Search Results

Overview

Uniprot IDQ16531
Protein NameDNA damage-binding protein 1
Gene NameDDB1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 NYVVTAQKPTAVNGC
383 VTCSGAFKEGSLRII
723 PLYESPRKICYQEVS

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:14739464, PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16407252, PubMed:16482215, PubMed:16940174, PubMed:17079684, PubMed:25970626). 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:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). Also functions 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 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355, PubMed:28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355). 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 (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). 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 (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143, PubMed:32355176, PubMed:38316879). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity)

Protein Sequence

10 MSYNYVVTAQ 20 KPTAVNGCVT 30 GHFTSAEDLN 40 LLIAKNTRLE 50 IYVVTAEGLR 60 PVKEVGMYGK 70 IAVMELFRPK 80 GESKDLLFIL 90 TAKYNACILE 100 YKQSGESIDI 110 ITRAHGNVQD 120 RIGRPSETGI 130 IGIIDPECRM 140 IGLRLYDGLF 150 KVIPLDRDNK 160 ELKAFNIRLE 170 ELHVIDVKFL 180 YGCQAPTICF 190 VYQDPQGRHV 200 KTYEVSLREK 210 EFNKGPWKQE 220 NVEAEASMVI 230 AVPEPFGGAI 240 IIGQESITYH 250 NGDKYLAIAP 260 PIIKQSTIVC 270 HNRVDPNGSR 280 YLLGDMEGRL 290 FMLLLEKEEQ 300 MDGTVTLKDL 310 RVELLGETSI 320 AECLTYLDNG 330 VVFVGSRLGD 340 SQLVKLNVDS 350 NEQGSYVVAM 360 ETFTNLGPIV 370 DMCVVDLERQ 380 GQGQLVTCSG 390 AFKEGSLRII 400 RNGIGIHEHA 410 SIDLPGIKGL 420 WPLRSDPNRE 430 TDDTLVLSFV 440 GQTRVLMLNG 450 EEVEETELMG 460 FVDDQQTFFC 470 GNVAHQQLIQ 480 ITSASVRLVS 490 QEPKALVSEW 500 KEPQAKNISV 510 ASCNSSQVVV 520 AVGRALYYLQ 530 IHPQELRQIS 540 HTEMEHEVAC 550 LDITPLGDSN 560 GLSPLCAIGL 570 WTDISARILK 580 LPSFELLHKE 590 MLGGEIIPRS 600 ILMTTFESSH 610 YLLCALGDGA 620 LFYFGLNIET 630 GLLSDRKKVT 640 LGTQPTVLRT 650 FRSLSTTNVF 660 ACSDRPTVIY 670 SSNHKLVFSN 680 VNLKEVNYMC 690 PLNSDGYPDS 700 LALANNSTLT 710 IGTIDEIQKL 720 HIRTVPLYES 730 PRKICYQEVS 740 QCFGVLSSRI 750 EVQDTSGGTT 760 ALRPSASTQA 770 LSSSVSSSKL 780 FSSSTAPHET 790 SFGEEVEVHN 800 LLIIDQHTFE 810 VLHAHQFLQN 820 EYALSLVSCK 830 LGKDPNTYFI 840 VGTAMVYPEE 850 AEPKQGRIVV 860 FQYSDGKLQT 870 VAEKEVKGAV 880 YSMVEFNGKL 890 LASINSTVRL 900 YEWTTEKELR 910 TECNHYNNIM 920 ALYLKTKGDF 930 ILVGDLMRSV 940 LLLAYKPMEG 950 NFEEIARDFN 960 PNWMSAVEIL 970 DDDNFLGAEN 980 AFNLFVCQKD 990 SAATTDEERQ 1000 HLQEVGLFHL 1010 GEFVNVFCHG 1020 SLVMQNLGET 1030 STPTQGSVLF 1040 GTVNGMIGLV 1050 TSLSESWYNL 1060 LLDMQNRLNK 1070 VIKSVGKIEH 1080 SFWRSFHTER 1090 KTEPATGFID 1100 GDLIESFLDI 1110 SRPKMQEVVA 1120 NLQYDDGSGM 1130 KREATADDLI 1140 KVVEELTRIH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000781 chromosome, telomeric region
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0160072 ubiquitin ligase complex scaffold activity
Molecular Function GO:0071987 WD40-repeat domain binding
Biological Process GO:0051702 biological process involved in interaction with symbiont
Biological Process GO:0008283 cell population proliferation
Biological Process GO:0034644 cellular response to UV
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006281 DNA repair
Biological Process GO:0044725 epigenetic programming in the zygotic pronuclei
Biological Process GO:0040029 epigenetic regulation of gene expression
Biological Process GO:1904178 negative regulation of adipose tissue development
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:0046726 positive regulation by virus of viral protein levels in host cell
Biological Process GO:0045722 positive regulation of gluconeogenesis
Biological Process GO:0045732 positive regulation of protein catabolic process
Biological Process GO:0045070 positive regulation of viral genome replication
Biological Process GO:0010498 proteasomal protein catabolic process
Biological Process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process GO:0016567 protein ubiquitination
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0010506 regulation of autophagy
Biological Process GO:1901987 regulation of cell cycle phase transition
Biological Process GO:0042127 regulation of cell population proliferation
Biological Process GO:0080135 regulation of cellular response to stress
Biological Process GO:0042752 regulation of circadian rhythm
Biological Process GO:0030174 regulation of DNA-templated DNA replication initiation
Biological Process GO:0045995 regulation of embryonic development
Biological Process GO:0060964 regulation of miRNA-mediated gene silencing
Biological Process GO:1901990 regulation of mitotic cell cycle phase transition
Biological Process GO:1902412 regulation of mitotic cytokinesis
Biological Process GO:0032814 regulation of natural killer cell activation
Biological Process GO:2000036 regulation of stem cell population maintenance
Biological Process GO:0031297 replication fork processing
Biological Process GO:0048511 rhythmic process
Biological Process GO:0007283 spermatogenesis
Biological Process GO:0007056 spindle assembly involved in female meiosis
Biological Process GO:0006511 ubiquitin-dependent protein catabolic process
Biological Process GO:0070914 UV-damage excision repair
Biological Process GO:0019076 viral release from host cell
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:0005737 cytoplasm
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0097602 cullin family protein binding
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0044877 protein-containing complex binding

Reference

[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.