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Protein

RING finger protein 11

Gene

RNF11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri99 – 140RING-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • ubiquitin-protein transferase activity Source: FlyBase
  • zinc ion binding Source: ProtInc

GO - Biological processi

  • protein autoubiquitination Source: FlyBase
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000123091-MONOMER.
SIGNORiQ9Y3C5.

Names & Taxonomyi

Protein namesi
Recommended name:
RING finger protein 11
Gene namesi
Name:RNF11
ORF Names:CGI-123
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10056. RNF11.

Subcellular locationi

GO - Cellular componenti

  • early endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • recycling endosome Source: UniProtKB-SubCell
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding. 1 Publication1
Mutagenesisi4C → S: Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination. 1 Publication1
Mutagenesisi12D → A: Loss of GGA1-binding. 1 Publication1
Mutagenesisi15L → A: Loss of GGA1-binding. 1 Publication1
Mutagenesisi16L → A: Loss of GGA1-binding. 1 Publication1
Mutagenesisi40Y → A: Loss of ITCH-, SMURF2- and WWP1-binding. Partial loss of ubiquitination by ITCH. No effect on STAMBP-binding; when associated with S-99 and S-102. Persistent TNF-mediated NFKBIA phosphorylation. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. 5 Publications1
Mutagenesisi99C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-102. Persistent TNF-mediated NFKBIA phosphorylation. No effect on STAMBP-binding; when associated with A-40 and S-102. No effect on ubiquitination by ITCH; when associated with S-102. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. 4 Publications1
Mutagenesisi102C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-99. No effect on ubiquitination by ITCH; when associated with S-102. No effect on STAMBP-binding; when associated with A-40 and S-99. 3 Publications1
Mutagenesisi103M → A or G: Loss of UBE2N-binding. No gain of UBE2L3-binding. 1 Publication1
Mutagenesisi103M → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128. 1 Publication1
Mutagenesisi103M → V: No effect on UBE2N-binding. Gain of UBE2L3-binding. 1 Publication1
Mutagenesisi127D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128. 1 Publication1
Mutagenesisi128D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding. 1 Publication1
Mutagenesisi135T → E: Loss of phosphorylation and of 14-3-3-binding. 1 Publication1

Organism-specific databases

DisGeNETi26994.
OpenTargetsiENSG00000123091.
PharmGKBiPA34420.

Polymorphism and mutation databases

BioMutaiRNF11.
DMDMi21362884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000560502 – 154RING finger protein 11Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine2 Publications1
Lipidationi4S-palmitoyl cysteine1 Publication1
Modified residuei14PhosphoserineCombined sources1
Modified residuei25PhosphoserineBy similarity1
Modified residuei135Phosphothreonine; by PKB/AKT11 Publication1

Post-translational modificationi

Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1.2 Publications
Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome.1 Publication
Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y3C5.
MaxQBiQ9Y3C5.
PaxDbiQ9Y3C5.
PeptideAtlasiQ9Y3C5.
PRIDEiQ9Y3C5.

PTM databases

iPTMnetiQ9Y3C5.
PhosphoSitePlusiQ9Y3C5.
SwissPalmiQ9Y3C5.

Expressioni

Tissue specificityi

Expressed at low levels in the lung, liver, kidney, pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and peripheral blood lymphocytes, and, at intermediate levels, in the testis, heart, brain and placenta. Highest expression in the skeletal muscle. In the brain, expressed at different levels in several regions: high levels in the amygdala, moderate in the hippocampus and thalamus, low in the caudate and extremely low levels in the corpus callosum (at protein level). Restricted to neurons, enriched in somatodendritic compartments and excluded from white matter (at protein level). In substantia nigra, present in cell bodies and processes of dopaminergic and nondopaminergic cells (at protein level). In Parkinson disease, sequestered in Lewy bodies and neurites. Overexpressed in breast cancer cells, but not detected in the surrounding stroma and weakly, if at all, in normal breast epithelial cells (at protein level). Also expressed in several tumor cell lines.3 Publications

Gene expression databases

BgeeiENSG00000123091.
CleanExiHS_RNF11.
GenevisibleiQ9Y3C5. HS.

Organism-specific databases

HPAiHPA045781.
HPA050359.

Interactioni

Subunit structurei

Interacts (when phosphorylated) with 14-3-3. Interacts with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity). Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350, EPS15 and STAMBP. After TNF stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they are lost after 1 hour of stimulation with TNF (By similarity). Interacts with GGA1.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GGA1Q9UJY53EBI-396669,EBI-447141
ITCHQ96J022EBI-396669,EBI-1564678
NEDD4P469342EBI-396669,EBI-726944
QARSP478974EBI-396669,EBI-347462
SMURF2Q9HAU45EBI-396669,EBI-396727
STAMBPO956302EBI-396669,EBI-396676
TAX1BP1Q86VP12EBI-396669,EBI-529518
TNFAIP3P215802EBI-396669,EBI-527670
UBBP0CG472EBI-396669,EBI-413034
UBE2D1P516686EBI-396669,EBI-743540
UBE2D2P628377EBI-396669,EBI-347677
UBE2D3P610773EBI-396669,EBI-348268
UBE2D4Q9Y2X86EBI-396669,EBI-745527
UBE2E1P519652EBI-396669,EBI-348546
UBE2NP610884EBI-396669,EBI-1052908

Protein-protein interaction databases

BioGridi117941. 104 interactors.
IntActiQ9Y3C5. 61 interactors.
MINTiMINT-1180165.
STRINGi9606.ENSP00000242719.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3C5.
SMRiQ9Y3C5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi37 – 40WW-binding4

Domaini

The WW-binding motif mediates interaction with NEDD4.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri99 – 140RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00730000110988.
HOGENOMiHOG000007448.
HOVERGENiHBG058444.
InParanoidiQ9Y3C5.
KOiK11980.
OMAiHLDCIDN.
OrthoDBiEOG091G0T50.
PhylomeDBiQ9Y3C5.
TreeFamiTF318022.

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.

Q9Y3C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH
60 70 80 90 100
PTPSQTRLAT QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV
110 120 130 140 150
ICMMDFVYGD PIRFLPCMHI YHLDCIDDWL MRSFTCPSCM EPVDAALLSS

YETN
Length:154
Mass (Da):17,444
Last modified:November 1, 1999 - v1
Checksum:iC368E38148FC1D0D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti124D → G in BAF85736 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05827211D → E.Corresponds to variant rs12077069dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024703 mRNA. Translation: BAA84683.1.
AF151881 mRNA. Translation: AAD34118.1.
AK293047 mRNA. Translation: BAF85736.1.
AK313140 mRNA. Translation: BAG35959.1.
AL162430 Genomic DNA. Translation: CAI13140.1.
CH471059 Genomic DNA. Translation: EAX06831.1.
BC020964 mRNA. Translation: AAH20964.1.
BC047654 mRNA. Translation: AAH47654.1.
CCDSiCCDS556.1.
RefSeqiNP_055187.1. NM_014372.4.
UniGeneiHs.309641.

Genome annotation databases

EnsembliENST00000242719; ENSP00000242719; ENSG00000123091.
GeneIDi26994.
KEGGihsa:26994.
UCSCiuc001csi.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024703 mRNA. Translation: BAA84683.1.
AF151881 mRNA. Translation: AAD34118.1.
AK293047 mRNA. Translation: BAF85736.1.
AK313140 mRNA. Translation: BAG35959.1.
AL162430 Genomic DNA. Translation: CAI13140.1.
CH471059 Genomic DNA. Translation: EAX06831.1.
BC020964 mRNA. Translation: AAH20964.1.
BC047654 mRNA. Translation: AAH47654.1.
CCDSiCCDS556.1.
RefSeqiNP_055187.1. NM_014372.4.
UniGeneiHs.309641.

3D structure databases

ProteinModelPortaliQ9Y3C5.
SMRiQ9Y3C5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117941. 104 interactors.
IntActiQ9Y3C5. 61 interactors.
MINTiMINT-1180165.
STRINGi9606.ENSP00000242719.

PTM databases

iPTMnetiQ9Y3C5.
PhosphoSitePlusiQ9Y3C5.
SwissPalmiQ9Y3C5.

Polymorphism and mutation databases

BioMutaiRNF11.
DMDMi21362884.

Proteomic databases

EPDiQ9Y3C5.
MaxQBiQ9Y3C5.
PaxDbiQ9Y3C5.
PeptideAtlasiQ9Y3C5.
PRIDEiQ9Y3C5.

Protocols and materials databases

DNASUi26994.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242719; ENSP00000242719; ENSG00000123091.
GeneIDi26994.
KEGGihsa:26994.
UCSCiuc001csi.5. human.

Organism-specific databases

CTDi26994.
DisGeNETi26994.
GeneCardsiRNF11.
HGNCiHGNC:10056. RNF11.
HPAiHPA045781.
HPA050359.
MIMi612598. gene.
neXtProtiNX_Q9Y3C5.
OpenTargetsiENSG00000123091.
PharmGKBiPA34420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00730000110988.
HOGENOMiHOG000007448.
HOVERGENiHBG058444.
InParanoidiQ9Y3C5.
KOiK11980.
OMAiHLDCIDN.
OrthoDBiEOG091G0T50.
PhylomeDBiQ9Y3C5.
TreeFamiTF318022.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000123091-MONOMER.
SIGNORiQ9Y3C5.

Miscellaneous databases

ChiTaRSiRNF11. human.
GeneWikiiRNF11.
GenomeRNAii26994.
PROiQ9Y3C5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000123091.
CleanExiHS_RNF11.
GenevisibleiQ9Y3C5. HS.

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 nameiRNF11_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3C5
Secondary accession number(s): A8KAI2, Q5T7R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.