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EID3_BOVIN
ID   EID3_BOVIN              Reviewed;         379 AA.
AC   A6QPC8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=EP300-interacting inhibitor of differentiation 3;
DE            Short=EID-3;
DE   AltName: Full=EID-1-like inhibitor of differentiation 3;
DE   AltName: Full=Non-structural maintenance of chromosomes element 4 homolog B;
DE            Short=NS4EB;
DE            Short=Non-SMC element 4 homolog B;
GN   Name=EID3 {ECO:0000250|UniProtKB:Q8N140};
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] {ECO:0000312|EMBL:AAI49258.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI49258.1};
RC   TISSUE=Fetal pons {ECO:0000312|EMBL:AAI49258.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tissue-specific component of the SMC5-SMC6 complex, a complex
CC       involved in repair of DNA double-strand breaks by homologous
CC       recombination. The complex may promote sister chromatid homologous
CC       recombination by recruiting the SMC1-SMC3 cohesin complex to double-
CC       strand breaks. The complex is required for telomere maintenance via
CC       recombination and mediates sumoylation of shelterin complex (telosome)
CC       components (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Acts as a repressor of nuclear receptor-dependent
CC       transcription possibly by interfering with CREBBP-dependent
CC       coactivation. May function as a coinhibitor of other CREBBP/EP300-
CC       dependent transcription factors (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC       SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC       or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC       domains of the SMC5:SMC6 heterodimer (By similarity). Homodimer, and
CC       heterodimer with EID2. Interacts with the C-terminal region of CREBBP
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N140}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8N140}. Chromosome, telomere {ECO:0000250}.
CC       Note=May shuttle between nucleus and cytoplasm.
CC       {ECO:0000250|UniProtKB:Q8N140}.
CC   -!- SIMILARITY: Belongs to the NSE4 family. {ECO:0000255}.
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DR   EMBL; BC149257; AAI49258.1; -; mRNA.
DR   RefSeq; NP_001093782.1; NM_001100312.1.
DR   AlphaFoldDB; A6QPC8; -.
DR   SMR; A6QPC8; -.
DR   PRIDE; A6QPC8; -.
DR   GeneID; 507232; -.
DR   KEGG; bta:507232; -.
DR   CTD; 493861; -.
DR   InParanoid; A6QPC8; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   InterPro; IPR027786; Nse4/EID.
DR   InterPro; IPR014854; Nse4_C.
DR   InterPro; IPR029225; Nse4_Nse3-bd.
DR   PANTHER; PTHR16140; PTHR16140; 1.
DR   Pfam; PF15412; Nse4-Nse3_bdg; 1.
DR   Pfam; PF08743; Nse4_C; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Coiled coil; Cytoplasm; DNA damage; DNA recombination;
KW   DNA repair; Nucleus; Reference proteome; Repressor; Telomere;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..379
FT                   /note="EP300-interacting inhibitor of differentiation 3"
FT                   /id="PRO_0000315904"
FT   COILED          32..58
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   379 AA;  42969 MW;  CCFBFE41DC2C8BF0 CRC64;
     MADENGSLRE AGAGGKTRAQ AVVTIPSSAY FLKQVEEEEE VEALKVEVAA ASDTESDTSS
     DDLSCGKADI DPSLLERVDE EKCRSIRKQY RQLIYTVQQN RDDIVNTASD SLTEALEEAN
     VLFDAVSRTR EAALDSQFLV LASDLGKEKA KHLNSDMNFF NQVAFCDFLF IFVGLNWMED
     DERDPLNNCD DNIALSFWET VQKEATSCIS QAETFHFLFG SFKPESAARK PRRNHRRKVQ
     KMEENGVMPT KLRKLDLSGN QEATEKEVER ILGLLQTYFR KYPDTPVSYF EFVIDPNSFS
     RTVENIFYVS FIIRDGFARI RLDQDRLPIL EPININLAGE GNDPSFHSRK QGVISLSLQD
     WKNIVAAFEI SEAMITNSY
 
 
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