RING2_PONAB
ID RING2_PONAB Reviewed; 336 AA.
AC Q5R9J5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=E3 ubiquitin-protein ligase RING2;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q99496};
DE AltName: Full=RING finger protein 1B;
DE Short=RING1b;
DE AltName: Full=RING finger protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase RING2 {ECO:0000305};
GN Name=RNF2; Synonyms=RING1B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role
CC in histone code and gene regulation. H2AK119Ub gives a specific tag for
CC epigenetic transcriptional repression and participates in X chromosome
CC inactivation of female mammals. May be involved in the initiation of
CC both imprinted and random X inactivation. Essential component of a
CC Polycomb group (PcG) multiprotein PRC1-like complex, a complex class
CC required to maintain the transcriptionally repressive state of many
CC genes, including Hox genes, throughout development. PcG PRC1 complex
CC acts via chromatin remodeling and modification of histones, rendering
CC chromatin heritably changed in its expressibility. E3 ubiquitin-protein
CC ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3
CC ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may
CC rather act as a modulator of RNF2/RING2 activity. Plays a role in the
CC transcriptional repression of genes that are required for pluripotency
CC in embryonic stem cells, thereby contributing to differentiation of the
CC ectodermal and endodermal germ layers. Association with the chromosomal
CC DNA is cell-cycle dependent. In resting B- and T-lymphocytes,
CC interaction with AURKB leads to block its activity, thereby maintaining
CC transcription in resting lymphocytes. Also acts as a negative regulator
CC of autophagy by mediating ubiquitination of AMBRA1, leading to its
CC subsequent degradation. {ECO:0000250|UniProtKB:Q9CQJ4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q99496};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q99496}.
CC -!- SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes.
CC Component of a number of PRC1-like complexes; these complexes contain
CC either the polycomb group ring finger protein PCGF1, or PCGF2, or
CC PCGF3, or BMI1, or PCGF5, or PCGF6. Distinct PRC1-like complexes are
CC composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF
CC proteins (PCGF1, PCGF2, PCGF3, BMI1, PCGF5 or PCGF6), one PHC protein
CC (PHC1, PHC2 or PHC3) and one of the CBX proteins (CBX2, CBX4, CBX6,
CC CBX7 or CBX8) (By similarity). Part of a complex that contains RNF2,
CC UB2D3 and BMI1; within that complex RNF2 and BMI1 form a tight
CC heterodimer, where UB2D3 interacts only with RNF2. The complex composed
CC of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with
CC nucleosomal histone H2A (By similarity). Part of a complex that
CC contains PCGF5, RNF2 and UBE2D3. Part of a complex that contains AUTS2,
CC PCGF5, RNF2, CSNK2B AND RYBP (By similarity). Interacts with CBX6 and
CC CBX8 (By similarity). Interacts with PHC1, PCGF2, RYBP, CBX7, CBX4,
CC CBX2, RNF1/RING1, BMI1 and PHC2. Interaction with RYBP and CBX7 is
CC mutually exclusive; both compete for the same binding site on RNF2 (By
CC similarity). Component of repressive BCOR complex containing a Polycomb
CC group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 (By
CC similarity). Interacts with CBX2 and PHC1. Interacts with CHTOP.
CC Interacts with AURKB (By similarity). Part of the E2F6.com-1 complex in
CC G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1,
CC RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2 (By similarity).
CC Component of some MLL1/MLL complex, at least composed of the core
CC components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as
CC the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Interacts with RYBP, HIP2 and TFCP2 (By similarity). Interacts
CC with NUPR1 (By similarity). {ECO:0000250|UniProtKB:Q99496,
CC ECO:0000250|UniProtKB:Q9CQJ4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CQJ4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9CQJ4}. Chromosome
CC {ECO:0000250|UniProtKB:Q9CQJ4}. Note=Enriched on inactive X chromosome
CC (Xi) in female trophoblast stem (TS) cells as well as differentiating
CC embryonic stem (ES) cells. The enrichment on Xi is transient during TS
CC and ES cell differentiation. The association with Xi is mitotically
CC stable in non-differentiated TS cells. {ECO:0000250|UniProtKB:Q9CQJ4}.
CC -!- PTM: Monoubiquitinated, by auto-ubiquitination (By similarity).
CC Polyubiquitinated in the presence of UBE2D3 (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:Q99496, ECO:0000250|UniProtKB:Q9CQJ4}.
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DR EMBL; CR859392; CAH91565.1; -; mRNA.
DR RefSeq; NP_001127433.1; NM_001133961.1.
DR AlphaFoldDB; Q5R9J5; -.
DR BMRB; Q5R9J5; -.
DR SMR; Q5R9J5; -.
DR STRING; 9601.ENSPPYP00000000473; -.
DR GeneID; 100174504; -.
DR KEGG; pon:100174504; -.
DR CTD; 6045; -.
DR eggNOG; KOG0311; Eukaryota.
DR InParanoid; Q5R9J5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISS:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR037937; RING2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076; PTHR46076; 1.
DR PANTHER; PTHR46076:SF4; PTHR46076:SF4; 1.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Cytoplasm; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT CHAIN 2..336
FT /note="E3 ubiquitin-protein ligase RING2"
FT /id="PRO_0000056040"
FT ZN_FING 51..91
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 2..179
FT /note="Interaction with HIP2"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT REGION 93..98
FT /note="Interaction with nucleosomes via an acidic patch on
FT histone H2A and histone H2B"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT REGION 157..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9CQJ4"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
SQ SEQUENCE 336 AA; 37639 MW; FCE1787E5F4DB7FC CRC64;
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS
NASTHSNQEA GPSNKRTKTS DDSGLEPDNN NAAMAIDPVM DGASEIELVF RPHPTLMEKD
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK
