NUCKS_MOUSE
ID NUCKS_MOUSE Reviewed; 234 AA.
AC Q80XU3; Q8BVD8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1;
DE AltName: Full=JC7 {ECO:0000303|Ref.1};
GN Name=Nucks1; Synonyms=Nucks;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoshitaka T.;
RT "A search for cell proliferation related new genes.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61; THR-179
RP AND SER-181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61; SER-130
RP AND SER-132, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13; SER-14; SER-19; SER-54;
RP SER-58; SER-61; SER-113; THR-179; SER-181 AND SER-214, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Chromatin-associated protein involved in DNA repair by
CC promoting homologous recombination (HR). Binds double-stranded DNA
CC (dsDNA) and secondary DNA structures, such as D-loop structures, but
CC with less affinity than RAD51AP1. {ECO:0000250|UniProtKB:Q9H1E3}.
CC -!- SUBUNIT: Does not interact with RAD51. {ECO:0000250|UniProtKB:Q9H1E3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H1E3}.
CC Chromosome {ECO:0000250|UniProtKB:Q9H1E3}.
CC -!- PTM: Phosphorylated in an ATM-dependent manner in response to DNA
CC damage. Phosphorylated by CDK1 and casein kinase.
CC {ECO:0000250|UniProtKB:Q9H1E3}.
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DR EMBL; AB049825; BAC06821.1; -; mRNA.
DR EMBL; AK078816; BAC37408.1; -; mRNA.
DR EMBL; BC039951; AAH39951.1; -; mRNA.
DR CCDS; CCDS48356.1; -.
DR RefSeq; NP_001139276.1; NM_001145804.1.
DR RefSeq; NP_780503.2; NM_175294.3.
DR AlphaFoldDB; Q80XU3; -.
DR BioGRID; 221055; 3.
DR IntAct; Q80XU3; 3.
DR MINT; Q80XU3; -.
DR STRING; 10090.ENSMUSP00000062576; -.
DR iPTMnet; Q80XU3; -.
DR PhosphoSitePlus; Q80XU3; -.
DR EPD; Q80XU3; -.
DR jPOST; Q80XU3; -.
DR MaxQB; Q80XU3; -.
DR PaxDb; Q80XU3; -.
DR PeptideAtlas; Q80XU3; -.
DR PRIDE; Q80XU3; -.
DR ProteomicsDB; 293778; -.
DR TopDownProteomics; Q80XU3; -.
DR Antibodypedia; 34570; 195 antibodies from 30 providers.
DR DNASU; 98415; -.
DR Ensembl; ENSMUST00000062264; ENSMUSP00000062576; ENSMUSG00000026434.
DR GeneID; 98415; -.
DR KEGG; mmu:98415; -.
DR UCSC; uc007cny.2; mouse.
DR CTD; 64710; -.
DR MGI; MGI:1934811; Nucks1.
DR VEuPathDB; HostDB:ENSMUSG00000026434; -.
DR eggNOG; ENOG502R8NJ; Eukaryota.
DR GeneTree; ENSGT00940000153414; -.
DR HOGENOM; CLU_067355_0_1_1; -.
DR InParanoid; Q80XU3; -.
DR OMA; PREIKHK; -.
DR OrthoDB; 1605786at2759; -.
DR PhylomeDB; Q80XU3; -.
DR BioGRID-ORCS; 98415; 3 hits in 109 CRISPR screens.
DR ChiTaRS; Nucks1; mouse.
DR PRO; PR:Q80XU3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80XU3; protein.
DR Bgee; ENSMUSG00000026434; Expressed in rostral migratory stream and 255 other tissues.
DR ExpressionAtlas; Q80XU3; baseline and differential.
DR Genevisible; Q80XU3; MM.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0001678; P:cellular glucose homeostasis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0071481; P:cellular response to X-ray; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR GO; GO:1990968; P:modulation by host of RNA binding by virus; ISO:MGI.
DR GO; GO:0044827; P:modulation by host of viral genome replication; ISO:MGI.
DR GO; GO:1990969; P:modulation by host of viral RNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ParkinsonsUK-UCL.
DR GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR InterPro; IPR026633; NUCKS1.
DR PANTHER; PTHR15361:SF1; PTHR15361:SF1; 2.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..234
FT /note="Nuclear ubiquitous casein and cyclin-dependent
FT kinase substrate 1"
FT /id="PRO_0000057979"
FT REGION 1..234
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 193..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT CONFLICT 128..129
FT /note="KD -> N (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> Q (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="K -> Q (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="K -> E (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="K -> Q (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="L -> V (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="K -> Q (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> Q (in Ref. 2; BAC37408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26313 MW; CB2075863AA0E87A CRC64;
MSRPVRNRKV VDYSQFQESD DADEDYGRDS GPPAKKIRSS PREAKNKRRS GKNSQEDSED
SEEKDVKTKK DDSHSAEDSE DEKDDHKNVR QQRQAASKAA SKQREMLLED VGSEEEPEED
DEAPFQEKDS GSDEDFLMED DDDSDYGSSK KKNKKMVKKS KPERKEKKMP KPRLKATVTP
SPVKGKAKVG RPTASKKSKE KTPSPKEEDE EAESPPEKKS GDEGSEDEAS SGED
