Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
DDB2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DDB2 Required for DNA repair. Binds to DDB1 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 the substrate recognition module for the DCX (DDB1- CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4- ROC1 complex 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. The DDB1-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. Isoform D1 and isoform D2 inhibit UV-damaged DNA repair. Component of the UV-DDB complex which includes DDB1 and DDB2. The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit. Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4- ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1), which includes CUL4A or CUL4B, DDB1, DDB2 and RBX1. DDB2 may function as the substrate recognition module within this complex. The DDB1- CUL4-ROC1 complex may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. A large number of other DCX complexes may also exist in which an alternate substrate targeting subunit replaces DDB2. These targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Isoform D1 and isoform D2 do not interact with DDB1. Expression is induced in response to treatment with IR or UV and this requires p53/TP53 activity. Ubiquitously expressed; with highest levels in corneal endothelium and lowest levels in brain. Isoform D1 is highly expressed in brain and heart. Isoform D2, isoform D3 and isoform D4 are weakly expressed. Belongs to the WD repeat DDB2/WDR76 family. 5 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Cellular Component: nucleoplasm; protein complex
Molecular Function: protein binding; DNA binding; ubiquitin-protein ligase activity; damaged DNA binding
Biological Process: protein autoubiquitination; protein polyubiquitination; nucleotide-excision repair; pyrimidine dimer repair; nucleotide-excision repair, DNA damage removal; DNA repair; response to UV
Reference #:  Q92466 (UniProtKB)
Alt. Names/Synonyms: damage-specific DNA binding protein 2, 48kDa; Damage-specific DNA-binding protein 2; DDB p48 subunit; DDB2; DDBb; DNA damage-binding protein 2; FLJ34321; UV-damaged DNA-binding protein 2; UV-DDB 2; UV-DDB2; xeroderma pigmentosum group E protein
Gene Symbols: DDB2
Molecular weight: 47,864 Da
Basal Isoelectric point: 9.56  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DDB2

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 12 S24-p LRPRNKRsRsPLELE
0 25 S26-p PRNKRsRsPLELEPE
0 1 S50-p GPSRRCDsDCLWVGL
0 1 S116-p PFDRRATsLAWHPtH
0 1 T122-p TsLAWHPtHPSTVAV
0 1 S131-p PSTVAVGsKGGDIML
0 4 K151-ub KDKPTFIkGIGAGGS
0 1 K163 GGSITGLKFNPLNTN
0 1 K163-ub GGSITGLkFNPLNTN
0 2 K187-ub TTRLQDFkGNILRVF
0 1 K278-ac DLRQVRGkASFLYSL
0 1 K278-ub DLRQVRGkASFLYSL
0 1 K309-ac RLLTTDQkSEIRVYS
0 1 K309-ub RLLTTDQkSEIRVYS
0 2 K362-ub RYPDPNFkSCTPYEL
  mouse

 
R24 VLLRSKSRRGPQELE
G26 LRSKSRRGPQELEPE
S50 VSSRTCESCCLLAEL
S116 PFDRRTTSLAWHPTH
T122 TSLAWHPTHPSTLAV
S131 PSTLAVGSKGGDIMI
K151 KDKPIFLKGIGAGGS
K163-ac GGSITGLkFNHLNTN
K163 GGSITGLKFNHLNTN
K187 TTRLQDFKGNILRVY
K278 DLRQIKGKDSFLYSL
K278 DLRQIKGKDSFLYSL
N309 RLLTTDQNNEIRVYS
N309 RLLTTDQNNEIRVYS
K362 RYPDPNLKSCVPYEL
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.