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Q5EBM0 (CMPK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UMP-CMP kinase 2, mitochondrial

EC=2.7.4.14
Alternative name(s):
Nucleoside-diphosphate kinase
EC=2.7.4.6
Gene names
Name:CMPK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. 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. Ref.1 Ref.5

Catalytic activity

ATP + (d)CMP = ADP + (d)CDP. Ref.5

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. Ref.5

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

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

Sequence similarities

Belongs to the thymidylate kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.09 mM for CMP

KM=6.3 mM for UMP

KM=1.31 mM for dCMP

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5EBM0-1)

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.
Isoform 2 (identifier: Q5EBM0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     280-303: LLKSPPSCIGQWRKIFDDEPTIIR → PQPITLCTSGQRTCSNLTLSCCSL
     304-449: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5EBM0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     332-449: YWHSTATYAI...SLIQNSFSEP → SQLGGTLYHPSLHLLGSEVCGTGILDSSHSSQGLE
Note: No experimental confirmation available.
Isoform 4 (identifier: Q5EBM0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     410-449: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9898Mitochondrion Potential
Chain99 – 449351UMP-CMP kinase 2, mitochondrial
PRO_0000331524

Regions

Nucleotide binding259 – 2668ATP Potential
Coiled coil380 – 41233 Potential

Natural variations

Alternative sequence280 – 30324LLKSP…PTIIR → PQPITLCTSGQRTCSNLTLS CCSL in isoform 2.
VSP_033238
Alternative sequence304 – 449146Missing in isoform 2.
VSP_033239
Alternative sequence332 – 449118YWHST…SFSEP → SQLGGTLYHPSLHLLGSEVC GTGILDSSHSSQGLE in isoform 3.
VSP_033240
Alternative sequence410 – 44940Missing in isoform 4.
VSP_033241
Natural variant4331K → R.
Corresponds to variant rs6712141 [ dbSNP | Ensembl ].
VAR_055997

Experimental info

Sequence conflict4481E → G in AAH89425. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 99F382E34332B6DE

FASTA44949,448
        10         20         30         40         50         60 
MAFARRLLRG PLSGPLLGRR GVCAGAMAPP RRFVLELPDC TLAHFALGAD APGDADAPDP 

        70         80         90        100        110        120 
RLAALLGPPE RSYSLCVPVT PDAGCGARVR AARLHQRLLH QLRRGPFQRC QLLRLLCYCP 

       130        140        150        160        170        180 
GGQAGGAQQG FLLRDPLDDP DTRQALLELL GACQEAPRPH LGEFEADPRG QLWQRLWEVQ 

       190        200        210        220        230        240 
DGRRLQVGCA QVVPVPEPPL HPVVPDLPSS VVFPDREAAR AVLEECTSFI PEARAVLDLV 

       250        260        270        280        290        300 
DQCPKQIQKG KFQVVAIEGL DATGKTTVTQ SVADSLKAVL LKSPPSCIGQ WRKIFDDEPT 

       310        320        330        340        350        360 
IIRRAFYSLG NYIVASEIAK ESAKSPVIVD RYWHSTATYA IATEVSGGLQ HLPPAHHPVY 

       370        380        390        400        410        420 
QWPEDLLKPD LILLLTVSPE ERLQRLQGRG MEKTREEAEL EANSVFRQKV EMSYQRMENP 

       430        440 
GCHVVDASPS REKVLQTVLS LIQNSFSEP 

« Hide

Isoform 2 [UniParc].

Checksum: 4C7D0715B7B970C6
Show »

FASTA30332,646
Isoform 3 [UniParc].

Checksum: CE09AA2A0A6E6DB3
Show »

FASTA36639,562
Isoform 4 [UniParc].

Checksum: A102FAA659D793D0
Show »

FASTA40944,959

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001243406.1. NM_001256477.1.
NP_001243407.1. NM_001256478.1.
NP_997198.2. NM_207315.3.
UniGeneHs.7155.

3D structure databases

ProteinModelPortalQ5EBM0.
SMRQ5EBM0. Positions 247-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126200. 1 interaction.
STRING9606.ENSP00000256722.

Polymorphism databases

DMDM296439392.

Proteomic databases

PaxDbQ5EBM0.
PRIDEQ5EBM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256722; ENSP00000256722; ENSG00000134326. [Q5EBM0-1]
ENST00000404168; ENSP00000384915; ENSG00000134326. [Q5EBM0-4]
ENST00000458098; ENSP00000396385; ENSG00000134326. [Q5EBM0-3]
GeneID129607.
KEGGhsa:129607.
UCSCuc002qyo.4. human. [Q5EBM0-1]
uc010yis.2. human. [Q5EBM0-3]

Organism-specific databases

CTD129607.
GeneCardsGC02M006980.
H-InvDBHIX0023970.
HGNCHGNC:27015. CMPK2.
HPAHPA041430.
MIM611787. gene.
neXtProtNX_Q5EBM0.
PharmGKBPA162382556.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259135.
HOGENOMHOG000082499.
HOVERGENHBG088202.
InParanoidQ5EBM0.
KOK13809.
OMAHPVYQWP.
OrthoDBEOG73NG3S.
PhylomeDBQ5EBM0.
TreeFamTF328875.

Enzyme and pathway databases

SABIO-RKQ5EBM0.

Gene expression databases

ArrayExpressQ5EBM0.
BgeeQ5EBM0.
CleanExHS_CMPK2.
GenevestigatorQ5EBM0.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR014505. UMP-CMP_kinase_mit.
[Graphical view]
PIRSFPIRSF019736. dTMP_TKRP1. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi129607.
NextBio82613.
PROQ5EBM0.
SOURCESearch...

Entry information

Entry nameCMPK2_HUMAN
AccessionPrimary (citable) accession number: Q5EBM0
Secondary accession number(s): A2RUB0 expand/collapse secondary AC list , A5D8T2, B7ZM18, Q6ZRU2, Q96AL8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM