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Protein

UMP-CMP kinase

Gene

Cmpk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

ATP + (d)CMP = ADP + (d)CDP.UniRule annotation
ATP + UMP = ADP + UDP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391NMPUniRule annotation
Binding sitei100 – 1001CMPUniRule annotation
Binding sitei134 – 1341ATPUniRule annotation
Binding sitei140 – 1401NMPUniRule annotation
Binding sitei151 – 1511NMPUniRule annotation
Binding sitei179 – 1791ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 186ATPUniRule annotation
Nucleotide bindingi61 – 633NMPUniRule annotation
Nucleotide bindingi93 – 964NMPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
UMP-CMP kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
Alternative name(s):
Deoxycytidylate kinaseUniRule annotation
Short name:
CKUniRule annotation
Short name:
dCMP kinaseUniRule annotation
Nucleoside-diphosphate kinaseUniRule annotation (EC:2.7.4.6UniRule annotation)
Uridine monophosphate/cytidine monophosphate kinaseUniRule annotation
Short name:
UMP/CMP kinaseUniRule annotation
Short name:
UMP/CMPKUniRule annotation
Gene namesi
Name:Cmpk1
Synonyms:Cmk, Cmpk, Uck, Umk, Umpk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1913838. Cmpk1.

Subcellular locationi

  • Nucleus UniRule annotation
  • Cytoplasm UniRule annotation

  • Note: Predominantly nuclear.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196UMP-CMP kinasePRO_0000158950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei43 – 431N6-acetyllysine1 Publication
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DBP5.
PaxDbiQ9DBP5.
PRIDEiQ9DBP5.

2D gel databases

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

PTM databases

PhosphoSiteiQ9DBP5.

Expressioni

Gene expression databases

BgeeiQ9DBP5.
CleanExiMM_CMPK1.
ExpressionAtlasiQ9DBP5. baseline and differential.
GenevisibleiQ9DBP5. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi211574. 1 interaction.
IntActiQ9DBP5. 4 interactions.
MINTiMINT-1869762.
STRINGi10090.ENSMUSP00000030491.

Structurei

3D structure databases

ProteinModelPortaliQ9DBP5.
SMRiQ9DBP5. Positions 3-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6331NMPbindUniRule annotationAdd
BLAST
Regioni133 – 14311LIDUniRule annotationAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiQ9DBP5.
KOiK13800.
OrthoDBiEOG7X0VJ0.
PhylomeDBiQ9DBP5.
TreeFamiTF354283.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG
60 70 80 90 100
ELIEKYIKEG KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN
110 120 130 140 150
LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK
160 170 180 190
RIQTYLESTK PIIDLYEEMG KVKKIDASKS VDEVFGEVVK IFDKEG
Length:196
Mass (Da):22,165
Last modified:June 1, 2001 - v1
Checksum:i7972B629D7542294
GO

Sequence cautioni

The sequence AAH17684.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB22163.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC36852.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE27170.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE29352.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE36771.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAM19996.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_079923.3. NM_025647.3.
UniGeneiMm.294159.

Genome annotation databases

GeneIDi66588.
KEGGimmu:66588.
UCSCiuc008ueg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_079923.3. NM_025647.3.
UniGeneiMm.294159.

3D structure databases

ProteinModelPortaliQ9DBP5.
SMRiQ9DBP5. Positions 3-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211574. 1 interaction.
IntActiQ9DBP5. 4 interactions.
MINTiMINT-1869762.
STRINGi10090.ENSMUSP00000030491.

PTM databases

PhosphoSiteiQ9DBP5.

2D gel databases

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

Proteomic databases

MaxQBiQ9DBP5.
PaxDbiQ9DBP5.
PRIDEiQ9DBP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66588.
KEGGimmu:66588.
UCSCiuc008ueg.2. mouse.

Organism-specific databases

CTDi51727.
MGIiMGI:1913838. Cmpk1.

Phylogenomic databases

eggNOGiCOG0563.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiQ9DBP5.
KOiK13800.
OrthoDBiEOG7X0VJ0.
PhylomeDBiQ9DBP5.
TreeFamiTF354283.

Enzyme and pathway databases

ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

NextBioi322084.
PROiQ9DBP5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBP5.
CleanExiMM_CMPK1.
ExpressionAtlasiQ9DBP5. baseline and differential.
GenevisibleiQ9DBP5. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiKCY_MOUSE
AccessioniPrimary (citable) accession number: Q9DBP5
Secondary accession number(s): Q8BK17, Q8VD05, Q9DCS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.