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Reviewed, UniProtKB/Swiss-Prot Q3U5Q7 (CMPK2_MOUSE)

Last modified October 13, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    UMP-CMP kinase 2, mitochondrial
    EC=2.7.4.14
Alternative name(s):
    Thymidylate kinase LPS-inducible member
      Short name=TYKi
Gene names
Name: Cmpk2
Synonyms: Tyki
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

ATP + (d)CMP = ADP + (d)CDP.

Subcellular location

Mitochondrion By similarity.

Induction

By lipopolysaccharides in macrophages and in primary microglia. Ref.3 Ref.4

Sequence similarities

Belongs to the thymidylate kinase family.

Sequence caution

The sequence AAA58770.1 differs from that shown. Reason: Miscellaneous discrepancy. Sequence differs due to frameshifts, sequencing errors and other discrepancies.

The sequence BAB23396.1 differs from that shown. Reason: Frameshift at position 74.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentMitochondrion
   DomainCoiled coil
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cytidylate kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7373Mitochondrion Potential
Chain74 – 447374UMP-CMP kinase 2, mitochondrial
PRO_0000331525

Regions

Nucleotide binding259 – 2668ATP Potential
Coiled coil380 – 41233 Potential

Experimental info

Sequence conflict141G → R in BAE29625. Ref.1
Sequence conflict1831R → K in BAE32020. Ref.1
Sequence conflict2251E → G in BAE32020. Ref.1
Sequence conflict3171E → G in BAE29625. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3U5Q7-1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 37CBACA251A40CFC

FASTA44750,036
        10         20         30         40         50         60 
MALISRPRAP LWLGRLSRRL CGRHQACMGT MARPRRFTVE LPDCSLTHFV LGDATDHRDA 

        70         80         90        100        110        120 
RLAELLGPPG RSYALCVPLA PGEGCGPRVQ AARVHHRLLQ QLRRGPLQRC QLSKLLGYGP 

       130        140        150        160        170        180 
GDQAGEAQHG FLLRDPCDHP DTRRDLLQLL GSCQEAARPQ LAEFQADSQG LLWQRLWELQ 

       190        200        210        220        230        240 
GDRQVQVDCA CVLPAQEPHL HPLLPDLLNS AVFQDRDAAR AVLEECTSFI PEARAVLDLV 

       250        260        270        280        290        300 
DQCPKEVQKG KFQVIAIEGL DATGKTTLTQ SVSESLKAVL LQSPPPCISQ WRKIFDDEPT 

       310        320        330        340        350        360 
IIRRAFYSLG NYLVASEIAK ESTNFPVIVD RYWHSTATYA IATEVSGGLQ YLPPAHHPVY 

       370        380        390        400        410        420 
QWPGDLLKPD LVLLLTVNSE ERVRRLQGRG QEKTKEEAEL EANNVFRQKV EMTYQRMENP 

       430        440 
SCHLVDASPS RETVLQKVLE LIQSSGR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 16141072] [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: 15489334] [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: 7751651] [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: 16996144] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00120113.
RefSeqNP_065582.3.
UniGeneMm.271839

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3U5Q7.

Proteomic databases

PRIDEQ3U5Q7.

Genome annotation databases

EnsemblENSMUST00000020969; ENSMUSP00000020969; ENSMUSG00000020638; Mus musculus. [Genome view]
GeneID22169.
KEGGmmu:22169.
UCSCuc007nfj.1. mouse.

Organism-specific databases

CTD22169.
MGIMGI:99830. Cmpk2.

Phylogenomic databases

HOVERGENQ3U5Q7.

Gene expression databases

ArrayExpressQ3U5Q7.
BgeeQ3U5Q7.
GenevestigatorQ3U5Q7.

Family and domain databases

InterProIPR014505. dTMP_TKRP1.
IPR000062. Thymidylate_kin-like.
IPR018095. Thymidylate_kin_CS.
[Graphical view]
PfamPF02223. Thymidylate_kin. 1 hit.
[Graphical view]
PIRSFPIRSF019736. dTMP_TKRP1. 1 hit.
PROSITEPS01331. THYMIDYLATE_KINASE. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio302112.
SOURCESearch...

Entry information

Entry nameCMPK2_MOUSE
AccessionPrimary (citable) accession number: Q3U5Q7
Secondary accession number(s): Q3UCI7 expand/collapse secondary AC list , Q5XKG5, Q62316, Q6PFG7, Q9DC34
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: October 13, 2009
This is version 30 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents