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Protein

E3 ubiquitin-protein ligase RNF34

Gene

Rnf34

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 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 (PubMed:22064484). 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 fingeri329 – 36436RING-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-MMU-6804757. Regulation of TP53 Degradation.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF34Curated (EC:6.3.2.-By similarity)
Alternative name(s):
Phafin-1Imported
RING finger protein 34Imported
Gene namesi
Name:Rnf34Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2153340. Rnf34.

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Endomembrane system By similarity; Peripheral membrane protein By similarity
  • Nucleus By similarity
  • Nucleus speckle By similarity
  • Cytoplasmcytosol By similarity

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 – 376376E3 ubiquitin-protein ligase RNF34PRO_0000056073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691PhosphoserineBy similarity
Modified residuei258 – 2581PhosphoserineCombined sources
Modified residuei260 – 2601PhosphoserineCombined sources

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei236 – 2372Cleavage; by caspase-3By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99KR6.
MaxQBiQ99KR6.
PaxDbiQ99KR6.
PeptideAtlasiQ99KR6.
PRIDEiQ99KR6.

PTM databases

iPTMnetiQ99KR6.
PhosphoSiteiQ99KR6.

Expressioni

Inductioni

Down-regulated in response to cold exposure.1 Publication

Gene expression databases

BgeeiENSMUSG00000029474.
CleanExiMM_RNF34.
ExpressionAtlasiQ99KR6. baseline and differential.
GenevisibleiQ99KR6. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031434.

Structurei

3D structure databases

ProteinModelPortaliQ99KR6.
SMRiQ99KR6. Positions 62-148, 319-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 13420SAP 1Add
BLAST
Domaini268 – 28215SAP 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi222 – 24524Asp/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 fingeri329 – 36436RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IMEF. Eukaryota.
ENOG410Y1GP. LUCA.
GeneTreeiENSGT00390000012719.
HOGENOMiHOG000068080.
HOVERGENiHBG055079.
InParanoidiQ99KR6.
OMAiEFSTYPP.
OrthoDBiEOG091G0S1S.
PhylomeDBiQ99KR6.
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.

Q99KR6-1 [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 NIPTDTCREK EDLVDLVLCH
160 170 180 190 200
RGLGSGDDLD SSSLNSSRSQ TSSFFTQSLF SNYTPPSATV SSFQGELMDR
210 220 230 240 250
DGAFRSEVLA QVQSEIASAN TDDDDDDDDD DDDDEDDDDE QEEEEQNPGL
260 270 280 290 300
SKKKARASLS DLSSLEEVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV
310 320 330 340 350
NRLYKENEEN QKSYGERMQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC
360 370
TKCGKRMSEC PICRQYVVRA VHVFKS
Length:376
Mass (Da):42,030
Last modified:June 1, 2001 - v1
Checksum:iFE4AB65DAE9381BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF434815 mRNA. Translation: AAL30770.1.
AK045696 mRNA. Translation: BAC32461.1.
AK046274 mRNA. Translation: BAC32666.1.
AK046381 mRNA. Translation: BAC32697.1.
AK077221 mRNA. Translation: BAC36693.1.
AK132330 mRNA. Translation: BAE21109.1.
AK137606 mRNA. Translation: BAE23428.1.
AK150976 mRNA. Translation: BAE30005.1.
AK159753 mRNA. Translation: BAE35344.1.
BC004042 mRNA. Translation: AAH04042.1.
CCDSiCCDS19656.1.
RefSeqiNP_085041.1. NM_030564.1.
UniGeneiMm.388529.

Genome annotation databases

EnsembliENSMUST00000031434; ENSMUSP00000031434; ENSMUSG00000029474.
GeneIDi80751.
KEGGimmu:80751.
UCSCiuc008zmn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF434815 mRNA. Translation: AAL30770.1.
AK045696 mRNA. Translation: BAC32461.1.
AK046274 mRNA. Translation: BAC32666.1.
AK046381 mRNA. Translation: BAC32697.1.
AK077221 mRNA. Translation: BAC36693.1.
AK132330 mRNA. Translation: BAE21109.1.
AK137606 mRNA. Translation: BAE23428.1.
AK150976 mRNA. Translation: BAE30005.1.
AK159753 mRNA. Translation: BAE35344.1.
BC004042 mRNA. Translation: AAH04042.1.
CCDSiCCDS19656.1.
RefSeqiNP_085041.1. NM_030564.1.
UniGeneiMm.388529.

3D structure databases

ProteinModelPortaliQ99KR6.
SMRiQ99KR6. Positions 62-148, 319-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031434.

PTM databases

iPTMnetiQ99KR6.
PhosphoSiteiQ99KR6.

Proteomic databases

EPDiQ99KR6.
MaxQBiQ99KR6.
PaxDbiQ99KR6.
PeptideAtlasiQ99KR6.
PRIDEiQ99KR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031434; ENSMUSP00000031434; ENSMUSG00000029474.
GeneIDi80751.
KEGGimmu:80751.
UCSCiuc008zmn.1. mouse.

Organism-specific databases

CTDi80196.
MGIiMGI:2153340. Rnf34.

Phylogenomic databases

eggNOGiENOG410IMEF. Eukaryota.
ENOG410Y1GP. LUCA.
GeneTreeiENSGT00390000012719.
HOGENOMiHOG000068080.
HOVERGENiHBG055079.
InParanoidiQ99KR6.
OMAiEFSTYPP.
OrthoDBiEOG091G0S1S.
PhylomeDBiQ99KR6.
TreeFamiTF325195.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ99KR6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029474.
CleanExiMM_RNF34.
ExpressionAtlasiQ99KR6. baseline and differential.
GenevisibleiQ99KR6. MM.

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...

Entry informationi

Entry nameiRNF34_MOUSE
AccessioniPrimary (citable) accession number: Q99KR6
Secondary accession number(s): Q3UV45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 128 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.