DDA1_MOUSE
ID DDA1_MOUSE Reviewed; 102 AA.
AC Q9D9Z5; Q3UDQ1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DET1- and DDB1-associated protein 1 {ECO:0000250|UniProtKB:Q9BW61};
GN Name=Dda1 {ECO:0000312|MGI:MGI:1913748};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Testis, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK006318; BAB24524.1; -; mRNA.
DR EMBL; AK032966; BAC28103.1; -; mRNA.
DR EMBL; AK149980; BAE29210.1; -; mRNA.
DR EMBL; AK168085; BAE40058.1; -; mRNA.
DR EMBL; BC034701; AAH34701.1; -; mRNA.
DR EMBL; BC093523; AAH93523.1; -; mRNA.
DR CCDS; CCDS52584.1; -.
DR RefSeq; NP_001281187.1; NM_001294258.1.
DR RefSeq; NP_001281188.1; NM_001294259.1.
DR RefSeq; NP_079876.1; NM_025600.2.
DR AlphaFoldDB; Q9D9Z5; -.
DR SMR; Q9D9Z5; -.
DR BioGRID; 211519; 11.
DR IntAct; Q9D9Z5; 6.
DR STRING; 10090.ENSMUSP00000121042; -.
DR iPTMnet; Q9D9Z5; -.
DR PhosphoSitePlus; Q9D9Z5; -.
DR EPD; Q9D9Z5; -.
DR jPOST; Q9D9Z5; -.
DR MaxQB; Q9D9Z5; -.
DR PaxDb; Q9D9Z5; -.
DR PeptideAtlas; Q9D9Z5; -.
DR PRIDE; Q9D9Z5; -.
DR ProteomicsDB; 279608; -.
DR Antibodypedia; 43757; 178 antibodies from 27 providers.
DR DNASU; 66498; -.
DR Ensembl; ENSMUST00000124745; ENSMUSP00000121042; ENSMUSG00000074247.
DR GeneID; 66498; -.
DR KEGG; mmu:66498; -.
DR UCSC; uc009mdi.3; mouse.
DR CTD; 79016; -.
DR MGI; MGI:1913748; Dda1.
DR VEuPathDB; HostDB:ENSMUSG00000074247; -.
DR eggNOG; KOG4816; Eukaryota.
DR GeneTree; ENSGT00390000007029; -.
DR HOGENOM; CLU_144562_1_0_1; -.
DR InParanoid; Q9D9Z5; -.
DR OMA; MARTDSE; -.
DR OrthoDB; 1521756at2759; -.
DR PhylomeDB; Q9D9Z5; -.
DR TreeFam; TF323534; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66498; 14 hits in 72 CRISPR screens.
DR ChiTaRS; Dda1; mouse.
DR PRO; PR:Q9D9Z5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D9Z5; protein.
DR Bgee; ENSMUSG00000074247; Expressed in embryonic brain and 259 other tissues.
DR ExpressionAtlas; Q9D9Z5; baseline and differential.
DR Genevisible; Q9D9Z5; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR InterPro; IPR033575; DDA1.
DR InterPro; IPR018276; DDA1_N.
DR PANTHER; PTHR31879; PTHR31879; 1.
DR Pfam; PF10172; DDA1; 1.
PE 1: Evidence at protein level;
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_0000310271"
FT REGION 67..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; 11753 MW; C4393C23A8589F09 CRC64;
MADFLKGLPV YNKSNFSRFH ADSVCKASNR RPSVYLPTRE YPSEQIIVTE KTNILLRYLH
QQWDKKNAAK KRDQEQVEAE GESSAPPRKV ARTDSPDMPE DT
