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: P07738 USC-OGP 2-DE database:  P07738 P07738 General information about the entry View entry in simple text format Entry name PMGE_HUMAN Primary accession number P07738 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=Bisphosphoglycerate mutase; Short=BPGM; EC=5.4.2.4 {ECO:0000269|PubMed:21045285}; AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte; AltName: Full=2,3-bisphosphoglycerate synthase; EC=5.4.2.11 {ECO:0000269|PubMed:21045285}; AltName: Full=2,3-diphosphoglycerate mutase; Short=DPGM; AltName: Full=BPG-dependent PGAM;. Gene name Name=BPGM 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 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1269: pI=6.38; Mw=28709 Cross-references UniProtKB/Swiss-Prot P07738; PMGE_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 PMGE_HUMAN Primary accession number P07738 Secondary accession number(s) A4D1N9 Sequence was last modified on  January 23, 2007 (version 2) Annotations were last modified on  March 15, 2017 (version 179) Name and origin of the protein Description RecName: Full=Bisphosphoglycerate mutase; Short=BPGM; EC=5.4.2.4 {ECO:0000269|PubMed:21045285}; AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte; AltName: Full=2,3-bisphosphoglycerate synthase; EC=5.4.2.11 {ECO:0000269|PubMed:21045285}; AltName: Full=2,3-diphosphoglycerate mutase; Short=DPGM; AltName: Full=BPG-dependent PGAM; Gene name Name=BPGM Encoded on Name=BPGM Keywords 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; Glycation; Glycolysis; Glycoprotein; Hereditary hemolytic anemia; 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 X04327; CAA27858.1; -; mRNA EMBL M23068; AAA51840.1; -; Genomic_DNA EMBL M23067; AAA51840.1; JOINED; Genomic_DNA EMBL AK315439; BAG37827.1; -; mRNA EMBL CH236950; EAL24067.1; -; Genomic_DNA EMBL CH471070; EAW83821.1; -; Genomic_DNA EMBL BC017050; AAH17050.1; -; mRNA CCDS CCDS5833.1; -; . PIR A31999; PMHUBM; . RefSeq NP_001280014.1; NM_001293085.1; . RefSeq NP_001715.1; NM_001724.4; . RefSeq NP_954655.1; NM_199186.2; . RefSeq XP_011514829.1; XM_011516527.1; . UniGene Hs.198365; -; . PDB 1T8P; X-ray; 2.50 A; A/B=1-259 PDB 2A9J; X-ray; 2.00 A; A/B=1-259 PDB 2F90; X-ray; 2.00 A; A/B=1-259 PDB 2H4X; X-ray; 1.85 A; A/B=1-259 PDB 2H4Z; X-ray; 2.00 A; A/B=1-259 PDB 2H52; X-ray; 2.00 A; A/B=1-259 PDB 2HHJ; X-ray; 1.50 A; A/B=1-259 PDB 3NFY; X-ray; 1.94 A; A/B=1-259 PDBsum 1T8P; -; . PDBsum 2A9J; -; . PDBsum 2F90; -; . PDBsum 2H4X; -; . PDBsum 2H4Z; -; . PDBsum 2H52; -; . PDBsum 2HHJ; -; . PDBsum 3NFY; -; . ProteinModelPortal P07738; -; . SMR P07738; -; . BioGrid 107137; 21; . IntAct P07738; 8; . STRING 9606.ENSP00000342032; -; . DEPOD P07738; -; . iPTMnet P07738; -; . PhosphoSitePlus P07738; -; . BioMuta BPGM; -; . DMDM 130350; -; . REPRODUCTION-2DPAGE IPI00215979; -; . EPD P07738; -; . MaxQB P07738; -; . PaxDb P07738; -; . PeptideAtlas P07738; -; . PRIDE P07738; -; . DNASU 669; -; . Ensembl ENST00000344924; ENSP00000342032; ENSG00000172331; . Ensembl ENST00000393132; ENSP00000376840; ENSG00000172331; . Ensembl ENST00000418040; ENSP00000399838; ENSG00000172331; . GeneID 669; -; . KEGG hsa:669; -; . UCSC uc003vrv.4; human; . CTD 669; -; . DisGeNET 669; -; . GeneCards BPGM; -; . HGNC HGNC:1093; BPGM; . HPA HPA016493; -; . HPA HPA028735; -; . MalaCards BPGM; -; . MIM 222800; phenotype; . MIM 613896; gene; . neXtProt NX_P07738; -; . OpenTargets ENSG00000172331; -; . Orphanet 714; Hemolytic anemia due to diphosphoglycerate mutase deficiency; . PharmGKB PA25401; -; . eggNOG KOG0235; Eukaryota; . eggNOG COG0588; LUCA; . GeneTree ENSGT00390000016700; -; . HOGENOM HOG000221682; -; . HOVERGEN HBG027528; -; . InParanoid P07738; -; . KO K01837; -; . OMA KEAQNCG; -; . OrthoDB EOG091G0GIS; -; . PhylomeDB P07738; -; . TreeFam TF300007; -; . BioCyc MetaCyc:HS10491-MONOMER; -; . BRENDA 3.1.3.13; 2681; . BRENDA 5.4.2.4; 2681; . Reactome R-HSA-70326; Glucose metabolism; . SABIO-RK P07738; -; . ChiTaRS BPGM; human; . EvolutionaryTrace P07738; -; . GenomeRNAi 669; -; . PRO PR:P07738; -; . Proteomes UP000005640; Chromosome 7; . Bgee ENSG00000172331; -; . CleanEx HS_BPGM; -; . ExpressionAtlas P07738; baseline and differential; . Genevisible P07738; HS; . GO GO:0005829; C:cytosol; IBA:GO_Central; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0046538; F:2; 3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IBA:GO_Central GO GO:0004082; F:bisphosphoglycerate mutase activity; TAS:Reactome; . GO GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW; . GO GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc; . GO GO:0006094; P:gluconeogenesis; IBA:GO_Central; . GO GO:0006006; P:glucose metabolic process; TAS:Reactome; . GO GO:0006096; P:glycolytic process; IBA:GO_Central; . GO GO:0043456; P:regulation of pentose-phosphate shunt; IBA:GO_Central; . GO GO:0007585; P:respiratory gaseous exchange; TAS:ProtInc; . 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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