dbPTM

VPS4B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VPS4B_MOUSE
UniProt AC	P46467
Protein Name	Vacuolar protein sorting-associated protein 4B
Gene Name	Vps4b
Organism	Mus musculus (Mouse).
Sequence Length	444
Subcellular Localization	Prevacuolar compartment membrane Peripheral membrane protein. Late endosome membrane Peripheral membrane protein. Membrane-associated in the prevacuolar endosomal compartment.
Protein Description	Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity)..
Protein Sequence	MASTNTNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKKKEKKPQKPVKEEQSGPVDEKGNDSDGEAESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEAHARAAMFRLHLGSTQNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRADPNCIVNDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTEDFGQEG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Acetylation	STNTNLQKAIDLASK CCCHHHHHHHHHHHH	50.94	-
17	Ubiquitination	KAIDLASKAAQEDKA HHHHHHHHHHHHHCC	41.98	22790023
40	Phosphorylation	LYQHAVQYFLHVVKY HHHHHHHHHHHHHHH	11.08	-
61	Malonylation	AKQSIRAKCTEYLDR HHHHHHHHHHHHHHH	31.66	26320211
75	Phosphorylation	RAEKLKEYLKKKEKK HHHHHHHHHHHHCCC	23.41	25367039
92	Phosphorylation	KPVKEEQSGPVDEKG CCCCHHHCCCCCCCC	48.63	25619855
102	Phosphorylation	VDEKGNDSDGEAESD CCCCCCCCCCCCCCC	52.06	27087446
108	Phosphorylation	DSDGEAESDDPEKKK CCCCCCCCCCHHHHH	55.12	25521595
147	Ubiquitination	EGAKEALKEAVILPI HHHHHHHHHCCEEEC	51.15	22790023
163	Ubiquitination	FPHLFTGKRTPWRGI CCCCCCCCCCCCEEE	50.47	22790023
217	Ubiquitination	GESEKLVKNLFQLAR CCHHHHHHHHHHHHH	59.37	22790023
297	Phosphorylation	RRFEKRIYIPLPEAH HHHHHCCEEECHHHH	10.66	-
375	Glutathionylation	PSRADPNCIVNDLLT CCCCCCCCEECCCCC	4.46	24333276
385	Phosphorylation	NDLLTPCSPGDPGAI CCCCCCCCCCCCCCE	32.87	28059163
410	Phosphorylation	KLLEPVVSMWDMLRS CCHHHHHHHHHHHHH	17.87	-

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 VPS4B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VPS4B_MOUSE !!

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 VPS4B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VTA1_MOUSE	Vta1	physical	15173323
ALBU_HUMAN	ALB	physical	26496610
VATA_HUMAN	ATP6V1A	physical	26496610
VATB2_HUMAN	ATP6V1B2	physical	26496610
VPP1_HUMAN	ATP6V0A1	physical	26496610
BRAF_HUMAN	BRAF	physical	26496610
CSK22_HUMAN	CSNK2A2	physical	26496610
FLOT2_HUMAN	FLOT2	physical	26496610
NSF_HUMAN	NSF	physical	26496610
CHM1A_HUMAN	CHMP1A	physical	26496610
RAD51_HUMAN	RAD51	physical	26496610
B3A2_HUMAN	SLC4A2	physical	26496610
SPAST_HUMAN	SPAST	physical	26496610
UVRAG_HUMAN	UVRAG	physical	26496610
NOP14_HUMAN	NOP14	physical	26496610
RAI3_HUMAN	GPRC5A	physical	26496610
VA0D1_HUMAN	ATP6V0D1	physical	26496610
VATF_HUMAN	ATP6V1F	physical	26496610
MED21_HUMAN	MED21	physical	26496610
ABCG2_HUMAN	ABCG2	physical	26496610
VATG1_HUMAN	ATP6V1G1	physical	26496610
VP9D1_HUMAN	VPS9D1	physical	26496610
IST1_HUMAN	IST1	physical	26496610
RHGBA_HUMAN	ARHGAP11A	physical	26496610
PDC6I_HUMAN	PDCD6IP	physical	26496610
FLOT1_HUMAN	FLOT1	physical	26496610
ZER1_HUMAN	ZER1	physical	26496610
DD19B_HUMAN	DDX19B	physical	26496610
CNOT1_HUMAN	CNOT1	physical	26496610
DJC13_HUMAN	DNAJC13	physical	26496610
CAN7_HUMAN	CAPN7	physical	26496610
CHM2B_HUMAN	CHMP2B	physical	26496610
CHM2A_HUMAN	CHMP2A	physical	26496610
CHM4A_HUMAN	CHMP4A	physical	26496610
CHMP5_HUMAN	CHMP5	physical	26496610
VTA1_HUMAN	VTA1	physical	26496610
CHMP3_HUMAN	CHMP3	physical	26496610
SARAF_HUMAN	SARAF	physical	26496610
STX18_HUMAN	STX18	physical	26496610
GAR1_HUMAN	GAR1	physical	26496610
IMPCT_HUMAN	IMPACT	physical	26496610
GRDN_HUMAN	CCDC88A	physical	26496610
BIN3_HUMAN	BIN3	physical	26496610
MUC13_HUMAN	MUC13	physical	26496610
CHM1B_HUMAN	CHMP1B	physical	26496610
RPR1B_HUMAN	RPRD1B	physical	26496610
SCNM1_HUMAN	SCNM1	physical	26496610
DERL1_HUMAN	DERL1	physical	26496610
CDT1_HUMAN	CDT1	physical	26496610
TB10A_HUMAN	TBC1D10A	physical	26496610
PP4P1_HUMAN	TMEM55B	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
MITD1_HUMAN	MITD1	physical	26496610
CA052_HUMAN	C1orf52	physical	26496610
GA2L3_HUMAN	GAS2L3	physical	26496610
AT11C_HUMAN	ATP11C	physical	26496610
TIM23_HUMAN	TIMM23	physical	26496610

Drug and Disease Associations

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

Regulatory Network of VPS4B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.	19367708 [Abstract]