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Searching in 'World-2DPAGE Repository [0054]' for entry matching: P11142




World-2DPAGE Repository (0054):  P11142


P11142


General information about the entry
View entry in simple text format
Entry nameHSP7C_HUMAN
Primary accession numberP11142
integrated into World-2DPAGE Repository (0054) on November 28, 2012 (release 1)
2D Annotations were last modified onNovember 28, 2012 (version 1)
General Annotations were last modified on October 23, 2014 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Heat shock cognate 71 kDa protein; AltName: Full=Heat shock 70 kDa protein 8; AltName: Full=Lipopolysaccharide-associated protein 1; Short=LAP-1; Short=LPS-associated protein 1;.
Gene nameName=HSPA8
Synonyms=HSC70, HSP73, HSPA10
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
DOI=10.1074/mcp.M112.022947;
Vernocchi S., Battello N., Schmitz S., Revets D., Billing A.M., Turner J.D., Muller C.P.
''Membrane glucocorticoid receptor activation induces proteomic changes aligning with classical glucocorticoid-effects''
Molecular & Cellular Proteomics 12(7):1764-1779 (2013)
2D PAGE maps for identified proteins
How to interpret a protein

HSAPIENS_CCRF-CEM_3-10 {CCRF-CEM cells stimulated with Cort-BSA (internal standard)}
Homo sapiens (Human)
HSAPIENS_CCRF-CEM_3-10
  map experimental info
 
HSAPIENS_CCRF-CEM_3-10

MAP LOCATIONS:
pI=5.37; Mw=70767  [identification data]

%COV: SPOT 535: 52 [1].
SCORE: SPOT 535: 901 [1].
SEARCH ENGINE: SPOT 535: Mascot [1].
MAPPING (identification):
SPOT 535: Peptide mass fingerprinting [1]; Tandem mass spectrometry [1].

Copyright
Data from Dr. Claude P. Muller, Centre de Recherche Public de la Sante / National Public Health Laboratory, Luxembourg
Cross-references
UniProtKB/Swiss-ProtP11142; HSP7C_HUMAN.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 0.0
Entry nameHSP7C_HUMAN
Primary accession numberP11142
Secondary accession number(s) Q9H3R6
Sequence was last modified on July 1, 1989 (version 1)
Annotations were last modified on October 1, 2014 (version 182)
Name and origin of the protein
DescriptionRecName: Full=Heat shock cognate 71 kDa protein; AltName: Full=Heat shock 70 kDa protein 8; AltName: Full=Lipopolysaccharide-associated protein 1; Short=LAP-1; Short=LPS-associated protein 1;
Gene nameName=HSPA8
Synonyms=HSC70, HSP73, HSPA10
Encoded onName=HSPA8; Synonyms=HSC70, HSP73, HSPA10
Keywords3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell membrane; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Membrane; Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Spliceosome; Stress response; Transcription; Transcription regulation; Ubl conjugation.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLY00371; CAA68445.1; -; Genomic_DNA
EMBLAB034951; BAB18615.1; -; mRNA
EMBLAF352832; AAK17898.1; -; mRNA
EMBLBC016179; AAH16179.1; -; mRNA
EMBLBC016660; AAH16660.1; -; mRNA
EMBLBC019816; AAH19816.1; -; mRNA
CCDSCCDS44754.1; -. [P11142-2]; .
CCDSCCDS8440.1; -. [P11142-1]; .
PIRA27077; A27077; .
RefSeqNP_006588.1; NM_006597.5. [P11142-1]; .
RefSeqNP_694881.1; NM_153201.3. [P11142-2]; .
RefSeqXP_006718894.1; XM_006718831.1. [P11142-1]; .
UniGeneHs.180414; -; .
PDB3AGY; X-ray; 1.85 A; C/D/F=639-646
PDB3AGZ; X-ray; 2.51 A; C/D/E/F=639-646
PDB3ESK; X-ray; 2.05 A; B=635-646
PDB3FZF; X-ray; 2.20 A; A=4-381
PDB3FZH; X-ray; 2.00 A; A=4-381
PDB3FZK; X-ray; 2.10 A; A=4-381
PDB3FZL; X-ray; 2.20 A; A=4-381
PDB3FZM; X-ray; 2.30 A; A=4-381
PDB3LDQ; X-ray; 1.90 A; A=4-381
PDB3M3Z; X-ray; 2.10 A; A=4-381
PDB4H5N; X-ray; 1.86 A; A/B=2-384
PDB4H5R; X-ray; 1.64 A; A/B=2-384
PDB4H5T; X-ray; 1.90 A; A=2-384
PDB4H5V; X-ray; 1.75 A; A=2-384
PDB4H5W; X-ray; 1.94 A; A/B=2-384
PDB4HWI; X-ray; 2.27 A; A=5-381
PDBsum3AGY; -; .
PDBsum3AGZ; -; .
PDBsum3ESK; -; .
PDBsum3FZF; -; .
PDBsum3FZH; -; .
PDBsum3FZK; -; .
PDBsum3FZL; -; .
PDBsum3FZM; -; .
PDBsum3LDQ; -; .
PDBsum3M3Z; -; .
PDBsum4H5N; -; .
PDBsum4H5R; -; .
PDBsum4H5T; -; .
PDBsum4H5V; -; .
PDBsum4H5W; -; .
PDBsum4HWI; -; .
ProteinModelPortalP11142; -; .
SMRP11142; 1-621; .
BioGrid109544; 254; .
IntActP11142; 91; .
MINTMINT-4998609; -; .
STRING9606.ENSP00000227378; -; .
BindingDBP11142; -; .
ChEMBLCHEMBL1275223; -; .
PhosphoSiteP11142; -; .
DMDM123648; -; .
DOSAC-COBS-2DPAGEP11142; -; .
OGPP11142; -; .
REPRODUCTION-2DPAGEIPI00003865; -; .
SWISS-2DPAGEP11142; -; .
UCD-2DPAGEP11142; -; .
MaxQBP11142; -; .
PaxDbP11142; -; .
PeptideAtlasP11142; -; .
PRIDEP11142; -; .
DNASU3312; -; .
EnsemblENST00000227378; ENSP00000227378; ENSG00000109971. [P11142-1]; .
EnsemblENST00000453788; ENSP00000404372; ENSG00000109971. [P11142-2]; .
EnsemblENST00000532636; ENSP00000437125; ENSG00000109971. [P11142-1]; .
EnsemblENST00000534624; ENSP00000432083; ENSG00000109971. [P11142-1]; .
GeneID3312; -; .
KEGGhsa:3312; -; .
UCSCuc001pyo.3; human. [P11142-1]; .
UCSCuc001pyp.3; human. [P11142-2]; .
CTD3312; -; .
GeneCardsGC11M122969; -; .
H-InvDBHIX0033867; -; .
HGNCHGNC:5241; HSPA8; .
HPACAB002056; -; .
MIM600816; gene; .
neXtProtNX_P11142; -; .
PharmGKBPA29507; -; .
eggNOGCOG0443; -; .
HOGENOMHOG000228135; -; .
HOVERGENHBG051845; -; .
InParanoidP11142; -; .
KOK03283; -; .
OMAGENKIFT; -; .
OrthoDBEOG7PCJGF; -; .
PhylomeDBP11142; -; .
TreeFamTF105042; -; .
ReactomeREACT_19287; Lysosome Vesicle Biogenesis; .
ReactomeREACT_19400; Golgi Associated Vesicle Biogenesis; .
ReactomeREACT_200624; Attenuation phase; .
ReactomeREACT_200775; HSF1-dependent transactivation; .
ReactomeREACT_200780; Regulation of HSF1-mediated heat shock response; .
ReactomeREACT_22292; CHL1 interactions; .
ReactomeREACT_23947; GABA synthesis; release; reuptake and degradation
ReactomeREACT_25325; AUF1 (hnRNP D0) destabilizes mRNA; .
ChiTaRSHSPA8; human; .
EvolutionaryTraceP11142; -; .
GeneWikiHSPA8; -; .
GenomeRNAi3312; -; .
NextBio13136; -; .
PMAP-CutDBP11142; -; .
PROPR:P11142; -; .
ArrayExpressP11142; -; .
BgeeP11142; -; .
CleanExHS_HSPA8; -; .
GenevestigatorP11142; -; .
GOGO:0072562; C:blood microparticle; IDA:UniProt; .
GOGO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome; .
GOGO:0005829; C:cytosol; IDA:UniProt; .
GOGO:0005615; C:extracellular space; IDA:UniProt; .
GOGO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB; .
GOGO:0005622; C:intracellular; NAS:UniProtKB; .
GOGO:0042470; C:melanosome; IEA:UniProtKB-SubCell; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005730; C:nucleolus; IDA:UniProtKB; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0005886; C:plasma membrane; TAS:Reactome; .
GOGO:0000974; C:Prp19 complex; IDA:UniProtKB; .
GOGO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB; .
GOGO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW; .
GOGO:0005524; F:ATP binding; IDA:BHF-UCL; .
GOGO:0016887; F:ATPase activity; IDA:BHF-UCL; .
GOGO:0042623; F:ATPase activity; coupled; NAS:UniProtKB
GOGO:0019899; F:enzyme binding; IPI:BHF-UCL; .
GOGO:0031072; F:heat shock protein binding; IPI:BHF-UCL; .
GOGO:0023026; F:MHC class II protein complex binding; IDA:UniProt; .
GOGO:0044822; F:poly(A) RNA binding; IDA:UniProtKB; .
GOGO:0005515; F:protein binding; IPI:UniProtKB; .
GOGO:0051082; F:unfolded protein binding; IDA:UniProt; .
GOGO:0006200; P:ATP catabolic process; IDA:BHF-UCL; .
GOGO:0007411; P:axon guidance; TAS:Reactome; .
GOGO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl; .
GOGO:0010467; P:gene expression; TAS:Reactome; .
GOGO:0061024; P:membrane organization; TAS:Reactome; .
GOGO:0016071; P:mRNA metabolic process; TAS:Reactome; .
GOGO:0006397; P:mRNA processing; IEA:UniProtKB-KW; .
GOGO:1902904; P:negative regulation of fibril organization; IDA:BHF-UCL; .
GOGO:0045892; P:negative regulation of transcription; DNA-templated; IDA:UniProtKB
GOGO:0007269; P:neurotransmitter secretion; TAS:Reactome; .
GOGO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome; .
GOGO:0006457; P:protein folding; NAS:UniProtKB; .
GOGO:0042026; P:protein refolding; IDA:UniProt; .
GOGO:0051726; P:regulation of cell cycle; IEA:Ensembl; .
GOGO:0006986; P:response to unfolded protein; NAS:UniProtKB; .
GOGO:0016070; P:RNA metabolic process; TAS:Reactome; .
GOGO:0008380; P:RNA splicing; IEA:UniProtKB-KW; .
GOGO:0007268; P:synaptic transmission; TAS:Reactome; .
GOGO:0006351; P:transcription; DNA-templated; IEA:UniProtKB-KW
GOGO:0016032; P:viral process; IEA:UniProtKB-KW; .
Gene3D1.20.1270.10; -; 1; .
Gene3D2.60.34.10; -; 1; .
InterProIPR018181; Heat_shock_70_CS; .
InterProIPR029048; HSP70_C; .
InterProIPR029047; HSP70_peptide-bd; .
InterProIPR013126; Hsp_70_fam; .
PfamPF00012; HSP70; 1; .
PRINTSPR00301; HEATSHOCK70; .
SUPFAMSSF100920; SSF100920; 1; .
SUPFAMSSF100934; SSF100934; 1; .
PROSITEPS00297; HSP70_1; 1; .
PROSITEPS00329; HSP70_2; 1; .
PROSITEPS01036; HSP70_3; 1; .



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World-2DPAGE Repository (search AC)


Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the Expasy web server