RING2_DANRE
ID RING2_DANRE Reviewed; 336 AA.
AC Q803I4; Q6PUR9; Q9PTH4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-259.
RA Murray B.W., Sueltmann H., Klein J.;
RT "Identification of a homologue of the murine RING1b gene in zebrafish.";
RL Submitted (OCT-1999) 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=AAS92634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY576996; AAS92634.1; ALT_INIT; mRNA.
DR EMBL; BC044472; AAH44472.1; -; mRNA.
DR EMBL; AF196346; AAF17506.1; -; mRNA.
DR AlphaFoldDB; Q803I4; -.
DR SMR; Q803I4; -.
DR BioGRID; 84269; 4.
DR STRING; 7955.ENSDARP00000002609; -.
DR PaxDb; Q803I4; -.
DR PRIDE; Q803I4; -.
DR Ensembl; ENSDART00000187760; ENSDARP00000149390; ENSDARG00000010381.
DR ZFIN; ZDB-GENE-030131-5243; rnf2.
DR eggNOG; KOG0311; Eukaryota.
DR GeneTree; ENSGT00940000154499; -.
DR HOGENOM; CLU_056557_1_1_1; -.
DR InParanoid; Q803I4; -.
DR PhylomeDB; Q803I4; -.
DR TreeFam; TF105501; -.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DRE-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DRE-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DRE-8953750; Transcriptional Regulation by E2F6.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q803I4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000010381; Expressed in cleaving embryo and 36 other tissues.
DR ExpressionAtlas; Q803I4; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
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:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISS:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:ZFIN.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0033339; P:pectoral fin development; IMP:ZFIN.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:ZFIN.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IGI:ZFIN.
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 Chromosome; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..336
FT /note="E3 ubiquitin-protein ligase RING2"
FT /id="PRO_0000056041"
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 158..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 291
FT /note="Y -> C (in Ref. 2; AAH44472)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="N -> D (in Ref. 2; AAH44472)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Y -> C (in Ref. 2; AAH44472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37539 MW; F35A010695E11013 CRC64;
MTQTVQTNGV QPLSKTWELS LYELQRTPQE AITDGLEIAV SPRSLHSELM CPICLDMLKN
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY
EAHQERVLAR ISKHNNQQAL SHSIEEGLKI QAMNRLQRGK KHQIENGSGA EDNGDSSHCS
NASVHSNQEA GPSIKRTKTS DDSGLDMDNA TENGGGDIAL DGVSEIELVF RPHPTLMEKE
DAAQTRYIKT SGNATVDHLS KYLAVRLALE EMRKNGEASP INVEAASEKQ YTIYIPTASN
QFTVLNGSFS LELVSEKYWK VNKPMELYFA PTKEHK
