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PGK1_BOVIN
ID   PGK1_BOVIN              Reviewed;         417 AA.
AC   Q3T0P6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Phosphoglycerate kinase 1;
DE            EC=2.7.2.3;
GN   Name=PGK1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes one of the two ATP producing reactions in the
CC       glycolytic pathway via the reversible conversion of 1,3-
CC       diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a
CC       glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha
CC       cofactor protein (primer recognition protein). May play a role in sperm
CC       motility. {ECO:0000250|UniProtKB:P00558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; BC102308; AAI02309.1; -; mRNA.
DR   RefSeq; NP_001029471.1; NM_001034299.1.
DR   AlphaFoldDB; Q3T0P6; -.
DR   SMR; Q3T0P6; -.
DR   BioGRID; 164115; 1.
DR   STRING; 9913.ENSBTAP00000001187; -.
DR   iPTMnet; Q3T0P6; -.
DR   PaxDb; Q3T0P6; -.
DR   PeptideAtlas; Q3T0P6; -.
DR   PRIDE; Q3T0P6; -.
DR   Ensembl; ENSBTAT00000001187; ENSBTAP00000001187; ENSBTAG00000000894.
DR   GeneID; 507476; -.
DR   KEGG; bta:507476; -.
DR   CTD; 5230; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000894; -.
DR   VGNC; VGNC:32789; PGK1.
DR   eggNOG; KOG1367; Eukaryota.
DR   GeneTree; ENSGT00390000008820; -.
DR   HOGENOM; CLU_025427_0_0_1; -.
DR   InParanoid; Q3T0P6; -.
DR   OMA; YVNDAYS; -.
DR   OrthoDB; 838642at2759; -.
DR   TreeFam; TF300489; -.
DR   SABIO-RK; Q3T0P6; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000000894; Expressed in infraspinatus muscle and 105 other tissues.
DR   ExpressionAtlas; Q3T0P6; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:Ensembl.
DR   GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 3.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Glycolysis; Hydroxylation; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   CHAIN           2..417
FT                   /note="Phosphoglycerate kinase 1"
FT                   /id="PRO_0000239848"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         373..376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         6
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         48
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         86
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         97
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         97
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         131
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         191
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         196
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         199
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         216
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         220
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         267
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         291
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         323
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         361
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
SQ   SEQUENCE   417 AA;  44538 MW;  DECD3DF6FBB783BD CRC64;
     MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKYC LDSGAKSVVL
     MSHLGRPDGV PMPDKYSLQP VAVELKSLLG KDVLFLKDCV GPEVEKACAD PAAGSVILLE
     NLRFHVEEEG KGKDASGNKV KAEPTKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
     LPKKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLISNMLDK VNEMIIGGGM
     AFTFLKVLNN MEIGTSLFDE EGSKIVKDLM SKADKNGVKI TLPVDFVTAD KFDENAKTGQ
     ATVASGIPAG WMGLDCGPES SKKYAEAVAR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV
     KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSSV
 
 
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