| UniProt ID | DDB1_HUMAN | |
|---|---|---|
| UniProt AC | Q16531 | |
| Protein Name | DNA damage-binding protein 1 | |
| Gene Name | DDB1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1140 | |
| Subcellular Localization | Cytoplasm. Nucleus. Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage. | |
| 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.. | |
| Protein Sequence | MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPNRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQAKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGLSPLCAIGLWTDISARILKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSYNYVVTA ------CCCEEEEEC | 33.13 | 19413330 | |
| 2 | Phosphorylation | ------MSYNYVVTA ------CCCEEEEEC | 33.13 | 26657352 | |
| 3 | Phosphorylation | -----MSYNYVVTAQ -----CCCEEEEECC | 23.52 | 25627689 | |
| 5 | Phosphorylation | ---MSYNYVVTAQKP ---CCCEEEEECCCC | 6.51 | 20068231 | |
| 8 | Phosphorylation | MSYNYVVTAQKPTAV CCCEEEEECCCCCEE | 17.21 | 26657352 | |
| 42 | Phosphorylation | KNTRLEIYVVTAEGL CCCEEEEEEEECCCC | 4.58 | - | |
| 60 | Ubiquitination | KEVGMYGKIAVMELF EEECCCCEEEEEECC | 15.25 | - | |
| 60 | Ubiquitination | KEVGMYGKIAVMELF EEECCCCEEEEEECC | 15.25 | - | |
| 70 | Ubiquitination | VMELFRPKGESKDLL EEECCCCCCCCCCEE | 71.68 | 23000965 | |
| 73 (in isoform 2) | Phosphorylation | - | 39.89 | 21964256 | |
| 74 | Acetylation | FRPKGESKDLLFILT CCCCCCCCCEEEEEE | 48.36 | 7662439 | |
| 74 | Ubiquitination | FRPKGESKDLLFILT CCCCCCCCCEEEEEE | 48.36 | 23000965 | |
| 74 (in isoform 2) | Phosphorylation | - | 48.36 | 21964256 | |
| 81 | Phosphorylation | KDLLFILTAKYNACI CCEEEEEEECCCEEE | 19.11 | - | |
| 84 | Phosphorylation | LFILTAKYNACILEY EEEEEECCCEEEEEE | 12.91 | 22817900 | |
| 91 | Phosphorylation | YNACILEYKQSGESI CCEEEEEEHHCCCCE | 15.75 | 22817900 | |
| 92 | Ubiquitination | NACILEYKQSGESID CEEEEEEHHCCCCEE | 28.72 | 21906983 | |
| 116 | Phosphorylation | QDRIGRPSETGIIGI HHCCCCCCCCCEEEE | 46.56 | 25850435 | |
| 118 | Phosphorylation | RIGRPSETGIIGIID CCCCCCCCCEEEEEC | 37.71 | 25850435 | |
| 128 | Glutathionylation | IGIIDPECRMIGLRL EEEECHHHCEECEEE | 4.33 | 22555962 | |
| 128 | S-palmitoylation | IGIIDPECRMIGLRL EEEECHHHCEECEEE | 4.33 | 29575903 | |
| 134 | Ubiquitination | ECRMIGLRLYDGLFK HHCEECEEECCCEEE | 26.45 | - | |
| 136 | Phosphorylation | RMIGLRLYDGLFKVI CEECEEECCCEEEEE | 11.09 | 28152594 | |
| 141 | Ubiquitination | RLYDGLFKVIPLDRD EECCCEEEEEECCCC | 44.27 | 23000965 | |
| 147 | Methylation | FKVIPLDRDNKELKA EEEEECCCCCCEEEE | 58.02 | - | |
| 150 | Acetylation | IPLDRDNKELKAFNI EECCCCCCEEEEEEE | 69.57 | 25953088 | |
| 150 | Ubiquitination | IPLDRDNKELKAFNI EECCCCCCEEEEEEE | 69.57 | 23000965 | |
| 153 | Acetylation | DRDNKELKAFNIRLE CCCCCEEEEEEEEEE | 52.61 | 19608861 | |
| 153 | Ubiquitination | DRDNKELKAFNIRLE CCCCCEEEEEEEEEE | 52.61 | 23000965 | |
| 168 | Ubiquitination | ELHVIDVKFLYGCQA EEEEEEEEEEECCCC | 26.38 | 21890473 | |
| 175 | Acetylation | KFLYGCQAPTICFVY EEEECCCCCEEEEEE | 13.79 | - | |
| 175 | Ubiquitination | KFLYGCQAPTICFVY EEEECCCCCEEEEEE | 13.79 | - | |
| 178 | Ubiquitination | YGCQAPTICFVYQDP ECCCCCEEEEEEECC | 1.35 | - | |
| 182 | Phosphorylation | APTICFVYQDPQGRH CCEEEEEEECCCCCE | 6.22 | 25147952 | |
| 191 | 2-Hydroxyisobutyrylation | DPQGRHVKTYEVSLR CCCCCEEEEEEEEEC | 38.98 | - | |
| 191 | Acetylation | DPQGRHVKTYEVSLR CCCCCEEEEEEEEEC | 38.98 | 27452117 | |
| 191 | Ubiquitination | DPQGRHVKTYEVSLR CCCCCEEEEEEEEEC | 38.98 | 23000965 | |
| 192 | Phosphorylation | PQGRHVKTYEVSLRE CCCCEEEEEEEEECH | 24.67 | 28152594 | |
| 193 | Phosphorylation | QGRHVKTYEVSLREK CCCEEEEEEEEECHH | 14.49 | 28152594 | |
| 196 | Phosphorylation | HVKTYEVSLREKEFN EEEEEEEEECHHHHC | 15.12 | - | |
| 200 | Ubiquitination | YEVSLREKEFNKGPW EEEEECHHHHCCCCC | 62.26 | 23000965 | |
| 204 | Ubiquitination | LREKEFNKGPWKQEN ECHHHHCCCCCCCCC | 72.22 | 23000965 | |
| 208 | Ubiquitination | EFNKGPWKQENVEAE HHCCCCCCCCCCEEE | 51.36 | - | |
| 208 | Ubiquitination | EFNKGPWKQENVEAE HHCCCCCCCCCCEEE | 51.36 | 23000965 | |
| 226 | Ubiquitination | VIAVPEPFGGAIIIG EEEECCCCCCEEEEC | 15.63 | - | |
| 228 | Ubiquitination | AVPEPFGGAIIIGQE EECCCCCCEEEECCE | 17.62 | 21890473 | |
| 245 | Phosphorylation | TYHNGDKYLAIAPPI EEECCCEEEEECCCE | 13.20 | 28152594 | |
| 247 | Ubiquitination | HNGDKYLAIAPPIIK ECCCEEEEECCCEEC | 7.88 | 21890473 | |
| 254 | Ubiquitination | AIAPPIIKQSTIVCH EECCCEECCCEEEEE | 38.63 | 21963094 | |
| 287 | Ubiquitination | LFMLLLEKEEQMDGT EEEHHHHHHHCCCCE | 67.53 | 21906983 | |
| 294 | Phosphorylation | KEEQMDGTVTLKDLR HHHCCCCEEEEHHHH | 13.17 | 21406692 | |
| 296 | Phosphorylation | EQMDGTVTLKDLRVE HCCCCEEEEHHHHHH | 28.11 | 21406692 | |
| 298 | 2-Hydroxyisobutyrylation | MDGTVTLKDLRVELL CCCEEEEHHHHHHHH | 45.40 | - | |
| 298 | Ubiquitination | MDGTVTLKDLRVELL CCCEEEEHHHHHHHH | 45.40 | 23000965 | |
| 316 | Phosphorylation | SIAECLTYLDNGVVF CHHHHHHHCCCCEEE | 10.10 | - | |
| 345 | O-linked_Glycosylation | VDSNEQGSYVVAMET ECCCCCCCEEEEEEE | 17.91 | 23301498 | |
| 378 | Acetylation | GQGQLVTCSGAFKEG CCCEEEEECCCCCCC | 2.48 | - | |
| 378 | Ubiquitination | GQGQLVTCSGAFKEG CCCEEEEECCCCCCC | 2.48 | 21890473 | |
| 383 | Acetylation | VTCSGAFKEGSLRII EEECCCCCCCCEEEE | 61.71 | 26051181 | |
| 383 | Ubiquitination | VTCSGAFKEGSLRII EEECCCCCCCCEEEE | 61.71 | 21963094 | |
| 392 | Ubiquitination | GSLRIIRNGIGIHEH CCEEEEECCCCCCCC | 35.71 | - | |
| 408 | Ubiquitination | SIDLPGIKGLWPLRS CCCCCCCCCEEECCC | 54.59 | 21963094 | |
| 415 | Ubiquitination | KGLWPLRSDPNRETD CCEEECCCCCCCCCC | 66.17 | - | |
| 432 | Ubiquitination | LVLSFVGQTRVLMLN EEEEECCCEEEEEEC | 22.34 | 21890473 | |
| 442 | Ubiquitination | VLMLNGEEVEETELM EEEECCEEEEEEEEE | 57.54 | 21890473 | |
| 480 | Phosphorylation | SASVRLVSQEPKALV HHEEEECCCCCCHHH | 33.16 | 22210691 | |
| 484 | Ubiquitination | RLVSQEPKALVSEWK EECCCCCCHHHHCCC | 54.31 | 21906983 | |
| 491 | 2-Hydroxyisobutyrylation | KALVSEWKEPQAKNI CHHHHCCCCCCCCCE | 56.30 | - | |
| 491 | Ubiquitination | KALVSEWKEPQAKNI CHHHHCCCCCCCCCE | 56.30 | 21906983 | |
| 496 | Ubiquitination | EWKEPQAKNISVASC CCCCCCCCCEEEECC | 49.95 | 22817900 | |
| 517 | Phosphorylation | VAVGRALYYLQIHPQ EEECHHHHHEECCHH | 10.93 | 28152594 | |
| 518 | Phosphorylation | AVGRALYYLQIHPQE EECHHHHHEECCHHH | 7.93 | 28152594 | |
| 570 | 2-Hydroxyisobutyrylation | DISARILKLPSFELL CHHHHHHCCCCHHHH | 56.85 | - | |
| 570 | Acetylation | DISARILKLPSFELL CHHHHHHCCCCHHHH | 56.85 | 25953088 | |
| 570 | Ubiquitination | DISARILKLPSFELL CHHHHHHCCCCHHHH | 56.85 | 23000965 | |
| 573 | Phosphorylation | ARILKLPSFELLHKE HHHHCCCCHHHHCHH | 41.61 | 23312004 | |
| 579 | 2-Hydroxyisobutyrylation | PSFELLHKEMLGGEI CCHHHHCHHHHCCCC | 44.80 | - | |
| 579 | Acetylation | PSFELLHKEMLGGEI CCHHHHCHHHHCCCC | 44.80 | 27452117 | |
| 579 | Ubiquitination | PSFELLHKEMLGGEI CCHHHHCHHHHCCCC | 44.80 | 21906983 | |
| 581 | Sulfoxidation | FELLHKEMLGGEIIP HHHHCHHHHCCCCCC | 5.13 | 21406390 | |
| 627 | Ubiquitination | TGLLSDRKKVTLGTQ CCCCCCCCCEECCCC | 57.49 | 24816145 | |
| 628 | 2-Hydroxyisobutyrylation | GLLSDRKKVTLGTQP CCCCCCCCEECCCCC | 41.15 | - | |
| 628 | Ubiquitination | GLLSDRKKVTLGTQP CCCCCCCCEECCCCC | 41.15 | - | |
| 630 | Phosphorylation | LSDRKKVTLGTQPTV CCCCCCEECCCCCCH | 28.49 | 20068231 | |
| 633 | Phosphorylation | RKKVTLGTQPTVLRT CCCEECCCCCCHHHH | 34.19 | 20068231 | |
| 636 | Phosphorylation | VTLGTQPTVLRTFRS EECCCCCCHHHHCCC | 23.50 | 20068231 | |
| 640 | Phosphorylation | TQPTVLRTFRSLSTT CCCCHHHHCCCCCCC | 21.17 | - | |
| 643 | Phosphorylation | TVLRTFRSLSTTNVF CHHHHCCCCCCCCEE | 23.60 | 23663014 | |
| 645 | Phosphorylation | LRTFRSLSTTNVFAC HHHCCCCCCCCEEEE | 34.14 | 27273156 | |
| 646 | Phosphorylation | RTFRSLSTTNVFACS HHCCCCCCCCEEEEC | 27.90 | 23663014 | |
| 647 | Phosphorylation | TFRSLSTTNVFACSD HCCCCCCCCEEEECC | 26.47 | 23663014 | |
| 653 | Phosphorylation | TTNVFACSDRPTVIY CCCEEEECCCCEEEE | 32.97 | 23186163 | |
| 657 | Phosphorylation | FACSDRPTVIYSSNH EEECCCCEEEECCCC | 22.04 | 23186163 | |
| 660 | Phosphorylation | SDRPTVIYSSNHKLV CCCCEEEECCCCEEE | 11.17 | 28152594 | |
| 661 | Phosphorylation | DRPTVIYSSNHKLVF CCCEEEECCCCEEEE | 17.34 | 23186163 | |
| 662 | Phosphorylation | RPTVIYSSNHKLVFS CCEEEECCCCEEEEE | 26.44 | 23186163 | |
| 669 | Phosphorylation | SNHKLVFSNVNLKEV CCCEEEEECCCCCEE | 32.18 | 21712546 | |
| 709 | Ubiquitination | GTIDEIQKLHIRTVP EEHHHHHHCEEEECC | 47.93 | 21963094 | |
| 714 | Phosphorylation | IQKLHIRTVPLYESP HHHCEEEECCCCCCC | 26.35 | 24719451 | |
| 718 | Phosphorylation | HIRTVPLYESPRKIC EEEECCCCCCCHHHH | 14.32 | 21945579 | |
| 720 | Phosphorylation | RTVPLYESPRKICYQ EECCCCCCCHHHHHH | 19.22 | 21945579 | |
| 723 | Ubiquitination | PLYESPRKICYQEVS CCCCCCHHHHHHHHH | 40.28 | 21963094 | |
| 738 | Phosphorylation | QCFGVLSSRIEVQDT HHHCHHHCCEEEEEC | 32.87 | 24719451 | |
| 745 | Phosphorylation | SRIEVQDTSGGTTAL CCEEEEECCCCCEEE | 16.51 | 25693802 | |
| 746 | Phosphorylation | RIEVQDTSGGTTALR CEEEEECCCCCEEEC | 43.44 | 25693802 | |
| 749 | Phosphorylation | VQDTSGGTTALRPSA EEECCCCCEEECCCH | 16.66 | 25693802 | |
| 750 | Phosphorylation | QDTSGGTTALRPSAS EECCCCCEEECCCHH | 27.28 | 27251275 | |
| 755 | Phosphorylation | GTTALRPSASTQALS CCEEECCCHHHHHHH | 28.55 | 20068231 | |
| 757 | Phosphorylation | TALRPSASTQALSSS EEECCCHHHHHHHCC | 25.95 | 30576142 | |
| 758 | Phosphorylation | ALRPSASTQALSSSV EECCCHHHHHHHCCC | 19.99 | 30576142 | |
| 762 | Phosphorylation | SASTQALSSSVSSSK CHHHHHHHCCCCCHH | 24.47 | 20068231 | |
| 763 | Phosphorylation | ASTQALSSSVSSSKL HHHHHHHCCCCCHHH | 35.29 | 30576142 | |
| 764 | Phosphorylation | STQALSSSVSSSKLF HHHHHHCCCCCHHHC | 23.73 | 30576142 | |
| 766 | Phosphorylation | QALSSSVSSSKLFSS HHHHCCCCCHHHCCC | 30.73 | 20068231 | |
| 767 | Phosphorylation | ALSSSVSSSKLFSSS HHHCCCCCHHHCCCC | 29.36 | 30576142 | |
| 768 | Phosphorylation | LSSSVSSSKLFSSST HHCCCCCHHHCCCCC | 26.35 | 20068231 | |
| 780 | Phosphorylation | SSTAPHETSFGEEVE CCCCCCCCCCCCEEE | 26.73 | 22468782 | |
| 781 | Phosphorylation | STAPHETSFGEEVEV CCCCCCCCCCCEEEE | 28.41 | 22468782 | |
| 820 | Ubiquitination | ALSLVSCKLGKDPNT HHHHHHHHCCCCCCC | 53.41 | 22817900 | |
| 823 | Acetylation | LVSCKLGKDPNTYFI HHHHHCCCCCCCEEE | 79.17 | 26051181 | |
| 823 | Ubiquitination | LVSCKLGKDPNTYFI HHHHHCCCCCCCEEE | 79.17 | 21906983 | |
| 828 | Phosphorylation | LGKDPNTYFIVGTAM CCCCCCCEEEEEEEE | 9.65 | - | |
| 844 | Acetylation | YPEEAEPKQGRIVVF CCHHCCCCCCEEEEE | 57.81 | 26051181 | |
| 844 | Ubiquitination | YPEEAEPKQGRIVVF CCHHCCCCCCEEEEE | 57.81 | - | |
| 854 | Phosphorylation | RIVVFQYSDGKLQTV EEEEEEECCCCEEEE | 29.15 | 21712546 | |
| 857 | Ubiquitination | VFQYSDGKLQTVAEK EEEECCCCEEEEEEH | 42.27 | 23000965 | |
| 860 | Phosphorylation | YSDGKLQTVAEKEVK ECCCCEEEEEEHHHC | 31.92 | - | |
| 864 | 2-Hydroxyisobutyrylation | KLQTVAEKEVKGAVY CEEEEEEHHHCCCEE | 59.06 | - | |
| 864 | Acetylation | KLQTVAEKEVKGAVY CEEEEEEHHHCCCEE | 59.06 | 23749302 | |
| 864 | Ubiquitination | KLQTVAEKEVKGAVY CEEEEEEHHHCCCEE | 59.06 | 21906983 | |
| 867 | Ubiquitination | TVAEKEVKGAVYSMV EEEEHHHCCCEEEEE | 42.09 | 33845483 | |
| 871 | Phosphorylation | KEVKGAVYSMVEFNG HHHCCCEEEEEEECC | 7.18 | 25147952 | |
| 886 | Phosphorylation | KLLASINSTVRLYEW EEEEECCCEEEEEEC | 26.98 | 23186163 | |
| 887 | Phosphorylation | LLASINSTVRLYEWT EEEECCCEEEEEECC | 12.73 | 23186163 | |
| 891 | Phosphorylation | INSTVRLYEWTTEKE CCCEEEEEECCCHHH | 10.00 | 28152594 | |
| 897 | Acetylation | LYEWTTEKELRTECN EEECCCHHHHHHHCC | 61.02 | 26051181 | |
| 897 | Ubiquitination | LYEWTTEKELRTECN EEECCCHHHHHHHCC | 61.02 | 21906983 | |
| 901 | Phosphorylation | TTEKELRTECNHYNN CCHHHHHHHCCCCCC | 58.47 | 29759185 | |
| 906 | Phosphorylation | LRTECNHYNNIMALY HHHHCCCCCCEEEEE | 8.91 | 29759185 | |
| 915 | Ubiquitination | NIMALYLKTKGDFIL CEEEEEEECCCCEEE | 34.33 | 21963094 | |
| 917 | 2-Hydroxyisobutyrylation | MALYLKTKGDFILVG EEEEEECCCCEEEHH | 55.70 | - | |
| 917 | Ubiquitination | MALYLKTKGDFILVG EEEEEECCCCEEEHH | 55.70 | 27667366 | |
| 936 | Ubiquitination | SVLLLAYKPMEGNFE HHHHHHHCCCCCCHH | 32.08 | 21963094 | |
| 1063 | Ubiquitination | NRLNKVIKSVGKIEH HHHHHHHHHHHHHHH | 41.92 | 23000965 | |
| 1067 | Acetylation | KVIKSVGKIEHSFWR HHHHHHHHHHHHHHH | 42.64 | 19608861 | |
| 1067 | Malonylation | KVIKSVGKIEHSFWR HHHHHHHHHHHHHHH | 42.64 | 26320211 | |
| 1067 | Ubiquitination | KVIKSVGKIEHSFWR HHHHHHHHHHHHHHH | 42.64 | 23000965 | |
| 1081 | Ubiquitination | RSFHTERKTEPATGF HHHCCCCCCCCCCCC | 51.51 | 21906983 | |
| 1101 | Phosphorylation | IESFLDISRPKMQEV HHHHHHCCCHHHHHH | 42.04 | 25159151 | |
| 1104 | 2-Hydroxyisobutyrylation | FLDISRPKMQEVVAN HHHCCCHHHHHHHHH | 52.70 | - | |
| 1104 | Ubiquitination | FLDISRPKMQEVVAN HHHCCCHHHHHHHHH | 52.70 | 23503661 | |
| 1121 | 2-Hydroxyisobutyrylation | YDDGSGMKREATADD CCCCCCCCCEECHHH | 51.08 | - | |
| 1121 | Acetylation | YDDGSGMKREATADD CCCCCCCCCEECHHH | 51.08 | 156813 | |
| 1121 | Sumoylation | YDDGSGMKREATADD CCCCCCCCCEECHHH | 51.08 | 28112733 | |
| 1121 | Ubiquitination | YDDGSGMKREATADD CCCCCCCCCEECHHH | 51.08 | 27667366 | |
| 1125 | Phosphorylation | SGMKREATADDLIKV CCCCCEECHHHHHHH | 26.35 | 28464451 | |
| 1131 | Ubiquitination | ATADDLIKVVEELTR ECHHHHHHHHHHHHC | 47.74 | 20639865 | |
| 1137 | Phosphorylation | IKVVEELTRIH---- HHHHHHHHCCC---- | 30.75 | 29083192 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DDB1_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 DDB1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| 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-153 AND LYS-1067, AND MASSSPECTROMETRY. | |
