UB2R2_MOUSE
ID UB2R2_MOUSE Reviewed; 238 AA.
AC Q6ZWZ2; Q8BW18; Q8VDE5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 R2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme R2;
DE AltName: Full=Ubiquitin carrier protein R2;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-CDC34B;
DE AltName: Full=Ubiquitin-protein ligase R2;
GN Name=Ube2r2; Synonyms=Cdc34b, Ubc3b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12037680; DOI=10.1038/sj.onc.1205574;
RA Semplici F., Meggio F., Pinna L.A., Oliviero S.;
RT "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B
RT induces its interaction with beta-TrCP and enhances beta-catenin
RT degradation.";
RL Oncogene 21:3978-3987(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, Lung, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes
CC monoubiquitination and 'Lys-48'-linked polyubiquitination. May be
CC involved in degradation of katenin. {ECO:0000250|UniProtKB:Q712K3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: When phosphorylated, interacts with beta-TrCP (BTRC).
CC {ECO:0000250|UniProtKB:Q712K3}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AJ240086; CAC80335.1; -; mRNA.
DR EMBL; AK003550; BAB22850.1; -; mRNA.
DR EMBL; AK007517; BAB25085.1; -; mRNA.
DR EMBL; AK075703; BAC35899.1; -; mRNA.
DR EMBL; AK075714; BAC35904.1; -; mRNA.
DR EMBL; AL807823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011112; AAH11112.1; -; mRNA.
DR CCDS; CCDS18057.1; -.
DR RefSeq; NP_080551.1; NM_026275.4.
DR AlphaFoldDB; Q6ZWZ2; -.
DR SMR; Q6ZWZ2; -.
DR BioGRID; 212312; 20.
DR IntAct; Q6ZWZ2; 4.
DR MINT; Q6ZWZ2; -.
DR STRING; 10090.ENSMUSP00000038813; -.
DR iPTMnet; Q6ZWZ2; -.
DR PhosphoSitePlus; Q6ZWZ2; -.
DR EPD; Q6ZWZ2; -.
DR MaxQB; Q6ZWZ2; -.
DR PaxDb; Q6ZWZ2; -.
DR PeptideAtlas; Q6ZWZ2; -.
DR PRIDE; Q6ZWZ2; -.
DR ProteomicsDB; 298167; -.
DR Antibodypedia; 25301; 168 antibodies from 31 providers.
DR DNASU; 67615; -.
DR Ensembl; ENSMUST00000040008; ENSMUSP00000038813; ENSMUSG00000036241.
DR GeneID; 67615; -.
DR KEGG; mmu:67615; -.
DR UCSC; uc008sij.1; mouse.
DR CTD; 54926; -.
DR MGI; MGI:1914865; Ube2r2.
DR VEuPathDB; HostDB:ENSMUSG00000036241; -.
DR eggNOG; KOG0425; Eukaryota.
DR GeneTree; ENSGT00940000158828; -.
DR HOGENOM; CLU_030988_1_2_1; -.
DR InParanoid; Q6ZWZ2; -.
DR OMA; DEYPYQP; -.
DR OrthoDB; 1116856at2759; -.
DR PhylomeDB; Q6ZWZ2; -.
DR TreeFam; TF101107; -.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67615; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ube2r2; mouse.
DR PRO; PR:Q6ZWZ2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6ZWZ2; protein.
DR Bgee; ENSMUSG00000036241; Expressed in undifferentiated genital tubercle and 264 other tissues.
DR Genevisible; Q6ZWZ2; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..238
FT /note="Ubiquitin-conjugating enzyme E2 R2"
FT /id="PRO_0000280514"
FT DOMAIN 8..174
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 194..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 233
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q712K3"
FT CONFLICT 16
FT /note="E -> D (in Ref. 2; BAC35899)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="R -> L (in Ref. 2; BAC35899)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="V -> L (in Ref. 2; BAC35899)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="E -> Y (in Ref. 2; BAC35899)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="D -> Y (in Ref. 2; BAC35899)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="R -> T (in Ref. 1; CAC80335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 27166 MW; E896CF0116A56308 CRC64;
MAQQQMTSSQ KALMLELKSL QEEPVEGFRI TLVDESDLYN WEVAIFGPPN TLYEGGYFKA
HIKFPIDYPY SPPTFRFLTK MWHPNIYENG DVCISILHPP VDDPQSGELP SERWNPTQNV
RTILLSVISL LNEPNTFSPA NVDASVMFRK WRDSKGKDKE YAEIIRKQVS ATKAEAEKDG
VKVPTTLAEY CIKTKVPSND NSSDLLYDDL YDDDIDDEDE EEEDADCYDD DDSGNEES
