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Protein

E3 ubiquitin-protein ligase RNF4

Gene

Rnf4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.1 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.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
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)DescriptionActionsGraphical viewLength
Zinc fingeri136 – 181RING-typePROSITE-ProRule annotationAdd BLAST46

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF4 (EC:2.3.2.27)
Alternative name(s):
RING finger protein 4
RING-type E3 ubiquitin transferase RNF4Curated
Gene namesi
Name:Rnf4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1201691. Rnf4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleus Source: MGI
  • PML body Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi134V → E: Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. 1 Publication1
Mutagenesisi155S → A: No effect. 1 Publication1
Mutagenesisi155S → E: Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. 1 Publication1
Mutagenesisi161V → A: Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. 1 Publication1
Mutagenesisi193Y → A: Abolishes homodimerization. Loss of E3 ubiquitin ligase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560441 – 194E3 ubiquitin-protein ligase RNF4Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98PhosphoserineCombined sources1
Modified residuei99PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated; conjugated by one or two SUMO1 moieties.By similarity
Autoubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9QZS2.
MaxQBiQ9QZS2.
PaxDbiQ9QZS2.
PRIDEiQ9QZS2.

PTM databases

iPTMnetiQ9QZS2.
PhosphoSitePlusiQ9QZS2.

Miscellaneous databases

PMAP-CutDBiQ9QZS2.

Expressioni

Tissue specificityi

In the embryo, expressed primarily in the developing nervous system with strong expression in the dorsal root ganglia and gonads. Ubiquitously expressed in the adult.

Developmental stagei

Expression is detected from embryonic day 7 and continues throughout development and into adulthood.

Gene expression databases

BgeeiENSMUSG00000029110.
CleanExiMM_RNF4.
ExpressionAtlasiQ9QZS2. baseline and differential.
GenevisibleiQ9QZS2. MM.

Interactioni

Subunit structurei

Homodimer (via RING-type zinc finger domain). Interacts with AR/the androgen receptor and TBP (By similarity). Interacts with PATZ1 (By similarity). Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent (By similarity). Interacts with TRPS1; negatively regulates the TRPS1 transcriptional repressor activity. Interacts with GSC2. Interacts with TCF20. Interacts with PARP1. Interacts with PML (By similarity).By similarity

GO - Molecular functioni

  • identical protein binding Source: MGI
  • SUMO polymer binding Source: UniProtKB
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi202920. 5 interactors.
IntActiQ9QZS2. 1 interactor.
STRINGi10090.ENSMUSP00000030992.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MP2NMR-C45-69[»]
ProteinModelPortaliQ9QZS2.
SMRiQ9QZS2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 20Required for ubiquitination activityAdd BLAST20
Regioni6 – 65Mediates interaction with TRPS11 PublicationAdd BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi40 – 43SUMO interaction motif 1; mediates the binding to polysumoylated substratesBy similarity4
Motifi50 – 53SUMO interaction motif 2; mediates the binding to polysumoylated substratesBy similarity4
Motifi61 – 63SUMO interaction motif 3; mediates the binding to polysumoylated substratesBy similarity3
Motifi71 – 74SUMO interaction motif 4; mediates the binding to polysumoylated substratesBy similarity4

Domaini

The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate.By similarity
The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri136 – 181RING-typePROSITE-ProRule annotationAdd BLAST46

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0320. Eukaryota.
ENOG410XV78. LUCA.
GeneTreeiENSGT00390000010318.
HOVERGENiHBG018577.
InParanoidiQ9QZS2.
OMAiTHRQYHP.
OrthoDBiEOG091G0AKN.
PhylomeDBiQ9QZS2.
TreeFamiTF328387.

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.
IPR017907. Znf_RING_CS.
PfamiView protein in Pfam
PF13639. zf-RING_2. 1 hit.
SMARTiView protein in SMART
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9QZS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRNPQRKR RGGTVNSRQT QKRTRETTST PEVSLETEPI ELVETVGDEI
60 70 80 90 100
VDLTCESLEP VVVDLTHNDS VVIVEERRRP RRNGRRLRQD HADSCVVSSD
110 120 130 140 150
DEELSRDKDV YVTTHTPRST KDDGATGPRP SGTVSCPICM DGYSEIVQNG
160 170 180 190
RLIVSTECGH VFCSQCLRDS LKNANTCPTC RKKINHKRYH PIYI
Length:194
Mass (Da):21,911
Last modified:May 1, 2000 - v1
Checksum:i9A0A4277725C62E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169300 mRNA. Translation: AAF00620.1.
AK019171 mRNA. Translation: BAB31585.1.
AK090162 mRNA. Translation: BAC41119.1.
AK147057 mRNA. Translation: BAE27641.1.
AK151116 mRNA. Translation: BAE30125.1.
AK158987 mRNA. Translation: BAE34757.1.
AK159778 mRNA. Translation: BAE35362.1.
AK159949 mRNA. Translation: BAE35505.1.
BC003282 mRNA. Translation: AAH03282.1.
U95141 mRNA. Translation: AAC53539.1.
CCDSiCCDS57336.1.
RefSeqiNP_001291198.1. NM_001304269.1.
NP_001291199.1. NM_001304270.1.
NP_035408.1. NM_011278.5.
UniGeneiMm.21281.

Genome annotation databases

EnsembliENSMUST00000030992; ENSMUSP00000030992; ENSMUSG00000029110.
ENSMUST00000182047; ENSMUSP00000138411; ENSMUSG00000029110.
ENSMUST00000182709; ENSMUSP00000138555; ENSMUSG00000029110.
GeneIDi19822.
KEGGimmu:19822.
UCSCiuc008xcc.2. mouse.

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.

Entry informationi

Entry nameiRNF4_MOUSE
AccessioniPrimary (citable) accession number: Q9QZS2
Secondary accession number(s): O35941, Q541Z6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: July 5, 2017
This is version 143 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