dbPTM

UB2V2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2V2_HUMAN
UniProt AC	Q15819
Protein Name	Ubiquitin-conjugating enzyme E2 variant 2
Gene Name	UBE2V2
Organism	Homo sapiens (Human).
Sequence Length	145
Subcellular Localization
Protein Description	Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination 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..
Protein Sequence	MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVSTGVKV ------CCCCCCCCC	12.17	22814378
4	Phosphorylation	----MAVSTGVKVPR ----CCCCCCCCCCC	15.20	24719451
5	Phosphorylation	---MAVSTGVKVPRN ---CCCCCCCCCCCC	39.12	24719451
8	Ubiquitination	MAVSTGVKVPRNFRL CCCCCCCCCCCCCHH	48.11	-
8	Acetylation	MAVSTGVKVPRNFRL CCCCCCCCCCCCCHH	48.11	25953088
41	Sulfoxidation	GLEDDEDMTLTRWTG CCCCCCCCEEEEEEE	2.88	30846556
49	Sulfoxidation	TLTRWTGMIIGPPRT EEEEEEEEEECCCCC	1.25	30846556
56	Phosphorylation	MIIGPPRTNYENRIY EEECCCCCCCCCCEE	48.18	21406692
58	Phosphorylation	IGPPRTNYENRIYSL ECCCCCCCCCCEEEE	17.61	21406692
61	Methylation	PRTNYENRIYSLKVE CCCCCCCCEEEEEEE	19.79	115919393
63	Phosphorylation	TNYENRIYSLKVECG CCCCCCEEEEEEECC	12.52	21406692
64	Phosphorylation	NYENRIYSLKVECGP CCCCCEEEEEEECCC	21.24	24719451
66	Acetylation	ENRIYSLKVECGPKY CCCEEEEEEECCCCC	30.01	25953088
66	Ubiquitination	ENRIYSLKVECGPKY CCCEEEEEEECCCCC	30.01	21890473
69	Glutathionylation	IYSLKVECGPKYPEA EEEEEEECCCCCCCC	14.67	22555962
72	Acetylation	LKVECGPKYPEAPPS EEEECCCCCCCCCCC	59.74	23749302
72	Ubiquitination	LKVECGPKYPEAPPS EEEECCCCCCCCCCC	59.74	21906983
79	Phosphorylation	KYPEAPPSVRFVTKI CCCCCCCCEEEEEEE	25.51	27251275
84	Phosphorylation	PPSVRFVTKINMNGI CCCEEEEEEEECCCC	24.40	28674151
88	Sulfoxidation	RFVTKINMNGINNSS EEEEEEECCCCCCCC	5.75	21406390
94	Phosphorylation	NMNGINNSSGMVDAR ECCCCCCCCCCCCCC	24.63	20068231
95	Phosphorylation	MNGINNSSGMVDARS CCCCCCCCCCCCCCH	32.79	20068231
101	Methylation	SSGMVDARSIPVLAK CCCCCCCCHHHEEEE	30.56	115919385
102	Phosphorylation	SGMVDARSIPVLAKW CCCCCCCHHHEEEEC	32.72	27251275
108	Acetylation	RSIPVLAKWQNSYSI CHHHEEEECCCCCCH	45.19	25953088
108	Ubiquitination	RSIPVLAKWQNSYSI CHHHEEEECCCCCCH	45.19	21890473
112	Phosphorylation	VLAKWQNSYSIKVVL EEEECCCCCCHHHHH	12.73	26091039
113	Phosphorylation	LAKWQNSYSIKVVLQ EEECCCCCCHHHHHH	23.20	20049867
114	Phosphorylation	AKWQNSYSIKVVLQE EECCCCCCHHHHHHH	18.76	24719451
123	Methylation	KVVLQELRRLMMSKE HHHHHHHHHHHCCHH	29.00	-
129	Ubiquitination	LRRLMMSKENMKLPQ HHHHHCCHHHCCCCC	34.90	-
133	Acetylation	MMSKENMKLPQPPEG HCCHHHCCCCCCCCC	69.47	25953088
133	Ubiquitination	MMSKENMKLPQPPEG HCCHHHCCCCCCCCC	69.47	-
143	Phosphorylation	QPPEGQTYNN----- CCCCCCCCCC-----	12.57	27642862

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 UB2V2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2V2_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 UB2V2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRIF1_HUMAN	LRIF1	physical	16169070
IGS21_HUMAN	IGSF21	physical	16169070
UBC35_ARATH	UBC35	physical	16786304
UBC36_ARATH	UBC36	physical	16786304
XIAP_HUMAN	XIAP	physical	19549727
ZNRF1_HUMAN	ZNRF1	physical	19549727
SIAH1_HUMAN	SIAH1	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
R144A_HUMAN	RNF144A	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
TRIM5_HUMAN	TRIM5	physical	19549727
UBE2N_HUMAN	UBE2N	physical	16129784
UBE2N_HUMAN	UBE2N	physical	21114314
UBE2N_HUMAN	UBE2N	physical	15147900
TRI32_HUMAN	TRIM32	physical	21143188
UBE2N_HUMAN	UBE2N	physical	14517261
UBC_HUMAN	UBC	physical	12834344
UBE2N_HUMAN	UBE2N	physical	12834344
UBC_HUMAN	UBC	physical	12569095
UBE2N_HUMAN	UBE2N	physical	12569095
UBE2N_HUMAN	UBE2N	physical	16122702
UBC_HUMAN	UBC	physical	16518696
UBE2N_HUMAN	UBE2N	physical	16112642
UBE2N_HUMAN	UBE2N	physical	15749714
UBE2N_HUMAN	UBE2N	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
UBXN1_HUMAN	UBXN1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
UBP34_HUMAN	USP34	physical	22939629
UBXN7_HUMAN	UBXN7	physical	22939629
VP26A_HUMAN	VPS26A	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
ZRAB2_HUMAN	ZRANB2	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
UBE2N_HUMAN	UBE2N	physical	11473255
UBE2N_HUMAN	UBE2N	physical	17964296
UBC_HUMAN	UBC	physical	11504715
UBE2N_HUMAN	UBE2N	physical	25909880
UBE2N_HUMAN	UBE2N	physical	26344197

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 UB2V2_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-72, AND MASS SPECTROMETRY.	19608861 [Abstract]