Full text data of UBE2R2
UBE2R2
(CDC34B, UBC3B)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-conjugating enzyme E2 R2; 6.3.2.19 (Ubiquitin carrier protein R2; Ubiquitin-conjugating enzyme E2-CDC34B; Ubiquitin-protein ligase R2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-conjugating enzyme E2 R2; 6.3.2.19 (Ubiquitin carrier protein R2; Ubiquitin-conjugating enzyme E2-CDC34B; Ubiquitin-protein ligase R2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q712K3
ID UB2R2_HUMAN Reviewed; 238 AA.
AC Q712K3; D3DRL5; Q9NX64;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 R2;
DE EC=6.3.2.19;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, INTERACTION
RP WITH BTRC, PHOSPHORYLATION AT SER-233, AND MUTAGENESIS OF CYS-93;
RP LEU-97 AND 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
RT UBC3B 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND MASS
RP SPECTROMETRY.
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.
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.,
RA Buerckstuemmer T., 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.
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: When phosphorylated, interacts with beta-TrCP (BTRC).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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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; CAI39656.1; -; 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 RefSeq; NP_060281.2; NM_017811.3.
DR UniGene; Hs.643648; -.
DR ProteinModelPortal; Q712K3; -.
DR SMR; Q712K3; 8-183.
DR IntAct; Q712K3; 11.
DR MINT; MINT-4828298; -.
DR STRING; 9606.ENSP00000263228; -.
DR PhosphoSite; Q712K3; -.
DR DMDM; 74749761; -.
DR PaxDb; Q712K3; -.
DR PeptideAtlas; Q712K3; -.
DR PRIDE; Q712K3; -.
DR Ensembl; ENST00000263228; ENSP00000263228; ENSG00000107341.
DR GeneID; 54926; -.
DR KEGG; hsa:54926; -.
DR UCSC; uc003ztm.3; human.
DR CTD; 54926; -.
DR GeneCards; GC09P033817; -.
DR HGNC; HGNC:19907; UBE2R2.
DR HPA; CAB019438; -.
DR MIM; 612506; gene.
DR neXtProt; NX_Q712K3; -.
DR PharmGKB; PA134946881; -.
DR eggNOG; COG5078; -.
DR HOGENOM; HOG000233454; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; Q712K3; -.
DR KO; K02207; -.
DR OMA; NSEETAM; -.
DR OrthoDB; EOG7VB2HT; -.
DR PhylomeDB; Q712K3; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q712K3; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2R2; human.
DR GeneWiki; UBE2R2; -.
DR GenomeRNAi; 54926; -.
DR NextBio; 58015; -.
DR PRO; PR:Q712K3; -.
DR Bgee; Q712K3; -.
DR CleanEx; HS_UBE2R2; -.
DR Genevestigator; Q712K3; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
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; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 238 Ubiquitin-conjugating enzyme E2 R2.
FT /FTId=PRO_0000280513.
FT COMPBIAS 200 238 Asp/Glu-rich (acidic).
FT ACT_SITE 93 93 Glycyl thioester intermediate.
FT MOD_RES 233 233 Phosphoserine; by CK2.
FT MUTAGEN 93 93 C->S: Loss of function.
FT MUTAGEN 97 97 L->S: Loss of function.
FT MUTAGEN 233 233 S->A: Abolishes phosphorylation by CK2.
FT CONFLICT 39 39 Y -> H (in Ref. 2; BAA91156).
FT CONFLICT 127 127 V -> A (in Ref. 2; BAA91156).
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
//
ID UB2R2_HUMAN Reviewed; 238 AA.
AC Q712K3; D3DRL5; Q9NX64;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 R2;
DE EC=6.3.2.19;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, INTERACTION
RP WITH BTRC, PHOSPHORYLATION AT SER-233, AND MUTAGENESIS OF CYS-93;
RP LEU-97 AND 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
RT UBC3B 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND MASS
RP SPECTROMETRY.
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.
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.,
RA Buerckstuemmer T., 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.
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: When phosphorylated, interacts with beta-TrCP (BTRC).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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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; CAI39656.1; -; 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 RefSeq; NP_060281.2; NM_017811.3.
DR UniGene; Hs.643648; -.
DR ProteinModelPortal; Q712K3; -.
DR SMR; Q712K3; 8-183.
DR IntAct; Q712K3; 11.
DR MINT; MINT-4828298; -.
DR STRING; 9606.ENSP00000263228; -.
DR PhosphoSite; Q712K3; -.
DR DMDM; 74749761; -.
DR PaxDb; Q712K3; -.
DR PeptideAtlas; Q712K3; -.
DR PRIDE; Q712K3; -.
DR Ensembl; ENST00000263228; ENSP00000263228; ENSG00000107341.
DR GeneID; 54926; -.
DR KEGG; hsa:54926; -.
DR UCSC; uc003ztm.3; human.
DR CTD; 54926; -.
DR GeneCards; GC09P033817; -.
DR HGNC; HGNC:19907; UBE2R2.
DR HPA; CAB019438; -.
DR MIM; 612506; gene.
DR neXtProt; NX_Q712K3; -.
DR PharmGKB; PA134946881; -.
DR eggNOG; COG5078; -.
DR HOGENOM; HOG000233454; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; Q712K3; -.
DR KO; K02207; -.
DR OMA; NSEETAM; -.
DR OrthoDB; EOG7VB2HT; -.
DR PhylomeDB; Q712K3; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q712K3; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2R2; human.
DR GeneWiki; UBE2R2; -.
DR GenomeRNAi; 54926; -.
DR NextBio; 58015; -.
DR PRO; PR:Q712K3; -.
DR Bgee; Q712K3; -.
DR CleanEx; HS_UBE2R2; -.
DR Genevestigator; Q712K3; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
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; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 238 Ubiquitin-conjugating enzyme E2 R2.
FT /FTId=PRO_0000280513.
FT COMPBIAS 200 238 Asp/Glu-rich (acidic).
FT ACT_SITE 93 93 Glycyl thioester intermediate.
FT MOD_RES 233 233 Phosphoserine; by CK2.
FT MUTAGEN 93 93 C->S: Loss of function.
FT MUTAGEN 97 97 L->S: Loss of function.
FT MUTAGEN 233 233 S->A: Abolishes phosphorylation by CK2.
FT CONFLICT 39 39 Y -> H (in Ref. 2; BAA91156).
FT CONFLICT 127 127 V -> A (in Ref. 2; BAA91156).
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
//
MIM
612506
*RECORD*
*FIELD* NO
612506
*FIELD* TI
*612506 UBIQUITIN-CONJUGATING ENZYME E2R 2; UBE2R2
;;UBIQUITIN-CONJUGATING ENZYME UBC3B; UBC3B
read more*FIELD* TX
CLONING
Using the casein kinase II (CK2) catalytic subunits alpha (CSNK2A1;
115440) and alpha-prime (CSNK2A2; 115442) as bait in a yeast 2-hybrid
screen of human and mouse cDNA libraries, Semplici et al. (2002) cloned
the full-length cDNAs corresponding to the UBE2R2 gene, which they
designated UBC3B, in both species. Both the human and mouse deduced
UBC3B proteins contain 238 amino acids. UBC3B is highly homologous to
UBC3 (CDC34; 116948), with only 47 amino acid differences, and has the
conserved cysteine and leucine residues that are part of the active site
in ubiquitin-conjugating enzymes (E2). The UBC3B protein shares 35%
sequence identity with S. cerevisiae cdc34.
GENE FUNCTION
Semplici et al. (2002) showed that human UBC3B complemented a yeast
cdc34 temperature-sensitive mutant. Deletion and site-directed
mutagenesis demonstrated that CK2 phosphorylated UBC3B in the C-terminal
domain at serine-233; mutagenesis of the corresponding serine residue at
position 231 of human CDC34/UBC3 showed that this was the major
CK2-phosphorylation site in this protein. In vitro binding experiments
demonstrated that phosphorylated UBC3B and CDC34 bound specifically to
the F-box protein beta-TRCP (BTRC; 603482), which resulted in enhanced
degradation of beta-catenin (116806), a substrate of BTRC. Semplici et
al. (2002) suggested that CK2-dependent phosphorylation of CDC34 and
UBC3B functions by regulating BTRC substrate recognition.
MAPPING
Semplici et al. (2002) stated that the UBC3B gene maps to chromosome
9p22.1.
*FIELD* RF
1. Semplici, F.; Meggio, F.; Pinna, L. A.; Oliviero, S.: CK2-dependent
phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces
its interaction with beta-TrCP and enhances beta-catenin degradation. Oncogene 21:
3978-3987, 2002.
*FIELD* CD
Carol A. Bocchini: 12/23/2008
*FIELD* ED
carol: 12/23/2008
*RECORD*
*FIELD* NO
612506
*FIELD* TI
*612506 UBIQUITIN-CONJUGATING ENZYME E2R 2; UBE2R2
;;UBIQUITIN-CONJUGATING ENZYME UBC3B; UBC3B
read more*FIELD* TX
CLONING
Using the casein kinase II (CK2) catalytic subunits alpha (CSNK2A1;
115440) and alpha-prime (CSNK2A2; 115442) as bait in a yeast 2-hybrid
screen of human and mouse cDNA libraries, Semplici et al. (2002) cloned
the full-length cDNAs corresponding to the UBE2R2 gene, which they
designated UBC3B, in both species. Both the human and mouse deduced
UBC3B proteins contain 238 amino acids. UBC3B is highly homologous to
UBC3 (CDC34; 116948), with only 47 amino acid differences, and has the
conserved cysteine and leucine residues that are part of the active site
in ubiquitin-conjugating enzymes (E2). The UBC3B protein shares 35%
sequence identity with S. cerevisiae cdc34.
GENE FUNCTION
Semplici et al. (2002) showed that human UBC3B complemented a yeast
cdc34 temperature-sensitive mutant. Deletion and site-directed
mutagenesis demonstrated that CK2 phosphorylated UBC3B in the C-terminal
domain at serine-233; mutagenesis of the corresponding serine residue at
position 231 of human CDC34/UBC3 showed that this was the major
CK2-phosphorylation site in this protein. In vitro binding experiments
demonstrated that phosphorylated UBC3B and CDC34 bound specifically to
the F-box protein beta-TRCP (BTRC; 603482), which resulted in enhanced
degradation of beta-catenin (116806), a substrate of BTRC. Semplici et
al. (2002) suggested that CK2-dependent phosphorylation of CDC34 and
UBC3B functions by regulating BTRC substrate recognition.
MAPPING
Semplici et al. (2002) stated that the UBC3B gene maps to chromosome
9p22.1.
*FIELD* RF
1. Semplici, F.; Meggio, F.; Pinna, L. A.; Oliviero, S.: CK2-dependent
phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces
its interaction with beta-TrCP and enhances beta-catenin degradation. Oncogene 21:
3978-3987, 2002.
*FIELD* CD
Carol A. Bocchini: 12/23/2008
*FIELD* ED
carol: 12/23/2008