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Ubiquitin-conjugating enzyme E2 T (EC 2.3.2.23) (Cell proliferation-inducing gene 50 protein) (E2 ubiquitin-conjugating enzyme T) (Ubiquitin carrier protein T) (Ubiquitin-protein ligase T)

 UBE2T_HUMAN             Reviewed;         197 AA.
Q9NPD8; Q2TU36;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 150.
RecName: Full=Ubiquitin-conjugating enzyme E2 T;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=Cell proliferation-inducing gene 50 protein;
AltName: Full=E2 ubiquitin-conjugating enzyme T;
AltName: Full=Ubiquitin carrier protein T;
AltName: Full=Ubiquitin-protein ligase T;
Name=UBE2T; ORFNames=HSPC150, PIG50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Okaze H., Hayashi A., Kozuma S., Saito T.;
"Ubiquitin-conjugating enzyme isolog.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Carcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human cell proliferation inducing gene.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91, AND
MUTAGENESIS OF CYS-86.
PubMed=16916645; DOI=10.1016/j.molcel.2006.06.024;
Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M.,
D'Andrea A.D., Dutta A.;
"UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative
autoregulation.";
Mol. Cell 23:589-596(2006).
[10]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FANCL, AND
MUTAGENESIS OF CYS-86.
PubMed=17938197; DOI=10.1128/MCB.00504-07;
Alpi A., Langevin F., Mosedale G., Machida Y.J., Dutta A., Patel K.J.;
"UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited
independently to chromatin: a basis for the regulation of FANCD2
monoubiquitination.";
Mol. Cell. Biol. 27:8421-8430(2007).
[11]
FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91 AND
LYS-182, AND MUTAGENESIS OF CYS-86; LYS-91 AND 182-LYS--LYS-191.
PubMed=19111657; DOI=10.1016/j.molcel.2008.12.003;
Alpi A.F., Pace P.E., Babu M.M., Patel K.J.;
"Mechanistic insight into site-restricted monoubiquitination of FANCD2
by Ube2t, FANCL, and FANCI.";
Mol. Cell 32:767-777(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-86, AND INTERACTION
WITH BRCA1.
PubMed=19887602; DOI=10.1158/0008-5472.CAN-09-1809;
Ueki T., Park J.H., Nishidate T., Kijima K., Hirata K., Nakamura Y.,
Katagiri T.;
"Ubiquitination and downregulation of BRCA1 by ubiquitin-conjugating
enzyme E2T overexpression in human breast cancer cells.";
Cancer Res. 69:8752-8760(2009).
[14]
FUNCTION, AND MUTAGENESIS OF CYS-86.
PubMed=19589784; DOI=10.1074/jbc.C109.038075;
Longerich S., San Filippo J., Liu D., Sung P.;
"FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.";
J. Biol. Chem. 284:23182-23186(2009).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND AUTOUBIQUITINATION.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH FANCL, AND MUTAGENESIS OF PHE-63.
PubMed=21775430; DOI=10.1074/jbc.M111.244632;
Hodson C., Cole A.R., Lewis L.P., Miles J.A., Purkiss A., Walden H.;
"Structural analysis of human FANCL, the E3 ligase in the Fanconi
anemia pathway.";
J. Biol. Chem. 286:32628-32637(2011).
[18]
INDUCTION.
PubMed=21722982; DOI=10.1016/j.radonc.2011.05.059;
Ramaekers C.H., van den Beucken T., Meng A., Kassam S., Thoms J.,
Bristow R.G., Wouters B.G.;
"Hypoxia disrupts the Fanconi anemia pathway and sensitizes cells to
chemotherapy through regulation of UBE2T.";
Radiother. Oncol. 101:190-197(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INVOLVEMENT IN FANCT, VARIANT FANCT GLU-2, AND CHARACTERIZATION OF
VARIANT FANCT GLU-2.
PubMed=26046368; DOI=10.1016/j.ajhg.2015.04.022;
Hira A., Yoshida K., Sato K., Okuno Y., Shiraishi Y., Chiba K.,
Tanaka H., Miyano S., Shimamoto A., Tahara H., Ito E., Kojima S.,
Kurumizaka H., Ogawa S., Takata M., Yabe H., Yabe M.;
"Mutations in the gene encoding the E2 conjugating enzyme UBE2T cause
Fanconi anemia.";
Am. J. Hum. Genet. 96:1001-1007(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191 AND LYS-192, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-167.
Walker J.R., Avvakumov G.V., Newman E.M., Mackenzie F.,
Kozieradzki I., Sundstrom M., Arrowsmith C., Edwards A., Bochkarev A.,
Dhe-Paganon S.;
"Ubiquitin-conjugating enzyme HSPC150.";
Submitted (FEB-2005) to the PDB data bank.
[23] {ECO:0000244|PDB:1YH2}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-167, AND
AUTOUBIQUITINATION.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
[24] {ECO:0000244|PDB:4CCG}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), INTERACTION WITH FANCL, AND
MUTAGENESIS OF SER-5; ARG-60 AND 99-ARG--SER-101.
PubMed=24389026; DOI=10.1016/J.STR.2013.12.004;
Hodson C., Purkiss A., Miles J.A., Walden H.;
"Structure of the human FANCL RING-Ube2T complex reveals determinants
of cognate E3-E2 selection.";
Structure 22:337-344(2014).
[25] {ECO:0000244|PDB:5NGZ}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH INHIBITOR
1-(1,3-BENZOTHIAZOL-2-YL)METHANAMINE, FUNCTION, AND MUTAGENESIS OF
PRO-73.
PubMed=28437106; DOI=10.1021/acs.jmedchem.7b00147;
Morreale F.E., Bortoluzzi A., Chaugule V.K., Arkinson C., Walden H.,
Ciulli A.;
"Allosteric targeting of the Fanconi anemia ubiquitin-conjugating
enzyme Ube2T by fragment screening.";
J. Med. Chem. 60:4093-4098(2017).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. Catalyzes
monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA
repair. Acts as a specific E2 ubiquitin-conjugating enzyme for the
Fanconi anemia complex by associating with E3 ubiquitin-protein
ligase FANCL and catalyzing monoubiquitination of FANCD2, a key
step in the DNA damage pathway (PubMed:16916645, PubMed:17938197,
PubMed:19111657, PubMed:19589784, PubMed:28437106). Also mediates
monoubiquitination of FANCL and FANCI (PubMed:16916645,
PubMed:17938197, PubMed:19111657, PubMed:19589784). May contribute
to ubiquitination and degradation of BRCA1 (PubMed:19887602). In
vitro able to promote polyubiquitination using all 7 ubiquitin Lys
residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-
63'-linked polyubiquitination (PubMed:20061386).
{ECO:0000269|PubMed:16916645, ECO:0000269|PubMed:17938197,
ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:19589784,
ECO:0000269|PubMed:19887602, ECO:0000269|PubMed:20061386,
ECO:0000269|PubMed:28437106}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Directly interacts with FANCL (PubMed:16916645,
PubMed:17938197, PubMed:19111657, PubMed:21775430,
PubMed:24389026). Interacts with BRCA1 (PubMed:19887602).
{ECO:0000269|PubMed:16916645, ECO:0000269|PubMed:17938197,
ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:19887602,
ECO:0000269|PubMed:21775430, ECO:0000269|PubMed:24389026}.
-!- INTERACTION:
Q9NW38-1:FANCL; NbExp=3; IntAct=EBI-2130165, EBI-16088720;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938197,
ECO:0000269|PubMed:19887602}. Note=Accumulates to chromatin.
-!- INDUCTION: Down-regulated following hypoxia. Up-regulated in
breast cancers. {ECO:0000269|PubMed:21722982}.
-!- PTM: Auto-ubiquitinated. Effects of auto-monoubiquitination at
Lys-91 and Lys-182 are unclear: according to a report,
monoubiquitination inactivates E2 enzyme activity
(PubMed:16916645). In contrast, according to another report,
autoubiquitination does not affect E2 enzyme activity
(PubMed:19111657). {ECO:0000269|PubMed:16916645,
ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:20061386,
ECO:0000269|PubMed:22496338}.
-!- DISEASE: Fanconi anemia complementation group T (FANCT)
[MIM:616435]: A disorder affecting all bone marrow elements and
resulting in anemia, leukopenia and thrombopenia. It is associated
with cardiac, renal and limb malformations, dermal pigmentary
changes, and a predisposition to the development of malignancies.
At the cellular level it is associated with hypersensitivity to
DNA-damaging agents, chromosomal instability (increased chromosome
breakage) and defective DNA repair. {ECO:0000269|PubMed:26046368}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; AB032931; BAA93711.1; -; mRNA.
EMBL; AF160215; AAF67016.1; -; mRNA.
EMBL; AF161499; AAF29114.1; -; mRNA.
EMBL; AK000504; BAA91211.1; -; mRNA.
EMBL; AY542309; AAT08178.1; -; mRNA.
EMBL; AL356953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91411.1; -; Genomic_DNA.
EMBL; BC004152; AAH04152.1; -; mRNA.
EMBL; BC019284; AAH19284.1; -; mRNA.
CCDS; CCDS1425.1; -.
RefSeq; NP_001297255.1; NM_001310326.1.
RefSeq; NP_054895.1; NM_014176.3.
UniGene; Hs.5199; -.
PDB; 1YH2; X-ray; 2.00 A; A=1-167.
PDB; 4CCG; X-ray; 2.40 A; A/B=1-197.
PDB; 5NGZ; X-ray; 2.40 A; A=1-197.
PDB; 5OJJ; X-ray; 1.85 A; A/B/C/D/E/F=1-154.
PDBsum; 1YH2; -.
PDBsum; 4CCG; -.
PDBsum; 5NGZ; -.
PDBsum; 5OJJ; -.
ProteinModelPortal; Q9NPD8; -.
SMR; Q9NPD8; -.
BioGrid; 118858; 44.
DIP; DIP-52740N; -.
IntAct; Q9NPD8; 13.
STRING; 9606.ENSP00000356243; -.
iPTMnet; Q9NPD8; -.
PhosphoSitePlus; Q9NPD8; -.
SwissPalm; Q9NPD8; -.
BioMuta; UBE2T; -.
DMDM; 73622065; -.
EPD; Q9NPD8; -.
MaxQB; Q9NPD8; -.
PaxDb; Q9NPD8; -.
PeptideAtlas; Q9NPD8; -.
PRIDE; Q9NPD8; -.
TopDownProteomics; Q9NPD8; -.
DNASU; 29089; -.
Ensembl; ENST00000367274; ENSP00000356243; ENSG00000077152.
GeneID; 29089; -.
KEGG; hsa:29089; -.
UCSC; uc001gxx.5; human.
CTD; 29089; -.
DisGeNET; 29089; -.
EuPathDB; HostDB:ENSG00000077152.9; -.
GeneCards; UBE2T; -.
HGNC; HGNC:25009; UBE2T.
HPA; HPA002831; -.
MalaCards; UBE2T; -.
MIM; 610538; gene.
MIM; 616435; phenotype.
neXtProt; NX_Q9NPD8; -.
OpenTargets; ENSG00000077152; -.
PharmGKB; PA142670655; -.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00540000070023; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; Q9NPD8; -.
KO; K13960; -.
OMA; KIPERYP; -.
OrthoDB; EOG091G0VPD; -.
PhylomeDB; Q9NPD8; -.
TreeFam; TF354203; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
SignaLink; Q9NPD8; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2T; human.
EvolutionaryTrace; Q9NPD8; -.
GenomeRNAi; 29089; -.
PRO; PR:Q9NPD8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000077152; -.
CleanEx; HS_UBE2T; -.
ExpressionAtlas; Q9NPD8; baseline and differential.
Genevisible; Q9NPD8; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
GO; GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Disease mutation;
DNA damage; DNA repair; Fanconi anemia; Isopeptide bond;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 197 Ubiquitin-conjugating enzyme E2 T.
/FTId=PRO_0000082509.
ACT_SITE 86 86 Glycyl thioester intermediate.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 91 91 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16916645,
ECO:0000269|PubMed:19111657}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19111657}.
CROSSLNK 191 191 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 192 192 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 2 2 Q -> E (in FANCT; abolishes FANCD2
monoubiquitination; abolishes interaction
with FANCL; dbSNP:rs774357609).
{ECO:0000269|PubMed:26046368}.
/FTId=VAR_073861.
MUTAGEN 5 5 S->R: No effect on FANCL-binding, nor on
FANCL-dependent monoubiquitination of
FANCD2. {ECO:0000269|PubMed:24389026}.
MUTAGEN 60 60 R->E: Loss of FANCL-binding and of FANCL-
dependent monoubiquitination of FANCD2.
{ECO:0000269|PubMed:24389026}.
MUTAGEN 63 63 F->A: Decreased binding to FANCL.
{ECO:0000269|PubMed:21775430}.
MUTAGEN 73 73 P->K: Decreased FANCD2 ubiquitination.
{ECO:0000269|PubMed:28437106}.
MUTAGEN 86 86 C->A: Loss of E2 enzyme activity.
{ECO:0000269|PubMed:16916645,
ECO:0000269|PubMed:17938197,
ECO:0000269|PubMed:19111657,
ECO:0000269|PubMed:19589784,
ECO:0000269|PubMed:19887602}.
MUTAGEN 91 91 K->R: Decreased monoubiquitination.
{ECO:0000269|PubMed:19111657}.
MUTAGEN 99 101 RPS->SPR: No effect on FANCL-binding, nor
on FANCL-dependent monoubiquitination of
FANCD2. {ECO:0000269|PubMed:24389026}.
MUTAGEN 182 191 Missing: Decreased monoubiquitination.
{ECO:0000269|PubMed:19111657}.
HELIX 1 16 {ECO:0000244|PDB:1YH2}.
STRAND 22 29 {ECO:0000244|PDB:1YH2}.
STRAND 33 39 {ECO:0000244|PDB:1YH2}.
TURN 45 48 {ECO:0000244|PDB:1YH2}.
STRAND 50 56 {ECO:0000244|PDB:1YH2}.
TURN 59 62 {ECO:0000244|PDB:1YH2}.
STRAND 67 72 {ECO:0000244|PDB:1YH2}.
HELIX 88 90 {ECO:0000244|PDB:1YH2}.
TURN 93 95 {ECO:0000244|PDB:1YH2}.
HELIX 104 116 {ECO:0000244|PDB:1YH2}.
HELIX 126 134 {ECO:0000244|PDB:1YH2}.
HELIX 136 150 {ECO:0000244|PDB:1YH2}.
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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