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Protein

Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1

Gene

NUCKS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1
Alternative name(s):
P1
Gene namesi
Name:NUCKS1
Synonyms:NUCKS
ORF Names:JC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29923. NUCKS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • nucleus Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671244.

Polymorphism and mutation databases

BioMutaiNUCKS1.
DMDMi13631947.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1PRO_0000057978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphotyrosineBy similarity
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei26 – 261PhosphotyrosineCombined sources
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei75 – 751PhosphoserineCombined sources
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei130 – 1301PhosphoserineCombined sources
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei144 – 1441PhosphoserineCombined sources
Modified residuei179 – 1791PhosphothreonineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources
Modified residuei202 – 2021PhosphothreonineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei223 – 2231PhosphoserineCombined sources
Modified residuei229 – 2291PhosphoserineCombined sources
Modified residuei234 – 2341PhosphoserineCombined sources
Modified residuei240 – 2401PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDK1 and casein kinase.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H1E3.
MaxQBiQ9H1E3.
PaxDbiQ9H1E3.
PeptideAtlasiQ9H1E3.
PRIDEiQ9H1E3.
TopDownProteomicsiQ9H1E3-1. [Q9H1E3-1]
Q9H1E3-2. [Q9H1E3-2]

PTM databases

iPTMnetiQ9H1E3.
PhosphoSiteiQ9H1E3.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in thyroid gland, prostate and uterus and in fetal liver, thymus and lung.1 Publication

Gene expression databases

BgeeiQ9H1E3.
CleanExiHS_NUCKS1.
GenevisibleiQ9H1E3. HS.

Interactioni

Protein-protein interaction databases

BioGridi122238. 15 interactions.
IntActiQ9H1E3. 4 interactions.
MINTiMINT-1419873.
STRINGi9606.ENSP00000356110.

Structurei

3D structure databases

ProteinModelPortaliQ9H1E3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi140 – 1456Poly-Asp
Compositional biasi150 – 20657Lys-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IH23. Eukaryota.
ENOG410XQNM. LUCA.
GeneTreeiENSGT00730000111108.
HOGENOMiHOG000113884.
HOVERGENiHBG052687.
InParanoidiQ9H1E3.
OMAiEDGGSDY.
OrthoDBiEOG7PVWS0.
PhylomeDBiQ9H1E3.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H1E3-1) [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
MSRPVRNRKV VDYSQFQESD DADEDYGRDS GPPTKKIRSS PREAKNKRRS
60 70 80 90 100
GKNSQEDSED SEDKDVKTKK DDSHSAEDSE DEKEDHKNVR QQRQAASKAA
110 120 130 140 150
SKQREMLMED VGSEEEQEEE DEAPFQEKDS GSDEDFLMED DDDSDYGSSK
160 170 180 190 200
KKNKKMVKKS KPERKEKKMP KPRLKATVTP SPVKGKGKVG RPTASKASKE
210 220 230 240
KTPSPKEEDE EPESPPEKKT STSPPPEKSG DEGSEDEAPS GED
Length:243
Mass (Da):27,296
Last modified:March 1, 2001 - v1
Checksum:i136BA1885F893950
GO
Isoform 2 (identifier: Q9H1E3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     14-53: Missing.

Show »
Length:203
Mass (Da):22,776
Checksum:i094C2FBDC4F2B694
GO

Sequence cautioni

The sequence BAB15076.1 differs from that shown. Reason: Erroneous termination at position 164. Translated as Arg.Curated
The sequence CAC20412.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121G → D in AAV83925 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191E → G.
Corresponds to variant rs3207505 [ dbSNP | Ensembl ].
VAR_051246
Natural varianti137 – 1371L → P.
Corresponds to variant rs17355035 [ dbSNP | Ensembl ].
VAR_051247

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei14 – 5340Missing in isoform 2. 1 PublicationVSP_021770Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012584 mRNA. Translation: CAC20408.1.
AB049824 mRNA. Translation: BAC06820.1.
AY823399 mRNA. Translation: AAV83925.1.
AJ237668 Genomic DNA. Translation: CAC20412.1. Sequence problems.
AK025133 mRNA. Translation: BAB15076.1. Sequence problems.
CH471067 Genomic DNA. Translation: EAW91578.1.
BC000805 mRNA. Translation: AAH00805.1.
CCDSiCCDS30987.1. [Q9H1E3-1]
RefSeqiNP_073568.2. NM_022731.4. [Q9H1E3-1]
UniGeneiHs.213061.
Hs.744865.

Genome annotation databases

EnsembliENST00000367142; ENSP00000356110; ENSG00000069275. [Q9H1E3-1]
GeneIDi64710.
KEGGihsa:64710.
UCSCiuc001hdb.4. human. [Q9H1E3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012584 mRNA. Translation: CAC20408.1.
AB049824 mRNA. Translation: BAC06820.1.
AY823399 mRNA. Translation: AAV83925.1.
AJ237668 Genomic DNA. Translation: CAC20412.1. Sequence problems.
AK025133 mRNA. Translation: BAB15076.1. Sequence problems.
CH471067 Genomic DNA. Translation: EAW91578.1.
BC000805 mRNA. Translation: AAH00805.1.
CCDSiCCDS30987.1. [Q9H1E3-1]
RefSeqiNP_073568.2. NM_022731.4. [Q9H1E3-1]
UniGeneiHs.213061.
Hs.744865.

3D structure databases

ProteinModelPortaliQ9H1E3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122238. 15 interactions.
IntActiQ9H1E3. 4 interactions.
MINTiMINT-1419873.
STRINGi9606.ENSP00000356110.

PTM databases

iPTMnetiQ9H1E3.
PhosphoSiteiQ9H1E3.

Polymorphism and mutation databases

BioMutaiNUCKS1.
DMDMi13631947.

Proteomic databases

EPDiQ9H1E3.
MaxQBiQ9H1E3.
PaxDbiQ9H1E3.
PeptideAtlasiQ9H1E3.
PRIDEiQ9H1E3.
TopDownProteomicsiQ9H1E3-1. [Q9H1E3-1]
Q9H1E3-2. [Q9H1E3-2]

Protocols and materials databases

DNASUi64710.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367142; ENSP00000356110; ENSG00000069275. [Q9H1E3-1]
GeneIDi64710.
KEGGihsa:64710.
UCSCiuc001hdb.4. human. [Q9H1E3-1]

Organism-specific databases

CTDi64710.
GeneCardsiNUCKS1.
HGNCiHGNC:29923. NUCKS1.
MIMi611912. gene.
neXtProtiNX_Q9H1E3.
PharmGKBiPA142671244.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH23. Eukaryota.
ENOG410XQNM. LUCA.
GeneTreeiENSGT00730000111108.
HOGENOMiHOG000113884.
HOVERGENiHBG052687.
InParanoidiQ9H1E3.
OMAiEDGGSDY.
OrthoDBiEOG7PVWS0.
PhylomeDBiQ9H1E3.

Miscellaneous databases

ChiTaRSiNUCKS1. human.
GeneWikiiNUCKS1.
GenomeRNAii64710.
PROiQ9H1E3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H1E3.
CleanExiHS_NUCKS1.
GenevisibleiQ9H1E3. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo."
    Oestvold A.C., Norum J.H., Mathiesen S., Wanvik B., Sefland I., Grundt K.
    Eur. J. Biochem. 268:2430-2440(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Blood.
  2. "A search for cell proliferation related new genes."
    Yoshitaka T., Park J., Ueki Y., Yonezawa T., Ninomiya Y.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Sequencing of E. coli expression clones for human proteins."
    Sievert V., Buessow K.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. "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] (ISOFORM 1).
    Tissue: Colon.
  5. 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].
    Tissue: Placenta.
  7. "Characterisation of the NUCKS gene on human chromosome 1q32.1 and the presence of a homologous gene in different species."
    Grundt K., Haga I.V., Aleporou-Marinou V., Drosos Y., Wanvik B., Ostvold A.C.
    Biochem. Biophys. Res. Commun. 323:796-801(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-79; SER-214; SER-229 AND SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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 THR-179 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; TYR-26; SER-113; SER-130; SER-132; SER-144; THR-179; SER-181; SER-234 AND SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-54; SER-58; SER-61; SER-73; SER-75; SER-79; SER-214; SER-229; SER-234 AND SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-19; SER-58; SER-61 AND SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "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-19; SER-54; SER-58; SER-61; SER-73; SER-75; SER-79; SER-113; SER-130; SER-132; SER-181; THR-202; SER-204; SER-214; SER-223; SER-229; SER-234 AND SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-19; SER-58; SER-61; SER-79; SER-130; SER-132; SER-144; THR-179; SER-181; THR-202; SER-204; SER-214; SER-223; SER-229; SER-234 AND SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-19; TYR-26; SER-75; SER-79; SER-113; THR-179; SER-181; THR-202; SER-204 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-54; SER-58; SER-61; SER-75; SER-79; SER-130; SER-132; SER-144; SER-214 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNUCKS_HUMAN
AccessioniPrimary (citable) accession number: Q9H1E3
Secondary accession number(s): Q54AC0
, Q5PXE7, Q9H1D6, Q9H723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 133 of the entry and version 1 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.