ID A0A0G2JTP7_RAT Unreviewed; 336 AA. AC A0A0G2JTP7; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 03-MAY-2023, entry version 54. DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; GN Name=Rnf2 {ECO:0000313|EMBL:EDM09570.1, GN ECO:0000313|Ensembl:ENSRNOP00000068794.1, ECO:0000313|RGD:1305491}; GN ORFNames=rCG_46168 {ECO:0000313|EMBL:EDM09570.1}; 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|Ensembl:ENSRNOP00000068794.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000068794.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068794.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|EMBL:EDM09570.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM09570.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [3] {ECO:0000313|EMBL:EDM09570.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM09570.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F., RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSRNOP00000068794.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068794.1}; RG Ensembl; RL Submitted (JAN-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 --------------------------------------------------------------------------- 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; CH473958; EDM09570.1; -; Genomic_DNA. DR RefSeq; XP_006250052.1; XM_006249990.3. DR RefSeq; XP_006250053.1; XM_006249991.3. DR Ensembl; ENSRNOT00000092053.2; ENSRNOP00000068794.1; ENSRNOG00000002454.8. DR GeneID; 304850; -. DR CTD; 6045; -. DR RGD; 1305491; Rnf2. DR GeneTree; ENSGT00940000154499; -. DR OMA; VLNFCIY; -. DR OrthoDB; 460116at2759; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000002494; Chromosome 13. DR Bgee; ENSRNOG00000002454; Expressed in thymus and 20 other tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035518; P:histone H2A monoubiquitination; IEA:InterPro. 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 1: Evidence at protein level; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JTP7}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; 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" SQ SEQUENCE 336 AA; 37623 MW; 84BA5B3E044DB7EC 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 QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK //