DDB1_MOUSE - dbPTM
DDB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDB1_MOUSE
UniProt AC Q3U1J4
Protein Name DNA damage-binding protein 1
Gene Name Ddb1
Organism Mus musculus (Mouse).
Sequence Length 1140
Subcellular Localization Cytoplasm. Nucleus. Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (By similarity)..
Protein Description 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 (By similarity)..
Protein Sequence MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPGRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQGKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGLSPLCAIGLWTDISARILKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDSSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGEASTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Oxidation-------MSYNYVVT
-------CCCEEEEE		42.0617203969
2Phosphorylation------MSYNYVVTA
------CCCEEEEEC		33.1323684622
2Acetylation------MSYNYVVTA
------CCCEEEEEC		33.13-
8PhosphorylationMSYNYVVTAQKPTAV
CCCEEEEECCCCCEE		17.2117203969
70UbiquitinationVMELFRPKGESKDLL
EEECCCCCCCCCCEE		71.6822790023
92UbiquitinationNACILEYKQSGESID
CEEEEEEHHCCCCEE		28.72-
116PhosphorylationQDRIGRPSETGIIGI
HHCCCCCCCCCEEEE		46.5624759943
118PhosphorylationRIGRPSETGIIGIID
CCCCCCCCCEEEEEC		37.7123984901
128S-nitrosocysteineIGIIDPECRMIGLRL
EEEECHHHCEECEEE		4.33-
128S-nitrosylationIGIIDPECRMIGLRL
EEEECHHHCEECEEE		4.3320925432
141AcetylationRLYDGLFKVIPLDRD
EECCCEEEEEECCCC		44.2722826441
141UbiquitinationRLYDGLFKVIPLDRD
EECCCEEEEEECCCC		44.2722790023
153UbiquitinationDRDNKELKAFNIRLE
CCCCCEEEEEEEEEE		52.6127667366
191UbiquitinationDPQGRHVKTYEVSLR
CCCCCEEEEEEEEEC		38.9822790023
192PhosphorylationPQGRHVKTYEVSLRE
CCCCEEEEEEEEECH		24.6725367039
193PhosphorylationQGRHVKTYEVSLREK
CCCEEEEEEEEECHH		14.4925367039
196PhosphorylationHVKTYEVSLREKEFN
EEEEEEEEECHHHHC		15.1225367039
203UbiquitinationSLREKEFNKGPWKQE
EECHHHHCCCCCCCC		49.8427667366
204UbiquitinationLREKEFNKGPWKQEN
ECHHHHCCCCCCCCC		72.2222790023
254UbiquitinationAIAPPIIKQSTIVCH
EECCCEECCCEEEEE		38.6322790023
298AcetylationMDGTVTLKDLRVELL
CCCEEEEHHHHHHHH		45.4019856813
378S-nitrosylationGQGQLVTCSGAFKEG
CCCEEEEECCCCCCC		2.4821278135
378S-nitrosocysteineGQGQLVTCSGAFKEG
CCCEEEEECCCCCCC		2.48-
383UbiquitinationVTCSGAFKEGSLRII
EEECCCCCCCCEEEE		61.7122790023
480PhosphorylationSASVRLVSQEPKALV
HHEEEECCCCCCHHH		33.1623737553
491UbiquitinationKALVSEWKEPQGKNI
CHHHCCCCCCCCCCE		56.3022790023
570UbiquitinationDISARILKLPSFELL
CHHHHHHCCCCHHHH		56.8522790023
628UbiquitinationGLLSDRKKVTLGTQP
CCCCCCCCEECCCCC		41.1522790023
630PhosphorylationLSDRKKVTLGTQPTV
CCCCCCEECCCCCCH		28.4928059163
633PhosphorylationRKKVTLGTQPTVLRT
CCCEECCCCCCHHHH		34.1927180971
636PhosphorylationVTLGTQPTVLRTFRS
EECCCCCCHHHHCCC		23.5028059163
643PhosphorylationTVLRTFRSLSTTNVF
CHHHHCCCCCCCCEE		23.6026643407
645PhosphorylationLRTFRSLSTTNVFAC
HHHCCCCCCCCEEEE		34.1426643407
646PhosphorylationRTFRSLSTTNVFACS
HHCCCCCCCCEEEEC		27.9026643407
647PhosphorylationTFRSLSTTNVFACSD
HCCCCCCCCEEEECC		26.4723984901
653PhosphorylationTTNVFACSDRPTVIY
CCCEEEECCCCEEEE		32.9725367039
657PhosphorylationFACSDRPTVIYSSNH
EEECCCCEEEECCCC		22.0425367039
660PhosphorylationSDRPTVIYSSNHKLV
CCCCEEEECCCCEEE		11.1725367039
661PhosphorylationDRPTVIYSSNHKLVF
CCCEEEECCCCEEEE		17.3425367039
662PhosphorylationRPTVIYSSNHKLVFS
CCEEEECCCCEEEEE		26.4425367039
718PhosphorylationHIRTVPLYESPRKIC
EEEECCCCCCCHHHH		14.3219854140
720PhosphorylationRTVPLYESPRKICYQ
EECCCCCCCHHHHHH		19.2228066266
745PhosphorylationSRIEVQDSSGGTTAL
CCEEEECCCCCCEEE		17.5025521595
746PhosphorylationRIEVQDSSGGTTALR
CEEEECCCCCCEEEC		49.9129472430
749PhosphorylationVQDSSGGTTALRPSA
EECCCCCCEEECCCH		16.6629472430
750PhosphorylationQDSSGGTTALRPSAS
ECCCCCCEEECCCHH		27.2829472430
755PhosphorylationGTTALRPSASTQALS
CCEEECCCHHHHHHH		28.5525293948
757PhosphorylationTALRPSASTQALSSS
EEECCCHHHHHHHCC		25.9517242355
758PhosphorylationALRPSASTQALSSSV
EECCCHHHHHHHCCC		19.9917242355
762PhosphorylationSASTQALSSSVSSSK
CHHHHHHHCCCCCHH		24.4723984901
763PhosphorylationASTQALSSSVSSSKL
HHHHHHHCCCCCHHH		35.2923984901
764PhosphorylationSTQALSSSVSSSKLF
HHHHHHCCCCCHHHC		23.7323984901
766PhosphorylationQALSSSVSSSKLFSS
HHHHCCCCCHHHCCC		30.7317242355
767PhosphorylationALSSSVSSSKLFSSS
HHHCCCCCHHHCCCC		29.3617242355
768PhosphorylationLSSSVSSSKLFSSST
HHCCCCCHHHCCCCC		26.3523984901
823UbiquitinationLVSCKLGKDPNTYFI
HHHHHCCCCCCCEEE		79.1722790023
857UbiquitinationVFQYSDGKLQTVAEK
EEEECCCCEEEEEEH		42.2722790023
864UbiquitinationKLQTVAEKEVKGAVY
CEEEEEEHHHCCCEE		59.0622790023
876UbiquitinationAVYSMVEFNGKLLAS
CEEEEEEECCEEEEE		11.2627667366
897AcetylationLYEWTTEKELRTECN
EEECCCHHHHHHHCC		61.0223954790
897UbiquitinationLYEWTTEKELRTECN
EEECCCHHHHHHHCC		61.02-
917UbiquitinationMALYLKTKGDFILVG
EEEEEECCCCEEEHH		55.7022790023
936UbiquitinationSVLLLAYKPMEGNFE
HHHHHHHCCCCCCHH		32.0822790023
1067UbiquitinationKVIKSVGKIEHSFWR
HHHHHHHHHHHHHHH		42.64-
1067AcetylationKVIKSVGKIEHSFWR
HHHHHHHHHHHHHHH		42.64-
1067MalonylationKVIKSVGKIEHSFWR
HHHHHHHHHHHHHHH		42.6426320211
1081UbiquitinationRSFHTERKTEPATGF
HHHCCCCCCCCCCCC		51.51-
1104UbiquitinationFLDISRPKMQEVVAN
HHHCCCHHHHHHHHH		52.70-
1118PhosphorylationNLQYDDGSGMKREAT
HCCCCCCCCCCCEEC		42.58-
1121AcetylationYDDGSGMKREATADD
CCCCCCCCCEECHHH		51.08156815
1121UbiquitinationYDDGSGMKREATADD
CCCCCCCCCEECHHH		51.0822790023
1125PhosphorylationSGMKREATADDLIKV
CCCCCEECHHHHHHH		26.3522006019
1131UbiquitinationATADDLIKVVEELTR
ECHHHHHHHHHHHHC		47.7422790023
1133UbiquitinationADDLIKVVEELTRIH
HHHHHHHHHHHHCCC		3.9327667366
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DDB1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDB1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DDB1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_MOUSETrp53physical
17967871
DDA1_HUMANDDA1physical
20360068
DDB1_HUMANDDB1physical
20360068
DTL_HUMANDTLphysical
20360068
CSN1_HUMANGPS1physical
20360068
TP4AP_HUMANTRPC4APphysical
20360068
CSN7B_HUMANCOPS7Bphysical
20360068
DCAF4_HUMANDCAF4physical
20360068
DCAF8_HUMANDCAF8physical
20360068
DCA10_HUMANDCAF10physical
20360068
CUL4B_HUMANCUL4Bphysical
20360068
DCA12_HUMANDCAF12physical
20360068
RCN1_HUMANRCN1physical
20360068
ERCC8_HUMANERCC8physical
20360068
CRBN_HUMANCRBNphysical
20360068
AMRA1_HUMANAMBRA1physical
20360068
CUL4A_HUMANCUL4Aphysical
20360068
CSN7A_HUMANCOPS7Aphysical
20360068
DCA15_HUMANDCAF15physical
20360068
CSN6_HUMANCOPS6physical
20360068
WDTC1_HUMANWDTC1physical
20360068
CSN5_HUMANCOPS5physical
20360068
DCAF1_HUMANVPRBPphysical
20360068
CSN3_HUMANCOPS3physical
20360068
DCAF6_HUMANDCAF6physical
20360068
SERA_HUMANPHGDHphysical
20360068
DCA16_HUMANDCAF16physical
20360068
PAGE1_HUMANPAGE1physical
20360068
DDB2_HUMANDDB2physical
20360068
CSN4_HUMANCOPS4physical
20360068
NUDC_HUMANNUDCphysical
20360068
DCA11_HUMANDCAF11physical
20360068
DDB2_MOUSEDdb2physical
12107171
DDB2_HUMANDDB2physical
26496610
DSC1_HUMANDSC1physical
26496610
XPF_HUMANERCC4physical
26496610
GMDS_HUMANGMDSphysical
26496610
CSN1_HUMANGPS1physical
26496610
TF3C2_HUMANGTF3C2physical
26496610
IMA1_HUMANKPNA2physical
26496610
K2C6A_HUMANKRT6Aphysical
26496610
PNPH_HUMANPNPphysical
26496610
TRA2B_HUMANTRA2Bphysical
26496610
QCR2_HUMANUQCRC2physical
26496610
CUL4B_HUMANCUL4Bphysical
26496610
CUL4A_HUMANCUL4Aphysical
26496610
CSN3_HUMANCOPS3physical
26496610
PRP18_HUMANPRPF18physical
26496610
NOLC1_HUMANNOLC1physical
26496610
DCAF1_HUMANVPRBPphysical
26496610
RBX1_HUMANRBX1physical
26496610
CSN6_HUMANCOPS6physical
26496610
ZC3H3_HUMANZC3H3physical
26496610
DCA12_HUMANDCAF12physical
26496610
CSN4_HUMANCOPS4physical
26496610
DTL_HUMANDTLphysical
26496610
SIR6_HUMANSIRT6physical
26496610
DCA16_HUMANDCAF16physical
26496610
AMRA1_HUMANAMBRA1physical
26496610
DCAF6_HUMANDCAF6physical
26496610
RM47_HUMANMRPL47physical
26496610
K1522_HUMANKIAA1522physical
26496610
DDA1_HUMANDDA1physical
26496610
DCA10_HUMANDCAF10physical
26496610
DCA11_HUMANDCAF11physical
26496610
TM263_HUMANTMEM263physical
26496610
TOIP2_HUMANTOR1AIP2physical
26496610
IFG15_HUMANTOR1AIP2physical
26496610
ZC3H1_HUMANZFC3H1physical
26496610
HORN_HUMANHRNRphysical
26496610
FILA2_HUMANFLG2physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDB1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND SER-766, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND MASSSPECTROMETRY.

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