dbPTM

UBE2N_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE2N_HUMAN
UniProt AC	P61088
Protein Name	Ubiquitin-conjugating enzyme E2 N
Gene Name	UBE2N
Organism	Homo sapiens (Human).
Sequence Length	152
Subcellular Localization	Nucleus . Cytoplasm .
Protein Description	The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes..
Protein Sequence	MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGLPRRII ------CCCCCHHHH	28.38	-
10	Acetylation	GLPRRIIKETQRLLA CCCHHHHHHHHHHHC	52.95	21791702
10	Ubiquitination	GLPRRIIKETQRLLA CCCHHHHHHHHHHHC	52.95	21890473
24	Ubiquitination	AEPVPGIKAEPDESN CCCCCCCCCCCCCCC	53.24	21890473
24	Sumoylation	AEPVPGIKAEPDESN CCCCCCCCCCCCCCC	53.24	-
24	Acetylation	AEPVPGIKAEPDESN CCCCCCCCCCCCCCC	53.24	23236377
34	Phosphorylation	PDESNARYFHVVIAG CCCCCCCEEEEEEEC	8.81	28152594
45	Phosphorylation	VIAGPQDSPFEGGTF EEECCCCCCCCCCEE	26.66	-
53	Acetylation	PFEGGTFKLELFLPE CCCCCEEEEEEECCC	40.67	7960459
64	Sulfoxidation	FLPEEYPMAAPKVRF ECCCCCCCCCCCEEE	4.93	30846556
68	Ubiquitination	EYPMAAPKVRFMTKI CCCCCCCCEEEEECC	41.12	21906983
68	2-Hydroxyisobutyrylation	EYPMAAPKVRFMTKI CCCCCCCCEEEEECC	41.12	-
74	2-Hydroxyisobutyrylation	PKVRFMTKIYHPNVD CCEEEEECCCCCCHH	29.49	-
74	Acetylation	PKVRFMTKIYHPNVD CCEEEEECCCCCCHH	29.49	23236377
74	Ubiquitination	PKVRFMTKIYHPNVD CCEEEEECCCCCCHH	29.49	21890473
76	Nitration	VRFMTKIYHPNVDKL EEEEECCCCCCHHHH	16.87	-
76	Phosphorylation	VRFMTKIYHPNVDKL EEEEECCCCCCHHHH	16.87	28152594
82	Malonylation	IYHPNVDKLGRICLD CCCCCHHHHHHHHHH	48.86	26320211
82	2-Hydroxyisobutyrylation	IYHPNVDKLGRICLD CCCCCHHHHHHHHHH	48.86	-
82	Ubiquitination	IYHPNVDKLGRICLD CCCCCHHHHHHHHHH	48.86	21890473
82	Acetylation	IYHPNVDKLGRICLD CCCCCHHHHHHHHHH	48.86	19608861
87	Glutathionylation	VDKLGRICLDILKDK HHHHHHHHHHHHCCC	2.42	22555962
87	S-nitrosylation	VDKLGRICLDILKDK HHHHHHHHHHHHCCC	2.42	22178444
87	S-nitrosocysteine	VDKLGRICLDILKDK HHHHHHHHHHHHCCC	2.42	-
92	Succinylation	RICLDILKDKWSPAL HHHHHHHCCCCCHHH	58.56	23954790
92	Ubiquitination	RICLDILKDKWSPAL HHHHHHHCCCCCHHH	58.56	21890473
92	Acetylation	RICLDILKDKWSPAL HHHHHHHCCCCCHHH	58.56	21791702
94	Ubiquitination	CLDILKDKWSPALQI HHHHHCCCCCHHHHH	48.24	21890473
94	Acetylation	CLDILKDKWSPALQI HHHHHCCCCCHHHHH	48.24	21791702
96	Phosphorylation	DILKDKWSPALQIRT HHHCCCCCHHHHHHH	13.16	28857561
139	Phosphorylation	NEAQAIETARAWTRL CHHHHHHHHHHHHHH	18.48	-
141	Methylation	AQAIETARAWTRLYA HHHHHHHHHHHHHHH	37.77	-
144	Phosphorylation	IETARAWTRLYAMNN HHHHHHHHHHHHHHC	15.15	-
145	Methylation	ETARAWTRLYAMNNI HHHHHHHHHHHHHCC	18.26	115919365
147	Phosphorylation	ARAWTRLYAMNNI-- HHHHHHHHHHHCC--	10.66	-

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 UBE2N_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBE2N_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 UBE2N_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AURKA_HUMAN	AURKA	physical	12881723
RN128_HUMAN	RNF128	physical	12705856
UEV1A_ARATH	MMZ1	physical	18178771
UEV1D_ARATH	UEV1D-4	physical	18178771
UB2V1_HUMAN	UBE2V1	physical	11057907
IKKA_HUMAN	CHUK	physical	11057907
TRI32_HUMAN	TRIM32	physical	17994549
AURKA_HUMAN	AURKA	physical	17060341
P53_HUMAN	TP53	physical	17000756
AMFR_HUMAN	AMFR	physical	19690564
BIRC3_HUMAN	BIRC3	physical	19690564
CAPS2_HUMAN	CADPS2	physical	19690564
CNOT4_HUMAN	CNOT4	physical	19690564
DTX1_HUMAN	DTX1	physical	19690564
RN103_HUMAN	RNF103	physical	19690564
LRSM1_HUMAN	LRSAM1	physical	19690564
MIB1_HUMAN	MIB1	physical	19690564
TRIM1_HUMAN	MID2	physical	19690564
NEUL1_HUMAN	NEURL1	physical	19690564
NFX1_HUMAN	NFX1	physical	19690564
PJA2_HUMAN	PJA2	physical	19690564
RNF11_HUMAN	RNF11	physical	19690564
RNF13_HUMAN	RNF13	physical	19690564
GOLI_HUMAN	RNF130	physical	19690564
RN152_HUMAN	RNF152	physical	19690564
RN165_HUMAN	RNF165	physical	19690564
RN167_HUMAN	RNF167	physical	19690564
RN182_HUMAN	RNF182	physical	19690564
RNF43_HUMAN	RNF43	physical	19690564
SH3R2_HUMAN	SH3RF2	physical	19690564
TOPRS_HUMAN	TOPORS	physical	19690564
TRI32_HUMAN	TRIM32	physical	19690564
ZNRF1_HUMAN	ZNRF1	physical	19690564
ZNRF2_HUMAN	ZNRF2	physical	19690564
ZNRF3_HUMAN	ZNRF3	physical	19690564
ZNRF4_HUMAN	ZNRF4	physical	19690564
XIAP_HUMAN	XIAP	physical	19549727
TRAF6_HUMAN	TRAF6	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
RNF11_HUMAN	RNF11	physical	19549727
SIAH1_HUMAN	SIAH1	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
RC3H2_HUMAN	RC3H2	physical	19549727
RNF8_HUMAN	RNF8	physical	19549727
TRI32_HUMAN	TRIM32	physical	19549727
HOIL1_HUMAN	RBCK1	physical	19549727
BIRC8_HUMAN	BIRC8	physical	19549727
RN125_HUMAN	RNF125	physical	19549727
MARH7_HUMAN	MARCH7	physical	19549727
LRSM1_HUMAN	LRSAM1	physical	19549727
AMFR_HUMAN	AMFR	physical	19549727
CHFR_HUMAN	CHFR	physical	19549727
MARH5_HUMAN	MARCH5	physical	19549727
RFWD3_HUMAN	RFWD3	physical	19549727
TRI25_HUMAN	TRIM25	physical	19549727
TRIM5_HUMAN	TRIM5	physical	19549727
CHIP_HUMAN	STUB1	physical	16307917
P53_HUMAN	TP53	physical	19651615
HERC2_HUMAN	HERC2	physical	20023648
RNF8_HUMAN	RNF8	physical	20023648
RNF8_HUMAN	RNF8	physical	21911360
TRAF2_HUMAN	TRAF2	physical	22184250
UB2V1_HUMAN	UBE2V1	physical	20613989
UBC_HUMAN	UBC	physical	20613989
TRAF6_MOUSE	Traf6	physical	15147900
UB2V2_HUMAN	UBE2V2	physical	15147900
TRAF6_HUMAN	TRAF6	physical	17709375
RNF8_HUMAN	RNF8	physical	16215985
UB2V1_HUMAN	UBE2V1	physical	16215985
UB2V2_HUMAN	UBE2V2	physical	16215985
RN103_HUMAN	RNF103	physical	16215985
ZNRF2_HUMAN	ZNRF2	physical	16215985
TRIM1_HUMAN	MID2	physical	21143188
TRI11_HUMAN	TRIM11	physical	21143188
TRI18_HUMAN	MID1	physical	21143188
TRI32_HUMAN	TRIM32	physical	21143188
TRI50_HUMAN	TRIM50	physical	21143188
TRI27_HUMAN	TRIM27	physical	21143188
OTUB1_HUMAN	OTUB1	physical	22679021
UBC_HUMAN	UBC	physical	14517261
ISG15_HUMAN	ISG15	physical	22693631
UB2V2_DANRE	ube2v2	physical	22055568
UBC_HUMAN	UBC	physical	12569095
UBC_HUMAN	UBC	physical	22367539
ISG15_HUMAN	ISG15	physical	16112642
UB2V2_HUMAN	UBE2V2	physical	15749714
RIPK1_HUMAN	RIPK1	physical	18029035
UB2V1_HUMAN	UBE2V1	physical	18678647
UB2V2_HUMAN	UBE2V2	physical	18678647
UBA1_HUMAN	UBA1	physical	18678647
PYC_HUMAN	PC	physical	18678647
PCCA_HUMAN	PCCA	physical	18678647
ACACA_HUMAN	ACACA	physical	18678647
PCCB_HUMAN	PCCB	physical	18678647
CHIP_HUMAN	STUB1	physical	18678647
ARI2_HUMAN	ARIH2	physical	19340006
UBC_HUMAN	UBC	physical	12847084
UB2V2_HUMAN	UBE2V2	physical	12847084
VATH_HUMAN	ATP6V1H	physical	22939629
VP33B_HUMAN	VPS33B	physical	22939629
ZDHC5_HUMAN	ZDHHC5	physical	22939629
UFD1_HUMAN	UFD1L	physical	22939629
VASP_HUMAN	VASP	physical	22939629
UBP14_HUMAN	USP14	physical	22939629
RNF8_HUMAN	RNF8	physical	23255131
NBN_HUMAN	NBN	physical	23115235
RN111_HUMAN	RNF111	physical	23751493
PRKN_HUMAN	PARK2	physical	24023840
ARI1_HUMAN	ARIH1	physical	24023840
CHIP_HUMAN	STUB1	physical	24023840
MFN2_HUMAN	MFN2	physical	24023840
RNF8_HUMAN	RNF8	physical	24732096
RN168_HUMAN	RNF168	physical	24732096
UBE2N_HUMAN	UBE2N	physical	20061386
SLX5_YEAST	SLX5	physical	18032921
SLX8_YEAST	SLX8	physical	18032921
RN168_HUMAN	RNF168	physical	19203578
BFAR_HUMAN	BFAR	physical	19549727
UBC_HUMAN	UBC	physical	22325355
UBC_HUMAN	UBC	physical	17964296
UB2V1_HUMAN	UBE2V1	physical	18029035
TRAF2_HUMAN	TRAF2	physical	23007157
UB2V2_HUMAN	UBE2V2	physical	16122702
UBC_HUMAN	UBC	physical	23105008
UB2V1_HUMAN	UBE2V1	physical	18082144
UB2V2_HUMAN	UBE2V2	physical	11504715
UBC_HUMAN	UBC	physical	11504715
UBE2N_HUMAN	UBE2N	physical	11504715
AT2B3_HUMAN	ATP2B3	physical	26344197
GNA1_HUMAN	GNPNAT1	physical	26344197
UBL5_HUMAN	UBL5	physical	26344197
TRIM5_HUMAN	TRIM5	physical	26212332
NEPR1_HUMAN	CNEP1R1	physical	25548215
RNF4_HUMAN	RNF4	physical	26148049
UB2V2_HUMAN	UBE2V2	physical	26148049
EPM2A_HUMAN	EPM2A	physical	26546463
NHLC1_HUMAN	NHLRC1	physical	26546463
FA12_HUMAN	F12	physical	18838541
ANXA5_HUMAN	ANXA5	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
SND1_HUMAN	SND1	physical	27173435
HPRT_HUMAN	HPRT1	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435
CRNN_HUMAN	CRNN	physical	27173435
ZNRF1_HUMAN	ZNRF1	physical	27173435
ZNRF2_HUMAN	ZNRF2	physical	27173435
UB2V1_HUMAN	UBE2V1	physical	27173435
UB2V2_HUMAN	UBE2V2	physical	27173435
MED15_HUMAN	MED15	physical	27173435
CPNE3_HUMAN	CPNE3	physical	27173435
PYGL_HUMAN	PYGL	physical	27173435
SF3A3_HUMAN	SF3A3	physical	27173435
CPSF6_HUMAN	CPSF6	physical	27173435
SF3A1_HUMAN	SF3A1	physical	27173435
SRP68_HUMAN	SRP68	physical	27173435
AIMP1_HUMAN	AIMP1	physical	27173435
CBS_HUMAN	CBS	physical	27173435
ATP5E_HUMAN	ATP5E	physical	27173435
CYC_HUMAN	CYCS	physical	27173435
MNS1_HUMAN	MNS1	physical	27173435
VIME_HUMAN	VIM	physical	27173435
FEN1_HUMAN	FEN1	genetic	28628639
TRAF6_HUMAN	TRAF6	physical	28244869
RNF8_HUMAN	RNF8	physical	28244869

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 UBE2N_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-82 AND LYS-94, ANDMASS SPECTROMETRY.	19608861 [Abstract]