ID   RNG2B_XENLA             Reviewed;         343 AA.
AC   Q7ZWM8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=E3 ubiquitin-protein ligase RING2-B;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q99496};
DE   AltName: Full=RING finger protein 1B-B;
DE            Short=RING1b-B;
DE   AltName: Full=RING finger protein 2-B;
DE   AltName: Full=RING-type E3 ubiquitin transferase RING2-B {ECO:0000305};
GN   Name=rnf2-b; Synonyms=ring1b-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) 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. 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.
CC       {ECO:0000250|UniProtKB:Q99496, 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 PRC1-like complex. Component of some MLL1/MLL complex
CC       (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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC046935; AAH46935.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q7ZWM8; -.
DR   SMR; Q7ZWM8; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Genome assembly.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; 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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076; PTHR46076; 2.
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   Chromosome; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..343
FT                   /note="E3 ubiquitin-protein ligase RING2-B"
FT                   /id="PRO_0000228722"
FT   ZN_FING         47..87
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          2..180
FT                   /note="Interaction with HIP2"
FT                   /evidence="ECO:0000250|UniProtKB:Q99496"
FT   REGION          89..94
FT                   /note="Interaction with nucleosomes via an acidic patch on
FT                   histone H2A and histone H2B"
FT                   /evidence="ECO:0000250|UniProtKB:Q99496"
FT   REGION          147..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  38082 MW;  59F59A06517B9F79 CRC64;
     MATPVTAQCS SKTWELSLYE LHRTPQAIMD GTEIAVSPRS LHSELMCPIC LDMLKNTMTT
     KECLHRFCSD CIVTALRSGN KECPTCRKKL VSKRSLRPDP NFDALISKIY PSRDEYEAHQ
     DRVLAKLSRL HNQQALSSSI EEGLKMQAMH RAQRVRKHQH ESDNTTFSGG EDNCDSRSHV
     SNPSVHSNQE AGPSRKRSRA SEDSGAEPDL SHEGGVRSPD PPGGGENGSE IELVFRAHPL
     LVEKDGYSQT RYVKTTANAT VDHLSKYLAL RIALEEEALR GGAEGVTVGE VSEKQYTIYI
     CTGAAGGQYT TLNGSLTLEL VNEKYWKISK PLELYYAPTK EQK