Details for: RAD18

Gene ID: 56852

Symbol: RAD18

Ensembl ID: ENSG00000070950

Description: RAD18 E3 ubiquitin protein ligase

Associated with

Other Information

Genular Protein ID: 1090382980

Symbol: RAD18_HUMAN

Name: E3 ubiquitin-protein ligase RAD18

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10884424

Title: Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens.

PubMed ID: 10884424

DOI: 10.1073/pnas.97.14.7927

PubMed ID: 10908344

Title: The human RAD18 gene product interacts with HHR6A and HHR6B.

PubMed ID: 10908344

DOI: 10.1093/nar/28.14.2847

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 15632077

Title: BRCTx is a novel, highly conserved RAD18-interacting protein.

PubMed ID: 15632077

DOI: 10.1128/mcb.25.2.779-788.2005

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17130289

Title: Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination.

PubMed ID: 17130289

DOI: 10.1083/jcb.200606145

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17108083

Title: Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen.

PubMed ID: 17108083

DOI: 10.1073/pnas.0608595103

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18316726

Title: Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination.

PubMed ID: 18316726

DOI: 10.1073/pnas.0800563105

PubMed ID: 18719106

Title: Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks.

PubMed ID: 18719106

DOI: 10.1073/pnas.0805685105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 21659603

Title: A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling.

PubMed ID: 21659603

DOI: 10.1126/science.1203430

PubMed ID: 22036607

Title: RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage.

PubMed ID: 22036607

DOI: 10.1016/j.dnarep.2011.10.012

PubMed ID: 22742833

Title: Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks.

PubMed ID: 22742833

DOI: 10.1016/j.molcel.2012.05.045

PubMed ID: 22681887

Title: Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of UV-induced DNA damage response.

PubMed ID: 22681887

DOI: 10.1016/j.molcel.2012.05.020

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25931565

Title: DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links.

PubMed ID: 25931565

DOI: 10.1126/science.1253671

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 35849344

Title: LncRNA CTBP1-DT-encoded microprotein DDUP sustains DNA damage response signalling to trigger dual DNA repair mechanisms.

PubMed ID: 35849344

DOI: 10.1mw093/nar/gkac611

PubMed ID: 21549715

Title: Symmetry and asymmetry of the RING-RING dimer of Rad18.

PubMed ID: 21549715

DOI: 10.1016/j.jmb.2011.04.051

Sequence Information:

  • Length: 495
  • Mass: 56223
  • Checksum: 744A053A50C65DD7
  • Sequence:
  • MDSLAESRWP PGLAVMKTID DLLRCGICFE YFNIAMIIPQ CSHNYCSLCI RKFLSYKTQC 
    PTCCVTVTEP DLKNNRILDE LVKSLNFARN HLLQFALESP AKSPASSSSK NLAVKVYTPV 
    ASRQSLKQGS RLMDNFLIRE MSGSTSELLI KENKSKFSPQ KEASPAAKTK ETRSVEEIAP 
    DPSEAKRPEP PSTSTLKQVT KVDCPVCGVN IPESHINKHL DSCLSREEKK ESLRSSVHKR 
    KPLPKTVYNL LSDRDLKKKL KEHGLSIQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI 
    VREIENIEKT RMRLEASKLN ESVMVFTKDQ TEKEIDEIHS KYRKKHKSEF QLLVDQARKG 
    YKKIAGMSQK TVTITKEDES TEKLSSVCMG QEDNMTSVTN HFSQSKLDSP EELEPDREED 
    SSSCIDIQEV LSSSESDSCN SSSSDIIRDL LEEEEAWEAS HKNDLQDTEI SPRQNRRTRA 
    AESAEIEPRN KRNRN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.