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Protein

UMP-CMP kinase

Gene

Cmpk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

  • ATP binding Source: UniProtKB-KW
  • CMP kinase activity Source: RGD
  • nucleoside diphosphate kinase activity Source: UniProtKB
  • uridylate kinase activity Source: RGD

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

Keywordsi

Molecular functionKinase, Transferase
Biological processPyrimidine biosynthesis
LigandATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310116 Cmpk1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
Cross-linki73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei106N6-succinyllysineBy similarity1
Modified residuei180PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ4KM73
PeptideAtlasiQ4KM73
PRIDEiQ4KM73

2D gel databases

World-2DPAGEi0004:Q4KM73

PTM databases

iPTMnetiQ4KM73
PhosphoSitePlusiQ4KM73
SwissPalmiQ4KM73

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi255874, 1 interactor
STRINGi10116.ENSRNOP00000010318

Structurei

3D structure databases

ProteinModelPortaliQ4KM73
SMRiQ4KM73
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
HAMAPiMF_00235 Adenylate_kinase_Adk, 1 hit
MF_03172 Adenylate_kinase_UMP_CMP_kin, 1 hit
InterProiView protein in InterPro
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR027417 P-loop_NTPase
IPR006266 UMP_CMP_kinase
PANTHERiPTHR23359 PTHR23359, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01359 UMP_CMP_kin_fam, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiKCY_RAT
AccessioniPrimary (citable) accession number: Q4KM73
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: June 20, 2018
This is version 102 of the entry and version 2 of the sequence. See 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

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