DDB1_MOUSE
ID DDB1_MOUSE Reviewed; 1140 AA.
AC Q3U1J4; Q3U4D0; Q3U8G3; Q3UJC4; Q99LV3; Q9QYK0; Q9WV39;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DNA damage-binding protein 1;
DE AltName: Full=DDB p127 subunit;
DE AltName: Full=Damage-specific DNA-binding protein 1;
DE AltName: Full=UV-damaged DNA-binding factor;
GN Name=Ddb1;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Fetal brain;
RX PubMed=10574459; DOI=10.1093/dnares/6.5.319;
RA Seki N., Hayashi A., Hattori A., Kozuma S., Sasaki M., Suzuki Y.,
RA Sugano S., Muramatsu M., Saito T.;
RT "cDNA cloning, tissue expression, and chromosomal assignment of a mouse
RT gene, encoding a 127 kDa UV-damaged DNA binding protein which is defective
RT in XPE cells.";
RL DNA Res. 6:319-322(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Zhang L., Sabatinos S.A., Richardson C.D.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Bone marrow, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [5]
RP FUNCTION, INTERACTION WITH DDB2, AND PHOSPHORYLATION.
RX PubMed=12107171; DOI=10.1074/jbc.m204416200;
RA Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.;
RT "Interaction between UV-damaged DNA binding activity proteins and the c-Abl
RT tyrosine kinase.";
RL J. Biol. Chem. 277:34870-34878(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [8]
RP FUNCTION.
RX PubMed=26431207; DOI=10.1371/journal.pone.0139725;
RA Tong X., Zhang D., Guha A., Arthurs B., Cazares V., Gupta N., Yin L.;
RT "CUL4-DDB1-CDT2 E3 ligase regulates the molecular clock activity by
RT promoting ubiquitination-dependent degradation of the mammalian CRY1.";
RL PLoS ONE 10:E0139725-E0139725(2015).
RN [9]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=27123980; DOI=10.1371/journal.pone.0154263;
RA Hirano A., Nakagawa T., Yoshitane H., Oyama M., Kozuka-Hata H.,
RA Lanjakornsiripan D., Fukada Y.;
RT "USP7 and TDP-43: pleiotropic regulation of cryptochrome protein stability
RT paces the oscillation of the mammalian circadian clock.";
RL PLoS ONE 11:E0154263-E0154263(2016).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28790135; DOI=10.2337/db16-1600;
RA Tong X., Zhang D., Charney N., Jin E., VanDommelen K., Stamper K.,
RA Gupta N., Saldate J., Yin L.;
RT "DDB1-mediated CRY1 degradation promotes FOXO1-driven gluconeogenesis in
RT liver.";
RL Diabetes 66:2571-2582(2017).
CC -!- FUNCTION: Protein, which is both involved in DNA repair and protein
CC ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box)
CC complexes, respectively (PubMed:12107171, PubMed:26431207,
CC PubMed:28790135). Core component of the UV-DDB complex (UV-damaged DNA-
CC binding protein complex), a complex that recognizes UV-induced DNA
CC damage and recruit proteins of the nucleotide excision repair pathway
CC (the NER pathway) to initiate DNA repair (PubMed:12107171). The UV-DDB
CC complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-
CC 4 photoproducts (6-4 PP), apurinic sites and short mismatches (By
CC similarity). Also functions as a component of numerous distinct DCX
CC (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). The functional specificity of the DCX E3
CC ubiquitin-protein ligase complex is determined by the variable
CC substrate recognition component recruited by DDB1 (By similarity).
CC DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-
CC RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites
CC of UV-induced DNA damage (By similarity). The ubiquitination of
CC histones may facilitate their removal from the nucleosome and promote
CC subsequent DNA repair (By similarity). DCX(DDB2) also ubiquitinates
CC XPC, which may enhance DNA-binding by XPC and promote NER (By
CC similarity). DCX(DTL) plays a role in PCNA-dependent polyubiquitination
CC of CDT1 and MDM2-dependent ubiquitination of TP53 in response to
CC radiation-induced DNA damage and during DNA replication (By
CC similarity). DCX(ERCC8) (the CSA complex) plays a role in
CC transcription-coupled repair (TCR) (By similarity). The DDB1-CUL4A-DTL
CC E3 ligase complex regulates the circadian clock function by mediating
CC the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-
CC mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-
CC mediated gluconeogenesis in the liver (PubMed:28790135).
CC {ECO:0000250|UniProtKB:Q16531, ECO:0000269|PubMed:12107171,
CC ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:28790135}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q16531}.
CC -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2;
CC the heterodimer dimerizes to give rise to a heterotetramer when bound
CC to damaged DNA. The UV-DDB complex interacts with monoubiquitinated
CC histone H2A and binds to XPC via the DDB2 subunit. Component of
CC numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes
CC which consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may
CC recruit specific substrate targeting subunits to the DCX complex. These
CC substrate targeting subunits are generally known as DCAF (DDB1- and
CC CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat)
CC proteins. Interacts with AMBRA1, ATG16L1, BTRC, CRBN, DCAF1, DCAF4,
CC DCAF5, DCAF6, DCAF7, DCAF8, DCAF9, DCAF10, DCAF11, DCAF12, DCAF15,
CC DCAF16, DCAF17, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, KATNB1,
CC NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, COP1, SNRNP40,
CC DCAF1, WDR5, WDR5B, WDR12, WDR26, WDR39, WDR42, WDR53, WDR59, WDR61,
CC WSB1, WSB2, LRWD1 and WDTC1. DCX complexes may associate with the COP9
CC signalosome, and this inhibits the E3 ubiquitin-protein ligase activity
CC of the complex. Interacts with NF2, TSC1 and TSC2. Interacts with AGO1
CC and AGO2. Associates with the E3 ligase complex containing DYRK2,
CC EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts directly
CC with DYRK2. DCX(DTL) complex interacts with FBXO11; does not
CC ubiquitinate and degradate FBXO11. Interacts with TRPC4AP (By
CC similarity). Interacts with CRY1 and CRY2 (PubMed:27123980). The DDB1-
CC CUL4A complex interacts with CRY1 (PubMed:27123980).
CC {ECO:0000250|UniProtKB:Q16531, ECO:0000269|PubMed:27123980}.
CC -!- INTERACTION:
CC Q3U1J4; O08785: Clock; NbExp=4; IntAct=EBI-2552275, EBI-79859;
CC Q3U1J4; Q923J1: Trpm7; NbExp=2; IntAct=EBI-2552275, EBI-8010314;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16531}. Nucleus
CC {ECO:0000250|UniProtKB:Q16531}. Note=Primarily cytoplasmic.
CC Translocates to the nucleus following UV irradiation and subsequently
CC accumulates at sites of DNA damage. {ECO:0000250|UniProtKB:Q16531}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in pregnant,
CC lactating and involuting mammary gland. {ECO:0000269|PubMed:10574459,
CC ECO:0000269|PubMed:28790135}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at 8.5 dpc, 9.5 dpc, 12.5
CC dpc, and 19.5 dpc. {ECO:0000269|PubMed:10574459}.
CC -!- DOMAIN: The core of the protein consists of three WD40 beta-propeller
CC domains. {ECO:0000250|UniProtKB:Q16531}.
CC -!- PTM: Phosphorylated by ABL1. {ECO:0000269|PubMed:12107171}.
CC -!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-
CC dependent proteolysis. {ECO:0000250|UniProtKB:Q16531}.
CC -!- PTM: Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and
CC subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein
CC ligase complexes. Deacetylation by SIRT7 impairs the interaction with
CC CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4-X-box) E3
CC ubiquitin-protein ligase complexes. {ECO:0000250|UniProtKB:Q16531}.
CC -!- DISRUPTION PHENOTYPE: Mice showed impaired gluconeogenesis in the
CC liver. {ECO:0000269|PubMed:28790135}.
CC -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR EMBL; AB026432; BAA84699.1; -; mRNA.
DR EMBL; AF159853; AAD42230.1; -; mRNA.
DR EMBL; AK146522; BAE27231.1; -; mRNA.
DR EMBL; AK152228; BAE31055.1; -; mRNA.
DR EMBL; AK154303; BAE32502.1; -; mRNA.
DR EMBL; AK155020; BAE32993.1; -; mRNA.
DR EMBL; AK155920; BAE33503.1; -; mRNA.
DR EMBL; AK157491; BAE34102.1; -; mRNA.
DR EMBL; BC002210; AAH02210.1; -; mRNA.
DR EMBL; BC009661; AAH09661.1; -; mRNA.
DR CCDS; CCDS37915.1; -.
DR PIR; JC7152; JC7152.
DR RefSeq; NP_056550.1; NM_015735.1.
DR AlphaFoldDB; Q3U1J4; -.
DR SMR; Q3U1J4; -.
DR BioGRID; 199074; 187.
DR ComplexPortal; CPX-1122; UV DNA damage recognition complex DBB1-DBB2.
DR ComplexPortal; CPX-650; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant.
DR ComplexPortal; CPX-651; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR DIP; DIP-56812N; -.
DR IntAct; Q3U1J4; 71.
DR MINT; Q3U1J4; -.
DR STRING; 10090.ENSMUSP00000025649; -.
DR iPTMnet; Q3U1J4; -.
DR PhosphoSitePlus; Q3U1J4; -.
DR SwissPalm; Q3U1J4; -.
DR EPD; Q3U1J4; -.
DR jPOST; Q3U1J4; -.
DR MaxQB; Q3U1J4; -.
DR PaxDb; Q3U1J4; -.
DR PeptideAtlas; Q3U1J4; -.
DR PRIDE; Q3U1J4; -.
DR ProteomicsDB; 279610; -.
DR Antibodypedia; 14613; 535 antibodies from 46 providers.
DR Ensembl; ENSMUST00000025649; ENSMUSP00000025649; ENSMUSG00000024740.
DR GeneID; 13194; -.
DR KEGG; mmu:13194; -.
DR UCSC; uc008gqm.1; mouse.
DR CTD; 1642; -.
DR MGI; MGI:1202384; Ddb1.
DR VEuPathDB; HostDB:ENSMUSG00000024740; -.
DR eggNOG; KOG1897; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_002893_0_1_1; -.
DR InParanoid; Q3U1J4; -.
DR OMA; CTEMEHE; -.
DR OrthoDB; 146622at2759; -.
DR PhylomeDB; Q3U1J4; -.
DR TreeFam; TF105840; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 13194; 29 hits in 110 CRISPR screens.
DR ChiTaRS; Ddb1; mouse.
DR PRO; PR:Q3U1J4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3U1J4; protein.
DR Bgee; ENSMUSG00000024740; Expressed in ileal epithelium and 269 other tissues.
DR ExpressionAtlas; Q3U1J4; baseline and differential.
DR Genevisible; Q3U1J4; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0071987; F:WD40-repeat domain binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI.
DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI.
DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; ISO:MGI.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070914; P:UV-damage excision repair; ISO:MGI.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR031297; DDB1.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Acetylation; Biological rhythms; Cytoplasm; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16531"
FT CHAIN 2..1140
FT /note="DNA damage-binding protein 1"
FT /id="PRO_0000281036"
FT REGION 2..768
FT /note="Interaction with CDT1"
FT /evidence="ECO:0000250"
FT REGION 13..356
FT /note="WD repeat beta-propeller A"
FT /evidence="ECO:0000250"
FT REGION 391..708
FT /note="WD repeat beta-propeller B; Interaction with CUL4A"
FT /evidence="ECO:0000250"
FT REGION 709..1043
FT /note="WD repeat beta-propeller C"
FT /evidence="ECO:0000250"
FT REGION 771..1140
FT /note="Interaction with CDT1 and CUL4A"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q16531"
FT MOD_RES 1067
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16531"
FT MOD_RES 1125
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESW0"
FT CROSSLNK 1121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16531"
FT CONFLICT 40
FT /note="E -> K (in Ref. 2; AAD42230)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> P (in Ref. 2; AAD42230)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="H -> R (in Ref. 2; AAD42230)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="Y -> C (in Ref. 3; BAE32502)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="D -> N (in Ref. 3; BAE27231)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="V -> D (in Ref. 3; BAE32502)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="D -> G (in Ref. 3; BAE32502)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="Q -> L (in Ref. 3; BAE32502)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="K -> R (in Ref. 3; BAE33503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1140 AA; 126853 MW; 9799298D52E60AE4 CRC64;
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI
IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF
VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPGRE
TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
QEPKALVSEW KEPQGKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC
LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
PRKICYQEVS QCFGVLSSRI EVQDSSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET
SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGEA
STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH
