dbPTM

VAPB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VAPB_HUMAN
UniProt AC	O95292
Protein Name	Vesicle-associated membrane protein-associated protein B/C
Gene Name	VAPB
Organism	Homo sapiens (Human).
Sequence Length	243
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type IV membrane protein. Present in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane.
Protein Description	Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation..
Protein Sequence	MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPIVSKSLSSSLDDTEVKKVMEECKRLQGEVQRLREENKQFKEEDGLRMRKTVQSNSPISALAPTGKEEGLSTRLLALVVLFFIVGVIIGKIAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAKVEQVLS ------CCCCEEHHH	25.30	25944712
3	Acetylation	-----MAKVEQVLSL -----CCCCEEHHHC	45.03	23954790
3	Ubiquitination	-----MAKVEQVLSL -----CCCCEEHHHC	45.03	19608861
9	Phosphorylation	AKVEQVLSLEPQHEL CCCEEHHHCCCCCCC	31.65	23312004
17	Ubiquitination	LEPQHELKFRGPFTD CCCCCCCEECCCCCC	29.99	-
17	Acetylation	LEPQHELKFRGPFTD CCCCCCCEECCCCCC	29.99	26051181
23	Phosphorylation	LKFRGPFTDVVTTNL CEECCCCCCEEECCE	30.90	27362937
27	Phosphorylation	GPFTDVVTTNLKLGN CCCCCEEECCEECCC	15.15	27362937
28	Phosphorylation	PFTDVVTTNLKLGNP CCCCEEECCEECCCC	27.26	27362937
31	Acetylation	DVVTTNLKLGNPTDR CEEECCEECCCCCCC	57.32	26051181
38	Methylation	KLGNPTDRNVCFKVK ECCCCCCCCEEEEEE	39.70	115919753
43	Methylation	TDRNVCFKVKTTAPR CCCCEEEEEECCCCC	37.38	-
43	Acetylation	TDRNVCFKVKTTAPR CCCCEEEEEECCCCC	37.38	25953088
99	Phosphorylation	SMFAPTDTSDMEAVW EEECCCCCHHHHHHH	29.16	28348404
100	Phosphorylation	MFAPTDTSDMEAVWK EECCCCCHHHHHHHH	37.46	28348404
118	Ubiquitination	PEDLMDSKLRCVFEL HHHHCCCCCEEEEEE	35.37	-
118	Malonylation	PEDLMDSKLRCVFEL HHHHCCCCCEEEEEE	35.37	26320211
118	Acetylation	PEDLMDSKLRCVFEL HHHHCCCCCEEEEEE	35.37	23749302
131	Acetylation	ELPAENDKPHDVEIN EECCCCCCCCCEEEC	56.70	26051181
131	Ubiquitination	ELPAENDKPHDVEIN EECCCCCCCCCEEEC	56.70	-
139	Ubiquitination	PHDVEINKIISTTAS CCCEEECEEEEECCC	47.26	-
142	Phosphorylation	VEINKIISTTASKTE EEECEEEEECCCCCC	24.15	25867546
143	Phosphorylation	EINKIISTTASKTET EECEEEEECCCCCCC	18.90	23911959
143	O-linked_Glycosylation	EINKIISTTASKTET EECEEEEECCCCCCC	18.90	23301498
144	Phosphorylation	INKIISTTASKTETP ECEEEEECCCCCCCC	23.34	21712546
146	Phosphorylation	KIISTTASKTETPIV EEEEECCCCCCCCEE	37.71	21712546
147	Acetylation	IISTTASKTETPIVS EEEECCCCCCCCEEC	48.17	23236377
147	Ubiquitination	IISTTASKTETPIVS EEEECCCCCCCCEEC	48.17	21906983
147	Sumoylation	IISTTASKTETPIVS EEEECCCCCCCCEEC	48.17	25114211
147 (in isoform 1)	Ubiquitination	-	48.17	21890473
148	Phosphorylation	ISTTASKTETPIVSK EEECCCCCCCCEECH	42.47	30266825
150	Phosphorylation	TTASKTETPIVSKSL ECCCCCCCCEECHHH	24.44	25159151
154	O-linked_Glycosylation	KTETPIVSKSLSSSL CCCCCEECHHHCCCC	19.76	23301498
154	Phosphorylation	KTETPIVSKSLSSSL CCCCCEECHHHCCCC	19.76	30266825
155 (in isoform 1)	Ubiquitination	-	44.51	21890473
155	Acetylation	TETPIVSKSLSSSLD CCCCEECHHHCCCCC	44.51	25953088
155	Ubiquitination	TETPIVSKSLSSSLD CCCCEECHHHCCCCC	44.51	21890473
156	Phosphorylation	ETPIVSKSLSSSLDD CCCEECHHHCCCCCH	26.44	29255136
158	Phosphorylation	PIVSKSLSSSLDDTE CEECHHHCCCCCHHH	25.60	22167270
159	Phosphorylation	IVSKSLSSSLDDTEV EECHHHCCCCCHHHH	39.97	22167270
160	Phosphorylation	VSKSLSSSLDDTEVK ECHHHCCCCCHHHHH	32.23	22167270
164	Phosphorylation	LSSSLDDTEVKKVME HCCCCCHHHHHHHHH	42.20	30266825
167	Acetylation	SLDDTEVKKVMEECK CCCHHHHHHHHHHHH	33.16	26051181
188	Acetylation	QRLREENKQFKEEDG HHHHHHHHHHHHHHC	61.46	26051181
188	Ubiquitination	QRLREENKQFKEEDG HHHHHHHHHHHHHHC	61.46	-
191	Acetylation	REENKQFKEEDGLRM HHHHHHHHHHHCCCC	58.67	26051181
201	Phosphorylation	DGLRMRKTVQSNSPI HCCCCHHHHCCCCCC	17.26	30266825
204	Phosphorylation	RMRKTVQSNSPISAL CCHHHHCCCCCCCCC	34.63	30266825
206	Phosphorylation	RKTVQSNSPISALAP HHHHCCCCCCCCCCC	28.94	30266825
209	Phosphorylation	VQSNSPISALAPTGK HCCCCCCCCCCCCCC	22.18	30266825
214	Phosphorylation	PISALAPTGKEEGLS CCCCCCCCCCCCCHH	56.10	30266825
216	Acetylation	SALAPTGKEEGLSTR CCCCCCCCCCCHHHH	55.88	30593321
221	Phosphorylation	TGKEEGLSTRLLALV CCCCCCHHHHHHHHH	23.49	-
222	Phosphorylation	GKEEGLSTRLLALVV CCCCCHHHHHHHHHH	30.31	-

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 VAPB_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INSI1_HUMAN	INSIG1	physical	16606821
ZO1_HUMAN	TJP1	physical	22939629
VINC_HUMAN	VCL	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
FAF1_HUMAN	FAF1	physical	24885147
TERA_HUMAN	VCP	physical	24885147
ASNA_HUMAN	ASNA1	physical	24885147
UBC_HUMAN	UBC	physical	24885147
BAG6_HUMAN	BAG6	physical	24885147
UBL4A_HUMAN	UBL4A	physical	24885147
GET4_HUMAN	GET4	physical	24885147
RPN2_HUMAN	RPN2	physical	24885147
OST48_HUMAN	DDOST	physical	24885147
RB3GP_HUMAN	RAB3GAP1	physical	24885147
RBGPR_HUMAN	RAB3GAP2	physical	24885147
WDR44_HUMAN	WDR44	physical	24885147
OSBP1_HUMAN	OSBP	physical	24885147
OSBP2_HUMAN	OSBP2	physical	24885147
OSBL2_HUMAN	OSBPL2	physical	24885147
OSBL3_HUMAN	OSBPL3	physical	24885147
OSBL6_HUMAN	OSBPL6	physical	24885147
OSBL9_HUMAN	OSBPL9	physical	24885147
OSB10_HUMAN	OSBPL10	physical	24885147
OSB11_HUMAN	OSBPL11	physical	24885147
PITM1_HUMAN	PITPNM1	physical	24885147
OSBL2_HUMAN	OSBPL2	physical	25416956
UBP20_HUMAN	USP20	physical	25416956
RMD2_HUMAN	RMDN2	physical	25416956
RBGPR_HUMAN	RAB3GAP2	physical	26186194
PITM1_HUMAN	PITPNM1	physical	26186194
TT39B_HUMAN	TTC39B	physical	26186194
OSBL3_HUMAN	OSBPL3	physical	26186194
AKA11_HUMAN	AKAP11	physical	26186194
LSG1_HUMAN	LSG1	physical	26186194
OSBL2_HUMAN	OSBPL2	physical	26186194
RMD3_HUMAN	RMDN3	physical	26186194
TACC1_HUMAN	TACC1	physical	26186194
SYNRG_HUMAN	SYNRG	physical	26186194
VP13A_HUMAN	VPS13A	physical	26186194
OSBL1_HUMAN	OSBPL1A	physical	26186194
RB3GP_HUMAN	RAB3GAP1	physical	26186194
CCNB2_HUMAN	CCNB2	physical	26186194
POTEF_HUMAN	POTEF	physical	26186194
STK4_HUMAN	STK4	physical	26186194
CEBPZ_HUMAN	CEBPZ	physical	26186194
SNX5_HUMAN	SNX5	physical	26186194
NDUA7_HUMAN	NDUFA7	physical	26186194
OSBL6_HUMAN	OSBPL6	physical	26186194
RBCC1_HUMAN	RB1CC1	physical	26186194
OSBP2_HUMAN	OSBP2	physical	26186194
OSBP1_HUMAN	OSBP	physical	26186194
KAPCB_HUMAN	PRKACB	physical	26186194
ARHGC_HUMAN	ARHGEF12	physical	26186194
OSBL9_HUMAN	OSBPL9	physical	26186194
OSB11_HUMAN	OSBPL11	physical	26186194
OSB10_HUMAN	OSBPL10	physical	26186194
AFTIN_HUMAN	AFTPH	physical	26186194
FANCJ_HUMAN	BRIP1	physical	26186194
ELYS_HUMAN	AHCTF1	physical	26186194
ACBD5_HUMAN	ACBD5	physical	26186194
S6A15_HUMAN	SLC6A15	physical	26186194
NDUB8_HUMAN	NDUFB8	physical	26186194
WDR44_HUMAN	WDR44	physical	26186194
SNX6_HUMAN	SNX6	physical	26186194
UBE4A_HUMAN	UBE4A	physical	26186194
VAPA_HUMAN	VAPA	physical	26186194
STAR3_HUMAN	STARD3	physical	26186194
SNX2_HUMAN	SNX2	physical	26186194
NACAD_HUMAN	NACAD	physical	26186194
CTU2_HUMAN	CTU2	physical	26186194
JMY_HUMAN	JMY	physical	26186194
ZDBF2_HUMAN	ZDBF2	physical	26186194
RFT1_HUMAN	RFT1	physical	26186194
ACBD4_HUMAN	ACBD4	physical	26186194
SNX25_HUMAN	SNX25	physical	26186194
CTR2_HUMAN	SLC7A2	physical	26186194
PITM2_HUMAN	PITPNM2	physical	26186194
RHBD3_HUMAN	RHBDD3	physical	26186194
FA83G_HUMAN	FAM83G	physical	26186194
KAP1_HUMAN	PRKAR1B	physical	26186194
UBP33_HUMAN	USP33	physical	26186194
NBR1_HUMAN	NBR1	physical	26186194
NDUV3_HUMAN	NDUFV3	physical	26186194
F118B_HUMAN	FAM118B	physical	26186194
MIGA2_HUMAN	FAM73B	physical	26186194
NU5M_HUMAN	ND5	physical	26186194
S26A2_HUMAN	SLC26A2	physical	26186194
NOL11_HUMAN	NOL11	physical	26186194
S2535_HUMAN	SLC25A35	physical	26186194
HTR5B_HUMAN	HEATR5B	physical	26186194
ABCE1_HUMAN	ABCE1	physical	26344197
COX41_HUMAN	COX4I1	physical	26344197
COX5B_HUMAN	COX5B	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
PITM2_HUMAN	PITPNM2	physical	28514442
OSBL2_HUMAN	OSBPL2	physical	28514442
ACBD5_HUMAN	ACBD5	physical	28514442
OSBL9_HUMAN	OSBPL9	physical	28514442
RMD2_HUMAN	RMDN2	physical	28514442
OSBL6_HUMAN	OSBPL6	physical	28514442
FA83G_HUMAN	FAM83G	physical	28514442
RASF1_HUMAN	RASSF1	physical	28514442
OSB10_HUMAN	OSBPL10	physical	28514442
SNX25_HUMAN	SNX25	physical	28514442
PITM1_HUMAN	PITPNM1	physical	28514442
NACAD_HUMAN	NACAD	physical	28514442
OSBL3_HUMAN	OSBPL3	physical	28514442
OSB11_HUMAN	OSBPL11	physical	28514442
MPRIP_HUMAN	MPRIP	physical	28514442
TT39B_HUMAN	TTC39B	physical	28514442
JMY_HUMAN	JMY	physical	28514442
TACC1_HUMAN	TACC1	physical	28514442
MIGA2_HUMAN	FAM73B	physical	28514442
OSBL1_HUMAN	OSBPL1A	physical	28514442
ARHGC_HUMAN	ARHGEF12	physical	28514442
AFTIN_HUMAN	AFTPH	physical	28514442
RAI14_HUMAN	RAI14	physical	28514442
OSBP1_HUMAN	OSBP	physical	28514442
M4K3_HUMAN	MAP4K3	physical	28514442
OSBP2_HUMAN	OSBP2	physical	28514442
RB3GP_HUMAN	RAB3GAP1	physical	28514442
LSG1_HUMAN	LSG1	physical	28514442
RBCC1_HUMAN	RB1CC1	physical	28514442
AKA11_HUMAN	AKAP11	physical	28514442
UBP33_HUMAN	USP33	physical	28514442
ZDBF2_HUMAN	ZDBF2	physical	28514442
SYNRG_HUMAN	SYNRG	physical	28514442
UBP20_HUMAN	USP20	physical	28514442
TTC1_HUMAN	TTC1	physical	28514442
MICA3_HUMAN	MICAL3	physical	28514442
SYNE2_HUMAN	SYNE2	physical	28514442
S2535_HUMAN	SLC25A35	physical	28514442
NBR1_HUMAN	NBR1	physical	28514442
RMD3_HUMAN	RMDN3	physical	28514442
TARA_HUMAN	TRIOBP	physical	28514442
NDUS4_HUMAN	NDUFS4	physical	28514442
DOP1_HUMAN	DOPEY1	physical	28514442
VP13A_HUMAN	VPS13A	physical	28514442
SNX2_HUMAN	SNX2	physical	28514442
SPEG_HUMAN	SPEG	physical	28514442
KAPCB_HUMAN	PRKACB	physical	28514442
KAP1_HUMAN	PRKAR1B	physical	28514442
CCNB2_HUMAN	CCNB2	physical	28514442
FANCJ_HUMAN	BRIP1	physical	28514442
NDUB8_HUMAN	NDUFB8	physical	28514442
HTR5B_HUMAN	HEATR5B	physical	28514442
WDR44_HUMAN	WDR44	physical	28514442
F118B_HUMAN	FAM118B	physical	28514442
KAPCG_HUMAN	PRKACG	physical	28514442
S26A2_HUMAN	SLC26A2	physical	28514442
STK3_HUMAN	STK3	physical	28514442
S6A15_HUMAN	SLC6A15	physical	28514442
STK4_HUMAN	STK4	physical	28514442
ACBD4_HUMAN	ACBD4	physical	28514442
SNX6_HUMAN	SNX6	physical	28514442
CEBPZ_HUMAN	CEBPZ	physical	28514442
NDUAC_HUMAN	NDUFA12	physical	28514442
CTR2_HUMAN	SLC7A2	physical	28514442
NDUA7_HUMAN	NDUFA7	physical	28514442
NDUS6_HUMAN	NDUFS6	physical	28514442
CTU2_HUMAN	CTU2	physical	28514442
CELR2_HUMAN	CELSR2	physical	28514442
RBGPR_HUMAN	RAB3GAP2	physical	28514442
PITM3_HUMAN	PITPNM3	physical	28514442
KAP0_HUMAN	PRKAR1A	physical	28514442
SNX5_HUMAN	SNX5	physical	28514442
NDUB3_HUMAN	NDUFB3	physical	28514442
VP13C_HUMAN	VPS13C	physical	28514442
GPN3_HUMAN	GPN3	physical	28514442
INTU_HUMAN	INTU	physical	27173435
CCD40_HUMAN	CCDC40	physical	27173435

Drug and Disease Associations

Kegg Disease
H00058	Amyotrophic lateral sclerosis (ALS); Lou Gehrig's disease
H00455	Spinal muscular atrophy (SMA), including: SMA type I (SMA1) / Werdning-Hoffman disease; SMA type II
OMIM Disease
608627	Amyotrophic lateral sclerosis 8 (ALS8)
182980	Spinal muscular atrophy, proximal, adult, autosomal dominant (SMAPAD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VAPB_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-156; SER-160 AND SER-206, AND MASSSPECTROMETRY.	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-3, AND MASS SPECTROMETRY.	19608861 [Abstract]
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-156; SER-160 AND SER-206, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150; SER-156 ANDSER-160, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150; SER-160 ANDSER-206, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-160, ANDMASS SPECTROMETRY.	17081983 [Abstract]