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Q9BZX2 (UCK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.13 Ref.14

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 diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCTP 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: Ensembl

feeding behavior

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

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: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP 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: UniProtKB-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 261260Uridine-cytidine kinase 2
PRO_0000164455

Regions

Nucleotide binding27 – 359ATP

Sites

Binding site841Substrate
Binding site1121Substrate
Binding site1171Substrate
Binding site1661Substrate
Binding site1761Substrate
Binding site1841Substrate
Binding site2131ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue2541Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 150150Missing in isoform 2.
VSP_014262

Experimental info

Sequence conflict2021K → Q in BAA11349. Ref.1
Sequence conflict2221V → E in BAA11349. Ref.1

Secondary structure

............................................ 261
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 71791346F091EBFD

FASTA26129,299
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E6688B1B86F432A9
Show »

FASTA11112,587

References

« Hide '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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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.
[11]"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].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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.
CCDSCCDS1252.1. [Q9BZX2-1]
RefSeqNP_036606.2. NM_012474.4. [Q9BZX2-1]
UniGeneHs.458360.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UDWX-ray2.60A/B1-250[»]
1UEIX-ray2.60A/B1-250[»]
1UEJX-ray2.61A/B1-250[»]
1UFQX-ray2.50A/B/C/D1-250[»]
1UJ2X-ray1.80A/B1-250[»]
1XRJX-ray2.00A/B1-261[»]
ProteinModelPortalQ9BZX2.
SMRQ9BZX2. Positions 19-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113217. 3 interactions.
IntActQ9BZX2. 1 interaction.
STRING9606.ENSP00000356853.

Chemistry

ChEMBLCHEMBL2469.

PTM databases

PhosphoSiteQ9BZX2.

Polymorphism databases

DMDM20455356.

Proteomic databases

MaxQBQ9BZX2.
PaxDbQ9BZX2.
PeptideAtlasQ9BZX2.
PRIDEQ9BZX2.

Protocols and materials databases

DNASU7371.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367879; ENSP00000356853; ENSG00000143179. [Q9BZX2-1]
ENST00000469256; ENSP00000476692; ENSG00000143179. [Q9BZX2-2]
ENST00000470820; ENSP00000476327; ENSG00000143179. [Q9BZX2-2]
GeneID7371.
KEGGhsa:7371.
UCSCuc001gdp.3. human. [Q9BZX2-1]
uc010plb.2. human. [Q9BZX2-2]

Organism-specific databases

CTD7371.
GeneCardsGC01P165796.
HGNCHGNC:12562. UCK2.
HPAHPA051286.
MIM609329. gene.
neXtProtNX_Q9BZX2.
PharmGKBPA362.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0572.
HOGENOMHOG000262756.
HOVERGENHBG023339.
InParanoidQ9BZX2.
KOK00876.
OMAHTSIARD.
OrthoDBEOG7Q8CP2.
PhylomeDBQ9BZX2.
TreeFamTF316686.

Enzyme and pathway databases

BioCycMetaCyc:HS07003-MONOMER.
BRENDA2.7.1.48. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ9BZX2.
UniPathwayUPA00574; UER00637.
UPA00579; UER00640.

Gene expression databases

ArrayExpressQ9BZX2.
BgeeQ9BZX2.
CleanExHS_UCK2.
GenevestigatorQ9BZX2.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR006083. PRK/URK.
IPR000764. Uridine_kinase_like.
[Graphical view]
PfamPF00485. PRK. 1 hit.
[Graphical view]
PRINTSPR00988. URIDINKINASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00235. udk. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUCK2. human.
EvolutionaryTraceQ9BZX2.
GeneWikiUCK2.
GenomeRNAi7371.
NextBio28862.
PROQ9BZX2.
SOURCESearch...

Entry information

Entry nameUCK2_HUMAN
AccessionPrimary (citable) accession number: Q9BZX2
Secondary accession number(s): Q5VV91 expand/collapse secondary AC list , Q7KZV3, Q92528, Q96KG5, Q9BU42
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 121 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM