dbPTM

UB2E1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2E1_HUMAN
UniProt AC	P51965
Protein Name	Ubiquitin-conjugating enzyme E2 E1
Gene Name	UBE2E1
Organism	Homo sapiens (Human).
Sequence Length	193
Subcellular Localization	Nucleus .
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination..
Protein Sequence	MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAKRIQKELADITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFTPEYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEHDRMARQWTKRYAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDDDSRAS ------CCCCCCCCC	50.15	28355574
2	Acetylation	------MSDDDSRAS ------CCCCCCCCC	50.15	19413330
6	Phosphorylation	--MSDDDSRASTSSS --CCCCCCCCCCCCC	36.42	28450419
9	Phosphorylation	SDDDSRASTSSSSSS CCCCCCCCCCCCCCC	27.93	22115753
10	Phosphorylation	DDDSRASTSSSSSSS CCCCCCCCCCCCCCC	31.48	28450419
11	Phosphorylation	DDSRASTSSSSSSSS CCCCCCCCCCCCCCC	26.23	28450419
12	Phosphorylation	DSRASTSSSSSSSSN CCCCCCCCCCCCCCC	34.04	28450419
13	Phosphorylation	SRASTSSSSSSSSNQ CCCCCCCCCCCCCCC	33.72	28450419
14	Phosphorylation	RASTSSSSSSSSNQQ CCCCCCCCCCCCCCC	35.87	28450419
15	Phosphorylation	ASTSSSSSSSSNQQT CCCCCCCCCCCCCCC	35.87	28450419
16	Phosphorylation	STSSSSSSSSNQQTE CCCCCCCCCCCCCCC	39.47	28450419
17	Phosphorylation	TSSSSSSSSNQQTEK CCCCCCCCCCCCCCC	34.94	26074081
18	Phosphorylation	SSSSSSSSNQQTEKE CCCCCCCCCCCCCCC	40.37	23401153
22	Phosphorylation	SSSSNQQTEKETNTP CCCCCCCCCCCCCCC	38.98	28450419
24	Ubiquitination	SSNQQTEKETNTPKK CCCCCCCCCCCCCCH	73.55	21906983
26	Phosphorylation	NQQTEKETNTPKKKE CCCCCCCCCCCCHHH	56.30	28450419
28	Phosphorylation	QTEKETNTPKKKESK CCCCCCCCCCHHHHH	43.86	26055452
43	Acetylation	VSMSKNSKLLSTSAK CCCCHHHHHHHHHHH	63.94	25953088
43	Sumoylation	VSMSKNSKLLSTSAK CCCCHHHHHHHHHHH	63.94	-
43	Ubiquitination	VSMSKNSKLLSTSAK CCCCHHHHHHHHHHH	63.94	21906983
43	Sumoylation	VSMSKNSKLLSTSAK CCCCHHHHHHHHHHH	63.94	-
46	Phosphorylation	SKNSKLLSTSAKRIQ CHHHHHHHHHHHHHH	30.65	23312004
47	Phosphorylation	KNSKLLSTSAKRIQK HHHHHHHHHHHHHHH	32.45	23312004
50	Ubiquitination	KLLSTSAKRIQKELA HHHHHHHHHHHHHHH	50.21	-
50	Acetylation	KLLSTSAKRIQKELA HHHHHHHHHHHHHHH	50.21	25953088
54	Ubiquitination	TSAKRIQKELADITL HHHHHHHHHHHHCCC	52.93	-
55	Acetylation	SAKRIQKELADITLD HHHHHHHHHHHCCCC	32.58	-
72	Ubiquitination	PNCSAGPKGDNIYEW CCCCCCCCCCCEEEE	77.35	-
77	Phosphorylation	GPKGDNIYEWRSTIL CCCCCCEEEECCCEE	18.72	28152594
136	Acetylation	VICLDILKDNWSPAL EEEEEHHCCCCCCCH	49.72	26051181
136	Ubiquitination	VICLDILKDNWSPAL EEEEEHHCCCCCCCH	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 UB2E1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2E1_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 UB2E1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEDD4_HUMAN	NEDD4	physical	9990509
RNF14_HUMAN	RNF14	physical	11322894
RNF8_HUMAN	RNF8	physical	11322894
CBWD3_HUMAN	CBWD5	physical	16169070
CBWD5_HUMAN	CBWD5	physical	16169070
PAEP_HUMAN	PAEP	physical	16169070
ATX1_HUMAN	ATXN1	physical	18439907
EPS15_HUMAN	EPS15	physical	17588522
DPOLM_HUMAN	POLM	physical	17588522
DPOLL_HUMAN	POLL	physical	17588522
HDAC6_HUMAN	HDAC6	physical	17588522
UBS3B_HUMAN	UBASH3B	physical	17588522
UFM1_HUMAN	UFM1	physical	19690564
MUL1_HUMAN	MUL1	physical	19690564
CAPS2_HUMAN	CADPS2	physical	19690564
DTX1_HUMAN	DTX1	physical	19690564
RN181_HUMAN	RNF181	physical	19690564
M3K1_HUMAN	MAP3K1	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
RN152_HUMAN	RNF152	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
ZNRF1_HUMAN	ZNRF1	physical	19690564
ZNRF4_HUMAN	ZNRF4	physical	19690564
RNF5_HUMAN	RNF5	physical	19549727
RNF14_HUMAN	RNF14	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
DTX3L_HUMAN	DTX3L	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
RNF10_HUMAN	RNF10	physical	19549727
RN166_HUMAN	RNF166	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
RNF25_HUMAN	RNF25	physical	19549727
BIRC8_HUMAN	BIRC8	physical	19549727
RNF4_HUMAN	RNF4	physical	19549727
RNF37_HUMAN	UBOX5	physical	19549727
RING1_HUMAN	RING1	physical	19549727
MARH3_HUMAN	MARCH3	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
RNF12_HUMAN	RLIM	physical	19549727
RN114_HUMAN	RNF114	physical	19549727
LRSM1_HUMAN	LRSAM1	physical	19549727
RNF11_HUMAN	RNF11	physical	19549727
CHFR_HUMAN	CHFR	physical	19549727
ARI2_HUMAN	ARIH2	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
MGRN1_HUMAN	MGRN1	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
RFWD3_HUMAN	RFWD3	physical	19549727
RN111_HUMAN	RNF111	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
TRIM2_HUMAN	TRIM2	physical	19549727
TRIM1_HUMAN	MID2	physical	21143188
TRI11_HUMAN	TRIM11	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
IPO11_HUMAN	IPO11	physical	11032817
TF65_HUMAN	RELA	physical	14690596
BRE1A_HUMAN	RNF20	physical	16307923
CTR9_HUMAN	CTR9	physical	16307923
LEO1_HUMAN	LEO1	physical	16307923
PAF1_HUMAN	PAF1	physical	16307923
CUL3_HUMAN	CUL3	physical	19256485
ZN827_HUMAN	ZNF827	physical	22939629
UBP7_HUMAN	USP7	physical	23603909
UB2E1_HUMAN	UBE2E1	physical	20061386
SLX5_YEAST	SLX5	physical	18032921
SLX8_YEAST	SLX8	physical	18032921
RNF26_HUMAN	RNF26	physical	19549727
DDA1_HUMAN	DDA1	physical	17452440
ATX1_HUMAN	ATXN1	physical	25641559
FA12_HUMAN	F12	physical	18838541
UB2E1_HUMAN	UBE2E1	physical	25960396
RN114_HUMAN	RNF114	physical	28625874
UBP7_HUMAN	USP7	physical	28073915
OTUB1_HUMAN	OTUB1	physical	28073915
RING1_HUMAN	RING1	physical	28073915
PCGF5_HUMAN	PCGF5	physical	28073915
H2AZ_HUMAN	H2AFZ	physical	28073915
H2AY_HUMAN	H2AFY	physical	28073915
H10_HUMAN	H1F0	physical	28073915

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 UB2E1_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-2; SER-9 AND SER-12, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-77, AND MASSSPECTROMETRY.	19534553 [Abstract]