| UniProt ID | DDB2_HUMAN | |
|---|---|---|
| UniProt AC | Q92466 | |
| Protein Name | DNA damage-binding protein 2 | |
| Gene Name | DDB2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 427 | |
| Subcellular Localization | Nucleus . Accumulates at sites of DNA damage following UV irradiation. | |
| Protein Description | 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.. | |
| Protein Sequence | MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGDNVGNVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAACFSPDGARLLTTDQKSEIRVYSASQWDCPLGLIPHPHRHFQHLTPIKAAWHPRYNLIVVGRYPDPNFKSCTPYELRTIDVFDGNSGKMMCQLYDPESSGISSLNEFNPMGDTLASAMGYHILIWSQEEARTRK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 11 | Ubiquitination | KKRPETQKTSEIVLR CCCCCCCCCCEEEEC | 62.53 | 32015554 | |
| 12 | Phosphorylation | KRPETQKTSEIVLRP CCCCCCCCCEEEECC | 23.05 | 28555341 | |
| 13 | Phosphorylation | RPETQKTSEIVLRPR CCCCCCCCEEEECCC | 32.15 | 28555341 | |
| 24 | Phosphorylation | LRPRNKRSRSPLELE ECCCCCCCCCCCCCC | 38.43 | 29255136 | |
| 26 | Phosphorylation | PRNKRSRSPLELEPE CCCCCCCCCCCCCHH | 34.77 | 19664994 | |
| 35 | Ubiquitination | LELEPEAKKLCAKGS CCCCHHHHHHHHCCC | 44.62 | 23000965 | |
| 36 | Ubiquitination | ELEPEAKKLCAKGSG CCCHHHHHHHHCCCC | 56.71 | 23000965 | |
| 40 | Ubiquitination | EAKKLCAKGSGPSRR HHHHHHHCCCCCCCC | 53.25 | 23000965 | |
| 50 | Phosphorylation | GPSRRCDSDCLWVGL CCCCCCCCCCEEEEC | 33.57 | 21712546 | |
| 106 | Ubiquitination | DSYRILQKAAPFDRR HHHHHHHHHCCCCCC | 42.97 | 33845483 | |
| 116 | Phosphorylation | PFDRRATSLAWHPTH CCCCCCCCEEECCCC | 18.33 | - | |
| 122 | Phosphorylation | TSLAWHPTHPSTVAV CCEEECCCCCCCEEE | 33.27 | - | |
| 123 (in isoform 4) | Ubiquitination | - | 20.82 | 21890473 | |
| 131 | Phosphorylation | PSTVAVGSKGGDIML CCCEEECCCCCCEEE | 22.87 | - | |
| 146 | Ubiquitination | WNFGIKDKPTFIKGI EECCCCCCCCEEEEC | 40.74 | 23000965 | |
| 151 (in isoform 5) | Ubiquitination | - | 40.04 | 21890473 | |
| 151 | Ubiquitination | KDKPTFIKGIGAGGS CCCCCEEEECCCCCC | 40.04 | 23000965 | |
| 151 (in isoform 1) | Ubiquitination | - | 40.04 | 21890473 | |
| 158 | Phosphorylation | KGIGAGGSITGLKFN EECCCCCCEECEEEC | 18.96 | 22210691 | |
| 163 (in isoform 5) | Ubiquitination | - | 44.43 | 21890473 | |
| 163 (in isoform 1) | Ubiquitination | - | 44.43 | 21890473 | |
| 163 | Ubiquitination | GGSITGLKFNPLNTN CCCEECEEECCCCCC | 44.43 | 21906983 | |
| 169 | Phosphorylation | LKFNPLNTNQFYASS EEECCCCCCCEEEEC | 37.77 | 22210691 | |
| 173 (in isoform 2) | Ubiquitination | - | 8.87 | 21890473 | |
| 173 | Phosphorylation | PLNTNQFYASSMEGT CCCCCCEEEECCCCC | 8.87 | 22210691 | |
| 173 | Ubiquitination | PLNTNQFYASSMEGT CCCCCCEEEECCCCC | 8.87 | 23000965 | |
| 187 (in isoform 5) | Ubiquitination | - | 60.38 | 21890473 | |
| 187 (in isoform 1) | Ubiquitination | - | 60.38 | 21890473 | |
| 187 | Sumoylation | TTRLQDFKGNILRVF CCCCHHCCCCEEEEE | 60.38 | - | |
| 187 | Ubiquitination | TTRLQDFKGNILRVF CCCCHHCCCCEEEEE | 60.38 | 23000965 | |
| 187 | Sumoylation | TTRLQDFKGNILRVF CCCCHHCCCCEEEEE | 60.38 | - | |
| 214 (in isoform 4) | Ubiquitination | - | 21.30 | 21890473 | |
| 245 (in isoform 4) | Ubiquitination | - | 6.50 | 21890473 | |
| 278 | Acetylation | DLRQVRGKASFLYSL EHHHHCCCEEEHEEC | 30.23 | 19608861 | |
| 278 (in isoform 1) | Ubiquitination | - | 30.23 | 21890473 | |
| 278 | Ubiquitination | DLRQVRGKASFLYSL EHHHHCCCEEEHEEC | 30.23 | 22817900 | |
| 297 | Phosphorylation | PVNAACFSPDGARLL CCCEEEECCCCCCEE | 23.20 | 23312004 | |
| 298 (in isoform 4) | Ubiquitination | - | 24.65 | 21890473 | |
| 309 | Acetylation | RLLTTDQKSEIRVYS CEECCCCCCCEEEEE | 53.52 | 25953088 | |
| 309 | Malonylation | RLLTTDQKSEIRVYS CEECCCCCCCEEEEE | 53.52 | 26320211 | |
| 309 (in isoform 1) | Ubiquitination | - | 53.52 | 21890473 | |
| 309 | Sumoylation | RLLTTDQKSEIRVYS CEECCCCCCCEEEEE | 53.52 | - | |
| 309 | Ubiquitination | RLLTTDQKSEIRVYS CEECCCCCCCEEEEE | 53.52 | 21906983 | |
| 309 | Sumoylation | RLLTTDQKSEIRVYS CEECCCCCCCEEEEE | 53.52 | - | |
| 338 | Phosphorylation | HRHFQHLTPIKAAWH CCCCCCCCCCCCEEC | 22.35 | 23312004 | |
| 341 | Ubiquitination | FQHLTPIKAAWHPRY CCCCCCCCCEECCCC | 33.00 | - | |
| 362 | Acetylation | RYPDPNFKSCTPYEL CCCCCCCCCCCCCEE | 51.79 | 26051181 | |
| 362 (in isoform 1) | Ubiquitination | - | 51.79 | 21890473 | |
| 362 | Ubiquitination | RYPDPNFKSCTPYEL CCCCCCCCCCCCCEE | 51.79 | 23000965 | |
| 362 | Methylation | RYPDPNFKSCTPYEL CCCCCCCCCCCCCEE | 51.79 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DDB2_HUMAN !! | ||||||
* 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 DDB2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 278740 | Xeroderma pigmentosum complementation group E (XP-E) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-278, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND MASSSPECTROMETRY. | |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND MASSSPECTROMETRY. | |
