P00570 (KAD1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 86.
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: Adenylate kinase isoenzyme 1 Short name=AK 1 EC=2.7.4.3 Alternative name(s): ATP-AMP transphosphorylase 1 Myokinase | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 194 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. |
| Catalytic activity | ATP + AMP = 2 ADP. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the adenylate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | ATP metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 194 | 194 | Adenylate kinase isoenzyme 1 | PRO_0000158909 | |||||
Regions | |||||||||
| Nucleotide binding | 15 – 23 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 94 – 101 | 8 | AMP By similarity | ||||||
Sites | |||||||||
| Binding site | 39 | 1 | AMP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine | ||||||
Experimental info | |||||||||
| Sequence conflict | 8 | 1 | T → A AA sequence Ref.1 | ||||||
| Sequence conflict | 85 | 1 | D → N AA sequence Ref.1 | ||||||
| Sequence conflict | 98 | 1 | E → Q AA sequence Ref.1 | ||||||
| Sequence conflict | 126 | 1 | T → Q AA sequence Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase." Kuby S.A., Palmieri R.H., Frischat A., Fischer A.H., Wu L.H., Maland L., Manship M. Biochemistry 23:2393-2399(1984) [PubMed: 6089869] [Abstract] Cited for: PROTEIN SEQUENCE. |
| [2] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [3] | NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BT020951 mRNA. Translation: AAX08968.1. BC114796 mRNA. Translation: AAI14797.1. |
| IPI | IPI00905914. |
| PIR | KIBOA. A00681. |
| RefSeq | NP_001013600.1. NM_001013582.1. |
| UniGene | Bt.4224. |
3D structure databases | |
| ProteinModelPortal | P00570. |
| SMR | P00570. Positions 1-194. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P00570. |
Proteomic databases | |
| PRIDE | P00570. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000054038; ENSBTAP00000050234; ENSBTAG00000006305. |
| GeneID | 280715. |
| KEGG | bta:280715. |
Organism-specific databases | |
| CTD | 203. |
Phylogenomic databases | |
| eggNOG | maNOG16709. |
| GeneTree | ENSGT00390000016215. |
| HOVERGEN | HBG108060. |
| PhylomeDB | P00570. |
Enzyme and pathway databases | |
| BRENDA | 2.7.4.3. 908. |
Family and domain databases | |
| InterPro | IPR000850. Adenylate_kin. IPR006267. Adenylate_kin1. [Graphical view] |
| KO | K00939. |
| PANTHER | PTHR23359. Adenylate_kin. 1 hit. |
| Pfam | PF00406. ADK. 1 hit. [Graphical view] |
| PRINTS | PR00094. ADENYLTKNASE. |
| TIGRFAMs | TIGR01360. Aden_kin_iso1. 1 hit. |
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KAD1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P00570 Secondary accession number(s): Q5E9G9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with