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Protein

E3 ubiquitin-protein ligase RING2

Gene

Rnf2

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 mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Association to the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes.4 Publications

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 fingeri51 – 91RING-typePROSITE-ProRule annotationAdd BLAST41

GO - Molecular functioni

  • chromatin binding Source: MGI
  • ligase activity Source: UniProtKB-KW
  • RING-like zinc finger domain binding Source: MGI
  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • anterior/posterior axis specification Source: MGI
  • gastrulation with mouth forming second Source: MGI
  • germ cell development Source: CACAO
  • histone H2A-K119 monoubiquitination Source: UniProtKB
  • histone H2A monoubiquitination Source: MGI
  • histone ubiquitination Source: MGI
  • mitotic cell cycle Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RING2 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 1B
Short name:
RING1b
RING finger protein 2
Gene namesi
Name:Rnf2
Synonyms:DinG, Ring1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1101759. Rnf2.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells.

GO - Cellular componenti

  • euchromatin Source: MGI
  • heterochromatin Source: MGI
  • MLL1 complex Source: UniProtKB
  • nuclear body Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • PcG protein complex Source: MGI
  • PRC1 complex Source: MGI
  • sex chromatin Source: MGI
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000560392 – 336E3 ubiquitin-protein ligase RING2Add BLAST335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Cross-linki112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei143PhosphoserineBy similarity1
Modified residuei168PhosphoserineBy similarity1

Post-translational modificationi

Polyubiquitinated in the presence of UBE2D3 (in vitro).
Monoubiquitinated, by auto-ubiquitination.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CQJ4.
MaxQBiQ9CQJ4.
PaxDbiQ9CQJ4.
PeptideAtlasiQ9CQJ4.
PRIDEiQ9CQJ4.

PTM databases

iPTMnetiQ9CQJ4.
PhosphoSitePlusiQ9CQJ4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026484.
CleanExiMM_RNF2.
ExpressionAtlasiQ9CQJ4. baseline and differential.
GenevisibleiQ9CQJ4. MM.

Interactioni

Subunit structurei

Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2. Component of a PRC1-like complex. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with RYBP, HIP2 and TFCP2. Association to the chromosomal DNA is cell-cycle dependent. Interacts with CBX4, CBX6, CBX7 and CBX8. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 (By similarity). Component of chromatin-associated Polycomb (PcG) complexes. Interacts with RYBP, PCGF2, CBX2, RNF1/RING1, BMI1, PHC1 and PHC2. Interacts with CHTOP. Interacts with AURKB. Interacts with PCGF1 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q611774EBI-927321,EBI-1216438
Bmi1P2591611EBI-927321,EBI-927401
Cbx8Q9QXV15EBI-927321,EBI-1216641
Kdm1aQ6ZQ883EBI-927321,EBI-1216284
Kdm2bQ6P1G24EBI-927321,EBI-1216214
Pcgf2P2379815EBI-927321,EBI-926857
Phc1Q640283EBI-927321,EBI-927346
Phc2Q9QWH17EBI-927321,EBI-642357
Ring1O357303EBI-927321,EBI-929310
RybpQ8CCI58EBI-927321,EBI-929290
Skp1Q9WTX54EBI-927321,EBI-1202363

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202919. 123 interactors.
DIPiDIP-36109N.
IntActiQ9CQJ4. 58 interactors.
MINTiMINT-1341250.
STRINGi10090.ENSMUSP00000075476.

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 25Combined sources5
Helixi46 – 49Combined sources4
Turni52 – 54Combined sources3
Beta strandi55 – 57Combined sources3
Beta strandi59 – 64Combined sources6
Turni65 – 67Combined sources3
Beta strandi70 – 72Combined sources3
Helixi73 – 81Combined sources9
Turni88 – 90Combined sources3
Helixi97 – 99Combined sources3
Beta strandi100 – 102Combined sources3
Helixi104 – 113Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKLX-ray2.00B1-159[»]
ProteinModelPortaliQ9CQJ4.
SMRiQ9CQJ4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CQJ4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 179Interaction with HIP2By similarityAdd BLAST178

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri51 – 91RING-typePROSITE-ProRule annotationAdd BLAST41

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0311. Eukaryota.
ENOG410XQ5G. LUCA.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ9CQJ4.
KOiK10695.
OMAiPTLMEND.
OrthoDBiEOG091G06VO.
PhylomeDBiQ9CQJ4.
TreeFamiTF105501.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032443. RAWUL.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF16207. RAWUL. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM
60 70 80 90 100
CPICLDMLKN TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL
110 120 130 140 150
RPDPNFDALI SKIYPSRDEY EAHQERVLAR INKHNNQQAL SHSIEEGLKI
160 170 180 190 200
QAMNRLQRGK KQQIENGSGA EDNGDSSHCS NASTHSNQEA GPSNKRTKTS
210 220 230 240 250
DDSGLELDNN NAAVAIDPVM DGASEIELVF RPHPTLMEKD DSAQTRYIKT
260 270 280 290 300
SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
310 320 330
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK
Length:336
Mass (Da):37,623
Last modified:June 1, 2001 - v1
Checksum:i84BA5B3E044DB7EC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti253N → H in BAC41075 (PubMed:16141072).Curated1
Sequence conflicti299S → T in BAC41075 (PubMed:16141072).Curated1
Sequence conflicti304V → L in BAC41075 (PubMed:16141072).Curated1
Sequence conflicti332 – 336TKEHK → FTASGNVR in CAA73380 (PubMed:9312051).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12880 mRNA. Translation: CAA73380.1.
Y12783 mRNA. Translation: CAA73321.1.
AK145767 mRNA. Translation: BAE26638.1.
AK012358 mRNA. Translation: BAB28186.1.
AK013124 mRNA. Translation: BAB28663.1.
AK030319 mRNA. Translation: BAC26898.1.
AK090066 mRNA. Translation: BAC41075.1.
CT010297 mRNA. Translation: CAJ18505.1.
BC020122 mRNA. Translation: AAH20122.1.
CCDSiCCDS15362.1.
RefSeqiNP_035407.1. NM_011277.2.
UniGeneiMm.474038.

Genome annotation databases

EnsembliENSMUST00000076110; ENSMUSP00000075476; ENSMUSG00000026484.
ENSMUST00000187048; ENSMUSP00000140896; ENSMUSG00000026484.
GeneIDi19821.
KEGGimmu:19821.
UCSCiuc007cyx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12880 mRNA. Translation: CAA73380.1.
Y12783 mRNA. Translation: CAA73321.1.
AK145767 mRNA. Translation: BAE26638.1.
AK012358 mRNA. Translation: BAB28186.1.
AK013124 mRNA. Translation: BAB28663.1.
AK030319 mRNA. Translation: BAC26898.1.
AK090066 mRNA. Translation: BAC41075.1.
CT010297 mRNA. Translation: CAJ18505.1.
BC020122 mRNA. Translation: AAH20122.1.
CCDSiCCDS15362.1.
RefSeqiNP_035407.1. NM_011277.2.
UniGeneiMm.474038.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKLX-ray2.00B1-159[»]
ProteinModelPortaliQ9CQJ4.
SMRiQ9CQJ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202919. 123 interactors.
DIPiDIP-36109N.
IntActiQ9CQJ4. 58 interactors.
MINTiMINT-1341250.
STRINGi10090.ENSMUSP00000075476.

PTM databases

iPTMnetiQ9CQJ4.
PhosphoSitePlusiQ9CQJ4.

Proteomic databases

EPDiQ9CQJ4.
MaxQBiQ9CQJ4.
PaxDbiQ9CQJ4.
PeptideAtlasiQ9CQJ4.
PRIDEiQ9CQJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076110; ENSMUSP00000075476; ENSMUSG00000026484.
ENSMUST00000187048; ENSMUSP00000140896; ENSMUSG00000026484.
GeneIDi19821.
KEGGimmu:19821.
UCSCiuc007cyx.1. mouse.

Organism-specific databases

CTDi6045.
MGIiMGI:1101759. Rnf2.

Phylogenomic databases

eggNOGiKOG0311. Eukaryota.
ENOG410XQ5G. LUCA.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ9CQJ4.
KOiK10695.
OMAiPTLMEND.
OrthoDBiEOG091G06VO.
PhylomeDBiQ9CQJ4.
TreeFamiTF105501.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.

Miscellaneous databases

EvolutionaryTraceiQ9CQJ4.
PROiQ9CQJ4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026484.
CleanExiMM_RNF2.
ExpressionAtlasiQ9CQJ4. baseline and differential.
GenevisibleiQ9CQJ4. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032443. RAWUL.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF16207. RAWUL. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRING2_MOUSE
AccessioniPrimary (citable) accession number: Q9CQJ4
Secondary accession number(s): O35699
, O35729, Q4FJV5, Q8C1X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 146 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.