P16617 (PGK1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 102.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Phosphoglycerate kinase 1 EC=2.7.2.3 | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 417 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the phosphoglycerate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | gluconeogenesis Inferred from direct assay PubMed 15720133. Source: RGD glycolysisInferred from direct assay PubMed 6405813. Source: RGD |
| Cellular_component | cytosol Inferred from direct assay PubMed 1834654. Source: RGD |
| Molecular_function | ADP binding Inferred from direct assay PubMed 6405813. Source: RGD ATP bindingInferred from sequence or structural similarity. Source: UniProtKB phosphoglycerate kinase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 417 | 416 | Phosphoglycerate kinase 1 | PRO_0000145840 | |||||
Regions | |||||||||
| Nucleotide binding | 373 – 376 | 4 | ATP By similarity | ||||||
| Region | 24 – 26 | 3 | Substrate binding By similarity | ||||||
| Region | 63 – 66 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 39 | 1 | Substrate By similarity | ||||||
| Binding site | 123 | 1 | Substrate By similarity | ||||||
| Binding site | 171 | 1 | Substrate By similarity | ||||||
| Binding site | 220 | 1 | ATP By similarity | ||||||
| Binding site | 313 | 1 | ATP; via carbonyl oxygen By similarity | ||||||
| Binding site | 344 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 11 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 48 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 75 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 76 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 86 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 97 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 131 | 1 | N6-acetyllysine; alternate By similarity | ||||||
| Modified residue | 131 | 1 | N6-malonyllysine; alternate By similarity | ||||||
| Modified residue | 146 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 196 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 199 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 203 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 267 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 291 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 390 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 56 | 1 | K → N in AAA41838. Ref.1 | ||||||
| Sequence conflict | 271 | 1 | A → T in AAA41838. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and cDNA sequence of the rat X-chromosome linked phosphoglycerate kinase." Ciccarese S., Tommasi S., Vonghia G. Biochem. Biophys. Res. Commun. 165:1337-1344(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary and Pituitary. |
| [3] | Lubec G., Afjehi-Sadat L., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 98-123; 157-171; 200-216; 280-297 AND 333-350, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M31788 mRNA. Translation: AAA41838.1. BC063161 mRNA. Translation: AAH63161.1. BC087651 mRNA. Translation: AAH87651.1. |
| IPI | IPI00231426. |
| PIR | A33792. |
| RefSeq | NP_445743.2. NM_053291.3. |
| UniGene | Rn.108127. |
3D structure databases | |
| ProteinModelPortal | P16617. |
| SMR | P16617. Positions 2-417. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-4577521. |
PTM databases | |
| PhosphoSite | P16617. |
2D gel databases | |
| World-2DPAGE | 0004:P16617. |
Proteomic databases | |
| PaxDb | P16617. |
| PRIDE | P16617. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000003390; ENSRNOP00000003390; ENSRNOG00000002467. |
| GeneID | 24644. |
| KEGG | rno:24644. |
| UCSC | RGD:619878. rat. |
Organism-specific databases | |
| CTD | 5230. |
| RGD | 619878. Pgk1. |
Phylogenomic databases | |
| eggNOG | COG0126. |
| GeneTree | ENSGT00390000008820. |
| HOGENOM | HOG000227107. |
| HOVERGEN | HBG008177. |
| InParanoid | P16617. |
| KO | K00927. |
| OMA | NFANGTK. |
| OrthoDB | EOG44MXS6. |
Enzyme and pathway databases | |
| SABIO-RK | P16617. |
| UniPathway | UPA00109; UER00185. |
Gene expression databases | |
| Genevestigator | P16617. |
| GermOnline | ENSRNOG00000002467. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 3.40.50.1260. 1 hit. 3.40.50.1270. 1 hit. |
| InterPro | IPR001576. Phosphoglycerate_kinase. IPR015901. Phosphoglycerate_kinase_C. IPR015911. Phosphoglycerate_kinase_CS. IPR015824. Phosphoglycerate_kinase_N. [Graphical view] |
| PANTHER | PTHR11406. PTHR11406. 1 hit. |
| Pfam | PF00162. PGK. 1 hit. [Graphical view] |
| PIRSF | PIRSF000724. Pgk. 1 hit. |
| PRINTS | PR00477. PHGLYCKINASE. |
| SUPFAM | SSF53748. PGK. 1 hit. |
| PROSITE | PS00111. PGLYCERATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 603950. |
Entry information
| Entry name | PGK1_RAT | ||||||||
| Accession | Primary (citable) accession number: P16617 Secondary accession number(s): Q5M945, Q6P508 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
