USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

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Searching in 'USC-OGP 2-DE database' for entry matching: P11142 USC-OGP 2-DE database:  P11142 P11142 General information about the entry View entry in simple text format Entry name HSP7C_HUMAN Primary accession number P11142 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: 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 name Name=HSPA8 Synonyms=HSC70, HSP73, HSPA10 Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein PLATELET_4-5 {PLATELET 4-5} Homo sapiens (Human)   map experimental info   PLATELET_4-5 MAP LOCATIONS: SPOT OGP-0086: pI=4.92; Mw=44195 SPOT OGP-0088: pI=4.89; Mw=43348 PLATELET_4-7 {PLATELET 4-7} Homo sapiens (Human)   map experimental info   PLATELET_4-7 MAP LOCATIONS: SPOT OGP-0310: pI=5.19; Mw=71275 SPOT OGP-0311: pI=5.24; Mw=70401 SPOT OGP-0315: pI=5.28; Mw=67425 PLATELET_5-6 {PLATELET 5-6} Homo sapiens (Human)   map experimental info   PLATELET_5-6 MAP LOCATIONS: SPOT OGP-0629: pI=5.19; Mw=70504 SPOT OGP-0630: pI=5.22; Mw=70092 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1121: pI=5.77; Mw=83686 SPOT OGP-1133: pI=5.37; Mw=64830 SPOT OGP-1209: pI=5.53; Mw=37929 Cross-references UniProtKB/Swiss-Prot P11142; 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 name HSP7C_HUMAN Primary accession number P11142 Secondary accession number(s) Q9H3R6 Sequence was last modified on  July 1, 1989 (version 1) Annotations were last modified on  March 15, 2017 (version 209) Name and origin of the protein Description RecName: 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 name Name=HSPA8 Synonyms=HSC70, HSP73, HSPA10 Encoded on Name=HSPA8; Synonyms=HSC70, HSP73, HSPA10 Keywords 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell membrane; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Isopeptide bond; 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 http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL Y00371; CAA68445.1; -; Genomic_DNA EMBL AB034951; BAB18615.1; -; mRNA EMBL AF352832; AAK17898.1; -; mRNA EMBL BC016179; AAH16179.1; -; mRNA EMBL BC016660; AAH16660.1; -; mRNA EMBL BC019816; AAH19816.1; -; mRNA CCDS CCDS44754.1; -. [P11142-2]; . CCDS CCDS8440.1; -. [P11142-1]; . PIR A27077; A27077; . RefSeq NP_006588.1; NM_006597.5. [P11142-1]; . RefSeq NP_694881.1; NM_153201.3. [P11142-2]; . RefSeq XP_011541100.1; XM_011542798.1. [P11142-1]; . UniGene Hs.180414; -; . PDB 3AGY; X-ray; 1.85 A; C/D/F=639-646 PDB 3AGZ; X-ray; 2.51 A; C/D/E/F=639-646 PDB 3ESK; X-ray; 2.05 A; B=635-646 PDB 3FZF; X-ray; 2.20 A; A=4-381 PDB 3FZH; X-ray; 2.00 A; A=4-381 PDB 3FZK; X-ray; 2.10 A; A=4-381 PDB 3FZL; X-ray; 2.20 A; A=4-381 PDB 3FZM; X-ray; 2.30 A; A=4-381 PDB 3LDQ; X-ray; 1.90 A; A=4-381 PDB 3M3Z; X-ray; 2.10 A; A=4-381 PDB 4H5N; X-ray; 1.86 A; A/B=2-384 PDB 4H5R; X-ray; 1.64 A; A/B=2-384 PDB 4H5T; X-ray; 1.90 A; A=2-384 PDB 4H5V; X-ray; 1.75 A; A=2-384 PDB 4H5W; X-ray; 1.94 A; A/B=2-384 PDB 4HWI; X-ray; 2.27 A; A=5-381 PDB 4KBQ; X-ray; 2.91 A; C/D=541-646 PDB 5AQF; X-ray; 1.88 A; A/C=1-381 PDB 5AQG; X-ray; 2.24 A; A/C/E=1-381 PDB 5AQH; X-ray; 2.00 A; A=1-381 PDB 5AQI; X-ray; 1.98 A; A/C=1-381 PDB 5AQJ; X-ray; 1.96 A; A/C/E=1-381 PDB 5AQK; X-ray; 2.09 A; A=1-381 PDB 5AQL; X-ray; 1.69 A; A/C=1-381 PDB 5AQM; X-ray; 1.63 A; A/C=1-381 PDB 5AQN; X-ray; 2.45 A; A/C/E=1-381 PDB 5AQO; X-ray; 2.12 A; A/C/E=1-381 PDB 5AQP; X-ray; 2.08 A; A/C/E=1-381 PDB 5AQQ; X-ray; 2.72 A; A/C/E=1-381 PDB 5AQR; X-ray; 1.91 A; A/C/E=1-381 PDB 5AQS; X-ray; 2.00 A; A/C=1-381 PDB 5AQT; X-ray; 1.90 A; A=1-381 PDB 5AQU; X-ray; 1.92 A; A=1-381 PDB 5AQV; X-ray; 1.75 A; A=1-381 PDBsum 3AGY; -; . PDBsum 3AGZ; -; . PDBsum 3ESK; -; . PDBsum 3FZF; -; . PDBsum 3FZH; -; . PDBsum 3FZK; -; . PDBsum 3FZL; -; . PDBsum 3FZM; -; . PDBsum 3LDQ; -; . PDBsum 3M3Z; -; . PDBsum 4H5N; -; . PDBsum 4H5R; -; . PDBsum 4H5T; -; . PDBsum 4H5V; -; . PDBsum 4H5W; -; . PDBsum 4HWI; -; . PDBsum 4KBQ; -; . PDBsum 5AQF; -; . PDBsum 5AQG; -; . PDBsum 5AQH; -; . PDBsum 5AQI; -; . PDBsum 5AQJ; -; . PDBsum 5AQK; -; . PDBsum 5AQL; -; . PDBsum 5AQM; -; . PDBsum 5AQN; -; . PDBsum 5AQO; -; . PDBsum 5AQP; -; . PDBsum 5AQQ; -; . PDBsum 5AQR; -; . PDBsum 5AQS; -; . PDBsum 5AQT; -; . PDBsum 5AQU; -; . PDBsum 5AQV; -; . ProteinModelPortal P11142; -; . SMR P11142; -; . BioGrid 109544; 510; . DIP DIP-32874N; -; . IntAct P11142; 120; . MINT MINT-4998609; -; . STRING 9606.ENSP00000227378; -; . BindingDB P11142; -; . ChEMBL CHEMBL1275223; -; . iPTMnet P11142; -; . PhosphoSitePlus P11142; -; . SwissPalm P11142; -; . DMDM 123648; -; . DOSAC-COBS-2DPAGE P11142; -; . OGP P11142; -; . REPRODUCTION-2DPAGE IPI00003865; -; . SWISS-2DPAGE P11142; -; . UCD-2DPAGE P11142; -; . EPD P11142; -; . PaxDb P11142; -; . PeptideAtlas P11142; -; . PRIDE P11142; -; . TopDownProteomics P11142-1; -. [P11142-1]; . TopDownProteomics P11142-2; -. [P11142-2]; . DNASU 3312; -; . Ensembl ENST00000227378; ENSP00000227378; ENSG00000109971. [P11142-1]; . Ensembl ENST00000453788; ENSP00000404372; ENSG00000109971. [P11142-2]; . Ensembl ENST00000532636; ENSP00000437125; ENSG00000109971. [P11142-1]; . Ensembl ENST00000534624; ENSP00000432083; ENSG00000109971. [P11142-1]; . GeneID 3312; -; . KEGG hsa:3312; -; . UCSC uc001pyp.5; human. [P11142-1]; . CTD 3312; -; . DisGeNET 3312; -; . GeneCards HSPA8; -; . H-InvDB HIX0033867; -; . HGNC HGNC:5241; HSPA8; . HPA CAB002056; -; . HPA HPA052504; -; . MIM 600816; gene; . neXtProt NX_P11142; -; . OpenTargets ENSG00000109971; -; . PharmGKB PA29507; -; . eggNOG KOG0101; Eukaryota; . eggNOG COG0443; LUCA; . GeneTree ENSGT00870000136409; -; . HOGENOM HOG000228135; -; . HOVERGEN HBG051845; -; . InParanoid P11142; -; . KO K03283; -; . OMA RTQCERT; -; . OrthoDB EOG091G03SF; -; . PhylomeDB P11142; -; . TreeFam TF105042; -; . BRENDA 3.6.3.51; 2681; . Reactome R-HSA-3371453; Regulation of HSF1-mediated heat shock response; . Reactome R-HSA-3371568; Attenuation phase; . Reactome R-HSA-3371571; HSF1-dependent transactivation; . Reactome R-HSA-432720; Lysosome Vesicle Biogenesis; . Reactome R-HSA-432722; Golgi Associated Vesicle Biogenesis; . Reactome R-HSA-447041; CHL1 interactions; . Reactome R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA; . Reactome R-HSA-6785807; Interleukin-4 and 13 signaling; . Reactome R-HSA-6798695; Neutrophil degranulation; . Reactome R-HSA-72163; mRNA Splicing - Major Pathway; . Reactome R-HSA-8856828; Clathrin-mediated endocytosis; . Reactome R-HSA-8876725; Protein methylation; . Reactome R-HSA-888590; GABA synthesis; release; reuptake and degradation ChiTaRS HSPA8; human; . EvolutionaryTrace P11142; -; . GeneWiki HSPA8; -; . GenomeRNAi 3312; -; . PMAP-CutDB P11142; -; . PRO PR:P11142; -; . Proteomes UP000005640; Chromosome 11; . Bgee ENSG00000109971; -; . CleanEx HS_HSPA8; -; . ExpressionAtlas P11142; baseline and differential; . Genevisible P11142; HS; . GO GO:0072562; C:blood microparticle; IDA:UniProtKB; . GO GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0031012; C:extracellular matrix; IDA:BHF-UCL; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0005615; C:extracellular space; IDA:UniProtKB; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0005925; C:focal adhesion; IDA:UniProtKB; . GO GO:0005622; C:intracellular; NAS:UniProtKB; . GO GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB; . GO GO:0005770; C:late endosome; IEA:Ensembl; . GO GO:0098575; C:lumenal side of lysosomal membrane; TAS:ParkinsonsUK-UCL; . GO GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL; . GO GO:0005765; C:lysosomal membrane; ISS:ParkinsonsUK-UCL; . GO GO:0042470; C:melanosome; IEA:UniProtKB-SubCell; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0043209; C:myelin sheath; IEA:Ensembl; . GO GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell; . GO GO:0005654; C:nucleoplasm; TAS:Reactome; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0005886; C:plasma membrane; TAS:Reactome; . GO GO:0098793; C:presynapse; IEA:GOC; . GO GO:0000974; C:Prp19 complex; IDA:UniProtKB; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW; . GO GO:0005524; F:ATP binding; IDA:BHF-UCL; . GO GO:0016887; F:ATPase activity; IDA:BHF-UCL; . GO GO:0042623; F:ATPase activity; coupled; NAS:UniProtKB GO GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL; . GO GO:0045296; F:cadherin binding; IDA:BHF-UCL; . GO GO:0019899; F:enzyme binding; IPI:BHF-UCL; . GO GO:0001664; F:G-protein coupled receptor binding; IPI:ParkinsonsUK-UCL; . GO GO:0031072; F:heat shock protein binding; IPI:UniProtKB; . GO GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB; . GO GO:0001786; F:phosphatidylserine binding; IEA:Ensembl; . GO GO:0003723; F:RNA binding; IDA:UniProtKB; . GO GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL; . GO GO:0051082; F:unfolded protein binding; IDA:UniProtKB; . GO GO:0046034; P:ATP metabolic process; IDA:BHF-UCL; . GO GO:0009267; P:cellular response to starvation; TAS:ParkinsonsUK-UCL; . GO GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl; . GO GO:0061684; P:chaperone-mediated autophagy; ISS:ParkinsonsUK-UCL; . GO GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; ISS:ParkinsonsUK-UCL; . GO GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL; . GO GO:0072318; P:clathrin coat disassembly; IEA:Ensembl; . GO GO:0061738; P:late endosomal microautophagy; IEA:Ensembl; . GO GO:0061024; P:membrane organization; TAS:Reactome; . GO GO:0000398; P:mRNA splicing; via spliceosome; TAS:Reactome GO GO:1902904; P:negative regulation of supramolecular fiber organization; IDA:BHF-UCL; . GO GO:0045892; P:negative regulation of transcription; DNA-templated; IDA:UniProtKB GO GO:0007269; P:neurotransmitter secretion; TAS:Reactome; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0044829; P:positive regulation by host of viral genome replication; IEA:Ensembl; . GO GO:0048026; P:positive regulation of mRNA splicing; via spliceosome; IEA:Ensembl GO GO:0006457; P:protein folding; NAS:UniProtKB; . GO GO:0006479; P:protein methylation; TAS:Reactome; . GO GO:0042026; P:protein refolding; IDA:UniProtKB; . GO GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL; . GO GO:0051726; P:regulation of cell cycle; IEA:Ensembl; . GO GO:1900034; P:regulation of cellular response to heat; TAS:Reactome; . GO GO:0043488; P:regulation of mRNA stability; TAS:Reactome; . GO GO:0043254; P:regulation of protein complex assembly; TAS:ParkinsonsUK-UCL; . GO GO:0061635; P:regulation of protein complex stability; ISS:ParkinsonsUK-UCL; . GO GO:1904589; P:regulation of protein import; TAS:ParkinsonsUK-UCL; . GO GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL; . GO GO:0006986; P:response to unfolded protein; NAS:UniProtKB; . GO GO:0006351; P:transcription; DNA-templated; IEA:UniProtKB-KW GO GO:0016032; P:viral process; IEA:UniProtKB-KW; . Gene3D 1.20.1270.10; -; 1; . Gene3D 2.60.34.10; -; 1; . InterPro IPR018181; Heat_shock_70_CS; . InterPro IPR029048; HSP70_C; . InterPro IPR029047; HSP70_peptide-bd; . InterPro IPR013126; Hsp_70_fam; . Pfam PF00012; HSP70; 1; . PRINTS PR00301; HEATSHOCK70; . SUPFAM SSF100920; SSF100920; 1; . SUPFAM SSF100934; SSF100934; 1; . PROSITE PS00297; HSP70_1; 1; . PROSITE PS00329; HSP70_2; 1; . PROSITE PS01036; HSP70_3; 1; .

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