VPS4B_HUMAN - dbPTM
VPS4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS4B_HUMAN
UniProt AC O75351
Protein Name Vacuolar protein sorting-associated protein 4B
Gene Name VPS4B
Organism Homo sapiens (Human).
Sequence Length 444
Subcellular Localization Prevacuolar compartment membrane
Peripheral membrane protein. Late endosome membrane
Peripheral membrane protein . Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells.
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 and enveloped virus budding (HIV-1 and other lentiviruses). VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan. [PubMed: 22660413]
Protein Sequence MSSTSPNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKNKEKKAQKPVKEGQPSPADEKGNDSDGEGESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEPHARAAMFKLHLGTTQNSLTEADFRELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRADPNHLVDDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMSDMLRSLSNTKPTVNEHDLLKLKKFTEDFGQEG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSSTSPNLQ
------CCCCCHHHH		42.1829255136
3Phosphorylation-----MSSTSPNLQK
-----CCCCCHHHHH		31.4429255136
4Phosphorylation----MSSTSPNLQKA
----CCCCCHHHHHH		40.6829255136
5Phosphorylation---MSSTSPNLQKAI
---CCCCCHHHHHHH		17.4629255136
10AcetylationSTSPNLQKAIDLASK
CCCHHHHHHHHHHHH		50.9425953088
10UbiquitinationSTSPNLQKAIDLASK
CCCHHHHHHHHHHHH		50.94-
17UbiquitinationKAIDLASKAAQEDKA
HHHHHHHHHHHHHCC		41.98-
17MalonylationKAIDLASKAAQEDKA
HHHHHHHHHHHHHCC		41.9826320211
40PhosphorylationLYQHAVQYFLHVVKY
HHHHHHHHHHHHHHH		11.0822817900
53AcetylationKYEAQGDKAKQSIRA
HHHHCCHHHHHHHHH		65.3923749302
57PhosphorylationQGDKAKQSIRAKCTE
CCHHHHHHHHHHHHH		17.21-
61MalonylationAKQSIRAKCTEYLDR
HHHHHHHHHHHHHHH		31.6626320211
63PhosphorylationQSIRAKCTEYLDRAE
HHHHHHHHHHHHHHH		27.27-
88UbiquitinationKKAQKPVKEGQPSPA
HHCCCCCCCCCCCCC		65.73-
93PhosphorylationPVKEGQPSPADEKGN
CCCCCCCCCCCCCCC		25.4929255136
102PhosphorylationADEKGNDSDGEGESD
CCCCCCCCCCCCCCC		52.0629255136
108PhosphorylationDSDGEGESDDPEKKK
CCCCCCCCCCHHHHH		59.1622167270
143UbiquitinationVAGLEGAKEALKEAV
CCCCHHHHHHHHHCC		55.14-
147MalonylationEGAKEALKEAVILPI
HHHHHHHHHCCEEEC		51.1526320211
147UbiquitinationEGAKEALKEAVILPI
HHHHHHHHHCCEEEC		51.1521890473
147UbiquitinationEGAKEALKEAVILPI
HHHHHHHHHCCEEEC		51.1521890473
155UbiquitinationEAVILPIKFPHLFTG
HCCEEECCCCCCCCC		51.4021890473
155AcetylationEAVILPIKFPHLFTG
HCCEEECCCCCCCCC		51.4025953088
155UbiquitinationEAVILPIKFPHLFTG
HCCEEECCCCCCCCC		51.4021890473
163UbiquitinationFPHLFTGKRTPWRGI
CCCCCCCCCCCCEEE		50.4721890473
163UbiquitinationFPHLFTGKRTPWRGI
CCCCCCCCCCCCEEE		50.4721890473
163AcetylationFPHLFTGKRTPWRGI
CCCCCCCCCCCCEEE		50.4725953088
178PhosphorylationLLFGPPGTGKSYLAK
EEECCCCCCHHHHHH		47.40-
180UbiquitinationFGPPGTGKSYLAKAV
ECCCCCCHHHHHHHH		35.4521890473
180UbiquitinationFGPPGTGKSYLAKAV
ECCCCCCHHHHHHHH		35.4521890473
181PhosphorylationGPPGTGKSYLAKAVA
CCCCCCHHHHHHHHH		27.0728857561
182PhosphorylationPPGTGKSYLAKAVAT
CCCCCHHHHHHHHHH		17.73-
185UbiquitinationTGKSYLAKAVATEAN
CCHHHHHHHHHHHCC		40.58-
207UbiquitinationSSSDLVSKWLGESEK
CHHHHHHHHHCCHHH		38.67-
214AcetylationKWLGESEKLVKNLFQ
HHHCCHHHHHHHHHH		68.7925953088
214UbiquitinationKWLGESEKLVKNLFQ
HHHCCHHHHHHHHHH		68.79-
217UbiquitinationGESEKLVKNLFQLAR
CCHHHHHHHHHHHHH		59.3721890473
217UbiquitinationGESEKLVKNLFQLAR
CCHHHHHHHHHHHHH		59.3721890473
227UbiquitinationFQLARENKPSIIFID
HHHHHHCCCCEEEEE		35.08-
240GlutathionylationIDEIDSLCGSRSENE
EECHHHHCCCCCCCH		5.5722555962
316PhosphorylationMFKLHLGTTQNSLTE
HHHHHHCCCCCCCCH		31.4124732914
317PhosphorylationFKLHLGTTQNSLTEA
HHHHHCCCCCCCCHH		24.7717525332
320PhosphorylationHLGTTQNSLTEADFR
HHCCCCCCCCHHHHH		27.1817525332
322PhosphorylationGTTQNSLTEADFREL
CCCCCCCCHHHHHHH		29.0224732914
332UbiquitinationDFRELGRKTDGYSGA
HHHHHHHCCCCCCCC		49.52-
333PhosphorylationFRELGRKTDGYSGAD
HHHHHHCCCCCCCCC		33.0422210691
336PhosphorylationLGRKTDGYSGADISI
HHHCCCCCCCCCEEE		13.52-
337PhosphorylationGRKTDGYSGADISII
HHCCCCCCCCCEEEE		32.7922210691
342PhosphorylationGYSGADISIIVRDAL
CCCCCCEEEEEHHHH		13.55-
350SulfoxidationIIVRDALMQPVRKVQ
EEEHHHHHHHHHHHH		4.5421406390
355UbiquitinationALMQPVRKVQSATHF
HHHHHHHHHHHCCCH		44.88-
358PhosphorylationQPVRKVQSATHFKKV
HHHHHHHHCCCHHCC		37.8223312004
360PhosphorylationVRKVQSATHFKKVRG
HHHHHHCCCHHCCCC		32.8522210691
363AcetylationVQSATHFKKVRGPSR
HHHCCCHHCCCCCCC		42.6325953088
363UbiquitinationVQSATHFKKVRGPSR
HHHCCCHHCCCCCCC		42.63-
369PhosphorylationFKKVRGPSRADPNHL
HHCCCCCCCCCCCCC		42.8122210691
382PhosphorylationHLVDDLLTPCSPGDP
CCCCCCCCCCCCCCC		29.5528122231
385PhosphorylationDDLLTPCSPGDPGAI
CCCCCCCCCCCCCCE		32.8728192239
395PhosphorylationDPGAIEMTWMDVPGD
CCCCEEEEEEECCCC		12.5928122231
410PhosphorylationKLLEPVVSMSDMLRS
CCCCCCCCHHHHHHH		16.8918385515
422UbiquitinationLRSLSNTKPTVNEHD
HHHHCCCCCCCCHHH		42.83-
432AcetylationVNEHDLLKLKKFTED
CCHHHHHHHHHHHHH		66.6119608861
432UbiquitinationVNEHDLLKLKKFTED
CCHHHHHHHHHHHHH		66.6119608861
435UbiquitinationHDLLKLKKFTEDFGQ
HHHHHHHHHHHHHCC		68.87-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS4B_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 VPS4B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS4_YEASTVPS4physical
16193069
LIPA_YEASTLIP5physical
16193069
CHM2A_HUMANCHMP2Aphysical
14505570
PDC6I_HUMANPDCD6IPphysical
14505570
ZPR1_HUMANZPR1physical
22939629
YAP1_HUMANYAP1physical
22939629
ANCHR_HUMANZFYVE19physical
22939629
Z585B_HUMANZNF585Bphysical
22939629
CHMP5_HUMANCHMP5physical
25416956
ANCHR_HUMANZFYVE19physical
25416956
BIRC2_HUMANBIRC2physical
26186194
ITPA_HUMANITPAphysical
26186194
VTA1_HUMANVTA1physical
26186194
KPCA_HUMANPRKCAphysical
26186194
VP13A_HUMANVPS13Aphysical
26344197
VPS45_HUMANVPS45physical
26344197
ITPA_HUMANITPAphysical
28514442
EFR3A_HUMANEFR3Aphysical
28514442
BIRC2_HUMANBIRC2physical
28514442
VTA1_HUMANVTA1physical
28514442
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 VPS4B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-102, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.
"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 SER-102, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317 AND SER-320, ANDMASS SPECTROMETRY.
"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-102, AND MASSSPECTROMETRY.

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