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Q9DBP5

- KCY_MOUSE

UniProt

Q9DBP5 - KCY_MOUSE

Protein

UMP-CMP kinase

Gene

Cmpk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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. UMP kinase activity Source: Ensembl

    GO - Biological processi

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

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-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:Cmk, Cmpk, Uck, Umk, Umpk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1913838. Cmpk1.

    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_0000158950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-acetyllysine1 Publication
    Modified residuei55 – 551N6-acetyllysineBy similarity
    Modified residuei106 – 1061N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9DBP5.
    PaxDbiQ9DBP5.
    PRIDEiQ9DBP5.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00331146.
    Q9DBP5.
    UCD-2DPAGEQ9DBP5.

    PTM databases

    PhosphoSiteiQ9DBP5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DBP5.
    BgeeiQ9DBP5.
    CleanExiMM_CMPK1.
    GenevestigatoriQ9DBP5.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ9DBP5. 4 interactions.
    MINTiMINT-1869762.
    STRINGi10090.ENSMUSP00000030491.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBP5.
    SMRiQ9DBP5. 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.
    InParanoidiQ9DBP5.
    KOiK13800.
    OrthoDBiEOG7X0VJ0.
    PhylomeDBiQ9DBP5.
    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.

    Q9DBP5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG    50
    ELIEKYIKEG KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN 100
    LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK 150
    RIQTYLESTK PIIDLYEEMG KVKKIDASKS VDEVFGEVVK IFDKEG 196
    Length:196
    Mass (Da):22,165
    Last modified:June 1, 2001 - v1
    Checksum:i7972B629D7542294
    GO

    Sequence cautioni

    The sequence AAH17684.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB22163.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC36852.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE27170.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE29352.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE36771.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAM19996.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK077534 mRNA. Translation: BAC36852.1. Different initiation.
    AK002526 mRNA. Translation: BAB22163.1. Different initiation.
    AL670035 Genomic DNA. Translation: CAM19996.1. Different initiation.
    AK162173 mRNA. Translation: BAE36771.1. Different initiation.
    AK150162 mRNA. Translation: BAE29352.1. Different initiation.
    AK146436 mRNA. Translation: BAE27170.1. Different initiation.
    AK004827 mRNA. Translation: BAB23595.1.
    BC017684 mRNA. Translation: AAH17684.1. Different initiation.
    RefSeqiNP_079923.3. NM_025647.3.
    UniGeneiMm.294159.

    Genome annotation databases

    EnsembliENSMUST00000030491; ENSMUSP00000030491; ENSMUSG00000028719.
    GeneIDi66588.
    KEGGimmu:66588.
    UCSCiuc008ueg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK077534 mRNA. Translation: BAC36852.1 . Different initiation.
    AK002526 mRNA. Translation: BAB22163.1 . Different initiation.
    AL670035 Genomic DNA. Translation: CAM19996.1 . Different initiation.
    AK162173 mRNA. Translation: BAE36771.1 . Different initiation.
    AK150162 mRNA. Translation: BAE29352.1 . Different initiation.
    AK146436 mRNA. Translation: BAE27170.1 . Different initiation.
    AK004827 mRNA. Translation: BAB23595.1 .
    BC017684 mRNA. Translation: AAH17684.1 . Different initiation.
    RefSeqi NP_079923.3. NM_025647.3.
    UniGenei Mm.294159.

    3D structure databases

    ProteinModelPortali Q9DBP5.
    SMRi Q9DBP5. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DBP5. 4 interactions.
    MINTi MINT-1869762.
    STRINGi 10090.ENSMUSP00000030491.

    PTM databases

    PhosphoSitei Q9DBP5.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00331146.
    Q9DBP5.
    UCD-2DPAGE Q9DBP5.

    Proteomic databases

    MaxQBi Q9DBP5.
    PaxDbi Q9DBP5.
    PRIDEi Q9DBP5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030491 ; ENSMUSP00000030491 ; ENSMUSG00000028719 .
    GeneIDi 66588.
    KEGGi mmu:66588.
    UCSCi uc008ueg.2. mouse.

    Organism-specific databases

    CTDi 51727.
    MGIi MGI:1913838. Cmpk1.

    Phylogenomic databases

    eggNOGi COG0563.
    GeneTreei ENSGT00390000016215.
    HOGENOMi HOG000238771.
    HOVERGENi HBG108060.
    InParanoidi Q9DBP5.
    KOi K13800.
    OrthoDBi EOG7X0VJ0.
    PhylomeDBi Q9DBP5.
    TreeFami TF354283.

    Miscellaneous databases

    NextBioi 322084.
    PROi Q9DBP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBP5.
    Bgeei Q9DBP5.
    CleanExi MM_CMPK1.
    Genevestigatori Q9DBP5.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/N.
      Tissue: Kidney.
    4. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-16; 27-39; 62-73 AND 89-96, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiKCY_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBP5
    Secondary accession number(s): Q8BK17, Q8VD05, Q9DCS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3