NUCKS_RAT
ID NUCKS_RAT Reviewed; 243 AA.
AC Q9EPJ0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1 {ECO:0000303|PubMed:11298763};
GN Name=Nucks1 {ECO:0000312|RGD:620993};
GN Synonyms=Nucks {ECO:0000303|PubMed:11298763};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61; SER-73;
RP SER-75; SER-79; SER-113; SER-130; SER-132; SER-144; SER-181; SER-204;
RP SER-214; SER-223; SER-229; SER-234 AND SER-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AJ237669; CAC20862.1; -; mRNA.
DR EMBL; BC078818; AAH78818.1; -; mRNA.
DR RefSeq; NP_073636.1; NM_022799.2.
DR AlphaFoldDB; Q9EPJ0; -.
DR STRING; 10116.ENSRNOP00000065540; -.
DR iPTMnet; Q9EPJ0; -.
DR PhosphoSitePlus; Q9EPJ0; -.
DR PaxDb; Q9EPJ0; -.
DR PRIDE; Q9EPJ0; -.
DR Ensembl; ENSRNOT00000112895; ENSRNOP00000076606; ENSRNOG00000047287.
DR GeneID; 64709; -.
DR KEGG; rno:64709; -.
DR UCSC; RGD:620993; rat.
DR CTD; 64710; -.
DR RGD; 620993; Nucks1.
DR eggNOG; ENOG502R8NJ; Eukaryota.
DR GeneTree; ENSGT00940000153414; -.
DR HOGENOM; CLU_067355_0_1_1; -.
DR InParanoid; Q9EPJ0; -.
DR OMA; PREIKHK; -.
DR OrthoDB; 1605786at2759; -.
DR PhylomeDB; Q9EPJ0; -.
DR PRO; PR:Q9EPJ0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000047287; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q9EPJ0; baseline and differential.
DR Genevisible; Q9EPJ0; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISO:RGD.
DR GO; GO:0071481; P:cellular response to X-ray; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; ISO:RGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:RGD.
DR GO; GO:1990968; P:modulation by host of RNA binding by virus; ISO:RGD.
DR GO; GO:1990969; P:modulation by host of viral RNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:RGD.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:RGD.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:RGD.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0019046; P:release from viral latency; ISO:RGD.
DR GO; GO:0031297; P:replication fork processing; ISO:RGD.
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..243
FT /note="Nuclear ubiquitous casein and cyclin-dependent
FT kinase substrate 1"
FT /id="PRO_0000057980"
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:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 243 AA; 27140 MW; 98B5BB2A7F2133C8 CRC64;
MSRPVRNRKV VDYSQFQESD DADEDYGRDS GPPAKKIRSS PREAKNKRRS GKNSQEDSED
SEEKDVKTKK DDSHSAEDSE DEKDDHKSVR QQRQAASKAA SKQREMLLED VGSEEEPEED
DEAPFQEKDS GSDEDFLMED DDDSDYGSSK KKNKKMVKKS KPERKEKKMP KPRLKATVTP
SPVKGKGKVG RPTASKTSKE KTPSPKEEDE EAESPPEKKT SASPPLEKSG DEGSEDEAAS
GED
