UB2R2_HUMAN
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 03-AUG-2022, entry version 160.
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}.
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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; 61.
DR IntAct; Q712K3; 19.
DR MINT; Q712K3; -.
DR STRING; 9606.ENSP00000263228; -.
DR GlyGen; Q712K3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q712K3; -.
DR MetOSite; Q712K3; -.
DR PhosphoSitePlus; Q712K3; -.
DR BioMuta; UBE2R2; -.
DR DMDM; 74749761; -.
DR EPD; Q712K3; -.
DR jPOST; Q712K3; -.
DR MassIVE; Q712K3; -.
DR MaxQB; Q712K3; -.
DR PaxDb; Q712K3; -.
DR PeptideAtlas; Q712K3; -.
DR PRIDE; Q712K3; -.
DR ProteomicsDB; 68590; -.
DR Antibodypedia; 25301; 168 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 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; DEYPYQP; -.
DR OrthoDB; 1116856at2759; -.
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; 25 hits in 1088 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 189 other tissues.
DR Genevisible; Q712K3; HS.
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; -; 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 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
