Q9NS91 · RAD18_HUMAN

  • Protein
    E3 ubiquitin-protein ligase RAD18
  • Gene
    RAD18
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

149550100150200250300350400450
TypeIDPosition(s)Description
Binding site204Zn2+ (UniProtKB | ChEBI)
Binding site207Zn2+ (UniProtKB | ChEBI)
Binding site219Zn2+ (UniProtKB | ChEBI)
Binding site223Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentnuclear body
Cellular Componentnuclear inclusion body
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentRad6-Rad18 complex
Cellular Componentreplication fork
Cellular Componentsite of double-strand break
Molecular Functiondamaged DNA binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionpolyubiquitin modification-dependent protein binding
Molecular Functionprotein-containing complex binding
Molecular Functionsingle-stranded DNA binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin protein ligase binding
Molecular FunctionY-form DNA binding
Biological ProcessDNA damage response
Biological ProcessDNA repair
Biological Processpositive regulation of chromosome segregation
Biological Processpostreplication repair
Biological Processprotein autoubiquitination
Biological Processprotein monoubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RAD18
  • EC number
  • Alternative names
    • Postreplication repair protein RAD18 (hHR18; hRAD18)
    • RING finger protein 73
    • RING-type E3 ubiquitin transferase RAD18

Gene names

    • Name
      RAD18
    • Synonyms
      RNF73

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9NS91
  • Secondary accessions
    • Q58F55
    • Q9NRT6

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Note: Associates with chromatin (PubMed:25931565).
Colocalizes with SLF1 in the nucleus and to centrosomes (PubMed:15632077).
Relocalizes with SLF1 to nuclear foci in response to DNA damage (PubMed:22036607).
Accumulates with the SLF1-SLF2 and SMC5-SMC6 complexes at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner (PubMed:25931565).

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_0234236in dbSNP:rs45520133
Mutagenesis27Lower activity toward PCNA monoubiquitination.
Natural variantVAR_023424302in dbSNP:rs373572
Natural variantVAR_023425307in dbSNP:rs45569933
Mutagenesis442Does not interact with SLF1 and is defective in restoring cell survival after DNA damage; when associated with A-444.
Mutagenesis444Does not interact with SLF1 and is defective in restoring cell survival after DNA damage; when associated with A-442.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 613 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue, chain, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
Modified residue1UniProtN-acetylmethionine
ChainPRO_00000561491-495UniProtE3 ubiquitin-protein ligase RAD18
Modified residue (large scale data)7PRIDEPhosphoserine
Modified residue99UniProtPhosphoserine
Modified residue (large scale data)99PRIDEPhosphoserine
Modified residue103UniProtPhosphoserine
Modified residue (large scale data)103PRIDEPhosphoserine
Modified residue (large scale data)106PRIDEPhosphoserine
Modified residue118UniProtPhosphothreonine
Modified residue (large scale data)118PRIDEPhosphothreonine
Modified residue122UniProtPhosphoserine
Modified residue (large scale data)122PRIDEPhosphoserine
Modified residue125UniProtPhosphoserine
Modified residue (large scale data)125PRIDEPhosphoserine
Modified residue142UniProtPhosphoserine
Modified residue (large scale data)142PRIDEPhosphoserine
Modified residue (large scale data)155PRIDEPhosphoserine
Modified residue158UniProtPhosphoserine
Modified residue (large scale data)158PRIDEPhosphoserine
Modified residue164UniProtPhosphoserine
Modified residue (large scale data)164PRIDEPhosphoserine
Modified residue (large scale data)172PRIDEPhosphothreonine
Modified residue (large scale data)174PRIDEPhosphoserine
Modified residue (large scale data)194PRIDEPhosphoserine
Modified residue322UniProtPhosphoserine
Modified residue (large scale data)322PRIDEPhosphoserine
Cross-link376UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)403PRIDEPhosphoserine
Modified residue (large scale data)405PRIDEPhosphoserine
Modified residue (large scale data)409PRIDEPhosphoserine
Modified residue (large scale data)468PRIDEPhosphothreonine
Modified residue471UniProtPhosphoserine
Modified residue (large scale data)471PRIDEPhosphoserine
Modified residue483UniProtPhosphoserine
Modified residue (large scale data)483PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer (PubMed:21549715).
Interacts with UBE2A and UBE2B, one homodimer binding one molecule of UBE2B. Interacts with SHPRH (PubMed:17108083, PubMed:17130289).
Interacts with HLTF (PubMed:18316726, PubMed:18719106).
Interacts with SPRTN; leading to enhance chromatin association of RAD18 and RAD18-mediated PCNA ubiquitination and translesion DNA synthesis (PubMed:22681887).
Interacts (via C-terminus and phosphorylated form) with SLF1 (via BRCT domains); this interaction is required for efficient repair of UV-induced DNA damage (PubMed:15632077, PubMed:22036607, PubMed:25931565).
Interacts with SLF2 (PubMed:25931565).
Interacts with SMC5; this interaction is increased in a SLF1 or SLF2-dependent manner (PubMed:25931565).
Interacts with DNA damage up-regulated protein DDUP (PubMed:35849344).
Forms a complex with DDUP and H2AX following DDUP phosphorylation (PubMed:35849344).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for zinc finger, region, compositional bias, motif, domain.

TypeIDPosition(s)Description
Zinc finger25-64RING-type
Region152-197Disordered
Compositional bias166-184Basic and acidic residues
Zinc finger201-228UBZ4-type
Motif232-240LR motif
Domain248-282SAP
Region400-423Disordered
Region456-495Disordered

Sequence similarities

Belongs to the RAD18 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    495
  • Mass (Da)
    56,223
  • Last updated
    2010-11-30 v2
  • Checksum
    744A053A50C65DD7
MDSLAESRWPPGLAVMKTIDDLLRCGICFEYFNIAMIIPQCSHNYCSLCIRKFLSYKTQCPTCCVTVTEPDLKNNRILDELVKSLNFARNHLLQFALESPAKSPASSSSKNLAVKVYTPVASRQSLKQGSRLMDNFLIREMSGSTSELLIKENKSKFSPQKEASPAAKTKETRSVEEIAPDPSEAKRPEPPSTSTLKQVTKVDCPVCGVNIPESHINKHLDSCLSREEKKESLRSSVHKRKPLPKTVYNLLSDRDLKKKLKEHGLSIQGNKQQLIKRHQEFVHMYNAQCDALHPKSAAEIVREIENIEKTRMRLEASKLNESVMVFTKDQTEKEIDEIHSKYRKKHKSEFQLLVDQARKGYKKIAGMSQKTVTITKEDESTEKLSSVCMGQEDNMTSVTNHFSQSKLDSPEELEPDREEDSSSCIDIQEVLSSSESDSCNSSSSDIIRDLLEEEEAWEASHKNDLQDTEISPRQNRRTRAAESAEIEPRNKRNRN

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J0Q4C9J0Q4_HUMANRAD1891
F8WFA6F8WFA6_HUMANRAD18126
F8WE49F8WE49_HUMANRAD18310
F8WAZ7F8WAZ7_HUMANRAD1853
H7C3I2H7C3I2_HUMANRAD18131
H7C0A5H7C0A5_HUMANRAD1879

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias166-184Basic and acidic residues
Sequence conflict191in Ref. 2; AAF80856
Sequence conflict482-484in Ref. 2; AAF80856

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB035274
EMBL· GenBank· DDBJ
BAA99284.1
EMBL· GenBank· DDBJ
mRNA
AF169796
EMBL· GenBank· DDBJ
AAF80856.1
EMBL· GenBank· DDBJ
mRNA
AY004333
EMBL· GenBank· DDBJ
AAF86618.1
EMBL· GenBank· DDBJ
mRNA
AK023075
EMBL· GenBank· DDBJ
BAB14392.1
EMBL· GenBank· DDBJ
mRNA
AY961989
EMBL· GenBank· DDBJ
AAX44049.1
EMBL· GenBank· DDBJ
Genomic DNA
AC008151
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC034186
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC001302
EMBL· GenBank· DDBJ
AAH01302.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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