ID   UB2Q2_MOUSE             Reviewed;         378 AA.
AC   Q8K2Z8; Q3UBX3; Q3V3A5; Q8BUN2; Q8BVX5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   25-NOV-2008, entry version 58.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 Q2;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase Q2;
DE   AltName: Full=Ubiquitin carrier protein Q2;
GN   Name=Ube2q2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Fetal head, Hippocampus, and Thymus;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   THR-235.
RC   STRAIN=FVB/N; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2Z8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2Z8-2; Sequence=VSP_017300;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; AK083216; BAC38813.1; -; mRNA.
DR   EMBL; AK076148; BAC36218.1; -; mRNA.
DR   EMBL; AK042515; BAE20633.1; -; mRNA.
DR   EMBL; AK150776; BAE29841.1; -; mRNA.
DR   EMBL; BC029111; AAH29111.1; -; mRNA.
DR   RefSeq; NP_850931.1; -.
DR   UniGene; Mm.207894; -.
DR   SMR; Q8K2Z8; 204-365.
DR   PhosphoSite; Q8K2Z8; -.
DR   Ensembl; ENSMUSG00000032307; Mus musculus.
DR   GeneID; 109161; -.
DR   KEGG; mmu:109161; -.
DR   MGI; MGI:2388672; Ube2q2.
DR   HOGENOM; Q8K2Z8; -.
DR   HOVERGEN; Q8K2Z8; -.
DR   NextBio; 361712; -.
DR   ArrayExpress; Q8K2Z8; -.
DR   CleanEx; MM_UBE2Q2; -.
DR   GermOnline; ENSMUSG00000032307; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006575; RWD.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   PANTHER; PTHR11621; UBQ-conjugat_E2; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism;
KW   Ubl conjugation pathway.
FT   CHAIN         1    378       Ubiquitin-conjugating enzyme E2 Q2.
FT                                /FTId=PRO_0000223880.
FT   COMPBIAS     41     56       Pro-rich.
FT   COMPBIAS    138    181       Glu-rich.
FT   ACT_SITE    307    307       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     372    372       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    123       Missing (in isoform 2).
FT                                /FTId=VSP_017300.
FT   VARIANT     235    235       I -> T (in strain: FVB/N).
FT   CONFLICT    246    246       L -> Q (in Ref. 1; BAC38813).
SQ   SEQUENCE   378 AA;  42935 MW;  4A81D0AC4BD302E3 CRC64;
     MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PPPPPPPGSS LSPPPPLTLH
     CNITESYPSS SPIWFVDSDD PNLTSVLERL EDTKNNSSLR QQLKWLICDL CRLYNLPKHL
     DVEMLDQPLP TGQNGTTEEV TSEEEEEEEM AEDIEDLDHY EMKEEEPING KKSEDEGIEK
     ENLAILEKIR KTQRQDHLNG AVSGSVQASD RLMKELRDVY RSQSYKAGIY SVELINDSLY
     DWHVKLHKVD SDSPLHSDLQ ILKEKEGIEY ILLNFSFKDN FPFDPPFVRV VLPVLSGGYV
     LGGGALCMEL LTKQGWSSAY SIESVIMQIN ATLVKGKARV QFGANKNQYN LARAQQSYNS
     IVQIHEKNGW YTPPKEDG
//