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

USC-OGP 2-DE database  Search by                Maps             Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal World-2DPAGE Repository Exclude local DBs has only effect if a remote interface is selected

Searching in 'USC-OGP 2-DE database' for entry matching: P0DMV8 USC-OGP 2-DE database:  P0DMV8 P0DMV8 General information about the entry View entry in simple text format Entry name HS71A_HUMAN Primary accession number P0DMV8 Secondary accession number(s) P08107 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 70 kDa protein 1A {ECO:0000312|HGNC:HGNC:5232}; AltName: Full=Heat shock 70 kDa protein 1; Short=HSP70-1 {ECO:0000303|PubMed:14656967, ECO:0000303|PubMed:2538825}; Short=HSP70.1;. Gene name Name=HSPA1A Synonyms=HSP72 {ECO:0000303|PubMed:24318877}, HSPA1, HSX70 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_4-7 {PLATELET 4-7} Homo sapiens (Human)   map experimental info   PLATELET_4-7 MAP LOCATIONS: SPOT OGP-0312: pI=5.38; Mw=69968 SPOT OGP-0313: pI=5.33; Mw=69752 SPOT OGP-0315: pI=5.28; Mw=67425 SPOT OGP-0317: pI=5.32; Mw=67217 PLATELET_5-6 {PLATELET 5-6} Homo sapiens (Human)   map experimental info   PLATELET_5-6 MAP LOCATIONS: SPOT OGP-0631: pI=5.29; Mw=70092 SPOT OGP-0632: pI=5.41; Mw=69683 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1133: pI=5.37; Mw=64830 Cross-references UniProtKB/Swiss-Prot P0DMV8; HS71A_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 HS71A_HUMAN Primary accession number P0DMV8 Secondary accession number(s) B4E3B6 P08107 P19790 Q5JQI4 Q5SP17 Q9UQL9 Q9UQM0 Sequence was last modified on  May 27, 2015 (version 1) Annotations were last modified on  March 15, 2017 (version 21) Name and origin of the protein Description RecName: Full=Heat shock 70 kDa protein 1A {ECO:0000312|HGNC:HGNC:5232}; AltName: Full=Heat shock 70 kDa protein 1; Short=HSP70-1 {ECO:0000303|PubMed:14656967, ECO:0000303|PubMed:2538825}; Short=HSP70.1; Gene name Name=HSPA1A Synonyms=HSP72 {ECO:0000303|PubMed:24318877}, HSPA1, HSX70 Encoded on Name=HSPA1A; Synonyms=HSP72 {ECO:0000303|PubMed:24318877}, HSPA1, HSX70 Keywords 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Host cell receptor for virus entry; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Stress response. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL M11717; AAA52697.1; -; Genomic_DNA EMBL M59828; AAA63226.1; -; Genomic_DNA EMBL BA000025; BAB63300.1; -; Genomic_DNA EMBL AF134726; AAD21816.1; -; Genomic_DNA EMBL AK304652; BAG65428.1; -; mRNA EMBL DQ451402; ABD96830.1; -; Genomic_DNA EMBL AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL BC002453; AAH02453.1; -; mRNA EMBL M24743; AAA59844.1; -; Genomic_DNA EMBL X04676; CAA28381.1; -; Genomic_DNA EMBL X04677; CAA28382.1; -; Genomic_DNA CCDS CCDS34414.1; -. [P0DMV8-1]; . PIR A29160; A29160; . PIR A45871; A45871; . PIR I59139; I59139; . PIR I79540; I79540; . RefSeq NP_005336.3; NM_005345.5. [P0DMV8-1]; . RefSeq NP_005337.2; NM_005346.4. [P0DMV8-1]; . UniGene Hs.274402; -; . UniGene Hs.702139; -; . UniGene Hs.719966; -; . UniGene Hs.743411; -; . PDB 1HJO; X-ray; 2.30 A; A=3-382 PDB 1S3X; X-ray; 1.84 A; A=1-382 PDB 1XQS; X-ray; 2.90 A; C/D=184-371 PDB 2E88; X-ray; 1.80 A; A=1-388 PDB 2E8A; X-ray; 1.77 A; A=1-388 PDB 2LMG; NMR; -; A=537-610 PDB 3A8Y; X-ray; 2.30 A; A/B=1-388 PDB 3ATU; X-ray; 1.65 A; A=1-388 PDB 3ATV; X-ray; 1.58 A; A=1-388 PDB 3AY9; X-ray; 1.75 A; A=1-388 PDB 3D2E; X-ray; 2.35 A; B/D=1-382 PDB 3D2F; X-ray; 2.30 A; B/D=1-382 PDB 3JXU; X-ray; 2.14 A; A=1-387 PDB 3LOF; X-ray; 2.40 A; A/B/C/D/E/F=534-641 PDB 3Q49; X-ray; 1.54 A; C=634-641 PDB 4IO8; X-ray; 2.58 A; A=1-382 PDB 4J8F; X-ray; 2.70 A; A=1-382 PDB 4PO2; X-ray; 2.00 A; A/B=386-613 PDB 4WV5; X-ray; 2.04 A; A/B=395-543 PDB 4WV7; X-ray; 2.42 A; A/B=395-543 PDB 5AQW; X-ray; 1.53 A; A=1-380 PDB 5AQX; X-ray; 2.12 A; A=1-380 PDB 5AQY; X-ray; 1.56 A; A=1-380 PDB 5AQZ; X-ray; 1.65 A; A=1-380 PDB 5AR0; X-ray; 1.90 A; A=1-380 PDB 5BN8; X-ray; 1.34 A; A=1-388 PDB 5BN9; X-ray; 1.69 A; A=1-388 PDB 5BPL; X-ray; 1.93 A; A=1-388 PDB 5BPM; X-ray; 1.83 A; A=1-388 PDB 5BPN; X-ray; 2.10 A; A=1-388 PDBsum 1HJO; -; . PDBsum 1S3X; -; . PDBsum 1XQS; -; . PDBsum 2E88; -; . PDBsum 2E8A; -; . PDBsum 2LMG; -; . PDBsum 3A8Y; -; . PDBsum 3ATU; -; . PDBsum 3ATV; -; . PDBsum 3AY9; -; . PDBsum 3D2E; -; . PDBsum 3D2F; -; . PDBsum 3JXU; -; . PDBsum 3LOF; -; . PDBsum 3Q49; -; . PDBsum 4IO8; -; . PDBsum 4J8F; -; . PDBsum 4PO2; -; . PDBsum 4WV5; -; . PDBsum 4WV7; -; . PDBsum 5AQW; -; . PDBsum 5AQX; -; . PDBsum 5AQY; -; . PDBsum 5AQZ; -; . PDBsum 5AR0; -; . PDBsum 5BN8; -; . PDBsum 5BN9; -; . PDBsum 5BPL; -; . PDBsum 5BPM; -; . PDBsum 5BPN; -; . ProteinModelPortal P0DMV8; -; . SMR P0DMV8; -; . IntAct P0DMV8; 14; . MINT MINT-96699; -; . BindingDB P0DMV8; -; . ChEMBL CHEMBL5460; -; . iPTMnet P0DMV8; -; . PhosphoSitePlus P0DMV8; -; . SwissPalm P0DMV8; -; . DMDM 147744565; -; . REPRODUCTION-2DPAGE IPI00304925; -; . PeptideAtlas P0DMV8; -; . PRIDE P0DMV8; -; . DNASU 3303; -; . Ensembl ENST00000375651; ENSP00000364802; ENSG00000204389. [P0DMV8-1]; . Ensembl ENST00000400040; ENSP00000382915; ENSG00000215328; . Ensembl ENST00000430065; ENSP00000404524; ENSG00000235941. [P0DMV8-1]; . Ensembl ENST00000433487; ENSP00000408907; ENSG00000234475. [P0DMV8-1]; . Ensembl ENST00000441618; ENSP00000406359; ENSG00000237724. [P0DMV8-1]; . GeneID 3303; -; . GeneID 3304; -; . KEGG hsa:3303; -; . KEGG hsa:3304; -; . CTD 3303; -; . CTD 3304; -; . GeneCards HSPA1A; -; . H-InvDB HIX0058169; -; . H-InvDB HIX0058187; -; . H-InvDB HIX0166160; -; . HGNC HGNC:5232; HSPA1A; . HPA CAB017451; -; . HPA CAB032815; -; . HPA HPA052504; -; . MIM 140550; gene; . MIM 603012; gene; . neXtProt NX_P0DMV8; -; . OpenTargets ENSG00000204388; -; . OpenTargets ENSG00000204389; -; . HOGENOM HOG000228135; -; . HOVERGEN HBG051845; -; . KO K03283; -; . OrthoDB EOG093705LK; -; . PhylomeDB P0DMV8; -; . TreeFam TF105042; -; . Reactome R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus; . 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-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA; . Reactome R-HSA-6798695; Neutrophil degranulation; . SIGNOR P0DMV8; -; . ChiTaRS HSPA1A; human; . ChiTaRS HSPA1B; human; . GeneWiki HSPA1A; -; . PRO PR:P0DMV8; -; . Proteomes UP000005640; Chromosome 6; . CleanEx HS_HSPA1A; -; . ExpressionAtlas P0DMV8; baseline and differential; . GO GO:0072562; C:blood microparticle; IDA:UniProtKB; . GO GO:0005814; C:centriole; IDA:UniProtKB; . GO GO:0005813; C:centrosome; IDA:UniProtKB; . GO GO:0005737; C:cytoplasm; IDA:UniProtKB; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0005925; C:focal adhesion; IDA:UniProtKB; . GO GO:0016234; C:inclusion body; IDA:BHF-UCL; . GO GO:0005739; C:mitochondrion; IEA:GOC; . GO GO:0005654; C:nucleoplasm; TAS:Reactome; . GO GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL; . 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; IDA: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; IDA:ParkinsonsUK-UCL; . GO GO:0031072; F:heat shock protein binding; IPI:UniProtKB; . GO GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL; . GO GO:0044183; F:protein binding involved in protein folding; IDA:BHF-UCL; . GO GO:0005102; F:receptor binding; IPI:UniProtKB; . GO GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:UniProtKB; . GO GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL; . GO GO:0051082; F:unfolded protein binding; IDA:UniProtKB; . GO GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW; . GO GO:0046034; P:ATP metabolic process; IDA:BHF-UCL; . GO GO:0070370; P:cellular heat acclimation; IMP:UniProtKB; . GO GO:0034605; P:cellular response to heat; IDA:UniProtKB; . GO GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL; . GO GO:0060548; P:negative regulation of cell death; IMP:UniProtKB; . GO GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL; . GO GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL; . GO GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB; . GO GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:ParkinsonsUK-UCL; . GO GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL; . GO GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB; . GO GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:1902380; P:positive regulation of endoribonuclease activity; IDA:ParkinsonsUK-UCL; . GO GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL; . GO GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB; . GO GO:0090063; P:positive regulation of microtubule nucleation; IMP:UniProtKB; . GO GO:1904722; P:positive regulation of mRNA endonucleolytic cleavage involved in unfolded protein response; IDA:ParkinsonsUK-UCL; . GO GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB; . GO GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB; . GO GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB; . GO GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB; . GO GO:0042026; P:protein refolding; IDA:UniProtKB; . GO GO:0050821; P:protein stabilization; IMP:UniProtKB; . GO GO:1900034; P:regulation of cellular response to heat; TAS:Reactome; . GO GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB; . GO GO:0043488; P:regulation of mRNA stability; TAS:Reactome; . GO GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL; . 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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