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Protein

DNA damage-binding protein 1

Gene

DDB1

Organism
Homo sapiens (Human)
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 SKP2.20 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • cullin family protein binding Source: UniProtKB
  • damaged DNA binding Source: ProtInc
  • DNA binding Source: ProtInc
  • protein binding, bridging Source: UniProtKB
  • protein-containing complex binding Source: UniProtKB
  • WD40-repeat domain binding Source: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi6.3.2.19 2681
ReactomeiR-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-8951664 Neddylation
SIGNORiQ16531
UniPathwayi
UPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
DNA damage-binding protein 1
Alternative name(s):
DDB p127 subunit
DNA damage-binding protein a
Short name:
DDBa
Damage-specific DNA-binding protein 1
HBV X-associated protein 1
Short name:
XAP-1
UV-damaged DNA-binding factor
UV-damaged DNA-binding protein 1
Short name:
UV-DDB 1
XPE-binding factor
Short name:
XPE-BF
Xeroderma pigmentosum group E-complementing protein
Short name:
XPCe
Gene namesi
Name:DDB1
Synonyms:XAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000167986.13
HGNCiHGNC:2717 DDB1
MIMi600045 gene
neXtProtiNX_Q16531

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi316 – 319YLDN → ALAA: Impairs interaction with DDA1. 1 Publication4
Mutagenesisi537E → A: Slightly impairs interaction with CUL4A. 1 Publication1
Mutagenesisi561W → A: Strongly impairs interaction with CUL4A. 1 Publication1
Mutagenesisi840 – 842EAE → AAA: Impairs interaction with AMBRA1, DTL, DET1, DCAF1, DCAF5, DCAF11 and DCAF8. 1 Publication3
Mutagenesisi910 – 913MALY → AAAA: Impairs interaction with AMBRA1, DTL and DCAF5. 1 Publication4
Mutagenesisi953W → A: Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11. 1 Publication1

Organism-specific databases

DisGeNETi1642
OpenTargetsiENSG00000167986
PharmGKBiPA27187

Chemistry databases

ChEMBLiCHEMBL3833061

Polymorphism and mutation databases

BioMutaiDDB1
DMDMi12643730

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000798402 – 1140DNA damage-binding protein 1Add BLAST1139

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei1067N6-acetyllysineCombined sources1
Cross-linki1121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1125PhosphothreonineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ16531
MaxQBiQ16531
PaxDbiQ16531
PeptideAtlasiQ16531
PRIDEiQ16531
ProteomicsDBi60895

PTM databases

iPTMnetiQ16531
PhosphoSitePlusiQ16531
SwissPalmiQ16531

Expressioni

Gene expression databases

BgeeiENSG00000167986 Expressed in 231 organ(s), highest expression level in left adrenal gland
CleanExiHS_DDB1
ExpressionAtlasiQ16531 baseline and differential
GenevisibleiQ16531 HS

Organism-specific databases

HPAiCAB032821
HPA045174
HPA068456

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 (PubMed:22822215). 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. Interaction with SV5 protein V may prevent the recruitment of DCAF proteins to DCX complexes. 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. DCX(DTL) complex interacts with FBXO11; does not ubiquitinate and degradate FBXO11. Interacts with TRPC4AP (PubMed:19966799).30 Publications
(Microbial infection) Interacts with Simian virus 5 protein V.3 Publications
(Microbial infection) Interacts with hepatitis B virus protein HBX; the viral protein contains a short helical motif that competes for the same binding site as the N-terminal helical motif found in endogenous DCAF proteins.2 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108009, 286 interactors
ComplexPortaliCPX-308 UV DNA damage recognition complex DBB1-DBB2
CPX-477 CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant
CPX-648 CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant
CORUMiQ16531
DIPiDIP-430N
IntActiQ16531, 105 interactors
MINTiQ16531
STRINGi9606.ENSP00000301764

Structurei

Secondary structure

11140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ16531
SMRiQ16531
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16531

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 768Interaction with CDT11 PublicationAdd BLAST767
Regioni13 – 356WD repeat beta-propeller AAdd BLAST344
Regioni392 – 708WD repeat beta-propeller B; Interaction with CUL4AAdd BLAST317
Regioni709 – 1043WD repeat beta-propeller CAdd BLAST335
Regioni771 – 1140Interaction with CDT1 and CUL4A1 PublicationAdd BLAST370

Domaini

The core of the protein consists of three WD40 beta-propeller domains.1 Publication

Sequence similaritiesi

Belongs to the DDB1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1897 Eukaryota
ENOG410XPF6 LUCA
GeneTreeiENSGT00530000063396
HOGENOMiHOG000007241
HOVERGENiHBG005460
InParanoidiQ16531
KOiK10610
OMAiGIGIQEH
OrthoDBiEOG091G017I
PhylomeDBiQ16531
TreeFamiTF105840

Family and domain databases

Gene3Di2.130.10.10, 5 hits
InterProiView protein in InterPro
IPR004871 Cleavage/polyA-sp_fac_asu_C
IPR031297 DDB1
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR10644:SF3 PTHR10644:SF3, 1 hit
PfamiView protein in Pfam
PF03178 CPSF_A, 1 hit
SUPFAMiSSF50978 SSF50978, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q16531-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 WPLRSDPNRE TDDTLVLSFV GQTRVLMLNG EEVEETELMG
460 470 480 490 500
FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS QEPKALVSEW KEPQAKNISV
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 EVQDTSGGTT
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 SLVMQNLGET 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):126,968
Last modified:November 1, 1996 - v1
Checksum:i74D082023E3D846D
GO
Isoform 2 (identifier: Q16531-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-759: Missing.

Note: No experimental confirmation available.
Show »
Length:451
Mass (Da):50,611
Checksum:i3288A0DB0A0FE535
GO

Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GY55F5GY55_HUMAN
DNA damage-binding protein 1
DDB1
1,092Annotation score:
F5H198F5H198_HUMAN
DNA damage-binding protein 1
DDB1
162Annotation score:
F5H2L3F5H2L3_HUMAN
DNA damage-binding protein 1
DDB1
165Annotation score:
F5GYG8F5GYG8_HUMAN
DNA damage-binding protein 1
DDB1
109Annotation score:
F5GWI0F5GWI0_HUMAN
DNA damage-binding protein 1
DDB1
139Annotation score:
F5GZY8F5GZY8_HUMAN
DNA damage-binding protein 1
DDB1
146Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti422D → Y in AAA88883 (PubMed:8538642).Curated1
Sequence conflicti533E → G in CAA05770 (Ref. 4) Curated1
Sequence conflicti869A → D in CAA05770 (Ref. 4) Curated1
Sequence conflicti898 – 899EL → DV in AAA88883 (PubMed:8538642).Curated2
Sequence conflicti898 – 899EL → DV in CAA05770 (Ref. 4) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023074427L → F1 PublicationCorresponds to variant dbSNP:rs28720299Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05554071 – 759Missing in isoform 2. 1 PublicationAdd BLAST689

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18299 mRNA Translation: AAC50349.1
L40326 mRNA Translation: AAA62838.1
U32986 mRNA Translation: AAA88883.1
AJ002955 mRNA Translation: CAA05770.1
AK294341 mRNA Translation: BAG57611.1
AK312436 mRNA Translation: BAG35345.1
AY960579 Genomic DNA Translation: AAX44048.1
AP003037 Genomic DNA No translation available.
AP003108 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW73935.1
BC011686 mRNA Translation: AAH11686.1
BC050530 mRNA Translation: AAH50530.1
BC051764 mRNA Translation: AAH51764.1
CCDSiCCDS31576.1 [Q16531-1]
PIRiI38908
RefSeqiNP_001914.3, NM_001923.4 [Q16531-1]
UniGeneiHs.290758

Genome annotation databases

EnsembliENST00000301764; ENSP00000301764; ENSG00000167986 [Q16531-1]
GeneIDi1642
KEGGihsa:1642
UCSCiuc001nrc.6 human [Q16531-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18299 mRNA Translation: AAC50349.1
L40326 mRNA Translation: AAA62838.1
U32986 mRNA Translation: AAA88883.1
AJ002955 mRNA Translation: CAA05770.1
AK294341 mRNA Translation: BAG57611.1
AK312436 mRNA Translation: BAG35345.1
AY960579 Genomic DNA Translation: AAX44048.1
AP003037 Genomic DNA No translation available.
AP003108 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW73935.1
BC011686 mRNA Translation: AAH11686.1
BC050530 mRNA Translation: AAH50530.1
BC051764 mRNA Translation: AAH51764.1
CCDSiCCDS31576.1 [Q16531-1]
PIRiI38908
RefSeqiNP_001914.3, NM_001923.4 [Q16531-1]
UniGeneiHs.290758

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B5LX-ray2.85A/B1-1140[»]
2B5MX-ray2.92A1-1140[»]
2B5NX-ray2.80A/B/C/D391-709[»]
2HYEX-ray3.10A1-1140[»]
3E0CX-ray2.41A1-1140[»]
3EI1X-ray2.80A1-1140[»]
3EI2X-ray2.60A1-1140[»]
3EI3X-ray2.30A1-1140[»]
3EI4X-ray3.30A/C/E1-1140[»]
3I7HX-ray2.90A1-1140[»]
3I7KX-ray2.80A1-1140[»]
3I7LX-ray2.80A1-1140[»]
3I7NX-ray2.80A1-1140[»]
3I7OX-ray2.80A1-1140[»]
3I7PX-ray3.00A1-1140[»]
3I89X-ray3.00A1-1140[»]
3I8CX-ray2.80A1-1140[»]
3I8EX-ray3.40A/B1-1140[»]
4A08X-ray3.00A1-1140[»]
4A09X-ray3.10A1-1140[»]
4A0AX-ray3.60A1-1140[»]
4A0BX-ray3.80A/C1-1140[»]
4A0KX-ray5.93C1-1140[»]
4A0LX-ray7.40A/C1-1140[»]
4A11X-ray3.31A1-1140[»]
4CI1X-ray2.98A1-1140[»]
4CI2X-ray2.95A1-1140[»]
4CI3X-ray3.50A1-1140[»]
4E54X-ray2.85A2-1140[»]
4E5ZX-ray3.22A2-1140[»]
4TZ4X-ray3.01A2-1140[»]
5FQDX-ray2.45A/D1-395[»]
A/D709-1140[»]
5HXBX-ray3.60B/Y1-1140[»]
5JK7X-ray3.49A/B1-1140[»]
5V3OX-ray3.20A1-1140[»]
6BN7X-ray3.50A1-395[»]
A706-1140[»]
6BN8X-ray3.99A1-395[»]
A706-1140[»]
6BN9X-ray4.38A1-395[»]
A706-1140[»]
6BNBX-ray6.34A1-395[»]
A706-1140[»]
6BOYX-ray3.33A1-395[»]
A706-1140[»]
ProteinModelPortaliQ16531
SMRiQ16531
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108009, 286 interactors
ComplexPortaliCPX-308 UV DNA damage recognition complex DBB1-DBB2
CPX-477 CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant
CPX-648 CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant
CORUMiQ16531
DIPiDIP-430N
IntActiQ16531, 105 interactors
MINTiQ16531
STRINGi9606.ENSP00000301764

Chemistry databases

ChEMBLiCHEMBL3833061

PTM databases

iPTMnetiQ16531
PhosphoSitePlusiQ16531
SwissPalmiQ16531

Polymorphism and mutation databases

BioMutaiDDB1
DMDMi12643730

Proteomic databases

EPDiQ16531
MaxQBiQ16531
PaxDbiQ16531
PeptideAtlasiQ16531
PRIDEiQ16531
ProteomicsDBi60895

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301764; ENSP00000301764; ENSG00000167986 [Q16531-1]
GeneIDi1642
KEGGihsa:1642
UCSCiuc001nrc.6 human [Q16531-1]

Organism-specific databases

CTDi1642
DisGeNETi1642
EuPathDBiHostDB:ENSG00000167986.13
GeneCardsiDDB1
H-InvDBiHIX0171380
HGNCiHGNC:2717 DDB1
HPAiCAB032821
HPA045174
HPA068456
MIMi600045 gene
neXtProtiNX_Q16531
OpenTargetsiENSG00000167986
PharmGKBiPA27187
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1897 Eukaryota
ENOG410XPF6 LUCA
GeneTreeiENSGT00530000063396
HOGENOMiHOG000007241
HOVERGENiHBG005460
InParanoidiQ16531
KOiK10610
OMAiGIGIQEH
OrthoDBiEOG091G017I
PhylomeDBiQ16531
TreeFamiTF105840

Enzyme and pathway databases

UniPathwayi
UPA00143

BRENDAi6.3.2.19 2681
ReactomeiR-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-8951664 Neddylation
SIGNORiQ16531

Miscellaneous databases

ChiTaRSiDDB1 human
EvolutionaryTraceiQ16531
GeneWikiiDDB1
GenomeRNAii1642
PROiPR:Q16531
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167986 Expressed in 231 organ(s), highest expression level in left adrenal gland
CleanExiHS_DDB1
ExpressionAtlasiQ16531 baseline and differential
GenevisibleiQ16531 HS

Family and domain databases

Gene3Di2.130.10.10, 5 hits
InterProiView protein in InterPro
IPR004871 Cleavage/polyA-sp_fac_asu_C
IPR031297 DDB1
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR10644:SF3 PTHR10644:SF3, 1 hit
PfamiView protein in Pfam
PF03178 CPSF_A, 1 hit
SUPFAMiSSF50978 SSF50978, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDDB1_HUMAN
AccessioniPrimary (citable) accession number: Q16531
Secondary accession number(s): A6NG77
, B2R648, B4DG00, O15176, Q13289, Q58F96
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1996
Last modified: October 10, 2018
This is version 189 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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