES   15    15        Phosphotyrosine. 
MOD_RES   41    41        Phosphotyrosine. 
MOD_RES   107   107        Phosphotyrosine. 
MOD_RES   113   113        Phosphoserine. 
MOD_RES   115   115        Phosphotyrosine. 
MOD_RES   120   120        Phosphoserine. 
MOD_RES   121   121        Phosphoserine. 
MOD_RES   153   153        Phosphoserine. 
MOD_RES   477   477        Phosphothreonine. 
VAR_SEQ   464   616        Missing (in isoform 2). VSP_002427
VARIANT   32    32  1     D -> Y (in dbSNP:rs11551602 [NCBI]). VAR_049619 [3D]
VARIANT   459   459  1     F -> L (in dbSNP:rs11551598 [NCBI]). VAR_049620 
Sequence information
Length: 646 AA [This is the length of the unprocessed precursor] Molecular weight: 70898 Da [This is the MW of the unprocessed precursor] CRC64: 9AA27B210730670C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 

        70         80         90        100        110        120 
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 

       130        140        150        160        170        180 
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 

       190        200        210        220        230        240 
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 

       250        260        270        280        290        300 
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 

       310        320        330        340        350        360 
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 

       370        380        390        400        410        420 
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI 

       430        440        450        460        470        480 
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI 

       490        500        510        520        530        540 
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN 

       550        560        570        580        590        600 
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE 

       610        620        630        640 
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD 

P11142 in FASTA format

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