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: P18669 USC-OGP 2-DE database:  P18669 P18669 General information about the entry View entry in simple text format Entry name PGAM1_HUMAN Primary accession number P18669 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=Phosphoglycerate mutase 1; EC=5.4.2.11 {ECO:0000269|PubMed:23653202}; EC=5.4.2.4 {ECO:0000269|PubMed:23653202}; AltName: Full=BPG-dependent PGAM 1; AltName: Full=Phosphoglycerate mutase isozyme B; Short=PGAM-B;. Gene name Name=PGAM1 Synonyms=PGAMA ORFNames=CDABP0006 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-0506: pI=6.74; Mw=27760 PLATELET_6-11 {PLATELET 6-11} Homo sapiens (Human)   map experimental info   PLATELET_6-11 MAP LOCATIONS: SPOT OGP-1008: pI=6.69; Mw=27158 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1277: pI=6.93; Mw=27368 SPOT OGP-1278: pI=5.09; Mw=26938 Cross-references UniProtKB/Swiss-Prot P18669; PGAM1_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 PGAM1_HUMAN Primary accession number P18669 Secondary accession number(s) Q9BWC0 Sequence was last modified on  January 23, 2007 (version 2) Annotations were last modified on  March 15, 2017 (version 201) Name and origin of the protein Description RecName: Full=Phosphoglycerate mutase 1; EC=5.4.2.11 {ECO:0000269|PubMed:23653202}; EC=5.4.2.4 {ECO:0000269|PubMed:23653202}; AltName: Full=BPG-dependent PGAM 1; AltName: Full=Phosphoglycerate mutase isozyme B; Short=PGAM-B; Gene name Name=PGAM1 Synonyms=PGAMA ORFNames=CDABP0006 Encoded on Name=PGAM1; Synonyms=PGAMA; ORFNames=CDABP0006 Keywords 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL J04173; AAA60071.1; -; mRNA EMBL AY007118; AAG01990.1; -; mRNA EMBL BC010038; AAH10038.1; -; mRNA EMBL BC011678; AAH11678.1; -; mRNA EMBL BC053356; AAH53356.1; -; mRNA EMBL BC066959; AAH66959.1; -; mRNA EMBL BC073742; AAH73742.1; -; mRNA CCDS CCDS7458.1; -; . PIR A31782; PMHUYB; . RefSeq NP_002620.1; NM_002629.3; . UniGene Hs.632918; -; . PDB 1LJD; Model; -; A=1-254 PDB 1YFK; X-ray; 2.70 A; A/B=1-254 PDB 1YJX; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-254 PDB 4GPI; X-ray; 2.08 A; B/C=1-254 PDB 4GPZ; X-ray; 1.65 A; A/B=1-254 PDBsum 1LJD; -; . PDBsum 1YFK; -; . PDBsum 1YJX; -; . PDBsum 4GPI; -; . PDBsum 4GPZ; -; . ProteinModelPortal P18669; -; . SMR P18669; -; . BioGrid 111244; 39; . IntAct P18669; 14; . MINT MINT-3008987; -; . STRING 9606.ENSP00000359991; -; . ChEMBL CHEMBL3334418; -; . DEPOD P18669; -; . iPTMnet P18669; -; . PhosphoSitePlus P18669; -; . SwissPalm P18669; -; . BioMuta PGAM1; -; . DMDM 130348; -; . DOSAC-COBS-2DPAGE P18669; -; . OGP P18669; -; . SWISS-2DPAGE P18669; -; . UCD-2DPAGE P18669; -; . EPD P18669; -; . PaxDb P18669; -; . PeptideAtlas P18669; -; . PRIDE P18669; -; . TopDownProteomics P18669; -; . DNASU 5223; -; . Ensembl ENST00000334828; ENSP00000359991; ENSG00000171314; . GeneID 5223; -; . KEGG hsa:5223; -; . CTD 5223; -; . DisGeNET 5223; -; . GeneCards PGAM1; -; . H-InvDB HIX0036336; -; . H-InvDB HIX0120028; -; . HGNC HGNC:8888; PGAM1; . HPA HPA042528; -; . HPA HPA049237; -; . HPA HPA060483; -; . MIM 172250; gene; . neXtProt NX_P18669; -; . OpenTargets ENSG00000171314; -; . PharmGKB PA33225; -; . eggNOG KOG0235; Eukaryota; . eggNOG COG0588; LUCA; . GeneTree ENSGT00390000016700; -; . HOGENOM HOG000221682; -; . HOVERGEN HBG027528; -; . InParanoid P18669; -; . KO K01834; -; . OMA VKNQGKK; -; . OrthoDB EOG091G0GIS; -; . PhylomeDB P18669; -; . TreeFam TF300007; -; . BioCyc MetaCyc:HS10286-MONOMER; -; . BRENDA 5.4.2.11; 2681; . Reactome R-HSA-6798695; Neutrophil degranulation; . Reactome R-HSA-70171; Glycolysis; . Reactome R-HSA-70263; Gluconeogenesis; . SABIO-RK P18669; -; . SIGNOR P18669; -; . ChiTaRS PGAM1; human; . EvolutionaryTrace P18669; -; . GenomeRNAi 5223; -; . PRO PR:P18669; -; . Proteomes UP000005640; Chromosome 10; . Bgee ENSG00000171314; -; . CleanEx HS_PGAM1; -; . ExpressionAtlas P18669; baseline and differential; . Genevisible P18669; HS; . GO GO:0005737; C:cytoplasm; IDA:UniProtKB; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0043209; C:myelin sheath; IEA:Ensembl; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0046538; F:2; 3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IBA:GO_Central GO GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC; . GO GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW; . GO GO:0004619; F:phosphoglycerate mutase activity; IDA:UniProtKB; . GO GO:0019901; F:protein kinase binding; IPI:UniProtKB; . GO GO:0061621; P:canonical glycolysis; TAS:Reactome; . GO GO:0006094; P:gluconeogenesis; IBA:GO_Central; . GO GO:0006096; P:glycolytic process; IDA:UniProtKB; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0006110; P:regulation of glycolytic process; IDA:UniProtKB; . GO GO:0043456; P:regulation of pentose-phosphate shunt; IDA:UniProtKB; . GO GO:0045730; P:respiratory burst; IDA:UniProtKB; . CDD cd07067; HP_PGM_like; 1; . Gene3D 3.40.50.1240; -; 1; . HAMAP MF_01039; PGAM_GpmA; 1; . InterPro IPR013078; His_Pase_superF_clade-1; . InterPro IPR029033; His_PPase_superfam; . InterPro IPR001345; PG/BPGM_mutase_AS; . InterPro IPR005952; Phosphogly_mut1; . PANTHER PTHR11931; PTHR11931; 1; . Pfam PF00300; His_Phos_1; 2; . SMART SM00855; PGAM; 1; . SUPFAM SSF53254; SSF53254; 1; . TIGRFAMs TIGR01258; pgm_1; 1; . PROSITE PS00175; PG_MUTASE; 1; .

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