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Protein

Uridine-cytidine kinase-like 1

Gene

UCKL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May contribute to UTP accumulation needed for blast transformation and proliferation.1 Publication

Catalytic activityi

ATP + uridine = ADP + UMP.
ATP + cytidine = ADP + CMP.

Pathwayi: CTP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes CTP from cytidine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Uridine-cytidine kinase 2 (UCK2), Uridine kinase (UCK1), Uridine-cytidine kinase, Uridine-cytidine kinase 1 (UCK1), Uridine-cytidine kinase-like 1 (UCKL1), Uridine kinase (UCK2)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway CTP biosynthesis via salvage pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CTP from cytidine, the pathway CTP biosynthesis via salvage pathway and in Pyrimidine metabolism.

Pathwayi: UMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes UMP from uridine.
Proteins known to be involved in this subpathway in this organism are:
  1. Uridine-cytidine kinase 2 (UCK2), Uridine kinase (UCK1), Uridine-cytidine kinase, Uridine-cytidine kinase 1 (UCK1), Uridine-cytidine kinase-like 1 (UCKL1), Uridine kinase (UCK2)
This subpathway is part of the pathway UMP biosynthesis via salvage pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UMP from uridine, the pathway UMP biosynthesis via salvage pathway and in Pyrimidine metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1128ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00574; UER00637.
UPA00579; UER00640.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridine-cytidine kinase-like 1 (EC:2.7.1.48)
Gene namesi
Name:UCKL1
Synonyms:URKL1
ORF Names:F538
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15938. UCKL1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: EBNA3 induces isoform 1 translocation to the nucleus, whereas it does change isoform 3 location.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38058.

Polymorphism and mutation databases

BioMutaiUCKL1.
DMDMi84029407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Uridine-cytidine kinase-like 1PRO_0000164460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei63 – 631PhosphoserineBy similarity
Modified residuei539 – 5391PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated by RNF19B; which induces proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NWZ5.
MaxQBiQ9NWZ5.
PaxDbiQ9NWZ5.
PRIDEiQ9NWZ5.

PTM databases

iPTMnetiQ9NWZ5.
PhosphoSiteiQ9NWZ5.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9NWZ5.
CleanExiHS_UCKL1.
ExpressionAtlasiQ9NWZ5. baseline and differential.
GenevisibleiQ9NWZ5. HS.

Organism-specific databases

HPAiHPA004722.
HPA004769.

Interactioni

Subunit structurei

Interacts with RNF19B and EBV EBNA3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EBNA3P129774EBI-2466660,EBI-993115From a different organism.
RNF19BQ6ZMZ04EBI-2466660,EBI-2466594

Protein-protein interaction databases

BioGridi120301. 12 interactions.
IntActiQ9NWZ5. 4 interactions.
STRINGi9606.ENSP00000346155.

Structurei

3D structure databases

ProteinModelPortaliQ9NWZ5.
SMRiQ9NWZ5. Positions 97-300, 326-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the uridine kinase family.Curated

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
COG0572. LUCA.
GeneTreeiENSGT00390000015696.
HOGENOMiHOG000262757.
HOVERGENiHBG055146.
InParanoidiQ9NWZ5.
KOiK00876.
OMAiMDCFYKI.
OrthoDBiEOG76T9QV.
PhylomeDBiQ9NWZ5.
TreeFamiTF105902.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR006083. PRK/URK.
IPR029057. PRTase-like.
IPR029933. UCKL1.
IPR000764. Uridine_kinase-like.
[Graphical view]
PANTHERiPTHR10285:SF68. PTHR10285:SF68. 2 hits.
PfamiPF00485. PRK. 1 hit.
PF14681. UPRTase. 1 hit.
[Graphical view]
PRINTSiPR00988. URIDINKINASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00235. udk. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NWZ5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAPPARADA DPSPTSPPTA RDTPGRQAEK SETACEDRSN AESLDRLLPP
60 70 80 90 100
VGTGRSPRKR TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA
110 120 130 140 150
IGLGGGSASG KTTVARMIIE ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN
160 170 180 190 200
NFNFDHPDAF DFDLIISTLK KLKQGKSVKV PIYDFTTHSR KKDWKTLYGA
210 220 230 240 250
NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR DISERGRDIE
260 270 280 290 300
GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL
310 320 330 340 350
EERELSVRAA LASAHQCHPL PRTLSVLKST PQVRGMHTII RDKETSRDEF
360 370 380 390 400
IFYSKRLMRL LIEHALSFLP FQDCVVQTPQ GQDYAGKCYA GKQITGVSIL
410 420 430 440 450
RAGETMEPAL RAVCKDVRIG TILIQTNQLT GEPELHYLRL PKDISDDHVI
460 470 480 490 500
LMDCTVSTGA AAMMAVRVLL DHDVPEDKIF LLSLLMAEMG VHSVAYAFPR
510 520 530 540
VRIITTAVDK RVNDLFRIIP GIGNFGDRYF GTDAVPDGSD EEEVAYTG
Length:548
Mass (Da):61,141
Last modified:September 13, 2005 - v2
Checksum:i0CD0351A802FE199
GO
Isoform 2 (identifier: Q9NWZ5-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:419
Mass (Da):45,972
Checksum:i1D1F11E75305AD25
GO
Isoform 3 (identifier: Q9NWZ5-3) [UniParc]FASTAAdd to basket

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

Show »
Length:395
Mass (Da):44,568
Checksum:i437D0B1A665CCE30
GO
Isoform 4 (identifier: Q9NWZ5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDR → MSSPPAYPGIRISGCRALGAEGS

Show »
Length:533
Mass (Da):59,466
Checksum:iE578C67A1AB86E15
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901D → N in CAE54074 (PubMed:12199906).Curated
Sequence conflicti290 – 2901D → N in BAA91230 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838MAAPP…ACEDR → MSSPPAYPGIRISGCRALGA EGS in isoform 4. 1 PublicationVSP_043171Add
BLAST
Alternative sequencei303 – 548246RELSV…VAYTG → GCAGLGTPVPPAAPDAERPE EHAAGTGHAHHHQVRAHLGT GRPRARAPAQLLAPQGQGDQ SRRVHLLLQETDAAAHRARA LLPALSGLRRTDPAGAGLCG QVLCGEADHRCVHSARR in isoform 2. 1 PublicationVSP_021802Add
BLAST
Alternative sequencei386 – 39510GKCYAGKQIT → DHRCVHSARR in isoform 3. 1 PublicationVSP_025641
Alternative sequencei396 – 548153Missing in isoform 3. 1 PublicationVSP_025642Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ605558 mRNA. Translation: CAE54074.1.
AK000524 mRNA. Translation: BAA91230.1.
AK303688 mRNA. Translation: BAH14018.1.
AK223220 mRNA. Translation: BAD96940.1.
AL118506 Genomic DNA. Translation: CAI21904.1.
BC033078 mRNA. Translation: AAH33078.1.
CCDSiCCDS13547.1. [Q9NWZ5-1]
CCDS54479.1. [Q9NWZ5-4]
RefSeqiNP_001180308.1. NM_001193379.1. [Q9NWZ5-4]
NP_060329.2. NM_017859.3. [Q9NWZ5-1]
UniGeneiHs.504998.
Hs.695829.

Genome annotation databases

EnsembliENST00000354216; ENSP00000346155; ENSG00000198276. [Q9NWZ5-1]
ENST00000358711; ENSP00000351546; ENSG00000198276. [Q9NWZ5-2]
ENST00000369908; ENSP00000358924; ENSG00000198276. [Q9NWZ5-4]
GeneIDi54963.
KEGGihsa:54963.
UCSCiuc010gkn.4. human. [Q9NWZ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ605558 mRNA. Translation: CAE54074.1.
AK000524 mRNA. Translation: BAA91230.1.
AK303688 mRNA. Translation: BAH14018.1.
AK223220 mRNA. Translation: BAD96940.1.
AL118506 Genomic DNA. Translation: CAI21904.1.
BC033078 mRNA. Translation: AAH33078.1.
CCDSiCCDS13547.1. [Q9NWZ5-1]
CCDS54479.1. [Q9NWZ5-4]
RefSeqiNP_001180308.1. NM_001193379.1. [Q9NWZ5-4]
NP_060329.2. NM_017859.3. [Q9NWZ5-1]
UniGeneiHs.504998.
Hs.695829.

3D structure databases

ProteinModelPortaliQ9NWZ5.
SMRiQ9NWZ5. Positions 97-300, 326-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120301. 12 interactions.
IntActiQ9NWZ5. 4 interactions.
STRINGi9606.ENSP00000346155.

PTM databases

iPTMnetiQ9NWZ5.
PhosphoSiteiQ9NWZ5.

Polymorphism and mutation databases

BioMutaiUCKL1.
DMDMi84029407.

Proteomic databases

EPDiQ9NWZ5.
MaxQBiQ9NWZ5.
PaxDbiQ9NWZ5.
PRIDEiQ9NWZ5.

Protocols and materials databases

DNASUi54963.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354216; ENSP00000346155; ENSG00000198276. [Q9NWZ5-1]
ENST00000358711; ENSP00000351546; ENSG00000198276. [Q9NWZ5-2]
ENST00000369908; ENSP00000358924; ENSG00000198276. [Q9NWZ5-4]
GeneIDi54963.
KEGGihsa:54963.
UCSCiuc010gkn.4. human. [Q9NWZ5-1]

Organism-specific databases

CTDi54963.
GeneCardsiUCKL1.
H-InvDBHIX0027741.
HGNCiHGNC:15938. UCKL1.
HPAiHPA004722.
HPA004769.
MIMi610866. gene.
neXtProtiNX_Q9NWZ5.
PharmGKBiPA38058.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
COG0572. LUCA.
GeneTreeiENSGT00390000015696.
HOGENOMiHOG000262757.
HOVERGENiHBG055146.
InParanoidiQ9NWZ5.
KOiK00876.
OMAiMDCFYKI.
OrthoDBiEOG76T9QV.
PhylomeDBiQ9NWZ5.
TreeFamiTF105902.

Enzyme and pathway databases

UniPathwayiUPA00574; UER00637.
UPA00579; UER00640.

Miscellaneous databases

GeneWikiiUCKL1.
GenomeRNAii54963.
NextBioi58176.
PROiQ9NWZ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWZ5.
CleanExiHS_UCKL1.
ExpressionAtlasiQ9NWZ5. baseline and differential.
GenevisibleiQ9NWZ5. HS.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR006083. PRK/URK.
IPR029057. PRTase-like.
IPR029933. UCKL1.
IPR000764. Uridine_kinase-like.
[Graphical view]
PANTHERiPTHR10285:SF68. PTHR10285:SF68. 2 hits.
PfamiPF00485. PRK. 1 hit.
PF14681. UPRTase. 1 hit.
[Graphical view]
PRINTSiPR00988. URIDINKINASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00235. udk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Kidney.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUCKL1_HUMAN
AccessioniPrimary (citable) accession number: Q9NWZ5
Secondary accession number(s): B7Z8N2
, Q5JWV0, Q70AQ5, Q8N524, Q9H3Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: September 13, 2005
Last modified: March 16, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.