Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Details on Person UniProt:Q16531 DDB1

Class:Id	ReferenceGeneProduct:53490
_chainChangeLog	initiator methionine:1 added on Fri February 6 2015;chain:2-1140 added on Fri February 6 2015;initiator methionine:1 for 53490 removed on Fri Nov 03 2023;initiator methionine: for 53490 added on Fri Nov 03 2023;initiator methionine: for 53490 removed on Fri Aug 15 2025;initiator methionine:1 for 53490 added on Fri Aug 15 2025
_displayName	UniProt:Q16531 DDB1
_timestamp	2026-02-20 23:04:32
chain	initiator methionine:1 chain:2-1140
checksum	74D082023E3D846D
comment	FUNCTION Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:14739464, PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16407252, PubMed:16482215, PubMed:16940174, PubMed:17079684, PubMed:25970626). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). Also functions 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 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355, PubMed:28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355). 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 (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). 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 (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143, PubMed:32355176, PubMed:38316879). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity).PATHWAY Protein modification; protein ubiquitination.SUBUNIT 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:16223728, PubMed:16527807, PubMed:19109893, PubMed:22822215, PubMed:9632823). The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit (PubMed:16473935). 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 (PubMed:11673459, PubMed:12732143, PubMed:15882621, PubMed:16678110, PubMed:18593899, PubMed:28302793, PubMed:28437394, PubMed:28886238, PubMed:31686031, PubMed:31693891, PubMed:32355176, PubMed:31693911, PubMed:31819272). DDB1 may recruit specific substrate targeting subunits to the DCX complex (PubMed:11673459, PubMed:12732143, PubMed:15882621, PubMed:18593899, PubMed:28886238). These substrate targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins (PubMed:16949367, PubMed:16964240, PubMed:17079684, PubMed:18606781, PubMed:19608861, PubMed:19966799). 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 (PubMed:14739464, PubMed:16949367, PubMed:17041588, PubMed:17079684, PubMed:18606781, PubMed:22118460, PubMed:22935713, PubMed:23478445, PubMed:32355176, PubMed:25043012, PubMed:25108355, PubMed:34526721, PubMed:38316879). DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex (PubMed:15448697, PubMed:16260596). Interacts with NF2, TSC1 and TSC2 (PubMed:18332868, PubMed:18381890). Interacts with AGO1 and AGO2 (PubMed:17932509). Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex) (PubMed:19287380). Interacts directly with DYRK2 (PubMed:19287380). DCX(DTL) complex interacts with FBXO11; does not ubiquitinate and degradate FBXO11 (PubMed:19287380). Interacts with TRPC4AP (PubMed:19966799). Interacts with CRY1 and CRY2 (By similarity). The DDB1-CUL4A complex interacts with CRY1 (PubMed:26431207). May also interact with DCUN1D1, DCUN1D2, DCUN1D3 and DCUN1D5 (PubMed:26906416). Component of the DCX(DCAF13) E3 ubiquitin ligase complex, at least composed of CUL4 (CUL4A or CUL4B), DDB1, DCAF13 and RBX1. Interacts with DCAF13 (via WD40 domain) (PubMed:30111536, PubMed:31492966). Interacts with FBXO44 (PubMed:25970626).SUBUNIT (Microbial infection) Interacts with Simian virus 5 protein V.SUBUNIT (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.SUBUNIT (Microbial infection) Interacts with human cytomegalovirus protein UL145; this interaction promotes STAT2 degradation.SUBUNIT (Microbial infection) Interacts with human cytomegalovirus protein RL1; this interaction allows RL1 to recruit the cullin4-RING E3 ubiquitin ligase (CRL4) complex and promote SLN11 degradation.INTERACTION Primarily cytoplasmic (PubMed:10777491, PubMed:11673459). Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459). More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes (By similarity).ALTERNATIVE PRODUCTS The core of the protein consists of three WD40 beta-propeller domains.PTM Phosphorylated by ABL1.PTM Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis.PTM Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238). Deacetylation by SIRT7 impairs the interaction with CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238).DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the DDB1 family.
description	recommendedName: DNA damage-binding protein 1 alternativeName: DDB p127 subunit alternativeName: DNA damage-binding protein a shortName: DDBa alternativeName: Damage-specific DNA-binding protein 1 alternativeName: HBV X-associated protein 1 shortName: XAP-1 alternativeName: UV-damaged DNA-binding factor alternativeName: UV-damaged DNA-binding protein 1 shortName: UV-DDB 1 alternativeName: XPE-binding factor shortName: XPE-BF alternativeName: Xeroderma pigmentosum group E-complementing protein shortName: XPCe
geneName	DDB1 XAP1
identifier	Q16531
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Alternative splicing Biological rhythms Cytoplasm Disease variant DNA damage DNA repair DNA-binding Host-virus interaction Intellectual disability Isopeptide bond Nucleus Phosphoprotein Proteomics identification Reference proteome Repeat Ubl conjugation Ubl conjugation pathway
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	DDB1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8958076] ENSEMBL:ENSG00000167986 DDB1 [Homo sapiens]
secondaryIdentifier	DDB1_HUMAN A6NG77 B2R648 B4DG00 O15176 Q13289 Q58F96
sequenceLength	1140
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:8975526] UniProt:Q16531-1 DDB1 [Homo sapiens] [ReferenceIsoform:8975527] UniProt:Q16531-2 DDB1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:53489] DDB1 [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:8958630] DDB1 [extracellular region] [Homo sapiens]
[Change default viewing format]

No pathways have been reviewed or authored by UniProt:Q16531 DDB1 (53490)