P10862

PR
Gene name
RAD18 (YCR066W, YCR66W)
Protein name
Postreplication repair E3 ubiquitin-protein ligase RAD18
Names
RING-type E3 ubiquitin transferase RAD18, Radiation sensitivity protein 18
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YCR066W
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

63-297 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P10862

Entry ID Method Resolution Chain Position Source
AF-P10862-F1 Predicted AlphaFoldDB

10 variants for P10862

Variant ID(s) Position Change Description Diseaes Association Provenance
s03-231854 120 W>L No SGRP
s03-232003 170 A>T No SGRP
s03-232211 239 R>K No SGRP
s03-232529 345 T>I No SGRP
s03-232528 345 T>P No SGRP
s03-232694 400 R>K No SGRP
s03-232816 441 E>K No SGRP
s03-232829 445 D>V No SGRP
s03-232886 464 S>L No SGRP
s03-232901 469 L>S No SGRP

No associated diseases with P10862

4 regional properties for P10862

Type Name Position InterPro Accession
domain Zinc finger, RING-type 28 - 65 IPR001841
domain SAP domain 278 - 312 IPR003034
domain Rad18, zinc finger UBZ4-type 187 - 215 IPR006642
conserved_site Zinc finger, RING-type, conserved site 43 - 52 IPR017907

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
Rad6-Rad18 complex A ubiquitin ligase complex found to be involved in post-replicative bypass of UV-damaged DNA and UV mutagenesis. In S. cerevisiae, the complex contains the ubiquitin conjugating enzyme Rad6 and Rad18, a protein containing a RING finger motif and a nucleotide binding motif. The yeast Rad6-Rad18 heterodimer has ubiquitin conjugating activity, binds single-stranded DNA, and possesses single-stranded DNA-dependent ATPase activity.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
single-stranded DNA binding Binding to single-stranded DNA.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.

6 GO annotations of biological process

Name Definition
DNA duplex unwinding The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating a region of unpaired single strands.
error-free postreplication DNA repair The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate.
error-free translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
error-prone translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
postreplication repair The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication.
protein monoubiquitination Addition of a single ubiquitin group to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDHQITTASD FTTTSIPSLY QLDTLLRCHI CKDFLKVPVL TPCGHTFCSL CIRTHLNNQP
70 80 90 100 110 120
NCPLCLFEFR ESLLRSEFLV SEIIQSYTSL RSSLLDALRI PKPTPVPENE EVPGPENSSW
130 140 150 160 170 180
IELISESESD SVNAADDDLQ IVATSERKLA KRSMTDILPL SSKPSKRNFA MFRSERIKKK
190 200 210 220 230 240
SKPNEQMAQC PICQQFYPLK ALEKTHLDEC LTLQSLGKKP KISTTFPTES NPHNKSSSRF
250 260 270 280 290 300
KVRTPEVDKS SCGETSHVDK YLNSMMSAEH QRLPKINFTS MTQSQIKQKL SSLGLSTNGT
310 320 330 340 350 360
RQNMIKRYNH YEMLWNSNFC DSLEPVDEAE LKRQLLSWDV SHNKTPQNSS NKGGISKLMI
370 380 390 400 410 420
MKSNGKSSSY RKLLENFKND KFNRKGWMVM FRKDFARLIR EAKMKIKTGS SDSSGSVGHS
430 440 450 460 470 480
NDGDGVEKVQ SDQGTEDQQM EKDQDTVINE DRVAGERNLP NEDSTDADLS RELMDLNEYS
KDPPGNN