Q9NWZ5 (UCKL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uridine-cytidine kinase-like 1
EC=2.7.1.48

Gene names

Name:	UCKL1
Synonyms:	URKL1
ORF Names:	F538

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May contribute to UTP accumulation needed for blast transformation and proliferation. Ref.1
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	Interacts with RNF19B and EBV EBNA3. Ref.1 Ref.6
Subcellular location	Cytoplasm. Nucleus. Note: EBNA3 induces isoform 1 translocation to the nucleus, whereas it does change isoform 3 location. Ref.1
Tissue specificity	Ubiquitous. Ref.1
Post-translational modification	Ubiquitinated by RNF19B; which induces proteasomal degradation. Ref.6
Sequence similarities	Belongs to the uridine kinase family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.6. Source: IntAct uridine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNF19B	Q6ZMZ0	4	EBI-2466660,EBI-2466594

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NWZ5-1)

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: Q9NWZ5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     303-548: RELSVRAALA...SDEEEVAYTG → GCAGLGTPVP...DHRCVHSARR

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NWZ5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     386-395: GKCYAGKQIT → DHRCVHSARR
     396-548: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	Uridine-cytidine kinase-like 1		PRO_0000164460
Regions
	Nucleotide binding	105 – 112	8	ATP Potential
Amino acid modifications
	Modified residue	16	1	Phosphoserine Ref.7 Ref.9
	Modified residue	56	1	Phosphoserine Ref.8
	Modified residue	107	1	Phosphoserine By similarity
	Modified residue	539	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	303 – 548	246	RELSV…VAYTG → GCAGLGTPVPPAAPDAERPE EHAAGTGHAHHHQVRAHLGT GRPRARAPAQLLAPQGQGDQ SRRVHLLLQETDAAAHRARA LLPALSGLRRTDPAGAGLCG QVLCGEADHRCVHSARR in isoform 2.		VSP_021802
	Alternative sequence	386 – 395	10	GKCYAGKQIT → DHRCVHSARR in isoform 3.		VSP_025641
	Alternative sequence	396 – 548	153	Missing in isoform 3.		VSP_025642
Experimental info
	Sequence conflict	290	1	D → N in CAE54074. Ref.1
	Sequence conflict	290	1	D → N in BAA91230. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 0CD0351A802FE199	FASTA	548	61,141
	10 20 30 40 50 60 MAAPPARADA DPSPTSPPTA RDTPGRQAEK SETACEDRSN AESLDRLLPP VGTGRSPRKR 70 80 90 100 110 120 TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE 130 140 150 160 170 180 ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN NFNFDHPDAF DFDLIISTLK KLKQGKSVKV 190 200 210 220 230 240 PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR 250 260 270 280 290 300 DISERGRDIE GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL 310 320 330 340 350 360 EERELSVRAA LASAHQCHPL PRTLSVLKST PQVRGMHTII RDKETSRDEF IFYSKRLMRL 370 380 390 400 410 420 LIEHALSFLP FQDCVVQTPQ GQDYAGKCYA GKQITGVSIL RAGETMEPAL RAVCKDVRIG 430 440 450 460 470 480 TILIQTNQLT GEPELHYLRL PKDISDDHVI LMDCTVSTGA AAMMAVRVLL DHDVPEDKIF 490 500 510 520 530 540 LLSLLMAEMG VHSVAYAFPR VRIITTAVDK RVNDLFRIIP GIGNFGDRYF GTDAVPDGSD EEEVAYTG
	Isoform 2 [UniParc]. Checksum: 1D1F11E75305AD25	FASTA	419	45,972
	10 20 30 40 50 60 MAAPPARADA DPSPTSPPTA RDTPGRQAEK SETACEDRSN AESLDRLLPP VGTGRSPRKR 70 80 90 100 110 120 TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE 130 140 150 160 170 180 ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN NFNFDHPDAF DFDLIISTLK KLKQGKSVKV 190 200 210 220 230 240 PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR 250 260 270 280 290 300 DISERGRDIE GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL 310 320 330 340 350 360 EEGCAGLGTP VPPAAPDAER PEEHAAGTGH AHHHQVRAHL GTGRPRARAP AQLLAPQGQG 370 380 390 400 410 DQSRRVHLLL QETDAAAHRA RALLPALSGL RRTDPAGAGL CGQVLCGEAD HRCVHSARR
	Isoform 3 [UniParc]. Checksum: 437D0B1A665CCE30	FASTA	395	44,568
	10 20 30 40 50 60 MAAPPARADA DPSPTSPPTA RDTPGRQAEK SETACEDRSN AESLDRLLPP VGTGRSPRKR 70 80 90 100 110 120 TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE 130 140 150 160 170 180 ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN NFNFDHPDAF DFDLIISTLK KLKQGKSVKV 190 200 210 220 230 240 PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR 250 260 270 280 290 300 DISERGRDIE GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL 310 320 330 340 350 360 EERELSVRAA LASAHQCHPL PRTLSVLKST PQVRGMHTII RDKETSRDEF IFYSKRLMRL 370 380 390 LIEHALSFLP FQDCVVQTPQ GQDYADHRCV HSARR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase." Kashuba E., Kashuba V., Sandalova T., Klein G., Szekely L. BMC Cell Biol. 3:23-23(2002) [PubMed: 12199906] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH EBV EBNA3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION. Tissue: Heart.
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	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] (ISOFORM 1). Tissue: Spleen.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 2). Tissue: Placenta.
[6]	"NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase." Fortier J.M., Kornbluth J. J. Immunol. 176:6454-6463(2006) [PubMed: 16709802] [Abstract] Cited for: INTERACTION WITH RNF19B, UBIQUITINATION.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-539, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ605558 mRNA. Translation: CAE54074.1. AK000524 mRNA. Translation: BAA91230.1. AK223220 mRNA. Translation: BAD96940.1. AL118506 Genomic DNA. Translation: CAI21904.1. BC033078 mRNA. Translation: AAH33078.1.
IPI	IPI00384294. IPI00844311. IPI00847664.
RefSeq	NP_060329.2. NM_017859.3.
UniGene	Hs.504998.
3D structure databases
ProteinModelPortal	Q9NWZ5.
SMR	Q9NWZ5. Positions 97-301, 323-532.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NWZ5. 3 interactions.
STRING	Q9NWZ5.
PTM databases
PhosphoSite	Q9NWZ5.
Polymorphism databases
DMDM	84029407.
Proteomic databases
PRIDE	Q9NWZ5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354216; ENSP00000346155; ENSG00000198276.
GeneID	54963.
KEGG	hsa:54963.
UCSC	uc010gkn.1. human.
Organism-specific databases
CTD	54963.
GeneCards	GC20M062571.
H-InvDB	HIX0016015.
HGNC	HGNC:15938. UCKL1.
HPA	HPA004722. HPA004769.
MIM	610866. gene.
neXtProt	NX_Q9NWZ5.
PharmGKB	PA38058.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000015696.
HOGENOM	HBG326432.
HOVERGEN	HBG055146.
InParanoid	Q9NWZ5.
OMA	PPDWSDE.
OrthoDB	EOG46HG9J.
PhylomeDB	Q9NWZ5.
Gene expression databases
ArrayExpress	Q9NWZ5.
Bgee	Q9NWZ5.
CleanEx	HS_UCKL1.
Genevestigator	Q9NWZ5.
GermOnline	ENSG00000198276. Homo sapiens.
Family and domain databases
InterPro	IPR006083. PRK/URK. IPR000764. Uridine_kinase. [Graphical view]
KO	K00876.
Pfam	PF00485. PRK. 1 hit. [Graphical view]
PRINTS	PR00988. URIDINKINASE.
TIGRFAMs	TIGR00235. Udk. 1 hit.
ProtoNet	Search...
Other
NextBio	58176.
SOURCE	Search...

Entry information

Entry name

UCKL1_HUMAN

Accession

Primary (citable) accession number: Q9NWZ5
Secondary accession number(s): Q5JWV0 , Q70AQ5, Q8N524, Q9H3Z2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 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.