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Q4KM73 (KCY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UMP-CMP kinase

EC=2.7.4.14
Alternative name(s):
Deoxycytidylate kinase
Short name=CK
Short name=dCMP kinase
Nucleoside-diphosphate kinase
EC=2.7.4.6
Uridine monophosphate/cytidine monophosphate kinase
Short name=UMP/CMP kinase
Short name=UMP/CMPK
Gene names
Name:Cmpk1
Synonyms:Cmpk
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Also displays broad nucleoside diphosphate kinase activity 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

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule MF_03172

Cofactor

Binds 1 magnesium ion per monomer By similarity. HAMAP-Rule MF_03172

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03172

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Predominantly nuclear By similarity. HAMAP-Rule MF_03172

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 AAH98727.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCDP biosynthetic process

Inferred from direct assay PubMed 3010881. Source: RGD

UDP biosynthetic process

Inferred from direct assay PubMed 3010881. Source: RGD

dCDP biosynthetic process

Inferred from direct assay PubMed 192455. Source: RGD

dUDP biosynthetic process

Inferred from direct assay PubMed 3010881. Source: RGD

nucleoside diphosphate phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoside triphosphate biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

ovulation cycle process

Inferred from expression pattern PubMed 16400681. Source: RGD

phthalate metabolic process

Inferred from expression pattern PubMed 16400681. Source: RGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

UMP kinase activity

Inferred from direct assay PubMed 3010881. Source: RGD

cytidylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

nucleoside diphosphate kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196UMP-CMP kinase HAMAP-Rule MF_03172
PRO_0000292951

Regions

Nucleotide binding13 – 186ATP By similarity
Nucleotide binding61 – 633NMP By similarity
Nucleotide binding93 – 964NMP By similarity
Region33 – 6331NMPbind By similarity
Region133 – 14311LID By similarity

Sites

Binding site391NMP By similarity
Binding site1001CMP By similarity
Binding site1341ATP By similarity
Binding site1401NMP By similarity
Binding site1511NMP By similarity
Binding site1791ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue431N6-acetyllysine By similarity
Modified residue551N6-acetyllysine By similarity
Modified residue1061N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4KM73 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: FB73F32866E42331

FASTA19622,169
        10         20         30         40         50         60 
MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKEG 

        70         80         90        100        110        120 
KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF 

       130        140        150        160        170        180 
DCNNEICIDR CLERGKSSGR SDDNRESLEK RIQTYLESTK PIIDLYEEMG KVKKIDASKS 

       190 
VDEVFGDVMK IFDKEG 

« Hide

References

« Hide 'large scale' references
[1]"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: Spleen.
[2]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 27-39, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC098727 mRNA. Translation: AAH98727.1. Different initiation.
RefSeqNP_001020826.1. NM_001025655.1.
UniGeneRn.162093.

3D structure databases

ProteinModelPortalQ4KM73.
SMRQ4KM73. Positions 3-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid255874. 1 interaction.
STRING10116.ENSRNOP00000010318.

PTM databases

PhosphoSiteQ4KM73.

2D gel databases

World-2DPAGE0004:Q4KM73.

Proteomic databases

PaxDbQ4KM73.
PRIDEQ4KM73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010318; ENSRNOP00000010318; ENSRNOG00000007775.
GeneID298410.
KEGGrno:298410.
UCSCRGD:1310116. rat.

Organism-specific databases

CTD51727.
RGD1310116. Cmpk1.

Phylogenomic databases

eggNOGCOG0563.
GeneTreeENSGT00390000016215.
HOGENOMHOG000238771.
HOVERGENHBG108060.
InParanoidQ4KM73.
KOK13800.
OrthoDBEOG7X0VJ0.
PhylomeDBQ4KM73.
TreeFamTF354283.

Gene expression databases

GenevestigatorQ4KM73.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio643641.
PROQ4KM73.

Entry information

Entry nameKCY_RAT
AccessionPrimary (citable) accession number: Q4KM73
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families