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Q4KM73 (KCY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
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 lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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

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 residue551N6-acetyllysine 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, 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.
IPIIPI00365217.
RefSeqNP_001020826.1. NM_001025655.1.
UniGeneRn.162093.

3D structure databases

HSSPHSSP built from PDB template 1TEV based on UniProtKB P30085.
ProteinModelPortalQ4KM73.
SMRQ4KM73. Positions 3-196.
ModBaseSearch...

Protein-protein interaction databases

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.
OrthoDBEOG4F1X45.

Gene expression databases

GenevestigatorQ4KM73.

Family and domain databases

HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProIPR000850. Adenylate_kin.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF00406. ADK. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
TIGRFAMsTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio643641.

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: May 1, 2013
This is version 65 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

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