NUCKS_BOVIN
ID NUCKS_BOVIN Reviewed; 243 AA.
AC Q29S11;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1;
GN Name=NUCKS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC113259; AAI13260.1; -; mRNA.
DR RefSeq; NP_001039385.1; NM_001045920.1.
DR AlphaFoldDB; Q29S11; -.
DR STRING; 9913.ENSBTAP00000049804; -.
DR iPTMnet; Q29S11; -.
DR PaxDb; Q29S11; -.
DR PRIDE; Q29S11; -.
DR Ensembl; ENSBTAT00000057198; ENSBTAP00000049804; ENSBTAG00000008001.
DR GeneID; 505585; -.
DR KEGG; bta:505585; -.
DR CTD; 64710; -.
DR VEuPathDB; HostDB:ENSBTAG00000008001; -.
DR VGNC; VGNC:32320; NUCKS1.
DR eggNOG; ENOG502R8NJ; Eukaryota.
DR GeneTree; ENSGT00940000153414; -.
DR HOGENOM; CLU_067355_0_1_1; -.
DR InParanoid; Q29S11; -.
DR OrthoDB; 1605786at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000008001; Expressed in theca cell and 111 other tissues.
DR ExpressionAtlas; Q29S11; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR InterPro; IPR026633; NUCKS1.
DR PANTHER; PTHR15361:SF1; PTHR15361:SF1; 2.
PE 2: Evidence at transcript 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_0000290031"
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:0000250|UniProtKB:Q9H1E3"
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:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
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:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
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:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1E3"
SQ SEQUENCE 243 AA; 27237 MW; A3CDDEB4063B3685 CRC64;
MSRPVRNRKV VDYSQFQESD DADEDYGRDS GPPAKKIRSS PREAKNKRRS GKNSQEDSED
SEEKDVKTKK DDSHSAEDSE DEKEDHKNVR QQRQAASKAA SKQREMLMED VGSEEEQEEE
DEAPFQEKDS GSDEDFLVED DDDSDYGSSK KKNKKMVKKS KPERKEKKMP KPRLKATVTP
SPVKGKGKVG RPTASKASKE KTPSPKEEDE EPESPLEKKA SSSPPPEKSG DEGSEDDAQS
GED
