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Names & Taxonomy

Uniprot ID:: Q16531
Entry Name:: DDB1_HUMAN
Status:: reviewed
Protein Names:: DNA damage-binding protein 1 (DDB p127 subunit) (DNA damage-binding protein a) (DDBa) (Damage-specific DNA-binding protein 1) (HBV X-associated protein 1) (XAP-1) (UV-damaged DNA-binding factor) (UV-damaged DNA-binding protein 1) (UV-DDB 1) (XPE-binding factor) (XPE-BF) (Xeroderma pigmentosum group E-complementing protein) (XPCe)
Gene Names:: DDB1 XAP1
Gene Names Primary:: DDB1
Organism:: Homo sapiens (Human)

Structure

Length:: 1140
Sequence:: MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPNRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQAKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGLSPLCAIGLWTDISARILKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
Proteomes:: UP000005640

Subcellular location

Subcellular Location:: Cytoplasm. Nucleus. Note=Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage.

Function

Function:: 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.
Pathway:: Protein modification; protein ubiquitination.
Gene Ontology Go:: Cul4-RING E3 ubiquitin ligase complex
Cul4A-RING E3 ubiquitin ligase complex
Cul4B-RING E3 ubiquitin ligase complex
cytoplasm
extracellular exosome
extracellular space
nuclear chromosome, telomeric region
nucleoplasm
nucleus
damaged DNA binding
DNA binding
DNA damage response, detection of DNA damage
DNA repair
global genome nucleotide-excision repair
histone H2A monoubiquitination
interaction with symbiont
negative regulation of apoptotic process
nucleotide-excision repair
nucleotide-excision repair, DNA damage recognition
nucleotide-excision repair, DNA incision
positive regulation by virus of viral protein levels in host cell
positive regulation of viral genome replication
positive regulation of viral release from host cell
proteasome-mediated ubiquitin-dependent protein catabolic process
protein ubiquitination involved in ubiquitin-dependent protein catabolic process
regulation of mitotic cell cycle phase transition
transcription-coupled nucleotide-excision repair
translesion synthesis
UV-damage excision repair
viral process
Wnt signaling pathway
Gene Ontology Biological Process:: DNA damage response, detection of DNA damage
DNA repair
global genome nucleotide-excision repair
histone H2A monoubiquitination
interaction with symbiont
negative regulation of apoptotic process
nucleotide-excision repair
nucleotide-excision repair, DNA damage recognition
nucleotide-excision repair, DNA incision
positive regulation by virus of viral protein levels in host cell
positive regulation of viral genome replication
positive regulation of viral release from host cell
proteasome-mediated ubiquitin-dependent protein catabolic process
protein ubiquitination involved in ubiquitin-dependent protein catabolic process
regulation of mitotic cell cycle phase transition
transcription-coupled nucleotide-excision repair
translesion synthesis
UV-damage excision repair
viral process
Wnt signaling pathway
Gene Ontology Molecular Function:: damaged DNA binding
DNA binding
Gene Ontology Cellular Component:: Cul4A-RING E3 ubiquitin ligase complex
Cul4B-RING E3 ubiquitin ligase complex
Cul4-RING E3 ubiquitin ligase complex
cytoplasm
extracellular exosome
extracellular space
nuclear chromosome, telomeric region
nucleoplasm
nucleus
Keywords:: 3D-structure
Acetylation
Alternative splicing
Complete proteome
Cytoplasm
DNA damage
DNA repair
DNA-binding
Host-virus interaction
Nucleus
Phosphoprotein
Polymorphism
Reference proteome
Repeat
Ubl conjugation
Ubl conjugation pathway
Interacts With:: Q9H9F9; Q13619; Q13620; Q92466; Q9NZJ0; O75530; Q9ULG1; P11207; P42224; Q04725; Q9Y4B6; Q9Y4B6-3; P18045

Names & Taxonomy

Structure

Subcellular location

Function

Publication