ID M5AJY0_RAT Unreviewed; 308 AA.
AC M5AJY0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
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};
DE Flags: Fragment;
GN Name=Rnf2 {ECO:0000313|EMBL:BAN09113.1, ECO:0000313|RGD:1305491};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|EMBL:BAN09113.1};
RN [1] {ECO:0000313|EMBL:BAN09113.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:BAN09113.1};
RA Takahashi M.;
RT "Expression of RingA and B in the rat hindbrain.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB568264; BAN09113.1; -; mRNA.
DR RefSeq; NP_001020838.1; NM_001025667.1.
DR AlphaFoldDB; M5AJY0; -.
DR SMR; M5AJY0; -.
DR KEGG; rno:304850; -.
DR RGD; 1305491; Rnf2.
DR OrthoDB; 460116at2759; -.
DR UniPathway; UPA00143; -.
DR ExpressionAtlas; M5AJY0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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..206
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 NON_TER 308
FT /evidence="ECO:0000313|EMBL:BAN09113.1"
SQ SEQUENCE 308 AA; 34242 MW; 83E451CA941515C1 CRC64;
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS
NASTHSNQEA GPSNKRTKTS DDSGLELDNN NAAVAIDPVM DGASEIELVF RPHPTLMEKD
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
QFTVSICQ
//
