dbPTM

UBE2T_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE2T_HUMAN
UniProt AC	Q9NPD8
Protein Name	Ubiquitin-conjugating enzyme E2 T
Gene Name	UBE2T
Organism	Homo sapiens (Human).
Sequence Length	197
Subcellular Localization	Nucleus . Accumulates to chromatin.
Protein Description	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]
Protein Sequence	MQRASRLKRELHMLATEPPPGITCWQDKDQMDDLRAQILGGANTPYEKGVFKLEVIIPERYPFEPPQIRFLTPIYHPNIDSAGRICLDVLKLPPKGAWRPSLNIATVLTSIQLLMSEPNPDDPLMADISSEFKYNKPAFLKNARQWTEKHARQKQKADEEEMLDNLPEAGDSRVHNSTQKRKASQLVGIEKKFHPDV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Acetylation	GITCWQDKDQMDDLR CCCCCCCHHHHHHHH	34.46	26051181
28	Ubiquitination	GITCWQDKDQMDDLR CCCCCCCHHHHHHHH	34.46	-
44	Phosphorylation	QILGGANTPYEKGVF HHHCCCCCCCCCCCE	27.06	29759185
46	Phosphorylation	LGGANTPYEKGVFKL HCCCCCCCCCCCEEE	28.38	29759185
48	Ubiquitination	GANTPYEKGVFKLEV CCCCCCCCCCEEEEE	55.31	21906983
48	Acetylation	GANTPYEKGVFKLEV CCCCCCCCCCEEEEE	55.31	27452117
48	Ubiquitination	GANTPYEKGVFKLEV CCCCCCCCCCEEEEE	55.31	21890473
72	Phosphorylation	PPQIRFLTPIYHPNI CCEEEEECCCCCCCC	12.62	-
91	Ubiquitination	RICLDVLKLPPKGAW CEEEEHHCCCCCCCC	59.81	21906983
91	Acetylation	RICLDVLKLPPKGAW CEEEEHHCCCCCCCC	59.81	26051181
91	Ubiquitination	RICLDVLKLPPKGAW CEEEEHHCCCCCCCC	59.81	21890473
136	Ubiquitination	SSEFKYNKPAFLKNA CHHHCCCCHHHHHHH	34.33	-
141	Ubiquitination	YNKPAFLKNARQWTE CCCHHHHHHHHHHHH	41.95	-
156	Ubiquitination	KHARQKQKADEEEML HHHHHHHHCCHHHHH	65.91	21906983
161	Acetylation	KQKADEEEMLDNLPE HHHCCHHHHHHCCCH	42.89	19608861
161	Ubiquitination	KQKADEEEMLDNLPE HHHCCHHHHHHCCCH	42.89	19608861
172	Phosphorylation	NLPEAGDSRVHNSTQ CCCHHCCCCCCCHHH	34.97	25849741
177	Phosphorylation	GDSRVHNSTQKRKAS CCCCCCCHHHHHHHH	19.82	25627689
178	Phosphorylation	DSRVHNSTQKRKASQ CCCCCCHHHHHHHHH	43.35	25849741
180	Ubiquitination	RVHNSTQKRKASQLV CCCCHHHHHHHHHHH	56.82	21890473
182	Ubiquitination	HNSTQKRKASQLVGI CCHHHHHHHHHHHCC	60.47	21906983
184	Phosphorylation	STQKRKASQLVGIEK HHHHHHHHHHHCCCC	27.38	23401153
191	Ubiquitination	SQLVGIEKKFHPDV- HHHHCCCCCCCCCC-	59.84	21906983
191	Acetylation	SQLVGIEKKFHPDV- HHHHCCCCCCCCCC-	59.84	23749302
191	Ubiquitination	SQLVGIEKKFHPDV- HHHHCCCCCCCCCC-	59.84	21890473
191	Sumoylation	SQLVGIEKKFHPDV- HHHHCCCCCCCCCC-	59.84	28112733
192	Ubiquitination	QLVGIEKKFHPDV-- HHHCCCCCCCCCC--	35.79	-
192	Sumoylation	QLVGIEKKFHPDV-- HHHCCCCCCCCCC--	35.79	28112733

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of UBE2T_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
91	K	ubiquitylation	16916645
Effects of auto-monoubiquitination at Lys-91 and Lys-182 are unclear: according to a report, monoubiquitination inactivates E2 enzyme activity.
182	K	ubiquitylation	19111657
Effects of auto-monoubiquitination at Lys-91 and Lys-182 are unclear: according to a report, monoubiquitination inactivates E2 enzyme activity.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of UBE2T_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AMFR_HUMAN	AMFR	physical	19690564
PCGF2_HUMAN	PCGF2	physical	19690564
RNF4_HUMAN	RNF4	physical	19690564
ARI2_HUMAN	ARIH2	physical	19549727
TRI27_HUMAN	TRIM27	physical	19549727
R144B_HUMAN	RNF144B	physical	19549727
LNX2_HUMAN	LNX2	physical	19549727
MARH5_HUMAN	MARCH5	physical	19549727
MGRN1_HUMAN	MGRN1	physical	19549727
RN128_HUMAN	RNF128	physical	19549727
FANCL_HUMAN	FANCL	physical	16916645
BRCA1_HUMAN	BRCA1	physical	19887602
VINEX_HUMAN	SORBS3	physical	22939629
FANCL_HUMAN	FANCL	physical	24623813
UBE2T_HUMAN	UBE2T	physical	19111657
UBE2T_HUMAN	UBE2T	physical	20061386
FANCL_HUMAN	FANCL	physical	25464845
RACK1_HUMAN	GNB2L1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
SRA1_HUMAN	SRA1	physical	26344197
UBE2T_HUMAN	UBE2T	physical	26046368
FANCL_HUMAN	FANCL	physical	26046368
FACD2_HUMAN	FANCD2	physical	26046368
UBE2T_HUMAN	UBE2T	physical	26149689
FANCB_HUMAN	FANCB	physical	28514442
FP100_HUMAN	C17orf70	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616435	Fanconi anemia complementation group T (FANCT)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UBE2T_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASSSPECTROMETRY.	17287340 [Abstract]
Ubiquitylation
Reference	PubMed
"Mechanistic insight into site-restricted monoubiquitination of FANCD2by Ube2t, FANCL, and FANCI."; Alpi A.F., Pace P.E., Babu M.M., Patel K.J.; Mol. Cell 32:767-777(2008). Cited for: FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91 ANDLYS-182, AND MUTAGENESIS OF CYS-86; LYS-91 AND 182-LYS--LYS-191.	19111657 [Abstract]
"UBE2T is the E2 in the Fanconi anemia pathway and undergoes negativeautoregulation."; Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M.,D'Andrea A.D., Dutta A.; Mol. Cell 23:589-596(2006). Cited for: FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91, ANDMUTAGENESIS OF CYS-86.	16916645 [Abstract]

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