Q9DBP5 (KCY_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 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: UMP-CMP kinase EC=2.7.4.14 Alternative name(s): Deoxycytidylate kinase Short name=CK Short name=dCMP kinase Uridine monophosphate/cytidine monophosphate kinase Short name=UMP/CMP kinase Short name=UMP/CMPK | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 196 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors By similarity. HAMAP-Rule MF_03172 |
| Catalytic activity | ATP + (d)CMP = ADP + (d)CDP. HAMAP-Rule MF_03172 ATP + UMP = ADP + UDP. HAMAP-Rule MF_03172 |
| Cofactor | Binds 1 magnesium ion per monomer By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Nucleus By similarity. Cytoplasm By similarity. Note: Predominantly nuclear By similarity. |
| Domain | Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis By similarity. HAMAP-Rule MF_03172 |
| Sequence similarities | Belongs to the adenylate kinase family. UMP-CMP kinase subfamily. |
| Sequence caution | The sequence AAH17684.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB22163.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC36852.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE27170.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE29352.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE36771.1 differs from that shown. Reason: Erroneous initiation. The sequence CAM19996.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 196 | 196 | UMP-CMP kinase HAMAP-Rule MF_03172 | PRO_0000158950 | |||||
Regions | |||||||||
| Nucleotide binding | 13 – 18 | 6 | ATP By similarity | ||||||
| Nucleotide binding | 61 – 63 | 3 | NMP By similarity | ||||||
| Nucleotide binding | 93 – 96 | 4 | NMP By similarity | ||||||
| Region | 33 – 63 | 31 | NMPbind By similarity | ||||||
| Region | 133 – 143 | 11 | LID By similarity | ||||||
Sites | |||||||||
| Binding site | 39 | 1 | NMP By similarity | ||||||
| Binding site | 100 | 1 | CMP By similarity | ||||||
| Binding site | 134 | 1 | ATP By similarity | ||||||
| Binding site | 140 | 1 | NMP By similarity | ||||||
| Binding site | 151 | 1 | NMP By similarity | ||||||
| Binding site | 179 | 1 | ATP; via carbonyl oxygen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 55 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK077534 mRNA. Translation: BAC36852.1. Different initiation. AK002526 mRNA. Translation: BAB22163.1. Different initiation. AL670035 Genomic DNA. Translation: CAM19996.1. Different initiation. AK162173 mRNA. Translation: BAE36771.1. Different initiation. AK150162 mRNA. Translation: BAE29352.1. Different initiation. AK146436 mRNA. Translation: BAE27170.1. Different initiation. AK004827 mRNA. Translation: BAB23595.1. BC017684 mRNA. Translation: AAH17684.1. Different initiation. |
| IPI | IPI00331146. |
| RefSeq | NP_079923.3. NM_025647.3. |
| UniGene | Mm.294159. |
3D structure databases | |
| ProteinModelPortal | Q9DBP5. |
| SMR | Q9DBP5. Positions 3-196. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9DBP5. 1 interaction. |
| STRING | 10090.ENSMUSP00000030491. |
PTM databases | |
| PhosphoSite | Q9DBP5. |
2D gel databases | |
| REPRODUCTION-2DPAGE | IPI00331146. Q9DBP5. |
| UCD-2DPAGE | Q9DBP5. |
Proteomic databases | |
| PaxDb | Q9DBP5. |
| PRIDE | Q9DBP5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000030491; ENSMUSP00000030491; ENSMUSG00000028719. |
| GeneID | 66588. |
| KEGG | mmu:66588. |
| UCSC | uc008ueg.2. mouse. |
Organism-specific databases | |
| CTD | 51727. |
| MGI | MGI:1913838. Cmpk1. |
Phylogenomic databases | |
| eggNOG | COG0563. |
| GeneTree | ENSGT00390000016215. |
| HOGENOM | HOG000238771. |
| HOVERGEN | HBG108060. |
| InParanoid | Q9DBP5. |
| KO | K13800. |
| OrthoDB | EOG4F1X45. |
Gene expression databases | |
| ArrayExpress | Q9DBP5. |
| Bgee | Q9DBP5. |
| CleanEx | MM_CMPK1. |
| Genevestigator | Q9DBP5. |
| GermOnline | ENSMUSG00000028719. Mus musculus. |
Family and domain databases | |
| HAMAP | MF_00235. Adenylate_kinase_Adk. MF_03172. Adenylate_kinase_UMP_CMP_kin. |
| InterPro | IPR000850. Adenylate_kin. IPR006266. UMP_CMP_kinase. [Graphical view] |
| PANTHER | PTHR23359. PTHR23359. 1 hit. |
| Pfam | PF00406. ADK. 1 hit. [Graphical view] |
| PRINTS | PR00094. ADENYLTKNASE. |
| TIGRFAMs | TIGR01359. UMP_CMP_kin_fam. 1 hit. |
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 322084. |
| SOURCE | Search... |
Entry information
| Entry name | KCY_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9DBP5 Secondary accession number(s): Q8BK17, Q8VD05, Q9DCS7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
