UB2E2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UB2E2_HUMAN
• UniProt AC: Q96LR5
• Protein Name: Ubiquitin-conjugating enzyme E2 E2
• Gene Name: UBE2E2
• Organism: Homo sapiens (Human).
• Sequence Length: 201
• 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. Catalyzes the ISGylation of influenza A virus NS1 protein..
• Protein Sequence: MSTEAQRVDDSPSTSGGSSDGDQRESVQQEPEREQVQPKKKEGKISSKTAAKLSTSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSPDYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEHDRMARQWTKRYAT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTEAQRVD ------CCCCCCCCC	34.65	19413330
2	Phosphorylation	------MSTEAQRVD ------CCCCCCCCC	34.65	23090842
3	Phosphorylation	-----MSTEAQRVDD -----CCCCCCCCCC	33.76	23090842
11	Phosphorylation	EAQRVDDSPSTSGGS CCCCCCCCCCCCCCC	19.11	23927012
13	Phosphorylation	QRVDDSPSTSGGSSD CCCCCCCCCCCCCCC	38.87	23927012
14	Phosphorylation	RVDDSPSTSGGSSDG CCCCCCCCCCCCCCH	34.47	23927012
15	Phosphorylation	VDDSPSTSGGSSDGD CCCCCCCCCCCCCHH	45.56	30278072
18	Phosphorylation	SPSTSGGSSDGDQRE CCCCCCCCCCHHHHH	28.87	30278072
19	Phosphorylation	PSTSGGSSDGDQRES CCCCCCCCCHHHHHH	49.22	30278072
26	Phosphorylation	SDGDQRESVQQEPER CCHHHHHHHHCCCHH	27.67	30108239
44	"N6,N6-dimethyllysine"	QPKKKEGKISSKTAA CCCCCCCCCCHHHHH	40.27	-
44	Methylation	QPKKKEGKISSKTAA CCCCCCCCCCHHHHH	40.27	-
48	Acetylation	KEGKISSKTAAKLST CCCCCCHHHHHHHHH	35.08	20167786
49	Phosphorylation	EGKISSKTAAKLSTS CCCCCHHHHHHHHHH	33.52	27251275
52	Methylation	ISSKTAAKLSTSAKR CCHHHHHHHHHHHHH	40.27	-
52	Acetylation	ISSKTAAKLSTSAKR CCHHHHHHHHHHHHH	40.27	25953088
52	"N6,N6-dimethyllysine"	ISSKTAAKLSTSAKR CCHHHHHHHHHHHHH	40.27	-
54	Phosphorylation	SKTAAKLSTSAKRIQ HHHHHHHHHHHHHHH	21.43	27251275
55	Phosphorylation	KTAAKLSTSAKRIQK HHHHHHHHHHHHHHH	43.04	28348404
56	Phosphorylation	TAAKLSTSAKRIQKE HHHHHHHHHHHHHHH	28.54	30177828
58	Ubiquitination	AKLSTSAKRIQKELA HHHHHHHHHHHHHHH	50.21	23000965
62	Ubiquitination	TSAKRIQKELAEITL HHHHHHHHHHHHCCC	52.93	23000965
80	Ubiquitination	PNCSAGPKGDNIYEW CCCCCCCCCCCEEEE	77.35	21963094
85	Phosphorylation	GPKGDNIYEWRSTIL CCCCCCEEEECCCEE	18.72	28152594
144	Ubiquitination	VICLDILKDNWSPAL EEEEEHHCCCCCCCH	49.72	21906983

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

Oops, there are no upstream regulatory protein records of UB2E2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UB2E2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UB2E2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RNF14_HUMAN	RNF14	physical	11322894
RNF8_HUMAN	RNF8	physical	11322894
PCGF2_HUMAN	PCGF2	physical	19690564
RNF5_HUMAN	RNF5	physical	19549727
RNF14_HUMAN	RNF14	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
RN114_HUMAN	RNF114	physical	19549727
RNF11_HUMAN	RNF11	physical	19549727
ARI2_HUMAN	ARIH2	physical	19549727
DTX3L_HUMAN	DTX3L	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
TRI23_HUMAN	TRIM23	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
RNF25_HUMAN	RNF25	physical	19549727
XIAP_HUMAN	XIAP	physical	19549727
RN125_HUMAN	RNF125	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
CHFR_HUMAN	CHFR	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
RNF10_HUMAN	RNF10	physical	19549727
RN111_HUMAN	RNF111	physical	19549727
RN166_HUMAN	RNF166	physical	19549727
TRIM2_HUMAN	TRIM2	physical	19549727
MTG8_HUMAN	RUNX1T1	physical	18073335
PRAM_HUMAN	PRAM1	physical	18073335
SIAH1_HUMAN	SIAH1	physical	18073335
RNF12_HUMAN	RLIM	physical	18073335
HDAC2_HUMAN	HDAC2	physical	18073335
PRKN_HUMAN	PARK2	physical	20089136
RNF8_HUMAN	RNF8	physical	20023648
RNF8_HUMAN	RNF8	physical	21911360
TRIM1_HUMAN	MID2	physical	21143188
TRI18_HUMAN	MID1	physical	21143188
TRI32_HUMAN	TRIM32	physical	21143188
TRI50_HUMAN	TRIM50	physical	21143188
TRI37_HUMAN	TRIM37	physical	21143188
TRI27_HUMAN	TRIM27	physical	21143188
TRI31_HUMAN	TRIM31	physical	21143188
MINT_HUMAN	SPEN	physical	16583136
NF2L2_HUMAN	NFE2L2	physical	20484052
CUL3_HUMAN	CUL3	physical	19256485
A4_HUMAN	APP	physical	21832049
UNG_HUMAN	UNG	physical	22939629
UB2E2_HUMAN	UBE2E2	physical	20061386
RNF14_HUMAN	RNF14	physical	25224329
RN103_HUMAN	RNF103	physical	25224329
DAZP2_HUMAN	DAZAP2	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
TRI39_HUMAN	TRIM39	physical	25416956
ARRD3_HUMAN	ARRDC3	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
DDA1_HUMAN	DDA1	physical	17452440
DZIP3_HUMAN	DZIP3	physical	21516116
RNF25_HUMAN	RNF25	physical	28514442
UBP15_HUMAN	USP15	physical	28514442
OTUB1_HUMAN	OTUB1	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-19, AND MASSSPECTROMETRY.
PubMed: 19413330