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Protein

E3 ubiquitin-protein ligase RING2

Gene

Rnf2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes (By similarity).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-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:Ring1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi1305491. Rnf2.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 308307E3 ubiquitin-protein ligase RING2PRO_0000228721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Cross-linki112 – 112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)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, Ubl conjugation

Proteomic databases

PaxDbiQ4KLY4.

PTM databases

PhosphoSiteiQ4KLY4.

Expressioni

Gene expression databases

ExpressionAtlasiQ4KLY4. baseline and differential.
GenevisibleiQ4KLY4. RN.

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. 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 similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061975.

Structurei

3D structure databases

ProteinModelPortaliQ4KLY4.
SMRiQ4KLY4. Positions 15-114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 179178Interaction with HIP2By similarityAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0311. Eukaryota.
ENOG410XQ5G. LUCA.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ4KLY4.
KOiK10695.
OMAiPTLMEND.
OrthoDBiEOG7NGQC3.

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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ4KLY4.
SMRiQ4KLY4. Positions 15-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061975.

PTM databases

PhosphoSiteiQ4KLY4.

Proteomic databases

PaxDbiQ4KLY4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6045.
RGDi1305491. Rnf2.

Phylogenomic databases

eggNOGiKOG0311. Eukaryota.
ENOG410XQ5G. LUCA.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ4KLY4.
KOiK10695.
OMAiPTLMEND.
OrthoDBiEOG7NGQC3.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi653721.
PROiQ4KLY4.

Gene expression databases

ExpressionAtlasiQ4KLY4. baseline and differential.
GenevisibleiQ4KLY4. RN.

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...

Publicationsi

  1. "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 nameiRING2_RAT
AccessioniPrimary (citable) accession number: Q4KLY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: August 2, 2005
Last modified: May 11, 2016
This is version 98 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.