dbPTM

UB2E3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2E3_HUMAN
UniProt AC	Q969T4
Protein Name	Ubiquitin-conjugating enzyme E2 E3
Gene Name	UBE2E3
Organism	Homo sapiens (Human).
Sequence Length	207
Subcellular Localization	Nucleus . Cytoplasm . Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner.
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest..
Protein Sequence	MSSDRQRSDDESPSTSSGSSDADQRDPAAPEPEEQEERKPSATQQKKNTKLSSKTTAKLSTSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSSDYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYLTNRAEHDRIARQWTKRYAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSDRQRSD ------CCCCCCCCC	40.73	28450419
2	Acetylation	------MSSDRQRSD ------CCCCCCCCC	40.73	19413330
3	Phosphorylation	-----MSSDRQRSDD -----CCCCCCCCCC	35.20	28450419
8	Phosphorylation	MSSDRQRSDDESPST CCCCCCCCCCCCCCC	40.87	29255136
12	Phosphorylation	RQRSDDESPSTSSGS CCCCCCCCCCCCCCC	31.01	22167270
14	Phosphorylation	RSDDESPSTSSGSSD CCCCCCCCCCCCCCC	50.64	22167270
15	Phosphorylation	SDDESPSTSSGSSDA CCCCCCCCCCCCCCH	30.23	22167270
16	Phosphorylation	DDESPSTSSGSSDAD CCCCCCCCCCCCCHH	36.72	23927012
17	Phosphorylation	DESPSTSSGSSDADQ CCCCCCCCCCCCHHH	42.66	23927012
19	Phosphorylation	SPSTSSGSSDADQRD CCCCCCCCCCHHHCC	27.30	23927012
20	Phosphorylation	PSTSSGSSDADQRDP CCCCCCCCCHHHCCC	40.10	23927012
39	Ubiquitination	PEEQEERKPSATQQK HHHHHHHCCCHHHHH	46.75	-
58	Ubiquitination	LSSKTTAKLSTSAKR CCHHHHHHHHHHHHH	40.66	-
58	Acetylation	LSSKTTAKLSTSAKR CCHHHHHHHHHHHHH	40.66	25953088
60	Phosphorylation	SKTTAKLSTSAKRIQ HHHHHHHHHHHHHHH	21.43	28348404
68	Ubiquitination	TSAKRIQKELAEITL HHHHHHHHHHHHCCC	52.93	-
86	Ubiquitination	PNCSAGPKGDNIYEW CCCCCCCCCCCEEEE	77.35	-
91	Phosphorylation	GPKGDNIYEWRSTIL CCCCCCEEEECCCEE	18.72	21082442
150	Ubiquitination	VICLDILKDNWSPAL EEEEHHHCCCCCCCH	49.72	21906983

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 UB2E3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2E3_HUMAN !!

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 UB2E3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RNF14_HUMAN	RNF14	physical	11322894
RNF8_HUMAN	RNF8	physical	11322894
UFM1_HUMAN	UFM1	physical	19690564
MUL1_HUMAN	MUL1	physical	19690564
CAPS2_HUMAN	CADPS2	physical	19690564
CNOT4_HUMAN	CNOT4	physical	19690564
RN181_HUMAN	RNF181	physical	19690564
RMD5B_HUMAN	RMND5B	physical	19690564
RN111_HUMAN	RNF111	physical	19690564
RNF13_HUMAN	RNF13	physical	19690564
GOLI_HUMAN	RNF130	physical	19690564
RN150_HUMAN	RNF150	physical	19690564
RN165_HUMAN	RNF165	physical	19690564
RN167_HUMAN	RNF167	physical	19690564
RNF25_HUMAN	RNF25	physical	19690564
RNF43_HUMAN	RNF43	physical	19690564
RN115_HUMAN	RNF115	physical	19690564
ZNRF4_HUMAN	ZNRF4	physical	19690564
RNF5_HUMAN	RNF5	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
RN114_HUMAN	RNF114	physical	19549727
RNF11_HUMAN	RNF11	physical	19549727
DTX3L_HUMAN	DTX3L	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
RNF10_HUMAN	RNF10	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
RNF25_HUMAN	RNF25	physical	19549727
RNF4_HUMAN	RNF4	physical	19549727
RING1_HUMAN	RING1	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
RNF14_HUMAN	RNF14	physical	19549727
CHFR_HUMAN	CHFR	physical	19549727
ARI2_HUMAN	ARIH2	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
RFWD3_HUMAN	RFWD3	physical	19549727
RN111_HUMAN	RNF111	physical	19549727
RN166_HUMAN	RNF166	physical	19549727
TRIM2_HUMAN	TRIM2	physical	19549727
TRIM1_HUMAN	MID2	physical	21143188
TRI18_HUMAN	MID1	physical	21143188
TRI32_HUMAN	TRIM32	physical	21143188
TRI27_HUMAN	TRIM27	physical	21143188
TRI50_HUMAN	TRIM50	physical	21143188
TRI37_HUMAN	TRIM37	physical	21143188
DET1_HUMAN	DET1	physical	17452440
DDB1_HUMAN	DDB1	physical	17452440
DDA1_HUMAN	DDA1	physical	17452440
IPO11_HUMAN	IPO11	physical	15545318
NF2L2_HUMAN	NFE2L2	physical	20484052
UB2E3_HUMAN	UBE2E3	physical	20484052
UBC_HUMAN	UBC	physical	22496338
CUL3_HUMAN	CUL3	physical	19256485
RCBT1_HUMAN	RCBTB1	physical	19256485
RCBT2_HUMAN	RCBTB2	physical	19256485
KLH42_HUMAN	KLHL42	physical	19256485
SPOP_HUMAN	SPOP	physical	19256485
CUL1_HUMAN	CUL1	physical	19256485
CUL4A_HUMAN	CUL4A	physical	19256485
RNF25_HUMAN	RNF25	physical	24901938
UB2E3_HUMAN	UBE2E3	physical	20061386
TRI39_HUMAN	TRIM39	physical	25416956
RN185_HUMAN	RNF185	physical	25416956
RAGP1_HUMAN	RANGAP1	physical	9920803
RNF25_HUMAN	RNF25	physical	28514442
RNF10_HUMAN	RNF10	physical	28514442
PECR_HUMAN	PECR	physical	28514442
UBP15_HUMAN	USP15	physical	28514442
UBB_HUMAN	UBB	physical	28514442
OTUB1_HUMAN	OTUB1	physical	28514442
RN220_HUMAN	RNF220	physical	28514442
TOPRS_HUMAN	TOPORS	physical	28514442
RCBT2_HUMAN	RCBTB2	physical	28514442
PCGF3_HUMAN	PCGF3	physical	28514442
UBP7_HUMAN	USP7	physical	28514442
CSK22_HUMAN	CSNK2A2	physical	28514442
FBRS_HUMAN	FBRS	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UB2E3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	15302935 [Abstract]