GenomeNet

Database: UniProt
Entry: P52487
LinkDB: P52487
Original site: P52487 
ID   UBC84_DROME             Reviewed;         153 AA.
AC   P52487; C4XVG9; Q9VIB4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   09-JUL-2014, entry version 108.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=Ubc84D; ORFNames=CG12799;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8703090; DOI=10.1007/BF02338832;
RA   Robin C., Russell R.J., Medveczky K.M., Oakeshott J.G.;
RT   "Duplication and divergence of the genes of the alpha-esterase cluster
RT   of Drosophila melanogaster.";
RL   J. Mol. Evol. 43:241-252(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; U51051; AAB01150.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54011.1; -; Genomic_DNA.
DR   EMBL; BT088773; ACR82498.1; -; mRNA.
DR   RefSeq; NP_524260.1; NM_079536.3.
DR   UniGene; Dm.5673; -.
DR   ProteinModelPortal; P52487; -.
DR   SMR; P52487; 1-152.
DR   BioGrid; 66090; 9.
DR   DIP; DIP-17217N; -.
DR   IntAct; P52487; 5.
DR   MINT; MINT-330527; -.
DR   STRING; 7227.FBpp0081076; -.
DR   EnsemblMetazoa; FBtr0081552; FBpp0081076; FBgn0017456.
DR   GeneID; 40900; -.
DR   KEGG; dme:Dmel_CG12799; -.
DR   CTD; 40900; -.
DR   FlyBase; FBgn0017456; Ubc84D.
DR   eggNOG; COG5078; -.
DR   GeneTree; ENSGT00740000115416; -.
DR   InParanoid; P52487; -.
DR   KO; K04552; -.
DR   OMA; WKPTTRT; -.
DR   OrthoDB; EOG7GXPD8; -.
DR   PhylomeDB; P52487; -.
DR   SignaLink; P52487; -.
DR   UniPathway; UPA00143; -.
DR   GenomeRNAi; 40900; -.
DR   NextBio; 821190; -.
DR   Bgee; P52487; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:FlyBase.
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   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN         1    153       Ubiquitin-conjugating enzyme E2-18 kDa.
FT                                /FTId=PRO_0000082524.
FT   ACT_SITE     86     86       Glycyl thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   153 AA;  17746 MW;  14464662FA7D2EA9 CRC64;
     MAATRRLTRE LSDLVEAKMS TLRNIESSDE SLLMWTGLLV PEKAPYNKGA FRIEINFPPQ
     YPFMPPKILF KTKIYHPNVD EKGEVCLPII STDNWKPTTR TEQVLQALVA IVHNPEPEHP
     LRSDLAEEFV REHKKFMKTA EEFTKKNAEK RPE
//
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