RNF2
entrez
6045
canonical
uniprot
Q99496
canonical
ensembl
ENSG00000121481
resolver
ensp
ENSP00000356480
resolver
genesymbol
RNF2
resolver
genesymbol_syn
BAP1
resolver
genesymbol_syn
DING
resolver
genesymbol_syn
HIPI3
resolver
genesymbol_syn
RING1B
resolver
hgnc
HGNC:10061
resolver
uniprot
B2RBS7
resolver
uniprot
B3KRH1
resolver
uniprot
Q5TEN1
resolver
uniprot
Q5TEN2
resolver
uniprot_entry
RING2_HUMAN
resolver
uniprot_sec
B2RBS7
resolver
uniprot_sec
B3KRH1
resolver
uniprot_sec
Q5TEN1
resolver
uniprot_sec
Q5TEN2
resolver
amino_acid_sequence
MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK
uniprot
proteins
disease_involvement
DISEASE: Luo-Schoch-Yamamoto syndrome (LUSYAM) [MIM:619460]: An autosomal dominant disorder characterized by intrauterine growth retardation, severe intellectual disability, behavioral problems, early-onset seizures, feeding difficulties, and dysmorphic features. White matter abnormalities and delayed myelination are observed on brain imaging. {ECO:0000269|PubMed:33864376}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: 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 (PubMed:15386022, PubMed:16359901, PubMed:21772249, PubMed:25355358, PubMed:25519132, PubMed:26151332, PubMed:33864376). 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 (By similarity). 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 (PubMed:16359901, PubMed:26151332). PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility (PubMed:26151332). E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4 (PubMed:21772249). 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 (Probable). 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). Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation (By similarity). {ECO:0000250|UniProtKB:Q9CQJ4, ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:20696397, ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:25355358, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:26151332, ECO:0000269|PubMed:33864376, ECO:0000305}.
uniprot
proteins
mass_dalton
37655
uniprot
proteins
mutagenesis
MUTAGEN 41; /note="S->A,D: No effect on ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:25519132"; MUTAGEN 51; /note="C->W: Strong decrease in HIP2-binding; when associated with S-54."; /evidence="ECO:0000269|PubMed:11513855"; MUTAGEN 54; /note="C->S: Strong decrease in HIP2-binding; when associated with W-51."; /evidence="ECO:0000269|PubMed:11513855"; MUTAGEN 56; /note="D->K: Loss of ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:21772249"; MUTAGEN 69; /note="H->Y: Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:15386022"; MUTAGEN 70; /note="R->C: Loss of ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:15386022"; MUTAGEN 81; /note="R->A: Decreases ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:25355358"; MUTAGEN 93; /note="K->A: Mildly decreases ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:25355358"; MUTAGEN 97..98; /note="KR->AA: Loss of ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:21772249"; MUTAGEN 97; /note="K->A: Strongly decreases ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:25355358"; MUTAGEN 98; /note="R->A: Nearly abolishes ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:25355358"; MUTAGEN 168; /note="S->E: Decreases ubiquitin ligase activity on histone H2A."; /evidence="ECO:0000269|PubMed:25519132"; MUTAGEN 247; /note="Y->A: Reduced interaction with CBX7."; /evidence="ECO:0000269|PubMed:20696397"; MUTAGEN 258; /note="H->A: Reduced interaction with CBX7."; /evidence="ECO:0000269|PubMed:20696397"; MUTAGEN 262; /note="Y->A: Reduced interaction with CBX7."; /evidence="ECO:0000269|PubMed:19791798, ECO:0000269|PubMed:20696397
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:26151332}.
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated, by auto-ubiquitination (By similarity). Polyubiquitinated in the presence of UBE2D3 (in vitro) (PubMed:26151332). {ECO:0000250|UniProtKB:Q9CQJ4, ECO:0000269|PubMed:26151332}.
uniprot
proteins
pubmed
11513855
uniprot
proteins
pubmed
11865070
uniprot
proteins
pubmed
12004135
uniprot
proteins
pubmed
12167701
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15386022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
16359901
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16714294
uniprot
proteins
pubmed
16943429
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19636380
uniprot
proteins
pubmed
19791798
uniprot
proteins
pubmed
20696397
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21282530
uniprot
proteins
pubmed
21772249
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25355358
uniprot
proteins
pubmed
25519132
uniprot
proteins
pubmed
26151332
uniprot
proteins
pubmed
26687479
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28720707
uniprot
proteins
pubmed
33864376
uniprot
proteins
sequence_length
336
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. Cytoplasm {ECO:0000250|UniProtKB:Q9CQJ4}. Chromosome {ECO:0000250|UniProtKB:Q9CQJ4}. 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. Co-localizes with SAMD7 in nuclear polycomb bodies. {ECO:0000250|UniProtKB:Q9CQJ4}.
uniprot
proteins