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Database: UniProt
Entry: Q9NPD8
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ID   UBE2T_HUMAN             Reviewed;         197 AA.
AC   Q9NPD8; Q2TU36;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-OCT-2014, entry version 120.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 T;
DE            EC=6.3.2.19;
DE   AltName: Full=Cell proliferation-inducing gene 50 protein;
DE   AltName: Full=Ubiquitin carrier protein T;
DE   AltName: Full=Ubiquitin-protein ligase T;
GN   Name=UBE2T; ORFNames=HSPC150, PIG50;
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].
RA   Okaze H., Hayashi A., Kozuma S., Saito T.;
RT   "Ubiquitin-conjugating enzyme isolog.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA   Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA   Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA   Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT   axis and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for
RT   300 previously undefined genes expressed in CD34+ hematopoietic
RT   stem/progenitor cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim J.W.;
RT   "Identification of a human cell proliferation inducing gene.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [9]
RP   FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91, AND
RP   MUTAGENESIS OF CYS-86.
RX   PubMed=16916645; DOI=10.1016/j.molcel.2006.06.024;
RA   Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M.,
RA   D'Andrea A.D., Dutta A.;
RT   "UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative
RT   autoregulation.";
RL   Mol. Cell 23:589-596(2006).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FANCL, AND
RP   MUTAGENESIS OF CYS-86.
RX   PubMed=17938197; DOI=10.1128/MCB.00504-07;
RA   Alpi A., Langevin F., Mosedale G., Machida Y.J., Dutta A., Patel K.J.;
RT   "UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited
RT   independently to chromatin: a basis for the regulation of FANCD2
RT   monoubiquitination.";
RL   Mol. Cell. Biol. 27:8421-8430(2007).
RN   [11]
RP   FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91 AND
RP   LYS-182, AND MUTAGENESIS OF CYS-86; LYS-91 AND 182-LYS--LYS-191.
RX   PubMed=19111657; DOI=10.1016/j.molcel.2008.12.003;
RA   Alpi A.F., Pace P.E., Babu M.M., Patel K.J.;
RT   "Mechanistic insight into site-restricted monoubiquitination of FANCD2
RT   by Ube2t, FANCL, and FANCI.";
RL   Mol. Cell 32:767-777(2008).
RN   [12]
RP   IDENTIFICATION BY 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   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-86, AND INTERACTION
RP   WITH BRCA1.
RX   PubMed=19887602; DOI=10.1158/0008-5472.CAN-09-1809;
RA   Ueki T., Park J.H., Nishidate T., Kijima K., Hirata K., Nakamura Y.,
RA   Katagiri T.;
RT   "Ubiquitination and downregulation of BRCA1 by ubiquitin-conjugating
RT   enzyme E2T overexpression in human breast cancer cells.";
RL   Cancer Res. 69:8752-8760(2009).
RN   [14]
RP   FUNCTION, AND MUTAGENESIS OF CYS-86.
RX   PubMed=19589784; DOI=10.1074/jbc.C109.038075;
RA   Longerich S., San Filippo J., Liu D., Sung P.;
RT   "FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.";
RL   J. Biol. Chem. 284:23182-23186(2009).
RN   [15]
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   [16]
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).
RN   [17]
RP   INTERACTION WITH FANCL, AND MUTAGENESIS OF PHE-63.
RX   PubMed=21775430; DOI=10.1074/jbc.M111.244632;
RA   Hodson C., Cole A.R., Lewis L.P., Miles J.A., Purkiss A., Walden H.;
RT   "Structural analysis of human FANCL, the E3 ligase in the Fanconi
RT   anemia pathway.";
RL   J. Biol. Chem. 286:32628-32637(2011).
RN   [18]
RP   INDUCTION.
RX   PubMed=21722982; DOI=10.1016/j.radonc.2011.05.059;
RA   Ramaekers C.H., van den Beucken T., Meng A., Kassam S., Thoms J.,
RA   Bristow R.G., Wouters B.G.;
RT   "Hypoxia disrupts the Fanconi anemia pathway and sensitizes cells to
RT   chemotherapy through regulation of UBE2T.";
RL   Radiother. Oncol. 101:190-197(2011).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-167.
RA   Walker J.R., Avvakumov G.V., Newman E.M., Mackenzie F.,
RA   Kozieradzki I., Sundstrom M., Arrowsmith C., Edwards A., Bochkarev A.,
RA   Dhe-Paganon S.;
RT   "Ubiquitin-conjugating enzyme HSPC150.";
RL   Submitted (FEB-2005) to the PDB data bank.
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Catalyzes
CC       monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA
CC       repair: acts as a specific E2 ubiquitin-conjugating enzyme for the
CC       Fanconi anemia complex by associating with E3 ubiquitin-protein
CC       ligase FANCL and catalyzing monoubiquitination of FANCD2, a key
CC       step in the DNA damage pathway. Also mediates monoubiquitination
CC       of FANCL and FANCI. May contribute to ubiquitination and
CC       degradation of BRCA1. In vitro able to promote polyubiquitination
CC       using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-,
CC       'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
CC       {ECO:0000269|PubMed:16916645, ECO:0000269|PubMed:17938197,
CC       ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:19589784,
CC       ECO:0000269|PubMed:19887602, ECO:0000269|PubMed:20061386}.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine. {ECO:0000255|PROSITE-
CC       ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with FANCL and BRCA1.
CC       {ECO:0000269|PubMed:16916645, ECO:0000269|PubMed:17938197,
CC       ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:19887602,
CC       ECO:0000269|PubMed:21775430}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938197,
CC       ECO:0000269|PubMed:19887602}. Note=Accumulates to chromatin.
CC   -!- INDUCTION: Down-regulated following hypoxia. Up-regulated in
CC       breast cancers. {ECO:0000269|PubMed:21722982}.
CC   -!- PTM: Auto-ubiquitinated. Effects of auto-monoubiquitination at
CC       Lys-91 and Lys-182 are unclear: according to a report,
CC       monoubiquitination inactivates E2 enzyme activity
CC       (PubMed:16916645). In contrast, according to another report,
CC       autoubiquitination does not affect E2 enzyme activity
CC       (PubMed:19111657). {ECO:0000269|PubMed:16916645,
CC       ECO:0000269|PubMed:19111657}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AB032931; BAA93711.1; -; mRNA.
DR   EMBL; AF160215; AAF67016.1; -; mRNA.
DR   EMBL; AF161499; AAF29114.1; -; mRNA.
DR   EMBL; AK000504; BAA91211.1; -; mRNA.
DR   EMBL; AY542309; AAT08178.1; -; mRNA.
DR   EMBL; AL356953; CAI15933.1; -; Genomic_DNA.
DR   EMBL; CH471067; EAW91411.1; -; Genomic_DNA.
DR   EMBL; BC004152; AAH04152.1; -; mRNA.
DR   EMBL; BC019284; AAH19284.1; -; mRNA.
DR   CCDS; CCDS1425.1; -.
DR   RefSeq; NP_054895.1; NM_014176.3.
DR   UniGene; Hs.5199; -.
DR   PDB; 1YH2; X-ray; 2.00 A; A=1-167.
DR   PDB; 4CCG; X-ray; 2.40 A; A/B=1-197.
DR   PDBsum; 1YH2; -.
DR   PDBsum; 4CCG; -.
DR   ProteinModelPortal; Q9NPD8; -.
DR   SMR; Q9NPD8; 1-154.
DR   BioGrid; 118858; 29.
DR   DIP; DIP-52740N; -.
DR   IntAct; Q9NPD8; 10.
DR   STRING; 9606.ENSP00000356243; -.
DR   PhosphoSite; Q9NPD8; -.
DR   DMDM; 73622065; -.
DR   MaxQB; Q9NPD8; -.
DR   PaxDb; Q9NPD8; -.
DR   PRIDE; Q9NPD8; -.
DR   DNASU; 29089; -.
DR   Ensembl; ENST00000367274; ENSP00000356243; ENSG00000077152.
DR   GeneID; 29089; -.
DR   KEGG; hsa:29089; -.
DR   UCSC; uc001gxx.4; human.
DR   CTD; 29089; -.
DR   GeneCards; GC01M202300; -.
DR   HGNC; HGNC:25009; UBE2T.
DR   HPA; HPA002831; -.
DR   MIM; 610538; gene.
DR   neXtProt; NX_Q9NPD8; -.
DR   PharmGKB; PA142670655; -.
DR   eggNOG; COG5078; -.
DR   GeneTree; ENSGT00540000070023; -.
DR   HOGENOM; HOG000233455; -.
DR   HOVERGEN; HBG063308; -.
DR   InParanoid; Q9NPD8; -.
DR   KO; K13960; -.
DR   OMA; IVPERYP; -.
DR   OrthoDB; EOG7BP84K; -.
DR   PhylomeDB; Q9NPD8; -.
DR   TreeFam; TF354203; -.
DR   Reactome; REACT_18410; Fanconi Anemia pathway.
DR   SignaLink; Q9NPD8; -.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; UBE2T; human.
DR   EvolutionaryTrace; Q9NPD8; -.
DR   GenomeRNAi; 29089; -.
DR   NextBio; 52094; -.
DR   PRO; PR:Q9NPD8; -.
DR   Bgee; Q9NPD8; -.
DR   CleanEx; HS_UBE2T; -.
DR   Genevestigator; Q9NPD8; -.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0070534; P:protein K63-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   3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair;
KW   Isopeptide bond; Ligase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    197       Ubiquitin-conjugating enzyme E2 T.
FT                                /FTId=PRO_0000082509.
FT   ACT_SITE     86     86       Glycyl thioester intermediate.
FT   CROSSLNK     91     91       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16916645,
FT                                ECO:0000269|PubMed:19111657}.
FT   CROSSLNK    182    182       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19111657}.
FT   MUTAGEN      63     63       F->A: Decreased binding to FANCL.
FT                                {ECO:0000269|PubMed:21775430}.
FT   MUTAGEN      86     86       C->A: Loss of E2 enzyme activity.
FT                                {ECO:0000269|PubMed:16916645,
FT                                ECO:0000269|PubMed:17938197,
FT                                ECO:0000269|PubMed:19111657,
FT                                ECO:0000269|PubMed:19589784,
FT                                ECO:0000269|PubMed:19887602}.
FT   MUTAGEN      91     91       K->R: Decreased monoubiquitination.
FT                                {ECO:0000269|PubMed:19111657}.
FT   MUTAGEN     182    191       Missing: Decreased monoubiquitination.
FT                                {ECO:0000269|PubMed:19111657}.
FT   HELIX         1     16
FT   STRAND       22     29
FT   STRAND       33     39
FT   TURN         45     48
FT   STRAND       50     56
FT   TURN         59     62
FT   STRAND       67     72
FT   HELIX        88     90
FT   TURN         93     95
FT   HELIX       104    116
FT   HELIX       126    134
FT   HELIX       136    150
SQ   SEQUENCE   197 AA;  22521 MW;  6C02D774A7FA928A CRC64;
     MQRASRLKRE LHMLATEPPP GITCWQDKDQ MDDLRAQILG GANTPYEKGV FKLEVIIPER
     YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP SLNIATVLTS IQLLMSEPNP
     DDPLMADISS EFKYNKPAFL KNARQWTEKH ARQKQKADEE EMLDNLPEAG DSRVHNSTQK
     RKASQLVGIE KKFHPDV
//
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