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Protein

UMP-CMP kinase

Gene

Cmpk1

Organism
Rattus norvegicus (Rat)
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)DescriptionActionsGraphical viewLength
Binding sitei39NMPUniRule annotation1
Binding sitei100CMPUniRule annotation1
Binding sitei134ATPUniRule annotation1
Binding sitei140NMPUniRule annotation1
Binding sitei151NMPUniRule annotation1
Binding sitei179ATP; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 18ATPUniRule annotation6
Nucleotide bindingi61 – 63NMPUniRule annotation3
Nucleotide bindingi93 – 96NMPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
  • CDP biosynthetic process Source: RGD
  • dCDP biosynthetic process Source: RGD
  • dUDP biosynthetic process Source: RGD
  • nucleoside diphosphate phosphorylation Source: UniProtKB
  • nucleoside triphosphate biosynthetic process Source: UniProtKB
  • ovulation cycle process Source: RGD
  • phthalate metabolic process Source: RGD
  • UDP biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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:Cmpk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310116. 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)DescriptionActionsGraphical viewLength
ChainiPRO_00002929511 – 196UMP-CMP kinaseAdd BLAST196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei33PhosphoserineBy similarity1
Modified residuei43N6-acetyllysineBy similarity1
Modified residuei55N6-acetyllysineBy similarity1
Modified residuei106N6-succinyllysineBy similarity1
Modified residuei180PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ4KM73.
PeptideAtlasiQ4KM73.
PRIDEiQ4KM73.

2D gel databases

World-2DPAGE0004:Q4KM73.

PTM databases

iPTMnetiQ4KM73.
PhosphoSitePlusiQ4KM73.

Expressioni

Gene expression databases

BgeeiENSRNOG00000007775.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi255874. 1 interactor.
STRINGi10116.ENSRNOP00000010318.

Structurei

3D structure databases

ProteinModelPortaliQ4KM73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 63NMPbindUniRule annotationAdd BLAST31
Regioni133 – 143LIDUniRule annotationAdd BLAST11

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

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiQ4KM73.
KOiK13800.
PhylomeDBiQ4KM73.
TreeFamiTF354283.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03172. Adenylate_kinase_UMP_CMP_kin. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
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.

Q4KM73-1 [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 DCNNEICIDR CLERGKSSGR SDDNRESLEK
160 170 180 190
RIQTYLESTK PIIDLYEEMG KVKKIDASKS VDEVFGDVMK IFDKEG
Length:196
Mass (Da):22,169
Last modified:June 26, 2007 - v2
Checksum:iFB73F32866E42331
GO

Sequence cautioni

The sequence AAH98727 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098727 mRNA. Translation: AAH98727.1. Different initiation.
RefSeqiNP_001020826.1. NM_001025655.1.
UniGeneiRn.162093.

Genome annotation databases

GeneIDi298410.
KEGGirno:298410.
UCSCiRGD:1310116. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098727 mRNA. Translation: AAH98727.1. Different initiation.
RefSeqiNP_001020826.1. NM_001025655.1.
UniGeneiRn.162093.

3D structure databases

ProteinModelPortaliQ4KM73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi255874. 1 interactor.
STRINGi10116.ENSRNOP00000010318.

PTM databases

iPTMnetiQ4KM73.
PhosphoSitePlusiQ4KM73.

2D gel databases

World-2DPAGE0004:Q4KM73.

Proteomic databases

PaxDbiQ4KM73.
PeptideAtlasiQ4KM73.
PRIDEiQ4KM73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi298410.
KEGGirno:298410.
UCSCiRGD:1310116. rat.

Organism-specific databases

CTDi51727.
RGDi1310116. Cmpk1.

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiQ4KM73.
KOiK13800.
PhylomeDBiQ4KM73.
TreeFamiTF354283.

Miscellaneous databases

PROiQ4KM73.

Gene expression databases

BgeeiENSRNOG00000007775.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03172. Adenylate_kinase_UMP_CMP_kin. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
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...

Entry informationi

Entry nameiKCY_RAT
AccessioniPrimary (citable) accession number: Q4KM73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: November 30, 2016
This is version 94 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.