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DDA1_PONAB
ID   DDA1_PONAB              Reviewed;         102 AA.
AC   Q5RD86;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=DET1- and DDB1-associated protein 1 {ECO:0000250|UniProtKB:Q9BW61};
GN   Name=DDA1 {ECO:0000250|UniProtKB:Q9BW61};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a component of numerous distinct DCX (DDB1-CUL4-
CC       X-box) E3 ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. In the DCX complexes, acts as a scaffolding subunit required
CC       to stabilize the complex. {ECO:0000250|UniProtKB:Q9BW61}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9BW61}.
CC   -!- SUBUNIT: Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC       protein ligase complexes which consist of a core of DDB1, cullin-4
CC       (CUL4A or CUL4B), DDA1 and RBX1. Component of the DCX(DCAF15) complex,
CC       also named CLR4(DCAF15) complex, composed of DCAF15, DDB1, cullin-4
CC       (CUL4A or CUL4B), DDA1 and RBX1. Part of the DDD core complex
CC       containing DET1, DDA1 and DDB1; the DDD core complex recruits a
CC       specific UBE2E enzyme, such as UBE2E1, UBE2E2 UBE2E3, to form specific
CC       DDD-E2 complexes. {ECO:0000250|UniProtKB:Q9BW61}.
CC   -!- SIMILARITY: Belongs to the DDA1 family. {ECO:0000305}.
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DR   EMBL; CR858030; CAH90271.1; -; mRNA.
DR   RefSeq; NP_001125121.1; NM_001131649.1.
DR   AlphaFoldDB; Q5RD86; -.
DR   SMR; Q5RD86; -.
DR   STRING; 9601.ENSPPYP00000010881; -.
DR   GeneID; 100172004; -.
DR   KEGG; pon:100172004; -.
DR   CTD; 79016; -.
DR   eggNOG; KOG4816; Eukaryota.
DR   HOGENOM; CLU_144562_1_0_1; -.
DR   InParanoid; Q5RD86; -.
DR   OMA; MARTDSE; -.
DR   OrthoDB; 1521756at2759; -.
DR   TreeFam; TF323534; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Chromosome 19.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR033575; DDA1.
DR   InterPro; IPR018276; DDA1_N.
DR   PANTHER; PTHR31879; PTHR31879; 1.
DR   Pfam; PF10172; DDA1; 1.
PE   3: Inferred from homology;
KW   Acetylation; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
FT   CHAIN           2..102
FT                   /note="DET1- and DDB1-associated protein 1"
FT                   /id="PRO_0000310272"
FT   REGION          66..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
SQ   SEQUENCE   102 AA;  11835 MW;  94E43C3528589F01 CRC64;
     MADFLKGLPV YNKSNFSRFH ADSVCKASNR RPSVYLPTRE YPSEQIIVTE KTNILLRYLH
     QQWDKKNAAK KRDQEQVELE GESSAPPRKV ARTDSPDMHE DT
 
 
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