Q9DBP5 (KCY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	Cmpk1
Synonyms:	Cmk, Cmpk, Uck, Umk, Umpk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm Nucleus
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	CDP biosynthetic process Inferred from electronic annotation. Source: Compara UDP biosynthetic process Inferred from electronic annotation. Source: Compara dCDP biosynthetic process Inferred from electronic annotation. Source: Compara dUDP biosynthetic process Inferred from electronic annotation. Source: Compara ovulation cycle process Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UMP kinase activity Inferred from electronic annotation. Source: Compara cytidylate kinase activity Inferred 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 – 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

	Sequence		Length	Mass (Da)
	Q9DBP5 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 7972B629D7542294	FASTA	196	22,165
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Brain and Hippocampus.
+	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.
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

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program