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Q9DBP5 (KCY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Cmk, Cmpk, Uck, Umk, Umpk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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

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 electronic annotation. Source: Ensembl

UDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

dCDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

dUDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

phthalate metabolic process

Inferred from electronic annotation. Source: Ensembl

   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 electronic annotation. Source: Ensembl

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_0000158950

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 Ref.5
Modified residue551N6-acetyllysine By similarity
Modified residue1061N6-succinyllysine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9DBP5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7972B629D7542294

FASTA19622,165
        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 
DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLESTK PIIDLYEEMG KVKKIDASKS 

       190 
VDEVFGEVVK IFDKEG 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Strain: FVB/N.
Tissue: Kidney.
[4]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-16; 27-39; 62-73 AND 89-96, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+Additional computationally mapped 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.
RefSeqNP_079923.3. NM_025647.3.
UniGeneMm.294159.

3D structure databases

ProteinModelPortalQ9DBP5.
SMRQ9DBP5. Positions 3-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DBP5. 4 interactions.
MINTMINT-1869762.
STRING10090.ENSMUSP00000030491.

PTM databases

PhosphoSiteQ9DBP5.

2D gel databases

REPRODUCTION-2DPAGEIPI00331146.
Q9DBP5.
UCD-2DPAGEQ9DBP5.

Proteomic databases

PaxDbQ9DBP5.
PRIDEQ9DBP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030491; ENSMUSP00000030491; ENSMUSG00000028719.
GeneID66588.
KEGGmmu:66588.
UCSCuc008ueg.2. mouse.

Organism-specific databases

CTD51727.
MGIMGI:1913838. Cmpk1.

Phylogenomic databases

eggNOGCOG0563.
GeneTreeENSGT00390000016215.
HOGENOMHOG000238771.
HOVERGENHBG108060.
InParanoidQ9DBP5.
KOK13800.
OrthoDBEOG7X0VJ0.
PhylomeDBQ9DBP5.
TreeFamTF354283.

Gene expression databases

ArrayExpressQ9DBP5.
BgeeQ9DBP5.
CleanExMM_CMPK1.
GenevestigatorQ9DBP5.

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

NextBio322084.
PROQ9DBP5.
SOURCESearch...

Entry information

Entry nameKCY_MOUSE
AccessionPrimary (citable) accession number: Q9DBP5
Secondary accession number(s): Q8BK17, Q8VD05, Q9DCS7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 110 of the entry and version 1 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot