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Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Sus scrofa (Pig)
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.

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

Keywordsi

Molecular functionKinase, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SSC-499943 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:CMPK1UniRule annotation
Synonyms:CMPKUniRule annotation, UCK
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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_00001589511 – 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 residuei180PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ29561
PeptideAtlasiQ29561
PRIDEiQ29561

Expressioni

Gene expression databases

BgeeiENSSSCG00000003885
ExpressionAtlasiQ29561 differential
GenevisibleiQ29561 SS

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004197

Structurei

3D structure databases

ProteinModelPortaliQ29561
SMRiQ29561
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
InParanoidiQ29561
OMAiFCHLSAG
OrthoDBiEOG091G0OQ7
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.

Q29561-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPKVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG
60 70 80 90 100
ELIEKYIKDG KIVPVEITIS LLRREMDQTM AANAQKNKFL IDGFPRNQDN
110 120 130 140 150
LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK
160 170 180 190
RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVK IFDKEG
Length:196
Mass (Da):22,279
Last modified:November 1, 1996 - v1
Checksum:i3780384E43900797
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29655 Genomic DNA Translation: BAA06130.1
PIRiJC4181
UniGeneiSsc.24276

Similar proteinsi

Entry informationi

Entry nameiKCY_PIG
AccessioniPrimary (citable) accession number: Q29561
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 116 of the entry and version 1 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
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Main funding by: National Institutes of Health