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Protein

E3 ubiquitin-protein ligase RNF34

Gene

Rnf34

Organism
Rattus norvegicus (Rat)
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 the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells. Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation.By similarity1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri56 – 10752FYVE-typeAdd
BLAST
Zinc fingeri334 – 36936RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-6804757. Regulation of TP53 Degradation.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF34Curated (EC:6.3.2.-1 Publication)
Alternative name(s):
RING finger protein 34Imported
RING finger protein MOMO1 Publication
Gene namesi
Name:Rnf34Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi628636. Rnf34.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381E3 ubiquitin-protein ligase RNF34PRO_0000056075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631PhosphoserineBy similarity
Modified residuei265 – 2651PhosphoserineBy similarity

Post-translational modificationi

Proteolytically cleaved by caspases upon induction of apoptosis by TNF.By similarity
Autoubiquitinated (in vitro).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei241 – 2422Cleavage; by caspase-3By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6AYH3.
PRIDEiQ6AYH3.

Expressioni

Tissue specificityi

Ubiquitous. Detected in brain, cerebellum, midbrain, hippocampus, striatum, heart, lung, kidney, muscle, spleen and testis.1 Publication

Gene expression databases

GenevisibleiQ6AYH3. RN.

Interactioni

Subunit structurei

Interacts with CASP8 and CASP10. Interacts with p53/TP53; involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc finger) with MDM2; the interaction stabilizes MDM2. Interacts (via RING-type zinc finger) with PPARGC1A. Interacts with NOD1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001799.

Structurei

3D structure databases

ProteinModelPortaliQ6AYH3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 13420SAP 1Add
BLAST
Domaini273 – 28715SAP 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi222 – 25029Asp/Glu-richAdd
BLAST

Domaini

The RING-type zinc finger is required for the ubiquitination of target proteins.By similarity
The FYVE-type zinc finger domain is required for localization and may confer affinity for cellular compartments enriched in phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate phospholipids.By similarity

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 2 SAP domains.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri56 – 10752FYVE-typeAdd
BLAST
Zinc fingeri334 – 36936RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IMEF. Eukaryota.
ENOG410Y1GP. LUCA.
GeneTreeiENSGT00390000012719.
HOGENOMiHOG000068080.
HOVERGENiHBG055079.
InParanoidiQ6AYH3.
OMAiEFSTYPP.
OrthoDBiEOG70GMFS.
PhylomeDBiQ6AYH3.
TreeFamiTF325195.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AYH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAGATSMWA SCCGLLNEVM GTGAVRGQQA GFPGSTGPFR FTPSSDFPTY
60 70 80 90 100
PPAATEGPNI VCKACGLSFS VFRKKHVCCD CKKDFCSLCS VSQENLRRCS
110 120 130 140 150
TCHLLQETAF QRPQLMRLKV KDLRQYLLLR NVPTDTCREK EDLVDLVLCH
160 170 180 190 200
RGLGSGDGLD SRSLSSSRSQ TSSFFTQSYF SNYTPPSATV SSFQGELMDR
210 220 230 240 250
EGTFRSEVLT QVQSELASAN TDDEDGEEDD DDDDDDDDED DDEQEENLEE
260 270 280 290 300
QNPGLSKKKA RASLSDLSSL EEVEGMSVRQ LKEILARNFV NYSGCCEKWE
310 320 330 340 350
LVEKVNRLYK ENEENQKSYG ERMQLQDEED DSLCRICMDA VIDCVLLECG
360 370 380
HMVTCTKCGK RMSECPICRQ YVVRAVHVFK S
Length:381
Mass (Da):42,681
Last modified:September 13, 2004 - v1
Checksum:i12A2E7BEB1CEA4EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531P → L in AAN60073 (PubMed:12859687).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157968 mRNA. Translation: AAN60073.1.
BC079044 mRNA. Translation: AAH79044.1.
RefSeqiNP_001004075.1. NM_001004075.1.
UniGeneiRn.14904.

Genome annotation databases

EnsembliENSRNOT00000001799; ENSRNOP00000001799; ENSRNOG00000001331.
GeneIDi282845.
KEGGirno:282845.
UCSCiRGD:628636. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157968 mRNA. Translation: AAN60073.1.
BC079044 mRNA. Translation: AAH79044.1.
RefSeqiNP_001004075.1. NM_001004075.1.
UniGeneiRn.14904.

3D structure databases

ProteinModelPortaliQ6AYH3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001799.

Proteomic databases

PaxDbiQ6AYH3.
PRIDEiQ6AYH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001799; ENSRNOP00000001799; ENSRNOG00000001331.
GeneIDi282845.
KEGGirno:282845.
UCSCiRGD:628636. rat.

Organism-specific databases

CTDi80196.
RGDi628636. Rnf34.

Phylogenomic databases

eggNOGiENOG410IMEF. Eukaryota.
ENOG410Y1GP. LUCA.
GeneTreeiENSGT00390000012719.
HOGENOMiHOG000068080.
HOVERGENiHBG055079.
InParanoidiQ6AYH3.
OMAiEFSTYPP.
OrthoDBiEOG70GMFS.
PhylomeDBiQ6AYH3.
TreeFamiTF325195.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-RNO-6804757. Regulation of TP53 Degradation.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ6AYH3.

Gene expression databases

GenevisibleiQ6AYH3. RN.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A palmitoylated RING finger ubiquitin ligase and its homologue in the brain membranes."
    Araki K., Kawamura M., Suzuki T., Matsuda N., Kanbe D., Ishii K., Ichikawa T., Kumanishi T., Chiba T., Tanaka K., Nawa H.
    J. Neurochem. 86:749-762(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, TISSUE SPECIFICITY.
    Tissue: Hippocampus.
  2. "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].
    Tissue: Testis.

Entry informationi

Entry nameiRNF34_RAT
AccessioniPrimary (citable) accession number: Q6AYH3
Secondary accession number(s): Q8CIP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 103 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.