VPS4A_HUMAN - dbPTM
VPS4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS4A_HUMAN
UniProt AC Q9UN37
Protein Name Vacuolar protein sorting-associated protein 4A
Gene Name VPS4A {ECO:0000312|EMBL:AAG01470.1}
Organism Homo sapiens (Human).
Sequence Length 437
Subcellular Localization Prevacuolar compartment membrane
Peripheral membrane protein. Late endosome membrane
Peripheral membrane protein . Midbody. Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells, interaction with
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). Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission. [PubMed: 24814515 VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan]
Protein Sequence MTTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCVQYLDRAEKLKDYLRSKEKHGKKPVKENQSEGKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIHELARKTEGYSGADISIIVRDSLMQPVRKVQSATHFKKVCGPSRTNPSMMIDDLLTPCSPGDPGAMEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFGQES
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------MTTSTLQKA
------CCHHHHHHH		29.4724043423
3Phosphorylation-----MTTSTLQKAI
-----CCHHHHHHHH		20.5824043423
4Phosphorylation----MTTSTLQKAID
----CCHHHHHHHHH		20.2524043423
5Phosphorylation---MTTSTLQKAIDL
---CCHHHHHHHHHH		30.9924043423
8AcetylationMTTSTLQKAIDLVTK
CCHHHHHHHHHHHHH		50.8819608861
15UbiquitinationKAIDLVTKATEEDKA
HHHHHHHHCCHHHHC		45.92-
23MethylationATEEDKAKNYEEALR
CCHHHHCCCHHHHHH		66.84115978737
25PhosphorylationEEDKAKNYEEALRLY
HHHHCCCHHHHHHHH		17.9129496907
59MalonylationAKESIRAKCVQYLDR
HHHHHHHHHHHHHHH		25.7026320211
59AcetylationAKESIRAKCVQYLDR
HHHHHHHHHHHHHHH		25.7020167786
69AcetylationQYLDRAEKLKDYLRS
HHHHHHHHHHHHHHH		60.9120167786
71AcetylationLDRAEKLKDYLRSKE
HHHHHHHHHHHHHHH		56.2320167786
73PhosphorylationRAEKLKDYLRSKEKH
HHHHHHHHHHHHHHH		11.4821253578
90PhosphorylationKPVKENQSEGKGSDS
CCCCCCCCCCCCCCC		60.9623927012
95PhosphorylationNQSEGKGSDSDSEGD
CCCCCCCCCCCCCCC		37.1129255136
97PhosphorylationSEGKGSDSDSEGDNP
CCCCCCCCCCCCCCH		44.7429255136
99PhosphorylationGKGSDSDSEGDNPEK
CCCCCCCCCCCCHHH		47.6423401153
121UbiquitinationMGAVVMEKPNIRWND
HHHHHCCCCCCCHHH		25.85-
136UbiquitinationVAGLEGAKEALKEAV
CCCCHHHHHHHHHCC		55.14-
140UbiquitinationEGAKEALKEAVILPI
HHHHHHHHHCCEEEC		51.1521890473
148UbiquitinationEAVILPIKFPHLFTG
HCCEEECCCCCCCCC		51.4021890473
156AcetylationFPHLFTGKRTPWRGI
CCCCCCCCCCCCEEE		50.4712435693
156UbiquitinationFPHLFTGKRTPWRGI
CCCCCCCCCCCCEEE		50.4721890473
171PhosphorylationLLFGPPGTGKSYLAK
EEECCCCCCHHHHHH		47.40-
173UbiquitinationFGPPGTGKSYLAKAV
ECCCCCCHHHHHHHH		35.4521890473
174PhosphorylationGPPGTGKSYLAKAVA
CCCCCCHHHHHHHHH		27.0728857561
175PhosphorylationPPGTGKSYLAKAVAT
CCCCCHHHHHHHHHH		17.73-
178UbiquitinationTGKSYLAKAVATEAN
CCHHHHHHHHHHHCC		40.58-
207UbiquitinationKWLGESEKLVKNLFE
HHHCCHHHHHHHHHH		68.79-
210UbiquitinationGESEKLVKNLFELAR
CCHHHHHHHHHHHHH		59.3721890473
220UbiquitinationFELARQHKPSIIFID
HHHHHHHCCCEEEEE		31.93-
231PhosphorylationIFIDEVDSLCGSRNE
EEEECHHHHCCCCCC		30.6325627689
235PhosphorylationEVDSLCGSRNENESE
CHHHHCCCCCCCHHH		30.8225627689
290PhosphorylationRRFEKRIYIPLPEEA
HHHHHCCCCCCCHHH		10.6627642862
309PhosphorylationMFRLHLGSTPHNLTD
HHHHHCCCCCCCCCH		45.1620873877
310PhosphorylationFRLHLGSTPHNLTDA
HHHHCCCCCCCCCHH		27.1120873877
315PhosphorylationGSTPHNLTDANIHEL
CCCCCCCCHHCHHHH		38.0820873877
329PhosphorylationLARKTEGYSGADISI
HHHHCCCCCCCCEEE		9.5622817900
335PhosphorylationGYSGADISIIVRDSL
CCCCCCEEEEEECCC		13.5524850871
348UbiquitinationSLMQPVRKVQSATHF
CCCCCHHHHHHCCCH		44.88-
351PhosphorylationQPVRKVQSATHFKKV
CCHHHHHHCCCHHHH		37.8223312004
353PhosphorylationVRKVQSATHFKKVCG
HHHHHHCCCHHHHHC		32.8523312004
356UbiquitinationVQSATHFKKVCGPSR
HHHCCCHHHHHCCCC		36.37-
378PhosphorylationDDLLTPCSPGDPGAM
HHCCCCCCCCCCCCC		32.8728348404
410PhosphorylationCMSDMLRSLATTRPT
CHHHHHHHHHHCCCC		20.5628857561
414PhosphorylationMLRSLATTRPTVNAD
HHHHHHHCCCCCCHH		29.1028857561
425UbiquitinationVNADDLLKVKKFSED
CCHHHHHHHHHHHHH		60.34-
428UbiquitinationDDLLKVKKFSEDFGQ
HHHHHHHHHHHHHCC		58.05-
437PhosphorylationSEDFGQES-------
HHHHCCCC-------		37.3225159151
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 VPS4A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS4A_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 VPS4A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPC1_HUMANNPC1physical
16757520
CHMP5_HUMANCHMP5physical
21543490
CHMP3_HUMANCHMP3physical
21543490
GAG_HV1H2gagphysical
20164219
VTA1_HUMANVTA1physical
20164219
CHM1B_HUMANCHMP1Bphysical
14505570
CHM2A_HUMANCHMP2Aphysical
14505570
CHM4A_HUMANCHMP4Aphysical
14505569
CHM1A_HUMANCHMP1Aphysical
16730941
CHM1B_HUMANCHMP1Bphysical
16730941
CHM4A_HUMANCHMP4Aphysical
16730941
CHM4B_HUMANCHMP4Bphysical
16730941
VPS4A_HUMANVPS4Aphysical
16730941
AT1A3_HUMANATP1A3physical
26186194
VPS4B_HUMANVPS4Bphysical
26186194
RHEB_HUMANRHEBphysical
26186194
ANCHR_HUMANZFYVE19physical
26186194
VTA1_HUMANVTA1physical
26186194
ARL8B_HUMANARL8Bphysical
26186194
ANCHR_HUMANZFYVE19physical
28514442
VPS4B_HUMANVPS4Bphysical
28514442
VTA1_HUMANVTA1physical
28514442
ARL8B_HUMANARL8Bphysical
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 VPS4A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-8, AND MASS SPECTROMETRY.

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