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Protein

E3 ubiquitin-protein ligase RING2

Gene

Rnf2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Plays a role in the transcriptional repression of genes that are required for pluripotency in embryonic stem cells, thereby contributing to differentiation of the ectodermal and endodermal germ layers. Association with 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.By similarity

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.By similarity

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)DescriptionActionsGraphical viewLength
Zinc fingeri51 – 91RING-typePROSITE-ProRule annotationAdd BLAST41

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-4551638. SUMOylation of chromatin organization proteins.
R-RNO-8939243. RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
R-RNO-8943724. Regulation of PTEN gene transcription.
R-RNO-8953750. Transcriptional Regulation by E2F6.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RING2 (EC:2.3.2.27By similarity)
Alternative name(s):
RING finger protein 1B
Short name:
RING1b
RING finger protein 2
RING-type E3 ubiquitin transferase RING2Curated
Gene namesi
Name:Rnf2
Synonyms:Ring1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi1305491. Rnf2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002287212 – 308E3 ubiquitin-protein ligase RING2Add BLAST307

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Cross-linki112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei143PhosphoserineBy similarity1
Modified residuei168PhosphoserineBy similarity1
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ4KLY4.

PTM databases

iPTMnetiQ4KLY4.
PhosphoSitePlusiQ4KLY4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000002454.
ExpressionAtlasiQ4KLY4. baseline.
GenevisibleiQ4KLY4. RN.

Interactioni

Subunit structurei

Component of chromatin-associated Polycomb (PcG) complexes. Component of a number of PRC1-like complexes; these complexes contain either the polycomb group ring finger protein PCGF1, or PCGF2, or PCGF3, or BMI1, or PCGF5, or PCGF6. Distinct PRC1-like complexes are composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1, PCGF2, PCGF3, BMI1, PCGF5 or PCGF6), one PHC protein (PHC1, PHC2 or PHC3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8) (By similarity). Part of a complex that contains RNF2, UB2D3 and BMI1; within that complex RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts only with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (By similarity). Part of a complex that contains PCGF5, RNF2 and UBE2D3. Part of a complex that contains AUTS2, PCGF5, RNF2, CSNK2B AND RYBP (By similarity). Interacts with CBX6 and CBX8 (By similarity). Interacts with PHC1, PCGF2, RYBP, CBX7, CBX4, CBX2, RNF1/RING1, BMI1 and PHC2. Interaction with RYBP and CBX7 is mutually exclusive; both compete for the same binding site on RNF2 (By similarity). Component of repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 (By similarity). Interacts with CBX2 and PHC1. Interacts with CHTOP. Interacts with AURKB (By similarity). 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 (By similarity). 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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061975.

Structurei

3D structure databases

ProteinModelPortaliQ4KLY4.
SMRiQ4KLY4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 179Interaction with HIP2By similarityAdd BLAST178
Regioni93 – 98Interaction with nucleosomes via an acidic patch on histone H2A and histone H2BBy similarity6

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.
InParanoidiQ4KLY4.
KOiK10695.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR032443. RAWUL.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
PfamiView protein in Pfam
PF16207. RAWUL. 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.

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

Q4KLY4-1 [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

QFTVSICQ
Length:308
Mass (Da):34,242
Last modified:August 2, 2005 - v1
Checksum:i83E451CA941515C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098941 mRNA. Translation: AAH98941.1.
RefSeqiNP_001020838.1. NM_001025667.1.
UniGeneiRn.19719.

Genome annotation databases

EnsembliENSRNOT00000065944; ENSRNOP00000061975; ENSRNOG00000002454.
GeneIDi304850.
KEGGirno:304850.
UCSCiRGD:1305491. rat.

Similar proteinsi

Entry informationi

Entry nameiRING2_RAT
AccessioniPrimary (citable) accession number: Q4KLY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: August 2, 2005
Last modified: November 22, 2017
This is version 113 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways