C1D_CRIGR
ID C1D_CRIGR Reviewed; 141 AA.
AC Q7TSU0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Nuclear nucleic acid-binding protein C1D;
GN Name=C1D;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guang L., Masabumi S., Maru Y.;
RT "Differential display analysis of BCR-ABL-regulated genes.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the recruitment of the RNA exosome complex to
CC pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this
CC function may include MPHOSPH6. Can activate PRKDC not only in the
CC presence of linear DNA but also in the presence of supercoiled DNA. Can
CC induce apoptosis in a p53/TP53 dependent manner. May regulate the
CC TRAX/TSN complex formation. Potentiates transcriptional repression by
CC NR1D1 and THRB (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with NR1D1, THRA, THRB, NCOR1
CC and NCOR2. Interacts with EXOSC10; the interaction probably mediates
CC the association with the nuclear form of the RNA exosome. The
CC homodimeric form interacts with TSNAX following gamma-radiation.
CC Interacts with RAC3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13901}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13901}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q13901}. Note=EXOSC10 is required for nucleolar
CC localization. Colocalizes with TSNAX in the nucleus.
CC {ECO:0000250|UniProtKB:Q13901}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the C1D family. {ECO:0000305}.
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DR EMBL; AY302220; AAP43113.1; -; mRNA.
DR RefSeq; NP_001233713.1; NM_001246784.1.
DR AlphaFoldDB; Q7TSU0; -.
DR SMR; Q7TSU0; -.
DR STRING; 10029.NP_001233713.1; -.
DR GeneID; 100689353; -.
DR KEGG; cge:100689353; -.
DR CTD; 10438; -.
DR eggNOG; KOG4835; Eukaryota.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR011082; Exosome-assoc_fac/DNA_repair.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR PANTHER; PTHR15341; PTHR15341; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Repressor; RNA-binding; rRNA processing; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..141
FT /note="Nuclear nucleic acid-binding protein C1D"
FT /id="PRO_0000316299"
FT REGION 1..100
FT /note="Required for transcriptional repression"
FT /evidence="ECO:0000250"
FT REGION 50..100
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000250"
FT REGION 100..141
FT /note="Interaction with NCOR1 and NCOR2"
FT /evidence="ECO:0000250"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13901"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13901"
SQ SEQUENCE 141 AA; 15945 MW; 0CFB6B47764B6566 CRC64;
MAGGEMNEDY PVEIHESLSA LESSLGAVDD MLKTMMSVSR NELLQKLDPL EQAKVDLVSA
YTLNSMFWVY LATQGVNPKE HPVKQELERI RVYMNRVKEI TDKKKAAKLD RGAASRFVKN
ALWEPKQKNT PNVANKGKSK H