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Overview

Uniprot IDQ92466
Protein NameDNA damage-binding protein 2
Gene NameDDB2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
40 EAKKLCAKGSGPSRR

Function

Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:12732143, PubMed:15882621, PubMed:16473935, PubMed:18593899, PubMed:32789493, PubMed:9892649). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:12944386, PubMed:14751237, PubMed:16260596, PubMed:32789493). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:12944386, PubMed:16260596). Also functions as the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1) (PubMed:12732143, PubMed:15882621, PubMed:16473935, PubMed:18593899, PubMed:26572825). The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16473935, PubMed:16678110). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16473935, PubMed:16678110). The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR (PubMed:26572825)

Protein Sequence

10 MAPKKRPETQ 20 KTSEIVLRPR 30 NKRSRSPLEL 40 EPEAKKLCAK 50 GSGPSRRCDS 60 DCLWVGLAGP 70 QILPPCRSIV 80 RTLHQHKLGR 90 ASWPSVQQGL 100 QQSFLHTLDS 110 YRILQKAAPF 120 DRRATSLAWH 130 PTHPSTVAVG 140 SKGGDIMLWN 150 FGIKDKPTFI 160 KGIGAGGSIT 170 GLKFNPLNTN 180 QFYASSMEGT 190 TRLQDFKGNI 200 LRVFASSDTI 210 NIWFCSLDVS 220 ASSRMVVTGD 230 NVGNVILLNM 240 DGKELWNLRM 250 HKKKVTHVAL 260 NPCCDWFLAT 270 ASVDQTVKIW 280 DLRQVRGKAS 290 FLYSLPHRHP 300 VNAACFSPDG 310 ARLLTTDQKS 320 EIRVYSASQW 330 DCPLGLIPHP 340 HRHFQHLTPI 350 KAAWHPRYNL 360 IVVGRYPDPN 370 FKSCTPYELR 380 TIDVFDGNSG 390 KMMCQLYDPE 400 SSGISSLNEF 410 NPMGDTLASA 420 MGYHILIWSQ EEARTRK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0080008 Cul4-RING E3 ubiquitin ligase complex
Cellular Component GO:0031464 Cul4A-RING E3 ubiquitin ligase complex
Cellular Component GO:0031465 Cul4B-RING E3 ubiquitin ligase complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0090734 site of DNA damage
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0044877 protein-containing complex binding
Biological Process GO:0034644 cellular response to UV
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006281 DNA repair
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:0051865 protein autoubiquitination
Biological Process GO:0000209 protein polyubiquitination
Biological Process GO:0009411 response to UV
Biological Process GO:0070914 UV-damage excision repair

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.