Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA damage-binding protein 1

Gene

Ddb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2 (By similarity).By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-110314 Recognition of DNA damage by PCNA-containing replication complex
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696400 Dual Incision in GG-NER
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-8951664 Neddylation
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
DNA damage-binding protein 1
Alternative name(s):
DDB p127 subunit
Damage-specific DNA-binding protein 1
UV-damaged DNA-binding factor
Gene namesi
Name:Ddb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1202384 Ddb1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002810362 – 1140DNA damage-binding protein 1Add BLAST1139

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei1067N6-acetyllysineBy similarity1
Cross-linki1121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1125PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated by ABL1.1 Publication
Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ3U1J4
MaxQBiQ3U1J4
PaxDbiQ3U1J4
PeptideAtlasiQ3U1J4
PRIDEiQ3U1J4

PTM databases

iPTMnetiQ3U1J4
PhosphoSitePlusiQ3U1J4
SwissPalmiQ3U1J4

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed in pregnant, lactating and involuting mammary gland.1 Publication

Developmental stagei

Ubiquitously expressed at E8.5, E9.5, E12.5, and E19.5.1 Publication

Gene expression databases

BgeeiENSMUSG00000024740
CleanExiMM_DDB1
GenevisibleiQ3U1J4 MM

Interactioni

Subunit structurei

Component of the UV-DDB complex which includes DDB1 and DDB2; the heterodimer dimerizes to give rise to a heterotetramer when bound to damaged DNA. The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit. Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may recruit specific substrate targeting subunits to the DCX complex. These substrate targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC, CRBN, DCAF1, DCAF4, DCAF5, DCAF6, DCAF7, DCAF8, DCAF9, DCAF10, DCAF11, DCAF12, DCAF15, DCAF16, DCAF17, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, COP1, SNRNP40, DCAF1, WDR5, WDR5B, WDR12, WDR26, WDR39, WDR42, WDR53, WDR59, WDR61, WSB1, WSB2, LRWD1 and WDTC1. DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. Interacts with NF2, TSC1 and TSC2. Interacts with AGO1 and AGO2. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts directly with DYRK2 (By similarity). Interacts with TRPC4AP (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi19907461 interactors.
DIPiDIP-56812N
IntActiQ3U1J4 66 interactors.
MINTiQ3U1J4
STRINGi10090.ENSMUSP00000025649

Structurei

3D structure databases

ProteinModelPortaliQ3U1J4
SMRiQ3U1J4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 768Interaction with CDT1By similarityAdd BLAST767
Regioni13 – 356WD repeat beta-propeller ABy similarityAdd BLAST344
Regioni391 – 708WD repeat beta-propeller B; Interaction with CUL4ABy similarityAdd BLAST318
Regioni709 – 1043WD repeat beta-propeller CBy similarityAdd BLAST335
Regioni771 – 1140Interaction with CDT1 and CUL4ABy similarityAdd BLAST370

Domaini

The core of the protein consists of three WD40 beta-propeller domains.By similarity

Sequence similaritiesi

Belongs to the DDB1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1897 Eukaryota
ENOG410XPF6 LUCA
GeneTreeiENSGT00530000063396
HOVERGENiHBG005460
InParanoidiQ3U1J4
KOiK10610
OMAiGIGIQEH
OrthoDBiEOG091G017I
PhylomeDBiQ3U1J4
TreeFamiTF105840

Family and domain databases

Gene3Di2.130.10.105 hits
InterProiView protein in InterPro
IPR004871 Cleavage/polyA-sp_fac_asu_C
IPR031297 DDB1
IPR011047 Quinoprotein_ADH-like_supfam
IPR015943 WD40/YVTN_repeat-like_dom_sf
PANTHERiPTHR10644:SF3 PTHR10644:SF3, 1 hit
PfamiView protein in Pfam
PF03178 CPSF_A, 1 hit
SUPFAMiSSF50998 SSF50998, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U1J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR
60 70 80 90 100
PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI
110 120 130 140 150
ITRAHGNVQD RIGRPSETGI IGIIDPECRM IGLRLYDGLF KVIPLDRDNK
160 170 180 190 200
ELKAFNIRLE ELHVIDVKFL YGCQAPTICF VYQDPQGRHV KTYEVSLREK
210 220 230 240 250
EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH NGDKYLAIAP
260 270 280 290 300
PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
310 320 330 340 350
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM
360 370 380 390 400
ETFTNLGPIV DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA
410 420 430 440 450
SIDLPGIKGL WPLRSDPGRE TDDTLVLSFV GQTRVLMLNG EEVEETELMG
460 470 480 490 500
FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS QEPKALVSEW KEPQGKNISV
510 520 530 540 550
ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC LDITPLGDSN
560 570 580 590 600
GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
610 620 630 640 650
YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF
660 670 680 690 700
ACSDRPTVIY SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT
710 720 730 740 750
IGTIDEIQKL HIRTVPLYES PRKICYQEVS QCFGVLSSRI EVQDSSGGTT
760 770 780 790 800
ALRPSASTQA LSSSVSSSKL FSSSTAPHET SFGEEVEVHN LLIIDQHTFE
810 820 830 840 850
VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE AEPKQGRIVV
860 870 880 890 900
FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
910 920 930 940 950
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN
960 970 980 990 1000
PNWMSAVEIL DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL
1010 1020 1030 1040 1050
GEFVNVFCHG SLVMQNLGEA STPTQGSVLF GTVNGMIGLV TSLSESWYNL
1060 1070 1080 1090 1100
LLDMQNRLNK VIKSVGKIEH SFWRSFHTER KTEPATGFID GDLIESFLDI
1110 1120 1130 1140
SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH
Length:1,140
Mass (Da):126,853
Last modified:March 20, 2007 - v2
Checksum:i9799298D52E60AE4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40E → K in AAD42230 (Ref. 2) Curated1
Sequence conflicti297L → P in AAD42230 (Ref. 2) Curated1
Sequence conflicti600H → R in AAD42230 (Ref. 2) Curated1
Sequence conflicti601Y → C in BAE32502 (PubMed:16141072).Curated1
Sequence conflicti689D → N in BAE27231 (PubMed:16141072).Curated1
Sequence conflicti715V → D in BAE32502 (PubMed:16141072).Curated1
Sequence conflicti795D → G in BAE32502 (PubMed:16141072).Curated1
Sequence conflicti845Q → L in BAE32502 (PubMed:16141072).Curated1
Sequence conflicti979K → R in BAE33503 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026432 mRNA Translation: BAA84699.1
AF159853 mRNA Translation: AAD42230.1
AK146522 mRNA Translation: BAE27231.1
AK152228 mRNA Translation: BAE31055.1
AK154303 mRNA Translation: BAE32502.1
AK155020 mRNA Translation: BAE32993.1
AK155920 mRNA Translation: BAE33503.1
AK157491 mRNA Translation: BAE34102.1
BC002210 mRNA Translation: AAH02210.1
BC009661 mRNA Translation: AAH09661.1
CCDSiCCDS37915.1
PIRiJC7152
RefSeqiNP_056550.1, NM_015735.1
UniGeneiMm.289915
Mm.466856

Genome annotation databases

EnsembliENSMUST00000025649; ENSMUSP00000025649; ENSMUSG00000024740
GeneIDi13194
KEGGimmu:13194
UCSCiuc008gqm.1 mouse

Similar proteinsi

Entry informationi

Entry nameiDDB1_MOUSE
AccessioniPrimary (citable) accession number: Q3U1J4
Secondary accession number(s): Q3U4D0
, Q3U8G3, Q3UJC4, Q99LV3, Q9QYK0, Q9WV39
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 25, 2018
This is version 118 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome