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Q5EBM0

- CMPK2_HUMAN

UniProt

Q5EBM0 - CMPK2_HUMAN

Protein

UMP-CMP kinase 2, mitochondrial

Gene

CMPK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Efficacy is highest for dUMP followed by dCMP; CMP and UMP are poor substrates. May be involved in mtDNA depletion caused by long term treatment with ddC or other pyrimidine analogs. Also displays broad nucleoside diphosphate kinase activity.2 Publications

    Catalytic activityi

    ATP + (d)CMP = ADP + (d)CDP.1 Publication
    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.1 Publication

    Kineticsi

    1. KM=3.09 mM for CMP
    2. KM=6.3 mM for UMP
    3. KM=1.31 mM for dCMP
    4. KM=0.1 mM for dUMP

    Vmax=1.64 µmol/min/mg enzyme towards CMP

    Vmax=0.19 µmol/min/mg enzyme towards UMP

    Vmax=1.77 µmol/min/mg enzyme towards dCMP

    Vmax=0.48 µmol/min/mg enzyme towards dUMP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi259 – 2668ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cytidylate kinase activity Source: MGI
    3. nucleoside diphosphate kinase activity Source: UniProtKB
    4. thymidylate kinase activity Source: Ensembl
    5. UMP kinase activity Source: MGI

    GO - Biological processi

    1. cellular response to lipopolysaccharide Source: Ensembl
    2. dTDP biosynthetic process Source: Ensembl
    3. dUDP biosynthetic process Source: Ensembl
    4. nucleoside diphosphate phosphorylation Source: UniProtKB
    5. nucleoside triphosphate biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ5EBM0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UMP-CMP kinase 2, mitochondrial (EC:2.7.4.14)
    Alternative name(s):
    Nucleoside-diphosphate kinase (EC:2.7.4.6)
    Gene namesi
    Name:CMPK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:27015. CMPK2.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162382556.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 9898MitochondrionSequence AnalysisAdd
    BLAST
    Chaini99 – 449351UMP-CMP kinase 2, mitochondrialPRO_0000331524Add
    BLAST

    Proteomic databases

    MaxQBiQ5EBM0.
    PaxDbiQ5EBM0.
    PRIDEiQ5EBM0.

    Expressioni

    Tissue specificityi

    Among all investigated tumors, leukemia cells show the most abundant expression.1 Publication

    Gene expression databases

    ArrayExpressiQ5EBM0.
    BgeeiQ5EBM0.
    CleanExiHS_CMPK2.
    GenevestigatoriQ5EBM0.

    Organism-specific databases

    HPAiHPA041430.

    Interactioni

    Protein-protein interaction databases

    BioGridi126200. 1 interaction.
    STRINGi9606.ENSP00000256722.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5EBM0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili380 – 41233Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thymidylate kinase family.Curated

    Keywords - Domaini

    Coiled coil, Transit peptide

    Phylogenomic databases

    eggNOGiNOG259135.
    HOGENOMiHOG000082499.
    HOVERGENiHBG088202.
    InParanoidiQ5EBM0.
    KOiK13809.
    OMAiHPVYQWP.
    OrthoDBiEOG73NG3S.
    PhylomeDBiQ5EBM0.
    TreeFamiTF328875.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR014505. UMP-CMP_kinase_mit.
    [Graphical view]
    PIRSFiPIRSF019736. dTMP_TKRP1. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5EBM0-1) [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

    MAFARRLLRG PLSGPLLGRR GVCAGAMAPP RRFVLELPDC TLAHFALGAD    50
    APGDADAPDP RLAALLGPPE RSYSLCVPVT PDAGCGARVR AARLHQRLLH 100
    QLRRGPFQRC QLLRLLCYCP GGQAGGAQQG FLLRDPLDDP DTRQALLELL 150
    GACQEAPRPH LGEFEADPRG QLWQRLWEVQ DGRRLQVGCA QVVPVPEPPL 200
    HPVVPDLPSS VVFPDREAAR AVLEECTSFI PEARAVLDLV DQCPKQIQKG 250
    KFQVVAIEGL DATGKTTVTQ SVADSLKAVL LKSPPSCIGQ WRKIFDDEPT 300
    IIRRAFYSLG NYIVASEIAK ESAKSPVIVD RYWHSTATYA IATEVSGGLQ 350
    HLPPAHHPVY QWPEDLLKPD LILLLTVSPE ERLQRLQGRG MEKTREEAEL 400
    EANSVFRQKV EMSYQRMENP GCHVVDASPS REKVLQTVLS LIQNSFSEP 449
    Length:449
    Mass (Da):49,448
    Last modified:May 18, 2010 - v3
    Checksum:i99F382E34332B6DE
    GO
    Isoform 2 (identifier: Q5EBM0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         280-303: LLKSPPSCIGQWRKIFDDEPTIIR → PQPITLCTSGQRTCSNLTLSCCSL
         304-449: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:303
    Mass (Da):32,646
    Checksum:i4C7D0715B7B970C6
    GO
    Isoform 3 (identifier: Q5EBM0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         332-449: YWHSTATYAI...SLIQNSFSEP → SQLGGTLYHPSLHLLGSEVCGTGILDSSHSSQGLE

    Note: No experimental confirmation available.

    Show »
    Length:366
    Mass (Da):39,562
    Checksum:iCE09AA2A0A6E6DB3
    GO
    Isoform 4 (identifier: Q5EBM0-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         410-449: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:409
    Mass (Da):44,959
    Checksum:iA102FAA659D793D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti448 – 4481E → G in AAH89425. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti433 – 4331K → R.
    Corresponds to variant rs6712141 [ dbSNP | Ensembl ].
    VAR_055997

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei280 – 30324LLKSP…PTIIR → PQPITLCTSGQRTCSNLTLS CCSL in isoform 2. 1 PublicationVSP_033238Add
    BLAST
    Alternative sequencei304 – 449146Missing in isoform 2. 1 PublicationVSP_033239Add
    BLAST
    Alternative sequencei332 – 449118YWHST…SFSEP → SQLGGTLYHPSLHLLGSEVC GTGILDSSHSSQGLE in isoform 3. 1 PublicationVSP_033240Add
    BLAST
    Alternative sequencei410 – 44940Missing in isoform 4. 1 PublicationVSP_033241Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK127983 mRNA. Translation: BAC87217.1.
    BC016969 mRNA. Translation: AAH16969.1.
    BC141802 mRNA. Translation: AAI41803.1.
    BC132821 mRNA. Translation: AAI32822.1.
    BC089425 mRNA. Translation: AAH89425.1.
    BC144202 mRNA. Translation: AAI44203.1.
    CCDSiCCDS42648.1. [Q5EBM0-1]
    CCDS58695.1. [Q5EBM0-3]
    CCDS58696.1. [Q5EBM0-4]
    RefSeqiNP_001243406.1. NM_001256477.1. [Q5EBM0-4]
    NP_001243407.1. NM_001256478.1. [Q5EBM0-3]
    NP_997198.2. NM_207315.3. [Q5EBM0-1]
    UniGeneiHs.7155.

    Genome annotation databases

    EnsembliENST00000256722; ENSP00000256722; ENSG00000134326. [Q5EBM0-1]
    ENST00000404168; ENSP00000384915; ENSG00000134326. [Q5EBM0-4]
    ENST00000458098; ENSP00000396385; ENSG00000134326. [Q5EBM0-3]
    GeneIDi129607.
    KEGGihsa:129607.
    UCSCiuc002qyo.4. human. [Q5EBM0-1]
    uc010yis.2. human. [Q5EBM0-3]

    Polymorphism databases

    DMDMi296439392.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK127983 mRNA. Translation: BAC87217.1 .
    BC016969 mRNA. Translation: AAH16969.1 .
    BC141802 mRNA. Translation: AAI41803.1 .
    BC132821 mRNA. Translation: AAI32822.1 .
    BC089425 mRNA. Translation: AAH89425.1 .
    BC144202 mRNA. Translation: AAI44203.1 .
    CCDSi CCDS42648.1. [Q5EBM0-1 ]
    CCDS58695.1. [Q5EBM0-3 ]
    CCDS58696.1. [Q5EBM0-4 ]
    RefSeqi NP_001243406.1. NM_001256477.1. [Q5EBM0-4 ]
    NP_001243407.1. NM_001256478.1. [Q5EBM0-3 ]
    NP_997198.2. NM_207315.3. [Q5EBM0-1 ]
    UniGenei Hs.7155.

    3D structure databases

    ProteinModelPortali Q5EBM0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126200. 1 interaction.
    STRINGi 9606.ENSP00000256722.

    Polymorphism databases

    DMDMi 296439392.

    Proteomic databases

    MaxQBi Q5EBM0.
    PaxDbi Q5EBM0.
    PRIDEi Q5EBM0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256722 ; ENSP00000256722 ; ENSG00000134326 . [Q5EBM0-1 ]
    ENST00000404168 ; ENSP00000384915 ; ENSG00000134326 . [Q5EBM0-4 ]
    ENST00000458098 ; ENSP00000396385 ; ENSG00000134326 . [Q5EBM0-3 ]
    GeneIDi 129607.
    KEGGi hsa:129607.
    UCSCi uc002qyo.4. human. [Q5EBM0-1 ]
    uc010yis.2. human. [Q5EBM0-3 ]

    Organism-specific databases

    CTDi 129607.
    GeneCardsi GC02M006980.
    H-InvDB HIX0023970.
    HGNCi HGNC:27015. CMPK2.
    HPAi HPA041430.
    MIMi 611787. gene.
    neXtProti NX_Q5EBM0.
    PharmGKBi PA162382556.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259135.
    HOGENOMi HOG000082499.
    HOVERGENi HBG088202.
    InParanoidi Q5EBM0.
    KOi K13809.
    OMAi HPVYQWP.
    OrthoDBi EOG73NG3S.
    PhylomeDBi Q5EBM0.
    TreeFami TF328875.

    Enzyme and pathway databases

    SABIO-RK Q5EBM0.

    Miscellaneous databases

    GenomeRNAii 129607.
    NextBioi 82613.
    PROi Q5EBM0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5EBM0.
    Bgeei Q5EBM0.
    CleanExi HS_CMPK2.
    Genevestigatori Q5EBM0.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR014505. UMP-CMP_kinase_mit.
    [Graphical view ]
    PIRSFi PIRSF019736. dTMP_TKRP1. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human UMP-CMP kinase 2, a novel nucleoside monophosphate kinase localized in mitochondria."
      Xu Y., Johansson M., Karlsson A.
      J. Biol. Chem. 283:1563-1571(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    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] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-449 (ISOFORM 1).
      Tissue: Lymph and Prostate.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase."
      Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.
      Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiCMPK2_HUMAN
    AccessioniPrimary (citable) accession number: Q5EBM0
    Secondary accession number(s): A2RUB0
    , A5D8T2, B7ZM18, Q6ZRU2, Q96AL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 83 of the entry and version 3 of the sequence. [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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3