ID A0A2R9A0Q0_PANPA Unreviewed; 336 AA.
AC A0A2R9A0Q0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase RING2 {ECO:0000256|ARBA:ARBA00019736};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein 1B {ECO:0000256|ARBA:ARBA00030504};
DE AltName: Full=RING finger protein 2 {ECO:0000256|ARBA:ARBA00032293};
DE AltName: Full=RING-type E3 ubiquitin transferase RING2 {ECO:0000256|ARBA:ARBA00030910};
GN Name=RNF2 {ECO:0000313|Ensembl:ENSPPAP00000008813.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000008813.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000008813.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000008813.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AJFE02052096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02052097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02052098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02052099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003815650.1; XM_003815602.3.
DR RefSeq; XP_008966811.1; XM_008968563.2.
DR AlphaFoldDB; A0A2R9A0Q0; -.
DR SMR; A0A2R9A0Q0; -.
DR STRING; 9597.ENSPPAP00000008813; -.
DR Ensembl; ENSPPAT00000031452.1; ENSPPAP00000008813.1; ENSPPAG00000027651.1.
DR GeneID; 100990262; -.
DR KEGG; pps:100990262; -.
DR CTD; 6045; -.
DR GeneTree; ENSGT00940000154499; -.
DR OMA; FCIYIAQ; -.
DR OrthoDB; 460116at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000240080; Chromosome 1.
DR Bgee; ENSPPAG00000027651; Expressed in placenta and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071339; C:MLL1 complex; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0035102; C:PRC1 complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd17167; RAWUL_RING2; 1.
DR CDD; cd16740; RING-HC_RING2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR037937; RING2_RAWUL_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR PANTHER; PTHR46076:SF4; E3 UBIQUITIN-PROTEIN LIGASE RING2; 1.
DR Pfam; PF16207; RAWUL; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 51..91
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 157..208
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"
SQ SEQUENCE 336 AA; 37655 MW; 90EA546E1F4DB7EC CRC64;
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS
NASTHSNQEA GPSNKRTKTS DDSGLELDNN NAAMAIDPVM DGASEIELVF RPHPTLMEKD
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK
//