DDB1
entrez
1642
canonical
uniprot
Q16531
canonical
ensembl
ENSG00000167986
resolver
ensp
ENSP00000301764
resolver
genesymbol
DDB1
resolver
genesymbol_syn
XAP1
resolver
hgnc
HGNC:2717
resolver
uniprot
A6NG77
resolver
uniprot
B2R648
resolver
uniprot
B4DG00
resolver
uniprot
O15176
resolver
uniprot
Q13289
resolver
uniprot
Q58F96
resolver
uniprot_entry
DDB1_HUMAN
resolver
uniprot_sec
A6NG77
resolver
uniprot_sec
B2R648
resolver
uniprot_sec
B4DG00
resolver
uniprot_sec
O15176
resolver
uniprot_sec
Q13289
resolver
uniprot_sec
Q58F96
resolver
amino_acid_sequence
MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPNRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQAKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGLSPLCAIGLWTDISARILKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
uniprot
proteins
disease_involvement
DISEASE: White-Kernohan syndrome (WHIKERS) [MIM:619426]: An autosomal dominant disorder characterized by global developmental delay, variably impaired intellectual development, hypotonia, and characteristic facial features. Some patients may have genitourinary and skeletal abnormalities. {ECO:0000269|PubMed:33743206}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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 recruits 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). 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, PubMed:41565821). 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 dioxygenases, 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). {ECO:0000250|UniProtKB:Q3U1J4, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:16407252, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16940174, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355, ECO:0000269|PubMed:25970626, ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:41565821}.
uniprot
proteins
mass_dalton
126968
uniprot
proteins
mutagenesis
MUTAGEN 316..319; /note="YLDN->ALAA: Impairs interaction with DDA1."; /evidence="ECO:0000269|PubMed:16949367"; MUTAGEN 537; /note="E->A: Slightly impairs interaction with CUL4A."; /evidence="ECO:0000269|PubMed:16413485"; MUTAGEN 561; /note="W->A: Strongly impairs interaction with CUL4A."; /evidence="ECO:0000269|PubMed:16413485"; MUTAGEN 840..842; /note="EAE->AAA: Impairs interaction with AMBRA1, DTL, DET1, DCAF1, DCAF5, DCAF11 and DCAF8."; /evidence="ECO:0000269|PubMed:16949367"; MUTAGEN 910..913; /note="MALY->AAAA: Impairs interaction with AMBRA1, DTL and DCAF5."; /evidence="ECO:0000269|PubMed:16949367"; MUTAGEN 953; /note="W->A: Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11."; /evidence="ECO:0000269|PubMed:16949367
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355, ECO:0000269|PubMed:41565821}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by ABL1. {ECO:0000250|UniProtKB:Q3U1J4}.; PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis. {ECO:0000269|PubMed:11673459}.; 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). {ECO:0000269|PubMed:28886238}.
uniprot
proteins
protein_family
DDB1 family
uniprot
proteins
pubmed
10777491
uniprot
proteins
pubmed
11531405
uniprot
proteins
pubmed
11673459
uniprot
proteins
pubmed
12732143
uniprot
proteins
pubmed
12743284
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14739464
uniprot
proteins
pubmed
15448697
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15882621
uniprot
proteins
pubmed
16223728
uniprot
proteins
pubmed
16227264
uniprot
proteins
pubmed
16260596
uniprot
proteins
pubmed
16407242
uniprot
proteins
pubmed
16407252
uniprot
proteins
pubmed
16413485
uniprot
proteins
pubmed
16473935
uniprot
proteins
pubmed
16482215
uniprot
proteins
pubmed
16527807
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16678110
uniprot
proteins
pubmed
16940174
uniprot
proteins
pubmed
16949367
uniprot
proteins
pubmed
16964240
uniprot
proteins
pubmed
17041588
uniprot
proteins
pubmed
17079684
uniprot
proteins
pubmed
17932509
uniprot
proteins
pubmed
18332868
uniprot
proteins
pubmed
18381890
uniprot
proteins
pubmed
18593899
uniprot
proteins
pubmed
18606781
uniprot
proteins
pubmed
19109893
uniprot
proteins
pubmed
19287380
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19966799
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21468892
uniprot
proteins
pubmed
22118460
uniprot
proteins
pubmed
22822215
uniprot
proteins
pubmed
22935713
uniprot
proteins
pubmed
23478445
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25043012
uniprot
proteins
pubmed
25108355
uniprot
proteins
pubmed
25970626
uniprot
proteins
pubmed
26431207
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28302793
uniprot
proteins
pubmed
28437394
uniprot
proteins
pubmed
28546157
uniprot
proteins
pubmed
28790135
uniprot
proteins
pubmed
28886238
uniprot
proteins
pubmed
30111536
uniprot
proteins
pubmed
30564455
uniprot
proteins
pubmed
31492966
uniprot
proteins
pubmed
31686031
uniprot
proteins
pubmed
31693891
uniprot
proteins
pubmed
31693911
uniprot
proteins
pubmed
31819272
uniprot
proteins
pubmed
32075763
uniprot
proteins
pubmed
32355176
uniprot
proteins
pubmed
33743206
uniprot
proteins
pubmed
34526721
uniprot
proteins
pubmed
35105802
uniprot
proteins
pubmed
35938868
uniprot
proteins
pubmed
38316879
uniprot
proteins
pubmed
41565821
uniprot
proteins
pubmed
7815490
uniprot
proteins
pubmed
8530102
uniprot
proteins
pubmed
8538642
uniprot
proteins
pubmed
9632823
uniprot
proteins
sequence_length
1140
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:18593899}. Nucleus {ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:18593899}. Note=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). {ECO:0000250|UniProtKB:Q3U1J4, ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11673459}.
uniprot
proteins