NUCKS_HUMAN
ID NUCKS_HUMAN Reviewed; 243 AA.
AC Q9H1E3; Q54AC0; Q5PXE7; Q9H1D6; Q9H723;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1 {ECO:0000303|PubMed:11298763};
DE AltName: Full=P1;
GN Name=NUCKS1 {ECO:0000303|PubMed:26323318, ECO:0000312|HGNC:HGNC:29923};
GN Synonyms=NUCKS {ECO:0000303|PubMed:11298763};
GN ORFNames=JC7 {ECO:0000303|Ref.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RC TISSUE=Blood;
RX PubMed=11298763; DOI=10.1046/j.1432-1327.2001.02120.x;
RA Oestvold A.C., Norum J.H., Mathiesen S., Wanvik B., Sefland I., Grundt K.;
RT "Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which
RT serves as a substrate for Cdk1 in vivo.";
RL Eur. J. Biochem. 268:2430-2440(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yoshitaka T., Park J., Ueki Y., Yonezawa T., Ninomiya Y.;
RT "A search for cell proliferation related new genes.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Sievert V., Buessow K.;
RT "Sequencing of E. coli expression clones for human proteins.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15381070; DOI=10.1016/j.bbrc.2004.08.153;
RA Grundt K., Haga I.V., Aleporou-Marinou V., Drosos Y., Wanvik B.,
RA Ostvold A.C.;
RT "Characterisation of the NUCKS gene on human chromosome 1q32.1 and the
RT presence of a homologous gene in different species.";
RL Biochem. Biophys. Res. Commun. 323:796-801(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-79; SER-214; SER-229
RP AND SER-240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; TYR-26; SER-113; SER-130;
RP SER-132; SER-144; THR-179; SER-181; SER-234 AND SER-240, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-54; SER-58; SER-61;
RP SER-73; SER-75; SER-79; SER-214; SER-229; SER-234 AND SER-240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61 AND
RP SER-113, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-54; SER-58; SER-61;
RP SER-73; SER-75; SER-79; SER-113; SER-130; SER-132; SER-181; THR-202;
RP SER-204; SER-214; SER-223; SER-229; SER-234 AND SER-240, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61; SER-79;
RP SER-130; SER-132; SER-144; THR-179; SER-181; THR-202; SER-204; SER-214;
RP SER-223; SER-229; SER-234 AND SER-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-19; TYR-26; SER-75;
RP SER-79; SER-113; THR-179; SER-181; THR-202; SER-204 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-54; SER-58; SER-61;
RP SER-75; SER-79; SER-130; SER-132; SER-144; SER-214 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP FUNCTION, SUBCELLULAR LOCATION, LACK OF INTERACTION WITH RAD51, AND
RP PHOSPHORYLATION AT SER-54.
RX PubMed=26323318; DOI=10.1093/nar/gkv859;
RA Parplys A.C., Zhao W., Sharma N., Groesser T., Liang F., Maranon D.G.,
RA Leung S.G., Grundt K., Dray E., Idate R., Oestvold A.C., Schild D.,
RA Sung P., Wiese C.;
RT "NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination
RT and genome stability.";
RL Nucleic Acids Res. 43:9817-9834(2015).
CC -!- FUNCTION: Chromatin-associated protein involved in DNA repair by
CC promoting homologous recombination (HR) (PubMed:26323318). Binds
CC double-stranded DNA (dsDNA) and secondary DNA structures, such as D-
CC loop structures, but with less affinity than RAD51AP1
CC (PubMed:26323318). {ECO:0000269|PubMed:26323318}.
CC -!- SUBUNIT: Does not interact with RAD51. {ECO:0000269|PubMed:26323318}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11298763,
CC ECO:0000269|PubMed:26323318}. Chromosome {ECO:0000269|PubMed:26323318}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H1E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1E3-2; Sequence=VSP_021770;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in thyroid
CC gland, prostate and uterus and in fetal liver, thymus and lung.
CC {ECO:0000269|PubMed:15381070}.
CC -!- PTM: Phosphorylated in an ATM-dependent manner in response to DNA
CC damage (PubMed:26323318). Phosphorylated by CDK1 and casein kinase
CC (PubMed:11298763). {ECO:0000269|PubMed:11298763,
CC ECO:0000269|PubMed:26323318}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15076.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC20412.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ012584; CAC20408.1; -; mRNA.
DR EMBL; AB049824; BAC06820.1; -; mRNA.
DR EMBL; AY823399; AAV83925.1; -; mRNA.
DR EMBL; AJ237668; CAC20412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK025133; BAB15076.1; ALT_SEQ; mRNA.
DR EMBL; CH471067; EAW91578.1; -; Genomic_DNA.
DR EMBL; BC000805; AAH00805.1; -; mRNA.
DR CCDS; CCDS30987.1; -. [Q9H1E3-1]
DR RefSeq; NP_073568.2; NM_022731.4. [Q9H1E3-1]
DR AlphaFoldDB; Q9H1E3; -.
DR BioGRID; 122238; 36.
DR IntAct; Q9H1E3; 11.
DR MINT; Q9H1E3; -.
DR STRING; 9606.ENSP00000356110; -.
DR iPTMnet; Q9H1E3; -.
DR PhosphoSitePlus; Q9H1E3; -.
DR SwissPalm; Q9H1E3; -.
DR BioMuta; NUCKS1; -.
DR DMDM; 13631947; -.
DR EPD; Q9H1E3; -.
DR jPOST; Q9H1E3; -.
DR MassIVE; Q9H1E3; -.
DR MaxQB; Q9H1E3; -.
DR PaxDb; Q9H1E3; -.
DR PeptideAtlas; Q9H1E3; -.
DR PRIDE; Q9H1E3; -.
DR ProteomicsDB; 80404; -. [Q9H1E3-1]
DR ProteomicsDB; 80405; -. [Q9H1E3-2]
DR TopDownProteomics; Q9H1E3-1; -. [Q9H1E3-1]
DR TopDownProteomics; Q9H1E3-2; -. [Q9H1E3-2]
DR Antibodypedia; 34570; 195 antibodies from 30 providers.
DR DNASU; 64710; -.
DR Ensembl; ENST00000367142.5; ENSP00000356110.4; ENSG00000069275.13. [Q9H1E3-1]
DR GeneID; 64710; -.
DR KEGG; hsa:64710; -.
DR MANE-Select; ENST00000367142.5; ENSP00000356110.4; NM_022731.5; NP_073568.2.
DR UCSC; uc001hdb.4; human. [Q9H1E3-1]
DR CTD; 64710; -.
DR DisGeNET; 64710; -.
DR GeneCards; NUCKS1; -.
DR HGNC; HGNC:29923; NUCKS1.
DR HPA; ENSG00000069275; Low tissue specificity.
DR MIM; 611912; gene.
DR neXtProt; NX_Q9H1E3; -.
DR OpenTargets; ENSG00000069275; -.
DR PharmGKB; PA142671244; -.
DR VEuPathDB; HostDB:ENSG00000069275; -.
DR eggNOG; ENOG502R8NJ; Eukaryota.
DR GeneTree; ENSGT00940000153414; -.
DR HOGENOM; CLU_067355_0_1_1; -.
DR InParanoid; Q9H1E3; -.
DR OMA; PREIKHK; -.
DR OrthoDB; 1605786at2759; -.
DR PhylomeDB; Q9H1E3; -.
DR PathwayCommons; Q9H1E3; -.
DR SignaLink; Q9H1E3; -.
DR SIGNOR; Q9H1E3; -.
DR BioGRID-ORCS; 64710; 44 hits in 1087 CRISPR screens.
DR ChiTaRS; NUCKS1; human.
DR GeneWiki; NUCKS1; -.
DR GenomeRNAi; 64710; -.
DR Pharos; Q9H1E3; Tbio.
DR PRO; PR:Q9H1E3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H1E3; protein.
DR Bgee; ENSG00000069275; Expressed in tendon of biceps brachii and 206 other tissues.
DR Genevisible; Q9H1E3; HS.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0071481; P:cellular response to X-ray; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006325; P:chromatin organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:ParkinsonsUK-UCL.
DR GO; GO:0035822; P:gene conversion; NAS:ParkinsonsUK-UCL.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:ParkinsonsUK-UCL.
DR GO; GO:1990968; P:modulation by host of RNA binding by virus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0044827; P:modulation by host of viral genome replication; IMP:ParkinsonsUK-UCL.
DR GO; GO:1990969; P:modulation by host of viral RNA-binding transcription factor activity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IGI:ParkinsonsUK-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ParkinsonsUK-UCL.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031297; P:replication fork processing; IDA:ParkinsonsUK-UCL.
DR InterPro; IPR026633; NUCKS1.
DR PANTHER; PTHR15361:SF1; PTHR15361:SF1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..243
FT /note="Nuclear ubiquitous casein and cyclin-dependent
FT kinase substrate 1"
FT /id="PRO_0000057978"
FT REGION 1..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80XU3"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26323318,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT VAR_SEQ 14..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021770"
FT VARIANT 119
FT /note="E -> G (in dbSNP:rs3207505)"
FT /id="VAR_051246"
FT VARIANT 137
FT /note="L -> P (in dbSNP:rs17355035)"
FT /id="VAR_051247"
FT CONFLICT 112
FT /note="G -> D (in Ref. 3; AAV83925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 27296 MW; 136BA1885F893950 CRC64;
MSRPVRNRKV VDYSQFQESD DADEDYGRDS GPPTKKIRSS PREAKNKRRS GKNSQEDSED
SEDKDVKTKK DDSHSAEDSE DEKEDHKNVR QQRQAASKAA SKQREMLMED VGSEEEQEEE
DEAPFQEKDS GSDEDFLMED DDDSDYGSSK KKNKKMVKKS KPERKEKKMP KPRLKATVTP
SPVKGKGKVG RPTASKASKE KTPSPKEEDE EPESPPEKKT STSPPPEKSG DEGSEDEAPS
GED
