Q9BZX2 (UCK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uridine-cytidine kinase 2
Short name=UCK 2
EC=2.7.1.48

Alternative name(s):
Cytidine monophosphokinase 2
Testis-specific protein TSA903
Uridine monophosphokinase 2

Gene names

Name:	UCK2
Synonyms:	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	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.
Catalytic activity	ATP + uridine = ADP + UMP. ATP + cytidine = ADP + CMP.
Pathway	Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3. Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
Subunit structure	Homotetramer. Ref.12 Ref.13
Tissue specificity	According to Ref.1; testis-specific. According to Ref.2, placenta-specific. Ref.1
Sequence similarities	Belongs to the uridine kinase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CTP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway UMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular response to oxygen levels Inferred from electronic annotation. Source: Compara feeding behavior Inferred from electronic annotation. Source: Compara pyrimidine nucleobase metabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside salvage Traceable author statement. Source: Reactome response to axon injury Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside kinase activity Inferred from experiment. Source: Reactome phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro uridine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BZX2-1)

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: Q9BZX2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Uridine-cytidine kinase 2

PRO_0000164455

Regions

Nucleotide binding

27 – 35

9

ATP

Sites

Binding site

84

1

Substrate

Binding site

112

1

Substrate

Binding site

117

1

Substrate

Binding site

166

1

Substrate

Binding site

176

1

Substrate

Binding site

184

1

Substrate

Binding site

213

1

ATP

Amino acid modifications

Modified residue

254

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 150

150

Missing in isoform 2.

VSP_014262

Experimental info

Sequence conflict

202

1

K → Q in BAA11349. Ref.1

Sequence conflict

222

1

V → E in BAA11349. Ref.1

Secondary structure

1

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261

Helix Strand Turn

Details...

Beta strand

21 – 26

6

Helix

33 – 43

11

Helix

46 – 48

3

Helix

51 – 53

3

Beta strand

55 – 60

6

Helix

61 – 64

4

Helix

70 – 77

8

Helix

86 – 88

3

Helix

91 – 102

12

Beta strand

107 – 113

7

Turn

114 – 117

4

Beta strand

118 – 126

9

Beta strand

130 – 135

6

Turn

137 – 140

4

Helix

143 – 148

6

Beta strand

150 – 156

7

Helix

159 – 173

15

Helix

178 – 187

10

Helix

189 – 196

8

Helix

198 – 203

6

Beta strand

205 – 209

5

Helix

211 – 213

3

Helix

215 – 230

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 71791346F091EBFD	FASTA	261	29,299
	10 20 30 40 50 60 MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YRQKQVVILS 70 80 90 100 110 120 QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK 130 140 150 160 170 180 EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ 190 200 210 220 230 240 ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG 250 260 CLNGYTPSRK RQASESSSRP H
	Isoform 2 [UniParc]. Checksum: E6688B1B86F432A9	FASTA	111	12,587
	10 20 30 40 50 60 MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ ILSQYITFVK PAFEEFCLPT KKYADVIIPR 70 80 90 100 110 GADNLVAINL IVQHIQDILN GGPSKRQTNG CLNGYTPSRK RQASESSSRP H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method." Ozaki K., Kuroki T., Hayashi S., Nakamura Y. Genomics 36:316-319(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]	"Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases." Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A. Mol. Pharmacol. 59:1181-1186(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]	"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].
[6]	"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] (ISOFORM 1). Tissue: Lung.
[7]	"Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells." Koizumi K., Shimamoto Y., Azuma A., Wataya Y., Matsuda A., Sasaki T., Fukushima M. Int. J. Mol. Med. 8:273-278(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-261 (ISOFORM 1). Tissue: Fibrosarcoma.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, MASS SPECTROMETRY.
[12]	"Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase." Suzuki N.N., Koizumi K., Fukushima M., Matsuda A., Inagaki F. Structure 12:751-764(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-250 IN COMPLEXES WITH ADP; CYTIDINE; CMP; CTP AND UTP, SUBUNIT.
[13]	"Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative." Appleby T.C., Larson G., Cheney I.W., Walker H., Wu J.Z., Zhong W., Hong Z., Yao N. Acta Crystallogr. D 61:278-284(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CMP, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D78335 mRNA. Translation: BAA11349.1.
AF236637 mRNA. Translation: AAK14053.1.
BT006860 mRNA. Translation: AAP35506.1.
CR456857 mRNA. Translation: CAG33138.1.
AL451074, AL358115 Genomic DNA. Translation: CAH74066.1.
AL358115, AL451074 Genomic DNA. Translation: CAI15121.1.
BC002906 mRNA. Translation: AAH02906.2.
AB062451 mRNA. Translation: BAB56162.1.

IPI

IPI00065671.
IPI00607810.

RefSeq

NP_036606.2. NM_012474.4.

UniGene

Hs.458360.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UDW	X-ray	2.60	A/B	1-250	[»]
1UEI	X-ray	2.60	A/B	1-250	[»]
1UEJ	X-ray	2.61	A/B	1-250	[»]
1UFQ	X-ray	2.50	A/B/C/D	1-250	[»]
1UJ2	X-ray	1.80	A/B	1-250	[»]
1XRJ	X-ray	2.00	A/B	1-261	[»]

ProteinModelPortal

Q9BZX2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BZX2. 1 interaction.

STRING

9606.ENSP00000356853.

PTM databases

PhosphoSite

Q9BZX2.

Polymorphism databases

DMDM

20455356.

Proteomic databases

PaxDb

Q9BZX2.

PeptideAtlas

Q9BZX2.

PRIDE

Q9BZX2.

Protocols and materials databases

DNASU

7371.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367879; ENSP00000356853; ENSG00000143179.

GeneID

7371.

KEGG

hsa:7371.

UCSC

uc001gdp.3. human.
uc010plb.2. human.

Organism-specific databases

CTD

7371.

GeneCards

GC01P165796.

HGNC

HGNC:12562. UCK2.

HPA

HPA051286.

MIM

609329. gene.

neXtProt

NX_Q9BZX2.

PharmGKB

PA362.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0572.

HOGENOM

HOG000262756.

HOVERGEN

HBG023339.

InParanoid

Q9BZX2.

KO

K00876.

OMA

DICFMRR.

OrthoDB

EOG4R7VBB.

PhylomeDB

Q9BZX2.

Enzyme and pathway databases

BioCyc

MetaCyc:HS07003-MONOMER.

BRENDA

2.7.1.48. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q9BZX2.

UniPathway

UPA00574; UER00637.
UPA00579; UER00640.

Gene expression databases

ArrayExpress

Q9BZX2.

Bgee

Q9BZX2.

CleanEx

HS_UCK2.

Genevestigator

Q9BZX2.

GermOnline

ENSG00000143179. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR006083. PRK/URK.
IPR000764. Uridine_kinase.
[Graphical view]

Pfam

PF00485. PRK. 1 hit.
[Graphical view]

PRINTS

PR00988. URIDINKINASE.

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00235. udk. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL2469.

ChiTaRS

UCK2. human.

EvolutionaryTrace

Q9BZX2.

GenomeRNAi

7371.

NextBio

28862.

SOURCE

Search...

Entry information

Entry name

UCK2_HUMAN

Accession

Primary (citable) accession number: Q9BZX2
Secondary accession number(s): Q5VV91 , Q7KZV3, Q92528, Q96KG5, Q9BU42

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 109 of the entry and version 1 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.