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Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Homo sapiens (Human)
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 annotation3 Publications

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+Note: Binds 1 Mg2+ ion per monomer.

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
  • cytidylate kinase activity Source: UniProtKB-EC
  • nucleoside diphosphate kinase activity Source: UniProtKB
  • nucleoside phosphate kinase activity Source: Reactome
  • uridine kinase activity Source: ProtInc
  • uridylate kinase activity Source: InterPro

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
  • nucleobase-containing small molecule interconversion Source: Reactome
  • nucleoside diphosphate phosphorylation Source: UniProtKB
  • nucleoside triphosphate biosynthetic process Source: UniProtKB
  • pyrimidine ribonucleotide biosynthetic process Source: ProtInc

Keywordsi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS08663-MONOMER
BRENDAi2.7.4.14 2681
ReactomeiR-HSA-499943 Interconversion of nucleotide di- and triphosphates
SABIO-RKiP30085

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:CMK, CMPKUniRule annotation, UCK, UMK, UMPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000162368.13
HGNCiHGNC:18170 CMPK1
MIMi191710 gene
neXtProtiNX_P30085

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi51727
PharmGKBiPA162382539

Chemistry databases

ChEMBLiCHEMBL5681
DrugBankiDB03403 Cytidine-5'-Monophosphate
DB00441 Gemcitabine
DB00709 Lamivudine
DB03664 P1-(Adenosine-5'-P5-(Uridine-5')Pentaphosphate
DB04444 Tetrafluoroaluminate Ion
DB03435 Uridine-5'-Diphosphate

Polymorphism and mutation databases

DMDMi12644008

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589491 – 196UMP-CMP kinaseAdd BLAST196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei33PhosphoserineCombined sources1
Modified residuei43N6-acetyllysineBy similarity1
Modified residuei55N6-acetyllysineCombined sources1
Cross-linki73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei106N6-succinyllysineBy similarity1
Modified residuei180PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP30085
MaxQBiP30085
PaxDbiP30085
PeptideAtlasiP30085
PRIDEiP30085
TopDownProteomicsiP30085-1 [P30085-1]

2D gel databases

OGPiP30085
SWISS-2DPAGEiP30085

PTM databases

iPTMnetiP30085
PhosphoSitePlusiP30085
SwissPalmiP30085

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000162368
CleanExiHS_CMPK1
ExpressionAtlasiP30085 baseline and differential
GenevisibleiP30085 HS

Organism-specific databases

HPAiHPA053730
HPA058604

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi119700, 13 interactors
IntActiP30085, 3 interactors
MINTiP30085
STRINGi9606.ENSP00000360939

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi16 – 27Combined sources12
Beta strandi30 – 33Combined sources4
Helixi34 – 43Combined sources10
Helixi50 – 58Combined sources9
Helixi65 – 82Combined sources18
Beta strandi88 – 93Combined sources6
Helixi98 – 108Combined sources11
Turni109 – 111Combined sources3
Beta strandi113 – 121Combined sources9
Helixi124 – 136Combined sources13
Helixi145 – 168Combined sources24
Beta strandi172 – 176Combined sources5
Helixi181 – 194Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TEVX-ray2.10A1-196[»]
ProteinModelPortaliP30085
SMRiP30085
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30085

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 63NMPbind1 PublicationAdd BLAST31
Regioni133 – 143LID1 PublicationAdd 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 annotation1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3079 Eukaryota
COG0563 LUCA
HOGENOMiHOG000238771
HOVERGENiHBG108060
InParanoidiP30085
KOiK13800
OrthoDBiEOG091G0OQ7
PhylomeDBiP30085
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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P30085-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVQ IFDKEG
Length:196
Mass (Da):22,222
Last modified:December 1, 2000 - v3
Checksum:i6837B1E6D7543768
GO
Isoform 2 (identifier: P30085-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-74: Missing.

Show »
Length:147
Mass (Da):16,548
Checksum:i535CD9D8F1B4A0F2
GO

Sequence cautioni

The sequence AAF17709 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH14961 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD96734 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG60709 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI13471 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI14972 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27Y → I AA sequence (PubMed:8313870).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04668326 – 74Missing in isoform 2. 1 PublicationAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070416 mRNA Translation: AAF17709.1 Different initiation.
AF259961 mRNA Translation: AAG22609.1
AF110643 mRNA Translation: AAD48583.1
AF087865 mRNA Translation: AAP97174.1
AF112216 mRNA Translation: AAF17204.1
AK223014 mRNA Translation: BAD96734.1 Different initiation.
AK298502 mRNA Translation: BAG60709.1 Different initiation.
AL513322, AL607122 Genomic DNA Translation: CAI13471.1 Sequence problems.
AL607122, AL513322 Genomic DNA Translation: CAI14972.1 Sequence problems.
BC014961 mRNA Translation: AAH14961.1 Different initiation.
PIRiB45482
RefSeqiNP_001129612.1, NM_001136140.1
NP_057392.1, NM_016308.2
UniGeneiHs.731647
Hs.745001

Genome annotation databases

EnsembliENST00000371873; ENSP00000360939; ENSG00000162368
ENST00000450808; ENSP00000398192; ENSG00000162368
GeneIDi51727
KEGGihsa:51727
UCSCiuc001cri.3 human [P30085-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiKCY_HUMAN
AccessioniPrimary (citable) accession number: P30085
Secondary accession number(s): B4DPU7
, E9PGI8, Q53GB7, Q5SVZ0, Q96C07, Q9UBQ8, Q9UIA2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 1, 2000
Last modified: May 23, 2018
This is version 186 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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