Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3U5Q7

- CMPK2_MOUSE

UniProt

Q3U5Q7 - CMPK2_MOUSE

Protein

UMP-CMP kinase 2, mitochondrial

Gene

Cmpk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 2 (29 Apr 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Also displays broad nucleoside diphosphate kinase activity By similarity.By similarity

    Catalytic activityi

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

    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: MGI
    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

    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)
    Thymidylate kinase LPS-inducible member
    Short name:
    TYKi
    Gene namesi
    Name:Cmpk2
    Synonyms:Tyki
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:99830. Cmpk2.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7373MitochondrionSequence AnalysisAdd
    BLAST
    Chaini74 – 447374UMP-CMP kinase 2, mitochondrialPRO_0000331525Add
    BLAST

    Proteomic databases

    MaxQBiQ3U5Q7.
    PaxDbiQ3U5Q7.
    PRIDEiQ3U5Q7.

    Expressioni

    Inductioni

    By lipopolysaccharides in macrophages and in primary microglia.2 Publications

    Gene expression databases

    BgeeiQ3U5Q7.
    GenevestigatoriQ3U5Q7.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3U5Q7.
    SMRiQ3U5Q7. Positions 248-445.
    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.
    GeneTreeiENSGT00640000091577.
    HOGENOMiHOG000082499.
    HOVERGENiHBG088202.
    InParanoidiQ3U5Q7.
    KOiK13809.
    OMAiHPVYQWP.
    OrthoDBiEOG73NG3S.
    PhylomeDBiQ3U5Q7.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q3U5Q7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALISRPRAP LWLGRLSRRL CGRHQACMGT MARPRRFTVE LPDCSLTHFV    50
    LGDATDHRDA RLAELLGPPG RSYALCVPLA PGEGCGPRVQ AARVHHRLLQ 100
    QLRRGPLQRC QLSKLLGYGP GDQAGEAQHG FLLRDPCDHP DTRRDLLQLL 150
    GSCQEAARPQ LAEFQADSQG LLWQRLWELQ GDRQVQVDCA CVLPAQEPHL 200
    HPLLPDLLNS AVFQDRDAAR AVLEECTSFI PEARAVLDLV DQCPKEVQKG 250
    KFQVIAIEGL DATGKTTLTQ SVSESLKAVL LQSPPPCISQ WRKIFDDEPT 300
    IIRRAFYSLG NYLVASEIAK ESTNFPVIVD RYWHSTATYA IATEVSGGLQ 350
    YLPPAHHPVY QWPGDLLKPD LVLLLTVNSE ERVRRLQGRG QEKTKEEAEL 400
    EANNVFRQKV EMTYQRMENP SCHLVDASPS RETVLQKVLE LIQSSGR 447
    Length:447
    Mass (Da):50,036
    Last modified:April 29, 2008 - v2
    Checksum:i37CBACA251A40CFC
    GO

    Sequence cautioni

    The sequence AAA58770.1 differs from that shown. Reason: Sequence differs due to frameshifts, sequencing errors and other discrepancies.
    The sequence BAB23396.1 differs from that shown. Reason: Frameshift at position 74.
    The sequence AAH27329.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH57565.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE29625.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE29646.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE29803.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE29932.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE31987.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141G → R in BAE29625. (PubMed:16141072)Curated
    Sequence conflicti183 – 1831R → K in BAE32020. (PubMed:16141072)Curated
    Sequence conflicti225 – 2251E → G in BAE32020. (PubMed:16141072)Curated
    Sequence conflicti317 – 3171E → G in BAE29625. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004595 mRNA. Translation: BAB23396.1. Frameshift.
    AK153469 mRNA. Translation: BAE32020.1.
    AK150512 mRNA. Translation: BAE29625.1. Different initiation.
    AK150543 mRNA. Translation: BAE29646.1. Different initiation.
    AK150725 mRNA. Translation: BAE29803.1. Different initiation.
    AK150885 mRNA. Translation: BAE29932.1. Different initiation.
    AK153429 mRNA. Translation: BAE31987.1. Different initiation.
    BC027329 mRNA. Translation: AAH27329.1. Different initiation.
    BC057565 mRNA. Translation: AAH57565.1. Different initiation.
    L32973 mRNA. Translation: AAA58770.1. Sequence problems.
    CCDSiCCDS49039.1.
    RefSeqiNP_065582.3. NM_020557.4.
    UniGeneiMm.271839.

    Genome annotation databases

    EnsembliENSMUST00000020969; ENSMUSP00000020969; ENSMUSG00000020638.
    GeneIDi22169.
    KEGGimmu:22169.
    UCSCiuc007nfj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004595 mRNA. Translation: BAB23396.1 . Frameshift.
    AK153469 mRNA. Translation: BAE32020.1 .
    AK150512 mRNA. Translation: BAE29625.1 . Different initiation.
    AK150543 mRNA. Translation: BAE29646.1 . Different initiation.
    AK150725 mRNA. Translation: BAE29803.1 . Different initiation.
    AK150885 mRNA. Translation: BAE29932.1 . Different initiation.
    AK153429 mRNA. Translation: BAE31987.1 . Different initiation.
    BC027329 mRNA. Translation: AAH27329.1 . Different initiation.
    BC057565 mRNA. Translation: AAH57565.1 . Different initiation.
    L32973 mRNA. Translation: AAA58770.1 . Sequence problems.
    CCDSi CCDS49039.1.
    RefSeqi NP_065582.3. NM_020557.4.
    UniGenei Mm.271839.

    3D structure databases

    ProteinModelPortali Q3U5Q7.
    SMRi Q3U5Q7. Positions 248-445.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    MaxQBi Q3U5Q7.
    PaxDbi Q3U5Q7.
    PRIDEi Q3U5Q7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020969 ; ENSMUSP00000020969 ; ENSMUSG00000020638 .
    GeneIDi 22169.
    KEGGi mmu:22169.
    UCSCi uc007nfj.1. mouse.

    Organism-specific databases

    CTDi 129607.
    MGIi MGI:99830. Cmpk2.

    Phylogenomic databases

    eggNOGi NOG259135.
    GeneTreei ENSGT00640000091577.
    HOGENOMi HOG000082499.
    HOVERGENi HBG088202.
    InParanoidi Q3U5Q7.
    KOi K13809.
    OMAi HPVYQWP.
    OrthoDBi EOG73NG3S.
    PhylomeDBi Q3U5Q7.
    TreeFami TF328875.

    Miscellaneous databases

    NextBioi 302112.
    PROi Q3U5Q7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3U5Q7.
    Genevestigatori Q3U5Q7.

    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. "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: Bone marrow and Lung.
    2. "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: C57BL/6 and Czech II.
      Tissue: Mammary tumor.
    3. "A unique member of the thymidylate kinase family that is induced during macrophage activation."
      Lee C.G.L., O'Brien W.E.
      J. Immunol. 154:6094-6102(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Strain: BALB/c.
    4. "The dynamics of the LPS triggered inflammatory response of murine microglia under different culture and in vivo conditions."
      Lund S., Christensen K.V., Hedtjarn M., Mortensen A.L., Hagberg H., Falsig J., Hasseldam H., Schrattenholz A., Poerzgen P., Leist M.
      J. Neuroimmunol. 180:71-87(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiCMPK2_MOUSE
    AccessioniPrimary (citable) accession number: Q3U5Q7
    Secondary accession number(s): Q3UCI7
    , Q5XKG5, Q62316, Q6PFG7, Q9DC34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 67 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. 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