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Protein

E3 ubiquitin-protein ligase RNF126

Gene

Rnf126

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that regulates several biological processes through ubiquitination of various target proteins. Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. Through their polyubiquitination, may play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4 (PubMed:23418353). May also be part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. May provide the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the mislocalized proteins and their targeting to the proteasome. May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor. By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation. May monoubiquitinate AICDA.By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
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 fingeri231 – 272RING-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF126Curated (EC:6.3.2.-1 Publication)
Alternative name(s):
RING finger protein 126Imported
Gene namesi
Name:Rnf126Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1917544. Rnf126.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13C → A: Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity but alters specificity for 'Lys-48'-linked chains; when associated with A-16. 1 Publication1
Mutagenesisi16C → A: Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity but alters specificity for 'Lys-48'-linked chains; when associated with A-13. 1 Publication1
Mutagenesisi231C → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000560942 – 313E3 ubiquitin-protein ligase RNF126Add BLAST312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei5PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated. May undergo autoubiquitination.1 PublicationBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91YL2.
MaxQBiQ91YL2.
PaxDbiQ91YL2.
PRIDEiQ91YL2.

PTM databases

iPTMnetiQ91YL2.
PhosphoSitePlusiQ91YL2.

Expressioni

Tissue specificityi

Detected in B-cells (at protein level).1 Publication

Inductioni

Up-regulated in B-cells that undergo class-switch recombination (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000035890.
CleanExiMM_RNF126.
ExpressionAtlasiQ91YL2. baseline and differential.
GenevisibleiQ91YL2. MM.

Interactioni

Subunit structurei

Interacts with CCDC50, EGFR, FLT3 and SCAMP3. Interacts with BAG6 (via ubiquitin-like domain); required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol. Interacts with CDKN1A. Interacts with AICDA.By similarity1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000039486.

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi225 – 228Combined sources4
Turni232 – 235Combined sources4
Beta strandi244 – 246Combined sources3
Beta strandi252 – 254Combined sources3
Turni255 – 257Combined sources3
Helixi259 – 262Combined sources4
Turni269 – 271Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ECTNMR-A221-291[»]
ProteinModelPortaliQ91YL2.
SMRiQ91YL2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91YL2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni5 – 100Required for interaction with BAG6By similarityAdd BLAST96
Regioni202 – 306Sufficient for interaction with AICDABy similarityAdd BLAST105

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi293 – 313Ser-richAdd BLAST21

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri231 – 272RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ91YL2.
KOiK11982.
OMAiFCHRCSE.
OrthoDBiEOG091G0SOO.
PhylomeDBiQ91YL2.
TreeFamiTF317985.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91YL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEASPQPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRNTENG
60 70 80 90 100
SAPSTAPTDQ NRQPFENVDQ HLFTLPQGYS QFAFGIFDDS FEIPTFPPGA
110 120 130 140 150
QADDGRDPES RREREHQSRH RYGARQPRAR LTARRATGRH EGVPTLEGII
160 170 180 190 200
QQLVNGIISP AAVPSLGLGP WGVLHSNPMD YAWGANGLDT IITQLLNQFE
210 220 230 240 250
NTGPPPADKE KIQALPTVPV TEEHVGSGLE CPVCKEDYAL GESVRQLPCN
260 270 280 290 300
HLFHDSCIVP WLEQHDSCPV CRKSLTGQNT ATNPPGLTGV GFSSSSSSSS
310
SSSPSNENAT SNS
Length:313
Mass (Da):34,081
Last modified:December 1, 2001 - v1
Checksum:iA1BA6A8C2711D0C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC016543 mRNA. Translation: AAH16543.1.
CCDSiCCDS23989.1.
RefSeqiNP_653111.1. NM_144528.3.
UniGeneiMm.466670.

Genome annotation databases

EnsembliENSMUST00000047203; ENSMUSP00000039486; ENSMUSG00000035890.
GeneIDi70294.
KEGGimmu:70294.
UCSCiuc007fzr.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC016543 mRNA. Translation: AAH16543.1.
CCDSiCCDS23989.1.
RefSeqiNP_653111.1. NM_144528.3.
UniGeneiMm.466670.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ECTNMR-A221-291[»]
ProteinModelPortaliQ91YL2.
SMRiQ91YL2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000039486.

PTM databases

iPTMnetiQ91YL2.
PhosphoSitePlusiQ91YL2.

Proteomic databases

EPDiQ91YL2.
MaxQBiQ91YL2.
PaxDbiQ91YL2.
PRIDEiQ91YL2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047203; ENSMUSP00000039486; ENSMUSG00000035890.
GeneIDi70294.
KEGGimmu:70294.
UCSCiuc007fzr.3. mouse.

Organism-specific databases

CTDi55658.
MGIiMGI:1917544. Rnf126.

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ91YL2.
KOiK11982.
OMAiFCHRCSE.
OrthoDBiEOG091G0SOO.
PhylomeDBiQ91YL2.
TreeFamiTF317985.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRnf126. mouse.
EvolutionaryTraceiQ91YL2.
PROiQ91YL2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000035890.
CleanExiMM_RNF126.
ExpressionAtlasiQ91YL2. baseline and differential.
GenevisibleiQ91YL2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRN126_MOUSE
AccessioniPrimary (citable) accession number: Q91YL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 110 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.