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Protein Page:
DDB1 (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
DDB1 the large subunit of theUV- damaged DNA-binding protein complex (the UV-DDB complex) required for DNA repair. 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 p53 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 p27kip when associated with CUL4 and SKP2. 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 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, DCAF1, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12, DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8, WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2 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. Interacts with Simian virus 5 protein V and the HBV X protein. Interaction with SV5 protein V may prevent the recruitment of DCAF proteins to DCX complexes. Interacts with EIF2C1 and EIF2C2. Associates with the E3 ligase complex containing DYRK2, UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts directly with DYRK2. Belongs to the DDB1 family. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Chromosomal Location of Human Ortholog: 11q12-q13
Cellular Component: nucleoplasm; extracellular space; cytoplasm; nucleus
Molecular Function: protein binding; DNA binding; damaged DNA binding
Biological Process: proteasomal ubiquitin-dependent protein catabolic process; Wnt receptor signaling pathway; viral reproduction; nucleotide-excision repair; protein ubiquitination during ubiquitin-dependent protein catabolic process; nucleotide-excision repair, DNA damage removal; DNA repair
Reference #:  Q16531 (UniProtKB)
Alt. Names/Synonyms: damage-specific DNA binding protein 1, 127kDa; Damage-specific DNA-binding protein 1; DDB p127 subunit; DDB1; DDBa; DNA damage-binding protein 1; DNA damage-binding protein a; HBV X-associated protein 1; UV-damaged DNA-binding factor; UV-damaged DNA-binding protein 1; UV-DDB 1; UV-DDB1; XAP-1; XAP1; Xeroderma pigmentosum group E-complementing protein; XPCe; XPE; XPE-BF; XPE-binding factor
Gene Symbols: DDB1
Molecular weight: 126,968 Da
Basal Isoelectric point: 5.14  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DDB1

Protein Structure Not Found.


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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 1 T8 MSYNYVVTAQKPTAV
0 1 Y42-p KNTRLEIyVVTAEGL
0 3 K70-ub VMELFRPkGESkDLL
0 1 K74-ac FRPkGESkDLLFILT
0 1 Y84-p LFILTAKyNACILEy
0 1 Y91-p yNACILEykQSGESI
0 4 K92-ub NACILEykQSGESID
0 1 S116-p QDRIGRPsETGIIGI
0 4 K141-ub RLYDGLFkVIPLDRD
0 1 K153-ac DRDNKELkAFNIRLE
0 2 K153-ub DRDNKELkAFNIRLE
0 7 K191-ub DPQGRHVkTyEVsLR
0 6 Y193-p QGRHVkTyEVsLREK
0 1 S196-p HVkTyEVsLREKEFN
0 2 K204-ub LREKEFNkGPWKQEN
0 1 K254 AIAPPIIKQSTIVCH
0 4 K287-ub LFMLLLEkEEQMDGt
0 1 T294-p kEEQMDGtVtLkDLR
0 1 T296-p EQMDGtVtLkDLRVE
0 1 K298 MDGtVtLKDLRVELL
0 2 K298-ub MDGtVtLkDLRVELL
0 7 K383-ac VTCSGAFkEGSLRII
0 3 K383 VTCSGAFKEGSLRII
0 1 K484-ub RLVSQEPkALVSEWk
0 2 K491-ub kALVSEWkEPQAKNI
0 2 K570-ub DISARILkLPSFELL
0 3 K579-ub PSFELLHkEMLGGEI
0 1 K628 GLLSDRKKVTLGTQP
0 1 T636-p VTLGTQPtVLRtFRS
0 5 T640-p TQPtVLRtFRSLstT
0 9 S645-p LRtFRSLstTNVFAC
0 2 T646-p RtFRSLstTNVFACS
0 20 Y660-p SDRPTVIySSNHKLV
0 1 S669-p SNHKLVFsNVNLKEV
0 16 Y718-p HIRTVPLyEsPRKIC
0 3 S720-p RTVPLyEsPRKICYQ
0 1 S755-p GTTALRPsASTQALS
0 1 S781-p STAPHETsFGEEVEV
0 20 K823-ub LVSCKLGkDPNTYFI
0 1 S854-p RIVVFQYsDGkLQtV
0 11 K857-ub VFQYsDGkLQtVAEk
0 1 T860-p YsDGkLQtVAEkEVK
0 3 K864-ub kLQtVAEkEVKGAVy
0 2 Y871-p kEVKGAVySMVEFNG
0 1 K897 LYEWTTEKELRTECN
0 4 K897-ub LYEWTTEkELRTECN
0 5 K917-ub MALYLKTkGDFILVG
0 10 K936-ub SVLLLAYkPMEGNFE
0 2 K1067-ac KVIKSVGkIEHSFWR
0 3 K1067-ub KVIKSVGkIEHSFWR
0 11 K1081-ub RSFHTERkTEPATGF
0 1 S1101-p IESFLDIsRPKMQEV
0 2 K1104 FLDIsRPKMQEVVAN
0 1 S1118 NLQYDDGSGMkREAt
0 9 K1121-ac YDDGSGMkREAtADD
0 93 K1121-ub YDDGSGMkREAtADD
0 12 T1125-p SGMkREAtADDLIkV
0 4 K1131-ub AtADDLIkVVEELtR
0 2 T1137-p IkVVEELtRIH____
  mouse

 
T8-p MSYNYVVtAQKPTAV
Y42 KNTRLEIYVVTAEGL
K70-ub VMELFRPkGESKDLL
K74 FRPkGESKDLLFILT
Y84 LFILTAKYNACILEY
Y91 YNACILEYkQSGESI
K92-ub NACILEYkQSGESID
S116 QDRIGRPSETGIIGI
K141-ub RLYDGLFkVIPLDRD
K153 DRDNKELKAFNIRLE
K153 DRDNKELKAFNIRLE
K191-ub DPQGRHVkTYEVSLR
Y193 QGRHVkTYEVSLREK
S196 HVkTYEVSLREKEFN
K204-ub LREKEFNkGPWKQEN
K254-ub AIAPPIIkQSTIVCH
K287 LFMLLLEKEEQMDGT
T294 KEEQMDGTVTLkDLR
T296 EQMDGTVTLkDLRVE
K298-ac MDGTVTLkDLRVELL
K298 MDGTVTLKDLRVELL
K383 VTCSGAFKEGSLRII
K383-ub VTCSGAFkEGSLRII
K484 RLVSQEPKALVSEWk
K491-ub KALVSEWkEPQGKNI
K570-ub DISARILkLPSFELL
K579 PSFELLHKEMLGGEI
K628-ub GLLSDRKkVTLGTQP
T636 VTLGTQPTVLRTFRS
T640 TQPTVLRTFRSLstT
S645-p LRTFRSLstTNVFAC
T646-p RTFRSLstTNVFACS
Y660-p SDRPTVIySSNHKLV
S669 SNHKLVFSNVNLKEV
Y718-p HIRTVPLyESPRKIC
S720 RTVPLyESPRKICYQ
S755 GTTALRPSASTQALS
S781 STAPHETSFGEEVEV
K823-ub LVSCKLGkDPNTYFI
S854 RIVVFQYSDGkLQTV
K857-ub VFQYSDGkLQTVAEk
T860 YSDGkLQTVAEkEVK
K864-ub kLQTVAEkEVKGAVY
Y871 kEVKGAVYSMVEFNG
K897-ac LYEWTTEkELRTECN
K897-ub LYEWTTEkELRTECN
K917-ub MALYLKTkGDFILVG
K936-ub SVLLLAYkPMEGNFE
K1067 KVIKSVGKIEHSFWR
K1067-ub KVIKSVGkIEHSFWR
K1081-ub RSFHTERkTEPATGF
S1101 IESFLDISRPkMQEV
K1104-ub FLDISRPkMQEVVAN
S1118-p NLQYDDGsGMkREAt
K1121-ac YDDGsGMkREAtADD
K1121-ub YDDGsGMkREAtADD
T1125-p sGMkREAtADDLIkV
K1131-ub AtADDLIkVVEELTR
T1137 IkVVEELTRIH____
  rat

 
T8 MSYNYVVTAQKPTAV
Y42 KNTRLEIYVVTAEGL
K70 VMELFRPKGESKDLL
K74 FRPKGESKDLLFILT
Y84 LFILTAKYNACILEY
Y91 YNACILEYKQSGESI
K92 NACILEYKQSGESID
S116 QDRIGRPSETGIIGI
K141 RLYDGLFKVIPLDRD
K153 DRDNKELKAFNIRLE
K153 DRDNKELKAFNIRLE
K191 DPQGRHVKTYEVSLR
Y193 QGRHVKTYEVSLREK
S196 HVKTYEVSLREKEFN
K204 LREKEFNKGPWKQEN
K254 AIAPPIIKQSTIVCH
K287 LFMLLLEKEEQMDGT
T294 KEEQMDGTVTLKDLR
T296 EQMDGTVTLKDLRVE
K298 MDGTVTLKDLRVELL
K298 MDGTVTLKDLRVELL
K383 VTCSGAFKEGSLRII
K383 VTCSGAFKEGSLRII
K484 RLVSQEPKALVSEWK
K491 KALVSEWKEPRAKNI
K570 DISARILKLPSFELL
K579 PSFELLHKEMLGGEI
K628 GLLSDRKKVTLGTQP
T636 VTLGTQPTVLRTFRS
T640 TQPTVLRTFRSLSTT
S645 LRTFRSLSTTNVFAC
T646 RTFRSLSTTNVFACS
Y660 SDRPTVIYSSNHKLV
S669 SNHKLVFSNVNLKEV
Y718 HIRTVPIYESPRKIC
S720 RTVPIYESPRKICYQ
S755 GTTALRPSASTQALS
S781 SAAPHETSFGEEVEV
K823 LVSCKLGKDPNTYFI
S854 RIVVFQYSGGKLQTV
K857 VFQYSGGKLQTVAEK
T860 YSGGKLQTVAEKEVK
K864 KLQTVAEKEVKGAVY
Y871 KEVKGAVYSMVEFNG
K897 LYEWTTEKELRTECN
K897 LYEWTTEKELRTECN
K917 MALYLKTKGDFILVG
K936 SVLLLAYKPMEGNFE
K1067-ac KVIKSVGkIEHSFWR
K1067 KVIKSVGKIEHSFWR
K1081 RSFHTERKTEPATGF
S1101 IESFLDISRPKMQEV
K1104 FLDISRPKMQEVVAN
S1118 NLQYDDGSGMkREAt
K1121 YDDGSGMKREAtADD
K1121-ub YDDGSGMkREAtADD
T1125-p SGMkREAtADDLIKV
K1131 AtADDLIKVVEELTR
T1137 IKVVEELTRIH____
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