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Q4KM73

- KCY_RAT

UniProt

Q4KM73 - KCY_RAT

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Protein

UMP-CMP kinase

Gene

Cmpk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 Mg(2+) 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

  1. ATP binding Source: UniProtKB-KW
  2. cytidylate kinase activity Source: UniProtKB-HAMAP
  3. nucleoside diphosphate kinase activity Source: UniProtKB
  4. UMP kinase activity Source: RGD

GO - Biological processi

  1. CDP biosynthetic process Source: RGD
  2. dCDP biosynthetic process Source: RGD
  3. dUDP biosynthetic process Source: RGD
  4. nucleoside diphosphate phosphorylation Source: UniProtKB
  5. nucleoside triphosphate biosynthetic process Source: UniProtKB
  6. ovulation cycle process Source: RGD
  7. phthalate metabolic process Source: RGD
  8. UDP biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_215006. 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:Cmpk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi1310116. Cmpk1.

Subcellular locationi

Nucleus UniRule annotation. Cytoplasm UniRule annotation
Note: Predominantly nuclear.UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196UMP-CMP kinasePRO_0000292951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ4KM73.
PRIDEiQ4KM73.

2D gel databases

World-2DPAGE0004:Q4KM73.

PTM databases

PhosphoSiteiQ4KM73.

Expressioni

Gene expression databases

GenevestigatoriQ4KM73.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi255874. 1 interaction.
STRINGi10116.ENSRNOP00000010318.

Structurei

3D structure databases

ProteinModelPortaliQ4KM73.
SMRiQ4KM73. 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.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiQ4KM73.
KOiK13800.
OrthoDBiEOG7X0VJ0.
PhylomeDBiQ4KM73.
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.

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 AAH98727.1 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

EnsembliENSRNOT00000010318; ENSRNOP00000010318; ENSRNOG00000007775.
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.
RefSeqi NP_001020826.1. NM_001025655.1.
UniGenei Rn.162093.

3D structure databases

ProteinModelPortali Q4KM73.
SMRi Q4KM73. Positions 3-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 255874. 1 interaction.
STRINGi 10116.ENSRNOP00000010318.

PTM databases

PhosphoSitei Q4KM73.

2D gel databases

World-2DPAGE 0004:Q4KM73.

Proteomic databases

PaxDbi Q4KM73.
PRIDEi Q4KM73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000010318 ; ENSRNOP00000010318 ; ENSRNOG00000007775 .
GeneIDi 298410.
KEGGi rno:298410.
UCSCi RGD:1310116. rat.

Organism-specific databases

CTDi 51727.
RGDi 1310116. Cmpk1.

Phylogenomic databases

eggNOGi COG0563.
GeneTreei ENSGT00390000016215.
HOGENOMi HOG000238771.
HOVERGENi HBG108060.
InParanoidi Q4KM73.
KOi K13800.
OrthoDBi EOG7X0VJ0.
PhylomeDBi Q4KM73.
TreeFami TF354283.

Enzyme and pathway databases

Reactomei REACT_215006. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

NextBioi 643641.
PROi Q4KM73.

Gene expression databases

Genevestigatori Q4KM73.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProi IPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Spleen.
  2. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 27-39, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

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 26, 2014
This is version 76 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

External Data

Dasty 3