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Protein

E3 ubiquitin-protein ligase RNF138

Gene

Rnf138

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination. Recruited to sites of double-strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination. Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination. According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri18 – 58RING-typePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri86 – 105C2HC RNF-typePROSITE-ProRule annotationAdd BLAST20
Zinc fingeri157 – 180C2H2-typePROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF138Curated (EC:6.3.2.-Curated)
Alternative name(s):
RING finger protein 138Curated
Gene namesi
Name:Rnf138Imported
ORF Names:RSD-41 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621485. Rnf138.

Subcellular locationi

  • Chromosome By similarity

  • Note: Recruited at DNA damage sites. Localizes to sites of double-strand break: localization to double-strand break sites is mediated by the zinc fingers.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002616092 – 209E3 ubiquitin-protein ligase RNF138Add BLAST208

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei142PhosphothreonineBy similarity1

Post-translational modificationi

Auto-ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ99PD2.

Interactioni

Subunit structurei

Interacts with NLK. Interacts with XRCC5/Ku80. Interacts with RBBP8/CtIP.By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ99PD2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini189 – 207UIMBy similarityAdd BLAST19

Domaini

The zinc finger domains (C2H2-type and C2HC-type zinc fingers) bind DNA and mediate recruitment to double-strand break sites. They show strong preference for DNA with 5'- or 3'-single-stranded overhangs, while they do not bind blunt-ended double-stranded DNA or poly(ADP-ribose) (PAR) polymers.By similarity

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
Contains 1 C2HC RNF-type zinc finger.PROSITE-ProRule annotationCurated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri18 – 58RING-typePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri86 – 105C2HC RNF-typePROSITE-ProRule annotationAdd BLAST20
Zinc fingeri157 – 180C2H2-typePROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOVERGENiHBG074331.
InParanoidiQ99PD2.
KOiK10668.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51803. ZF_C2HC_RNF. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99PD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEELSADTS YTEDDFYCPV CQEVLKTPVR TAACQHVFCR KCFLTAMRES
60 70 80 90 100
GIHCPLCRGS VTRRERACPE RAIDLENIMR RVSGSCRCCS KKIKFYRMRH
110 120 130 140 150
HYKSCKKYQD EYGVSSVIPN VKISQDSVRS SNRSETSASD NTETYQEDTS
160 170 180 190 200
SSGHPTFKCP LCQESNFTRQ RLLDHCNSNH LFQIVPVNLQ LDEETQYQTA

VEESFQVNM
Length:209
Mass (Da):24,072
Last modified:June 1, 2001 - v1
Checksum:i8C3A06E4EB24CFDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315468 mRNA. Translation: AAK11282.1.
BC061821 mRNA. Translation: AAH61821.1.
RefSeqiNP_446040.1. NM_053588.2.
UniGeneiRn.6814.

Genome annotation databases

GeneIDi94196.
KEGGirno:94196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315468 mRNA. Translation: AAK11282.1.
BC061821 mRNA. Translation: AAH61821.1.
RefSeqiNP_446040.1. NM_053588.2.
UniGeneiRn.6814.

3D structure databases

ProteinModelPortaliQ99PD2.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ99PD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi94196.
KEGGirno:94196.

Organism-specific databases

CTDi51444.
RGDi621485. Rnf138.

Phylogenomic databases

HOVERGENiHBG074331.
InParanoidiQ99PD2.
KOiK10668.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ99PD2.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51803. ZF_C2HC_RNF. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRN138_RAT
AccessioniPrimary (citable) accession number: Q99PD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: October 5, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.