ID UB2R2_HUMAN Reviewed; 238 AA. AC Q712K3; D3DRL5; Q9NX64; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 168. DE RecName: Full=Ubiquitin-conjugating enzyme E2 R2; DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386}; 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, INTERACTION WITH RP BTRC, PHOSPHORYLATION AT SER-233, AND MUTAGENESIS OF CYS-93; LEU-97 AND RP SER-233. 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 TISSUE=Carcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary, and Testis; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20061386; DOI=10.1074/jbc.m109.089003; RA David Y., Ziv T., Admon A., Navon A.; RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to RT preferred lysines."; RL J. Biol. Chem. 285:8595-8604(2010). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). 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:0000269|PubMed:12037680, CC ECO:0000269|PubMed:20061386}. 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, ECO:0000269|PubMed:12037680, CC ECO:0000269|PubMed:20061386}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBUNIT: When phosphorylated, interacts with beta-TrCP (BTRC). CC {ECO:0000269|PubMed:12037680}. CC -!- INTERACTION: CC Q712K3; Q92624: APPBP2; NbExp=3; IntAct=EBI-2340879, EBI-743771; CC Q712K3; O15499: GSC2; NbExp=3; IntAct=EBI-2340879, EBI-19954058; CC Q712K3; P50221: MEOX1; NbExp=6; IntAct=EBI-2340879, EBI-2864512; CC Q712K3; O00560: SDCBP; NbExp=3; IntAct=EBI-2340879, EBI-727004; CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. 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; AJ240087; CAC80336.1; -; mRNA. DR EMBL; AK000426; BAA91156.1; -; mRNA. DR EMBL; CR457233; CAG33514.1; -; mRNA. DR EMBL; AL139113; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58479.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58480.1; -; Genomic_DNA. DR EMBL; BC004862; AAH04862.1; -; mRNA. DR EMBL; BC047584; AAH47584.1; -; mRNA. DR CCDS; CCDS6546.1; -. DR RefSeq; NP_060281.2; NM_017811.3. DR PDB; 6NYO; X-ray; 1.50 A; A=1-202. DR PDBsum; 6NYO; -. DR AlphaFoldDB; Q712K3; -. DR SMR; Q712K3; -. DR BioGRID; 120266; 70. DR IntAct; Q712K3; 19. DR MINT; Q712K3; -. DR STRING; 9606.ENSP00000263228; -. DR GlyCosmos; Q712K3; 1 site, 1 glycan. DR GlyGen; Q712K3; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q712K3; -. DR MetOSite; Q712K3; -. DR PhosphoSitePlus; Q712K3; -. DR SwissPalm; Q712K3; -. DR BioMuta; UBE2R2; -. DR DMDM; 74749761; -. DR EPD; Q712K3; -. DR jPOST; Q712K3; -. DR MassIVE; Q712K3; -. DR MaxQB; Q712K3; -. DR PaxDb; 9606-ENSP00000263228; -. DR PeptideAtlas; Q712K3; -. DR ProteomicsDB; 68590; -. DR Pumba; Q712K3; -. DR Antibodypedia; 25301; 192 antibodies from 31 providers. DR DNASU; 54926; -. DR Ensembl; ENST00000263228.4; ENSP00000263228.3; ENSG00000107341.5. DR GeneID; 54926; -. DR KEGG; hsa:54926; -. DR MANE-Select; ENST00000263228.4; ENSP00000263228.3; NM_017811.4; NP_060281.2. DR UCSC; uc003ztm.4; human. DR AGR; HGNC:19907; -. DR CTD; 54926; -. DR DisGeNET; 54926; -. DR GeneCards; UBE2R2; -. DR HGNC; HGNC:19907; UBE2R2. DR HPA; ENSG00000107341; Low tissue specificity. DR MIM; 612506; gene. DR neXtProt; NX_Q712K3; -. DR OpenTargets; ENSG00000107341; -. DR PharmGKB; PA134946881; -. DR VEuPathDB; HostDB:ENSG00000107341; -. DR eggNOG; KOG0425; Eukaryota. DR GeneTree; ENSGT00940000158828; -. DR HOGENOM; CLU_030988_1_2_1; -. DR InParanoid; Q712K3; -. DR OMA; KTSHSSM; -. DR OrthoDB; 149628at2759; -. DR PhylomeDB; Q712K3; -. DR TreeFam; TF101107; -. DR BRENDA; 2.3.2.23; 2681. DR BRENDA; 2.3.2.24; 2681. DR PathwayCommons; Q712K3; -. DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q712K3; -. DR SIGNOR; Q712K3; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 54926; 26 hits in 1165 CRISPR screens. DR ChiTaRS; UBE2R2; human. DR GeneWiki; UBE2R2; -. DR GenomeRNAi; 54926; -. DR Pharos; Q712K3; Tbio. DR PRO; PR:Q712K3; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q712K3; Protein. DR Bgee; ENSG00000107341; Expressed in sperm and 191 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0006513; P:protein monoubiquitination; IDA: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; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR PANTHER; PTHR24067:SF148; UBIQUITIN-CONJUGATING ENZYME E2 R2; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. DR Genevisible; Q712K3; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Ubl conjugation pathway. FT CHAIN 1..238 FT /note="Ubiquitin-conjugating enzyme E2 R2" FT /id="PRO_0000280513" 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 MOD_RES 233 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:12037680, FT ECO:0007744|PubMed:18669648" FT MUTAGEN 93 FT /note="C->S: Loss of function." FT /evidence="ECO:0000269|PubMed:12037680" FT MUTAGEN 97 FT /note="L->S: Loss of function." FT /evidence="ECO:0000269|PubMed:12037680" FT MUTAGEN 233 FT /note="S->A: Abolishes phosphorylation by CK2." FT /evidence="ECO:0000269|PubMed:12037680" FT CONFLICT 39 FT /note="Y -> H (in Ref. 2; BAA91156)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="V -> A (in Ref. 2; BAA91156)" FT /evidence="ECO:0000305" FT HELIX 8..22 FT /evidence="ECO:0007829|PDB:6NYO" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:6NYO" FT STRAND 40..46 FT /evidence="ECO:0007829|PDB:6NYO" FT TURN 52..55 FT /evidence="ECO:0007829|PDB:6NYO" FT STRAND 57..63 FT /evidence="ECO:0007829|PDB:6NYO" FT TURN 66..69 FT /evidence="ECO:0007829|PDB:6NYO" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:6NYO" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:6NYO" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 120..132 FT /evidence="ECO:0007829|PDB:6NYO" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 142..153 FT /evidence="ECO:0007829|PDB:6NYO" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 160..171 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 173..178 FT /evidence="ECO:0007829|PDB:6NYO" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:6NYO" 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 //