dbPTM

UB2V1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2V1_HUMAN
UniProt AC	Q13404
Protein Name	Ubiquitin-conjugating enzyme E2 variant 1
Gene Name	UBE2V1
Organism	Homo sapiens (Human).
Sequence Length	147
Subcellular Localization	Nucleus . Excluded from the nucleolus.
Protein Description	Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. 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. 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	MAATTGSGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTIYENRIYSLKIECGPKYPEAPPFVRFVTKINMNGVNSSNGVVDPRAISVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQCYSN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAATTGSGV ------CCCCCCCCC	17.32	25944712
4	Phosphorylation	----MAATTGSGVKV ----CCCCCCCCCCC	23.35	29255136
5	Phosphorylation	---MAATTGSGVKVP ---CCCCCCCCCCCC	25.32	29255136
7	Phosphorylation	-MAATTGSGVKVPRN -CCCCCCCCCCCCCC	38.02	29255136
8 (in isoform 7)	Phosphorylation	-	25.30	20068231
8 (in isoform 2)	Phosphorylation	-	25.30	20068231
9 (in isoform 7)	Phosphorylation	-	6.39	20068231
9 (in isoform 2)	Phosphorylation	-	6.39	20068231
10	Ubiquitination	ATTGSGVKVPRNFRL CCCCCCCCCCCCCHH	50.47	23000965
10	Acetylation	ATTGSGVKVPRNFRL CCCCCCCCCCCCCHH	50.47	25953088
12	Ubiquitination	TGSGVKVPRNFRLLE CCCCCCCCCCCHHHH	21.56	23000965
18	Ubiquitination	VPRNFRLLEELEEGQ CCCCCHHHHHHHCCC	4.13	23000965
24	Ubiquitination	LLEELEEGQKGVGDG HHHHHHCCCCCCCCC	25.73	23000965
26	Ubiquitination	EELEEGQKGVGDGTV HHHHCCCCCCCCCCE	67.43	23000965
30 (in isoform 6)	Ubiquitination	-	47.38	21890473
30	Ubiquitination	EGQKGVGDGTVSWGL CCCCCCCCCCEECCC	47.38	23000965
32	Ubiquitination	QKGVGDGTVSWGLED CCCCCCCCEECCCCC	18.99	23000965
42	Ubiquitination	WGLEDDEDMTLTRWT CCCCCCCCCEEEEEE	42.22	27667366
54	Ubiquitination	RWTGMIIGPPRTIYE EEEEEEECCCCEEEC	18.42	32015554
63	Methylation	PRTIYENRIYSLKIE CCEEECCCEEEEEEE	19.79	115919381
65	Ubiquitination	TIYENRIYSLKIECG EEECCCEEEEEEECC	12.52	23000965
66	Phosphorylation	IYENRIYSLKIECGP EECCCEEEEEEECCC	22.33	24719451
66	Ubiquitination	IYENRIYSLKIECGP EECCCEEEEEEECCC	22.33	32015554
68	Ubiquitination	ENRIYSLKIECGPKY CCCEEEEEEECCCCC	30.44	23000965
68	Acetylation	ENRIYSLKIECGPKY CCCEEEEEEECCCCC	30.44	25953088
71	Ubiquitination	IYSLKIECGPKYPEA EEEEEEECCCCCCCC	14.93	23000965
74	Acetylation	LKIECGPKYPEAPPF EEEECCCCCCCCCCE	59.74	23749302
74 (in isoform 4)	Ubiquitination	-	59.74	21890473
74	Ubiquitination	LKIECGPKYPEAPPF EEEECCCCCCCCCCE	59.74	23000965
75	Ubiquitination	KIECGPKYPEAPPFV EEECCCCCCCCCCEE	14.94	23000965
79	Ubiquitination	GPKYPEAPPFVRFVT CCCCCCCCCEEEEEE	22.62	23000965
86	Phosphorylation	PPFVRFVTKINMNGV CCEEEEEEEECCCCC	24.40	18491316
87	Ubiquitination	PFVRFVTKINMNGVN CEEEEEEEECCCCCC	27.12	23000965
89	Ubiquitination	VRFVTKINMNGVNSS EEEEEEECCCCCCCC	21.30	23000965
90	Phosphorylation	RFVTKINMNGVNSSN EEEEEECCCCCCCCC	5.42	33259812
91	Ubiquitination	FVTKINMNGVNSSNG EEEEECCCCCCCCCC	46.93	23000965
93	Ubiquitination	TKINMNGVNSSNGVV EEECCCCCCCCCCCC	5.51	23000965
97 (in isoform 7)	Ubiquitination	-	47.28	21890473
97	Ubiquitination	MNGVNSSNGVVDPRA CCCCCCCCCCCCHHH	47.28	23000965
97 (in isoform 2)	Ubiquitination	-	47.28	21890473
102	Phosphorylation	SSNGVVDPRAISVLA CCCCCCCHHHHHHHH	18.92	33259812
104	Phosphorylation	NGVVDPRAISVLAKW CCCCCHHHHHHHHHH	12.09	33259812
106	Phosphorylation	VVDPRAISVLAKWQN CCCHHHHHHHHHHCC	15.30	26437602
107	Ubiquitination	VDPRAISVLAKWQNS CCHHHHHHHHHHCCC	5.01	32015554
110	Ubiquitination	RAISVLAKWQNSYSI HHHHHHHHHCCCCCH	45.19	32015554
114	Phosphorylation	VLAKWQNSYSIKVVL HHHHHCCCCCHHHHH	12.73	29116813
116	Phosphorylation	AKWQNSYSIKVVLQE HHHCCCCCHHHHHHH	18.76	24719451
125	Methylation	KVVLQELRRLMMSKE HHHHHHHHHHHHCHH	29.00	-
128	Ubiquitination	LQELRRLMMSKENMK HHHHHHHHHCHHHCC	2.43	23000965
131	Malonylation	LRRLMMSKENMKLPQ HHHHHHCHHHCCCCC	34.90	26320211
131	Acetylation	LRRLMMSKENMKLPQ HHHHHHCHHHCCCCC	34.90	23236377
131	Ubiquitination	LRRLMMSKENMKLPQ HHHHHHCHHHCCCCC	34.90	23000965
131	2-Hydroxyisobutyrylation	LRRLMMSKENMKLPQ HHHHHHCHHHCCCCC	34.90	-
132	Ubiquitination	RRLMMSKENMKLPQP HHHHHCHHHCCCCCC	56.07	23000965
133	Ubiquitination	RLMMSKENMKLPQPP HHHHCHHHCCCCCCC	36.30	32015554
135	Ubiquitination	MMSKENMKLPQPPEG HHCHHHCCCCCCCCC	69.47	23000965
143	Phosphorylation	LPQPPEGQCYSN--- CCCCCCCCCCCC---	22.70	33259812
145	Phosphorylation	QPPEGQCYSN----- CCCCCCCCCC-----	11.89	23911959
146	Phosphorylation	PPEGQCYSN------ CCCCCCCCC------	43.63	25159151
148 (in isoform 1)	Ubiquitination	-		21890473
154	Ubiquitination	N-------------- C--------------		23000965
158	Ubiquitination	------------------ ------------------		23000965
169	Phosphorylation	----------------------------- -----------------------------		33259812
291	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------		23000965
297	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------		23000965
333	Ubiquitination	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		32015554
354	Ubiquitination	---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		23000965
358	Ubiquitination	-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		23000965
369	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		33259812

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2V1_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 UB2V1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RNF37_HUMAN	UBOX5	physical	19549727
RNF14_HUMAN	RNF14	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
TRIM8_HUMAN	TRIM8	physical	19549727
TRI18_HUMAN	MID1	physical	19549727
XIAP_HUMAN	XIAP	physical	19549727
BIRC8_HUMAN	BIRC8	physical	19549727
RNF5_HUMAN	RNF5	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
ARI2_HUMAN	ARIH2	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
TRI39_HUMAN	TRIM39	physical	19549727
RNF10_HUMAN	RNF10	physical	19549727
RN111_HUMAN	RNF111	physical	19549727
R144A_HUMAN	RNF144A	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
TRI32_HUMAN	TRIM32	physical	19549727
TRIM5_HUMAN	TRIM5	physical	19549727
CHIP_HUMAN	STUB1	physical	16307917
UBE2N_HUMAN	UBE2N	physical	16307917
UBE2N_HUMAN	UBE2N	physical	16129784
UBE2N_HUMAN	UBE2N	physical	15147900
TRI32_HUMAN	TRIM32	physical	21143188
UBC_HUMAN	UBC	physical	12834344
UBE2N_HUMAN	UBE2N	physical	22939629
UB2V2_HUMAN	UBE2V2	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
UBP34_HUMAN	USP34	physical	22939629
UGDH_HUMAN	UGDH	physical	22939629
UBE2A_HUMAN	UBE2A	physical	22939629
UCHL3_HUMAN	UCHL3	physical	22939629
UBXN7_HUMAN	UBXN7	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
ULK4_HUMAN	ULK4	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
UBE2C_HUMAN	UBE2C	physical	22939629
VATG1_HUMAN	ATP6V1G1	physical	22939629
G6PD_HUMAN	G6PD	physical	22863883
LDHB_HUMAN	LDHB	physical	22863883
1433S_HUMAN	SFN	physical	22863883
TGM2_HUMAN	TGM2	physical	22863883
TXND5_HUMAN	TXNDC5	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
1433Z_HUMAN	YWHAZ	physical	22863883
F168A_HUMAN	FAM168A	physical	25416956
UBQL1_HUMAN	UBQLN1	physical	25416956
UBE2N_HUMAN	UBE2N	physical	17709375
CHRD1_HUMAN	CHORDC1	physical	26344197
RAB7A_HUMAN	RAB7A	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
UBE2K_HUMAN	UBE2K	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197
UBE2N_HUMAN	UBE2N	physical	25548215
RHDF2_HUMAN	RHBDF2	physical	29069608
UBE2N_HUMAN	UBE2N	physical	29069608

Drug and Disease Associations

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

Regulatory Network of UB2V1_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-146, AND MASSSPECTROMETRY.	19413330 [Abstract]