P30085 (KCY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UMP-CMP kinase
EC=2.7.4.14

Alternative name(s):
Deoxycytidylate kinase
Short name=CK
Short name=dCMP kinase
Uridine monophosphate/cytidine monophosphate kinase
Short name=UMP/CMP kinase
Short name=UMP/CMPK

Gene names

Name:	CMPK1
Synonyms:	CMK, CMPK, UCK, UMK, UMPK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.3
Catalytic activity	ATP + (d)CMP = ADP + (d)CDP. Ref.1 ATP + UMP = ADP + UDP. Ref.1
Cofactor	Binds 1 magnesium ion per monomer.
Subunit structure	Monomer By similarity.
Subcellular location	Nucleus. Cytoplasm. Note: Predominantly nuclear. Ref.1 Ref.3
Tissue specificity	Ubiquitously expressed. Ref.2
Domain	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. HAMAP-Rule MF_03172
Sequence similarities	Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Sequence caution	The sequence AAF17709.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH14961.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD96734.1 differs from that shown. Reason: Erroneous initiation. The sequence CAI13471.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI14972.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CDP biosynthetic process Inferred from electronic annotation. Source: Compara UDP biosynthetic process Inferred from electronic annotation. Source: Compara dCDP biosynthetic process Inferred from electronic annotation. Source: Compara dUDP biosynthetic process Inferred from electronic annotation. Source: Compara nucleobase-containing small molecule interconversion Traceable author statement. Source: Reactome ovulation cycle process Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UMP kinase activity Inferred from electronic annotation. Source: Compara cytidylate kinase activity Inferred from electronic annotation. Source: EC uridine kinase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

UMP-CMP kinase HAMAP-Rule MF_03172

PRO_0000158949

Regions

Nucleotide binding

13 – 18

6

ATP By similarity

Nucleotide binding

61 – 63

3

NMP By similarity

Nucleotide binding

93 – 96

4

NMP By similarity

Region

33 – 63

31

NMPbind HAMAP-Rule MF_03172

Region

133 – 143

11

LID HAMAP-Rule MF_03172

Sites

Binding site

39

1

NMP By similarity

Binding site

100

1

CMP By similarity

Binding site

134

1

ATP By similarity

Binding site

140

1

NMP By similarity

Binding site

151

1

NMP By similarity

Binding site

179

1

ATP; via carbonyl oxygen By similarity

Site

1

1

Not acetylated

Amino acid modifications

Modified residue

55

1

N6-acetyllysine Ref.13

Experimental info

Sequence conflict

27

1

Y → I AA sequence Ref.10

Secondary structure

1

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196

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

16 – 27

12

Beta strand

30 – 33

4

Helix

34 – 43

10

Helix

50 – 58

9

Helix

65 – 82

18

Beta strand

88 – 93

6

Helix

98 – 108

11

Turn

109 – 111

3

Beta strand

113 – 121

9

Helix

124 – 136

13

Helix

145 – 168

24

Beta strand

172 – 176

5

Helix

181 – 194

14

Sequences

	Sequence		Length	Mass (Da)
	P30085 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: 6837B1E6D7543768	FASTA	196	22,222
	10 20 30 40 50 60 MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKEG 70 80 90 100 110 120 KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF 130 140 150 160 170 180 DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLQSTK PIIDLYEEMG KVKKIDASKS 190 VDEVFDEVVQ IFDKEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme." Van Rompay A.R., Johansson M., Karlsson A. Mol. Pharmacol. 56:562-569(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION.
[2]	"Characterization of human UMP-CMP kinase enzymatic activity and 5' untranslated region." Pearman A.T., Castro-Faria-Neto H.C., McIntyre T.M., Prescott S.M., Stafforini D.M. Life Sci. 69:2361-2370(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHROMOSOMAL LOCATION, IDENTIFICATION OF START CODON. Tissue: Macrophage.
[3]	"Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates." Liou J.-Y., Dutschman G.E., Lam W., Jiang Z., Cheng Y.-C. Cancer Res. 62:1624-1631(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[4]	"Human UMP-CMP kinase gene." Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pituitary.
[5]	"Cloning and characterization of a new human cDNA homologous to pig UMP-CMP kinase mRNA." Fan Y.X., Yu L., Dai F.Y., Zhou Y., Huang J., Zhao S.Y. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hypothalamus.
[7]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Small intestine.
[8]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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]. Tissue: Muscle.
[10]	"Human liver protein map: update 1993." Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F. Electrophoresis 14:1216-1222(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-29. Tissue: Liver.
[11]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10. Tissue: Liver.
[12]	Bienvenut W.V., Bilsland A.E., Keith W.N. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-16; 62-73; 89-106; 152-171 AND 180-196, LACK OF N-TERMINAL ACETYLATION, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, MASS SPECTROMETRY.
[14]	"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].
[15]	"Substrate-induced conformational changes in human UMP/CMP kinase." Segura-Pena D., Sekulic N., Ort S., Konrad M., Lavie A. J. Biol. Chem. 279:33882-33889(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF070416 mRNA. Translation: AAF17709.1. Different initiation.
AF259961 mRNA. Translation: AAG22609.1.
AF110643 mRNA. Translation: AAD48583.1.
AF087865 mRNA. Translation: AAP97174.1.
AF112216 mRNA. Translation: AAF17204.1.
AK223014 mRNA. Translation: BAD96734.1. Different initiation.
AL513322, AL607122 Genomic DNA. Translation: CAI13471.1. Sequence problems.
AL607122, AL513322 Genomic DNA. Translation: CAI14972.1. Sequence problems.
BC014961 mRNA. Translation: AAH14961.1. Different initiation.

IPI

IPI00219953.

PIR

B45482.

RefSeq

NP_001129612.1. NM_001136140.1.
NP_057392.1. NM_016308.2.

UniGene

Hs.731647.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TEV	X-ray	2.10	A	1-196	[»]

ProteinModelPortal

P30085.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-5000978.

STRING

9606.ENSP00000360939.

PTM databases

PhosphoSite

P30085.

Polymorphism databases

DMDM

12644008.

2D gel databases

OGP

P30085.

SWISS-2DPAGE

P30085.

Proteomic databases

PaxDb

P30085.

PRIDE

P30085.

Protocols and materials databases

DNASU

51727.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371873; ENSP00000360939; ENSG00000162368.

GeneID

51727.

KEGG

hsa:51727.

Organism-specific databases

CTD

51727.

GeneCards

GC01P047799.

HGNC

HGNC:18170. CMPK1.

MIM

191710. gene.

neXtProt

NX_P30085.

PharmGKB

PA162382539.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0563.

HOVERGEN

HBG108060.

InParanoid

P30085.

KO

K13800.

Enzyme and pathway databases

BioCyc

MetaCyc:HS08663-MONOMER.

BRENDA

2.7.4.14. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P30085.

Gene expression databases

ArrayExpress

P30085.

Bgee

P30085.

CleanEx

HS_CMPK1.

Genevestigator

P30085.

Family and domain databases

HAMAP

MF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.

InterPro

IPR000850. Adenylate_kin.
IPR006266. UMP_CMP_kinase.
[Graphical view]

PANTHER

PTHR23359. PTHR23359. 1 hit.

Pfam

PF00406. ADK. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

TIGRFAMs

TIGR01359. UMP_CMP_kin_fam. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5681.

DrugBank

DB00441. Gemcitabine.

EvolutionaryTrace

P30085.

GenomeRNAi

51727.

NextBio

55784.

SOURCE

Search...

Entry information

Entry name

KCY_HUMAN

Accession

Primary (citable) accession number: P30085
Secondary accession number(s): Q53GB7 , Q5SVZ0, Q96C07, Q9UBQ8, Q9UIA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.