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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri231 – 27242RING-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → 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 Publication
Mutagenesisi16 – 161C → 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 Publication
Mutagenesisi231 – 2311C → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 313312E3 ubiquitin-protein ligase RNF126PRO_0000056094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity

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.
PhosphoSiteiQ91YL2.

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

BgeeiQ91YL2.
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

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi225 – 2284Combined sources
Turni232 – 2354Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi252 – 2543Combined sources
Turni255 – 2573Combined sources
Helixi259 – 2624Combined sources
Turni269 – 2713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ECTNMR-A221-291[»]
ProteinModelPortaliQ91YL2.
SMRiQ91YL2. Positions 221-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91YL2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 10096Required for interaction with BAG6By similarityAdd
BLAST
Regioni202 – 306105Sufficient for interaction with AICDABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi293 – 31321Ser-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri231 – 27242RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ91YL2.
KOiK11982.
OMAiNRHPFEN.
OrthoDBiEOG7353XB.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2ECTNMR-A221-291[»]
ProteinModelPortaliQ91YL2.
SMRiQ91YL2. Positions 221-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000039486.

PTM databases

iPTMnetiQ91YL2.
PhosphoSiteiQ91YL2.

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.
OMAiNRHPFEN.
OrthoDBiEOG7353XB.
PhylomeDBiQ91YL2.
TreeFamiTF317985.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

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

Gene expression databases

BgeeiQ91YL2.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.
  3. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-13; CYS-16 AND CYS-231, INTERACTION WITH CCDC50; EGFR; FLT3 AND SCAMP3.
  4. "Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase."
    Delker R.K., Zhou Y., Strikoudis A., Stebbins C.E., Papavasiliou F.N.
    Proc. Natl. Acad. Sci. U.S.A. 110:1029-1034(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  5. "Solution structure of the zinc finger, C3HC4 type (RING finger) domain of RING finger protein 126."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 221-291.

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: July 6, 2016
This is version 107 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.