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Q2KIW9

- KCY_BOVIN

UniProt

Q2KIW9 - KCY_BOVIN

Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    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

    Binds 1 magnesium 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. uridylate kinase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. nucleoside diphosphate phosphorylation Source: UniProtKB
    2. nucleoside triphosphate biosynthetic process Source: UniProtKB
    3. pyrimidine nucleotide biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_223832. 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:CMPK1UniRule annotation
    Synonyms:CMPKUniRule annotation
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 3

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 196196UMP-CMP kinasePRO_0000292023Add
    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

    PaxDbiQ2KIW9.
    PRIDEiQ2KIW9.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000026582.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2KIW9.
    SMRiQ2KIW9. 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.
    InParanoidiQ2KIW9.
    KOiK13800.
    OMAiKRPGSQY.
    OrthoDBiEOG7X0VJ0.
    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.

    Q2KIW9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPQVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG    50
    ELIEKYIKDG KIVPVEITIS LLRREMDQTM AANAQKNKFL IDGFPRNQDN 100
    LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK 150
    RIQTYLQSTK PIIDLYEEMG KVRKIDASKS VDEVFDEVVK IFDKEG 196
    Length:196
    Mass (Da):22,279
    Last modified:June 26, 2007 - v2
    Checksum:i6011E45A8085D28A
    GO

    Sequence cautioni

    The sequence AAI12479.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC112478 mRNA. Translation: AAI12479.1. Different initiation.
    RefSeqiNP_001039509.1. NM_001046044.1.
    UniGeneiBt.28263.

    Genome annotation databases

    EnsembliENSBTAT00000026582; ENSBTAP00000026582; ENSBTAG00000019956.
    GeneIDi509965.
    KEGGibta:509965.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC112478 mRNA. Translation: AAI12479.1 . Different initiation.
    RefSeqi NP_001039509.1. NM_001046044.1.
    UniGenei Bt.28263.

    3D structure databases

    ProteinModelPortali Q2KIW9.
    SMRi Q2KIW9. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000026582.

    Proteomic databases

    PaxDbi Q2KIW9.
    PRIDEi Q2KIW9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000026582 ; ENSBTAP00000026582 ; ENSBTAG00000019956 .
    GeneIDi 509965.
    KEGGi bta:509965.

    Organism-specific databases

    CTDi 51727.

    Phylogenomic databases

    eggNOGi COG0563.
    GeneTreei ENSGT00390000016215.
    HOGENOMi HOG000238771.
    HOVERGENi HBG108060.
    InParanoidi Q2KIW9.
    KOi K13800.
    OMAi KRPGSQY.
    OrthoDBi EOG7X0VJ0.
    TreeFami TF354283.

    Enzyme and pathway databases

    Reactomei REACT_223832. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    NextBioi 20869218.

    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

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Testis.

    Entry informationi

    Entry nameiKCY_BOVIN
    AccessioniPrimary (citable) accession number: Q2KIW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 65 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3