Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 mediates ubiquitination oF target proteins (By similarity). Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates (PubMed:23418353). 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 (By similarity). Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome (By similarity). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (By similarity). May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination (PubMed:23418353). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (By similarity). May monoubiquitinate AICDA (By similarity).By similarity1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.1 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13ZincBy similarity1
Metal bindingi16ZincBy similarity1
Metal bindingi29ZincBy similarity1
Metal bindingi32ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri13 – 32C4-typeBy similarityAdd BLAST20
Zinc fingeri231 – 272RING-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF126Curated (EC:2.3.2.271 Publication)
Alternative name(s):
RING finger protein 126Imported
Gene namesi
Name:Rnf126Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1917544. Rnf126.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

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 (PubMed:23418353). Interacts with BAG6 (via ubiquitin-like domain); required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol (By similarity). Interacts with CDKN1A (By similarity). Interacts with AICDA (By similarity).By similarity1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi213968. 2 interactors.
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

Domaini

The C4-type zinc finger is required for interaction with BAG6.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri13 – 32C4-typeBy similarityAdd BLAST20
Zinc fingeri231 – 272RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

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

Family and domain databases

CDDicd00162. RING. 1 hit.
Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF13639. zf-RING_2. 1 hit.
SMARTiView protein in SMART
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS50089. ZF_RING_2. 1 hit.

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

BioGridi213968. 2 interactors.
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.
OMAiWGMLHSN.
OrthoDBiEOG091G0SOO.
PhylomeDBiQ91YL2.
TreeFamiTF317985.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRnf126. mouse.
EvolutionaryTraceiQ91YL2.
PROiPR:Q91YL2.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

CDDicd00162. RING. 1 hit.
Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF13639. zf-RING_2. 1 hit.
SMARTiView protein in SMART
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS50089. ZF_RING_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRN126_MOUSE
AccessioniPrimary (citable) accession number: Q91YL2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: December 1, 2001
Last modified: June 7, 2017
This is version 114 of the entry and version 1 of the sequence. See 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

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.