DDA1_HUMAN
ID DDA1_HUMAN Reviewed; 102 AA.
AC Q9BW61;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DET1- and DDB1-associated protein 1 {ECO:0000303|PubMed:17452440};
DE AltName: Full=Placenta cross-immune reaction antigen 1 {ECO:0000303|Ref.2};
DE Short=PCIA-1 {ECO:0000303|Ref.2};
GN Name=DDA1 {ECO:0000303|PubMed:17452440, ECO:0000312|HGNC:HGNC:28360};
GN Synonyms=C19orf58 {ECO:0000312|HGNC:HGNC:28360}, PCIA1 {ECO:0000303|Ref.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN A DDD COMPLEX
RP WITH DET1 AND DDB1.
RX PubMed=17452440; DOI=10.1128/mcb.02432-06;
RA Pick E., Lau O.-S., Tsuge T., Menon S., Tong Y., Dohmae N., Plafker S.M.,
RA Deng X.W., Wei N.;
RT "Mammalian DET1 regulates Cul4A Activity and forms stable complexes with E2
RT ubiquitin-conjugating enzymes.";
RL Mol. Cell. Biol. 27:4708-4719(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Deng H.-X., Wei Y.-Q., Zhao X., Yang H.-S., Yang J.-L., Tian L.;
RT "Identification of placenta cross-immune reaction antigen.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=28437394; DOI=10.1038/nchembio.2363;
RA Uehara T., Minoshima Y., Sagane K., Sugi N.H., Mitsuhashi K.O.,
RA Yamamoto N., Kamiyama H., Takahashi K., Kotake Y., Uesugi M., Yokoi A.,
RA Inoue A., Yoshida T., Mabuchi M., Tanaka A., Owa T.;
RT "Selective degradation of splicing factor CAPERalpha by anticancer
RT sulfonamides.";
RL Nat. Chem. Biol. 13:675-680(2017).
RN [13]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=28302793; DOI=10.1126/science.aal3755;
RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y.,
RA Williams N.S., Nijhawan D.;
RT "Anticancer sulfonamides target splicing by inducing RBM39 degradation via
RT recruitment to DCAF15.";
RL Science 356:0-0(2017).
RN [14]
RP ERRATUM OF PUBMED:28302793.
RX PubMed=28546157; DOI=10.1126/science.aan7977;
RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y.,
RA Williams N.S., Nijhawan D.;
RL Science 356:0-0(2017).
RN [15] {ECO:0007744|PDB:6DSZ}
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) OF 1-19 IN COMPLEX WITH DDB1.
RX PubMed=30564455; DOI=10.1038/s41421-018-0064-8;
RA Shabek N., Ruble J., Waston C.J., Garbutt K.C., Hinds T.R., Li T.,
RA Zheng N.;
RT "Structural insights into DDA1 function as a core component of the CRL4-
RT DDB1 ubiquitin ligase.";
RL Cell Discov. 4:67-67(2018).
RN [16]
RP IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=31693891; DOI=10.1016/j.celrep.2019.09.079;
RA Ting T.C., Goralski M., Klein K., Wang B., Kim J., Xie Y., Nijhawan D.;
RT "Aryl sulfonamides degrade RBM39 and RBM23 by recruitment to CRL4-DCAF15.";
RL Cell Rep. 29:1499-1510(2019).
RN [17] {ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V, ECO:0007744|PDB:6Q0W}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH DDB1 AND DCAF15,
RP FUNCTION, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=31686031; DOI=10.1038/s41589-019-0378-3;
RA Faust T.B., Yoon H., Nowak R.P., Donovan K.A., Li Z., Cai Q.,
RA Eleuteri N.A., Zhang T., Gray N.S., Fischer E.S.;
RT "Structural complementarity facilitates E7820-mediated degradation of RBM39
RT by DCAF15.";
RL Nat. Chem. Biol. 16:7-14(2020).
RN [18] {ECO:0007744|PDB:6SJ7, ECO:0007744|PDB:6UD7, ECO:0007744|PDB:6UE5}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-102 IN COMPLEX WITH DDB1 AND
RP DCAF15, STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 2-102 IN
RP COMPLEX WITH DDB1 AND DCAF15, FUNCTION, AND IDENTIFICATION IN THE
RP DCX(DCAF15) COMPLEX.
RX PubMed=31819272; DOI=10.1038/s41589-019-0411-6;
RA Bussiere D.E., Xie L., Srinivas H., Shu W., Burke A., Be C., Zhao J.,
RA Godbole A., King D., Karki R.G., Hornak V., Xu F., Cobb J., Carte N.,
RA Frank A.O., Frommlet A., Graff P., Knapp M., Fazal A., Okram B., Jiang S.,
RA Michellys P.Y., Beckwith R., Voshol H., Wiesmann C., Solomon J.M.,
RA Paulk J.;
RT "Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3
RT ligase complex.";
RL Nat. Chem. Biol. 16:15-23(2020).
RN [19] {ECO:0007744|PDB:6PAI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH DDB1 AND DCAF15, AND
RP IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=31693911; DOI=10.1016/j.str.2019.10.005;
RA Du X., Volkov O.A., Czerwinski R.M., Tan H., Huerta C., Morton E.R.,
RA Rizzi J.P., Wehn P.M., Xu R., Nijhawan D., Wallace E.M.;
RT "Structural basis and kinetic pathway of RBM39 recruitment to DCAF15 by a
RT sulfonamide molecular glue E7820.";
RL Structure 27:1625-1633(2019).
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 (PubMed:17452440, PubMed:28437394, PubMed:28302793,
CC PubMed:31686031, PubMed:31819272). In the DCX complexes, acts as a
CC scaffolding subunit required to stabilize the complex (PubMed:31686031,
CC PubMed:31819272). {ECO:0000269|PubMed:17452440,
CC ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31819272}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:17452440, ECO:0000269|PubMed:28302793}.
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 (PubMed:28437394, PubMed:28302793,
CC PubMed:31693891, PubMed:31686031, PubMed:31819272, PubMed:31693911).
CC Component of the DCX(DCAF15) complex, also named CLR4(DCAF15) complex,
CC composed of DCAF15, DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and RBX1
CC (PubMed:28437394, PubMed:28302793, PubMed:31693891, PubMed:31686031,
CC PubMed:31819272, PubMed:31693911). 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 (PubMed:17452440). {ECO:0000269|PubMed:17452440,
CC ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31693891,
CC ECO:0000269|PubMed:31693911, ECO:0000269|PubMed:31819272}.
CC -!- INTERACTION:
CC Q9BW61; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2510241, EBI-741181;
CC Q9BW61; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-2510241, EBI-2548702;
CC Q9BW61; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2510241, EBI-11522780;
CC Q9BW61; Q96KN3: PKNOX2; NbExp=5; IntAct=EBI-2510241, EBI-2692890;
CC Q9BW61; O60260-5: PRKN; NbExp=3; IntAct=EBI-2510241, EBI-21251460;
CC Q9BW61; Q8IZV5: RDH10; NbExp=3; IntAct=EBI-2510241, EBI-11913715;
CC -!- SIMILARITY: Belongs to the DDA1 family. {ECO:0000305}.
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DR EMBL; DQ090952; AAZ41375.1; -; mRNA.
DR EMBL; AY563006; AAS66629.1; -; mRNA.
DR EMBL; CH471106; EAW84593.1; -; Genomic_DNA.
DR EMBL; BC000615; AAH00615.1; -; mRNA.
DR CCDS; CCDS12357.1; -.
DR RefSeq; NP_076955.1; NM_024050.5.
DR PDB; 6DSZ; X-ray; 3.09 A; C/D=1-19.
DR PDB; 6PAI; X-ray; 2.90 A; E=1-102.
DR PDB; 6Q0R; X-ray; 2.90 A; E=1-102.
DR PDB; 6Q0V; X-ray; 2.90 A; E=1-102.
DR PDB; 6Q0W; X-ray; 2.90 A; E=1-102.
DR PDB; 6SJ7; EM; 3.54 A; D=2-102.
DR PDB; 6UD7; X-ray; 2.30 A; D=2-102.
DR PDB; 6UE5; X-ray; 2.61 A; D=2-102.
DR PDBsum; 6DSZ; -.
DR PDBsum; 6PAI; -.
DR PDBsum; 6Q0R; -.
DR PDBsum; 6Q0V; -.
DR PDBsum; 6Q0W; -.
DR PDBsum; 6SJ7; -.
DR PDBsum; 6UD7; -.
DR PDBsum; 6UE5; -.
DR AlphaFoldDB; Q9BW61; -.
DR SMR; Q9BW61; -.
DR BioGRID; 122485; 153.
DR DIP; DIP-53527N; -.
DR IntAct; Q9BW61; 75.
DR MINT; Q9BW61; -.
DR STRING; 9606.ENSP00000352928; -.
DR iPTMnet; Q9BW61; -.
DR PhosphoSitePlus; Q9BW61; -.
DR BioMuta; DDA1; -.
DR DMDM; 74733400; -.
DR EPD; Q9BW61; -.
DR jPOST; Q9BW61; -.
DR MassIVE; Q9BW61; -.
DR MaxQB; Q9BW61; -.
DR PaxDb; Q9BW61; -.
DR PeptideAtlas; Q9BW61; -.
DR PRIDE; Q9BW61; -.
DR ProteomicsDB; 79255; -.
DR TopDownProteomics; Q9BW61; -.
DR Antibodypedia; 43757; 178 antibodies from 27 providers.
DR DNASU; 79016; -.
DR Ensembl; ENST00000359866.9; ENSP00000352928.3; ENSG00000130311.11.
DR Ensembl; ENST00000593466.5; ENSP00000473086.1; ENSG00000130311.11.
DR Ensembl; ENST00000596582.1; ENSP00000472171.1; ENSG00000130311.11.
DR GeneID; 79016; -.
DR KEGG; hsa:79016; -.
DR MANE-Select; ENST00000359866.9; ENSP00000352928.3; NM_024050.6; NP_076955.1.
DR UCSC; uc002ngd.4; human.
DR CTD; 79016; -.
DR DisGeNET; 79016; -.
DR GeneCards; DDA1; -.
DR HGNC; HGNC:28360; DDA1.
DR HPA; ENSG00000130311; Low tissue specificity.
DR neXtProt; NX_Q9BW61; -.
DR OpenTargets; ENSG00000130311; -.
DR PharmGKB; PA162383418; -.
DR VEuPathDB; HostDB:ENSG00000130311; -.
DR eggNOG; KOG4816; Eukaryota.
DR GeneTree; ENSGT00390000007029; -.
DR HOGENOM; CLU_144562_1_0_1; -.
DR InParanoid; Q9BW61; -.
DR OMA; MARTDSE; -.
DR OrthoDB; 1521756at2759; -.
DR PhylomeDB; Q9BW61; -.
DR TreeFam; TF323534; -.
DR PathwayCommons; Q9BW61; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9BW61; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 79016; 182 hits in 1086 CRISPR screens.
DR ChiTaRS; DDA1; human.
DR GenomeRNAi; 79016; -.
DR Pharos; Q9BW61; Tbio.
DR PRO; PR:Q9BW61; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BW61; protein.
DR Bgee; ENSG00000130311; Expressed in anterior cingulate cortex and 163 other tissues.
DR ExpressionAtlas; Q9BW61; baseline and differential.
DR Genevisible; Q9BW61; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IMP: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 3D-structure; Acetylation; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..102
FT /note="DET1- and DDB1-associated protein 1"
FT /id="PRO_0000310270"
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:0007744|PubMed:22814378"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:6PAI"
FT TURN 13..18
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6UD7"
SQ SEQUENCE 102 AA; 11835 MW; 94E43C3528589F01 CRC64;
MADFLKGLPV YNKSNFSRFH ADSVCKASNR RPSVYLPTRE YPSEQIIVTE KTNILLRYLH
QQWDKKNAAK KRDQEQVELE GESSAPPRKV ARTDSPDMHE DT
