ID   UB2E3_HUMAN             Reviewed;         207 AA.
AC   Q969T4; Q5U0R7; Q7Z4W4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   07-JUL-2009, entry version 73.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 E3;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase E3;
DE   AltName: Full=Ubiquitin carrier protein E3;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-23 kDa;
DE   AltName: Full=UbcH9;
DE   AltName: Full=UbcM2;
GN   Name=UBE2E3; Synonyms=UBCE4, UBCH9;
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], TISSUE SPECIFICITY, FUNCTION, AND
RP   MUTAGENESIS OF CYS-145.
RC   TISSUE=Gastric adenocarcinoma;
RX   MEDLINE=99276464; PubMed=10343118;
RA   Ito K., Kato S., Matsuda Y., Kimura M., Okano Y.;
RT   "cDNA cloning, characterization, and chromosome mapping of UBE2E3
RT   (alias UbcH9), encoding an N-terminally extended human ubiquitin-
RT   conjugating enzyme.";
RL   Cytogenet. Cell Genet. 84:99-104(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Umbilical cord blood;
RA   Shen Y., Ye M., Fu G., Zhou J., Zhang Q., Huang Q., Xu S., He K.,
RA   Chen S., Mao M., Chen Z.;
RT   "Human UbcM2 gene, complete cds.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-201.
RA   Xin Y.R., Yu L., Zhao S.Y.;
RT   "Cloning of a new human cDNA homologous to Mus musculus ubiquitin-
RT   conjugating enzyme UbcM2.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and PNS;
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   SUBCELLULAR LOCATION.
RX   PubMed=15545318; DOI=10.1083/jcb.200406001;
RA   Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G.;
RT   "Ubiquitin charging of human class III ubiquitin-conjugating enzymes
RT   triggers their nuclear import.";
RL   J. Cell Biol. 167:649-659(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [9]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Participates in the regulation of transepithelial sodium
CC       transport in renal cells. May be involved in cell growth arrest.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The ubiquitin-loaded form interacts specifically with
CC       importin-11 (IPO11), leading to its import into the nucleus (By
CC       similarity). Interacts with NEDD4L.
CC   -!- INTERACTION:
CC       Q99942:RNF5; NbExp=1; IntAct=EBI-348496, EBI-348482;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and cytoplasm in a IPO11-dependent manner.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Highly
CC       expressed in skeletal muscle.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; AB017644; BAA76544.1; -; mRNA.
DR   EMBL; AF085362; AAD40197.1; -; mRNA.
DR   EMBL; AF136176; AAP97266.1; -; mRNA.
DR   EMBL; BT019345; AAV38152.1; -; mRNA.
DR   EMBL; AC104076; AAY14882.1; -; Genomic_DNA.
DR   EMBL; BC003554; AAH03554.1; -; mRNA.
DR   EMBL; BC092407; AAH92407.1; -; mRNA.
DR   IPI; IPI00056504; -.
DR   RefSeq; NP_006348.1; -.
DR   RefSeq; NP_872619.1; -.
DR   UniGene; Hs.470804; -.
DR   UniGene; Hs.567831; -.
DR   HSSP; P15731; 1QCQ.
DR   SMR; Q969T4; 60-207.
DR   IntAct; Q969T4; 2.
DR   PhosphoSite; Q969T4; -.
DR   PRIDE; Q969T4; -.
DR   Ensembl; ENSG00000170035; Homo sapiens.
DR   GeneID; 10477; -.
DR   KEGG; hsa:10477; -.
DR   UCSC; uc002unq.1; human.
DR   GeneCards; GC02P181553; -.
DR   H-InvDB; HIX0002642; -.
DR   H-InvDB; HIX0056142; -.
DR   HGNC; HGNC:12479; UBE2E3.
DR   HPA; HPA003303; -.
DR   MIM; 604151; gene.
DR   PharmGKB; PA37129; -.
DR   HOGENOM; Q969T4; -.
DR   HOVERGEN; Q969T4; -.
DR   BRENDA; 6.3.2.19; 247.
DR   NextBio; 39740; -.
DR   Bgee; Q969T4; -.
DR   CleanEx; HS_UBE2E3; -.
DR   GermOnline; ENSG00000170035; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
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   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 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; Cytoplasm; Growth regulation; Ligase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Ubl conjugation pathway.
FT   CHAIN         1    207       Ubiquitin-conjugating enzyme E2 E3.
FT                                /FTId=PRO_0000082474.
FT   ACT_SITE    145    145       Glycyl thioester intermediate.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      91     91       Phosphotyrosine (By similarity).
FT   VARIANT     201    201       W -> R (in dbSNP:rs2368192).
FT                                /FTId=VAR_023392.
FT   MUTAGEN     145    145       C->S: Loss of activity.
FT   CONFLICT     65     65       R -> K (in Ref. 3; AAP97266).
FT   CONFLICT     91     91       Y -> C (in Ref. 3; AAP97266).
FT   CONFLICT    101    101       P -> L (in Ref. 3; AAP97266).
FT   CONFLICT    134    134       Y -> D (in Ref. 3; AAP97266).
FT   CONFLICT    159    159       I -> V (in Ref. 3; AAP97266).
FT   CONFLICT    171    171       T -> M (in Ref. 3; AAP97266).
FT   CONFLICT    176    176       A -> V (in Ref. 3; AAP97266).
SQ   SEQUENCE   207 AA;  22913 MW;  821CB1382478DC9F CRC64;
     MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK LSSKTTAKLS
     TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP PGSVYEGGVF FLDITFSSDY
     PFKPPKVTFR TRIYHCNINS QGVICLDILK DNWSPALTIS KVLLSICSLL TDCNPADPLV
     GSIATQYLTN RAEHDRIARQ WTKRYAT
//