VPS8_HUMAN - dbPTM
VPS8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS8_HUMAN
UniProt AC Q8N3P4
Protein Name Vacuolar protein sorting-associated protein 8 homolog
Gene Name VPS8
Organism Homo sapiens (Human).
Sequence Length 1428
Subcellular Localization Early endosome .
Protein Description Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. [PubMed: 25266290 Functions predominantly in APPL1-containing endosomes]
Protein Sequence MENEPDHENVEQSLCAKTSEEELNKSFNLEASLSKFSYIDMDKELEFKNDLIDDKEFDIPQVDTPPTLESILNETDDEDESFILEDPTLLNIDTIDSHSYDTSSVASSDSGDRTNLKRKKKLPDSFSLHGSVMRHSLLKGISAQIVSAADKVDAGLPTAIAVSSLIAVGTSHGLALIFGKDQNQALRLCLGSTSVGGQYGAISALSINNDCSRLLCGFAKGQITMWDLASGKLLRSITDAHPPGTAILHIKFTDDPTLAICNDSGGSVFELTFKRVMGVRTCESRCLFSGSKGEVCCIEPLHSKPELKDHPITQFSLLAMASLTKILVIGLKPSLKVWMTFPYGRMDPSSVPLLAWHFVAVQNYVNPMLAFCRGDVVHFLLVKRDESGAIHVTKQKHLHLYYDLINFTWINSRTVVLLDSVEKLHVIDRQTQEELETVEISEVQLVYNSSHFKSLATGGNVSQALALVGEKACYQSISSYGGQIFYLGTKSVYVMMLRSWRERVDHLLKQDCLTEALALAWSFHEGKAKAVVGLSGDASKRKAIVADRMVEILFHYADRALKKCPDQGKIQVMEQHFQDMVPVIVDYCLLLQRKDLLFSQMYDKLSENSVAKGVFLECLEPYILSDKLVGITPQVMKDLIVHFQDKKLMENVEALIVHMDITSLDIQQVVLMCWENRLYDAMIYVYNRGMNEFISPMEKLFRVIAPPLNAGKTLTDEQVVMGNKLLVYISCCLAGRAYPLGDIPEDLVPLVKNQVFEFLIRLHSAEASPEEEIYPYIRTLLHFDTREFLNVLALTFEDFKNDKQAVEYQQRIVDILLKVMVENSDFTPSQVGCLFTFLARQLAKPDNTLFVNRTLFDQVLEFLCSPDDDSRHSERQQVLLELLQAGGIVQFEESRLIRMAEKAEFYQICEFMYEREHQYDKIIDCYLRDPLREEEVFNYIHNILSIPGHSAEEKQSVWQKAMDHIEELVSLKPCKAAELVATHFSGHIETVIKKLQNQVLLFKFLRSLLDPREGIHVNQELLQISPCITEQFIELLCQFNPTQVIETLQVLECYRLEETIQITQKYQLHEVTAYLLEKKGDIHGAFLIMLERLQSKLQEVTHQGENTKEDPSLKDVEDTMVETIALCQRNSHNLNQQQREALWFPLLEAMMAPQKLSSSAIPHLHSEALKSLTMQVLNSMAAFIALPSILQRILQDPVYGKGKLGEIQGLILGMLDTFNYEQTLLETTTSLLNQDLHWSLCNLRASVTRGLNPKQDYCSICLQQYKRRQEMADEIIVFSCGHLYHSFCLQNKECTVEFEGQTRWTCYKCSSSNKVGKLSENSSEIKKGRITPSQVKMSPSYHQSKGDPTAKKGTSEPVLDPQQIQAFDQLCRLYRGSSRLALLTELSQNRSSESYRPFSGSQSAPAFNSIFQNENFQLQLIPPPVTED
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
13PhosphorylationDHENVEQSLCAKTSE
CCCCHHHHHHCCCCH		16.3527251275
18PhosphorylationEQSLCAKTSEEELNK
HHHHHCCCCHHHHHH		23.8923401153
19PhosphorylationQSLCAKTSEEELNKS
HHHHCCCCHHHHHHH		42.1628450419
26 (in isoform 3)Phosphorylation-20.49-
26PhosphorylationSEEELNKSFNLEASL
CHHHHHHHCCCCHHH		20.4923401153
32PhosphorylationKSFNLEASLSKFSYI
HHCCCCHHHHHCCCC		24.6530266825
34PhosphorylationFNLEASLSKFSYIDM
CCCCHHHHHCCCCCC		29.2030266825
37PhosphorylationEASLSKFSYIDMDKE
CHHHHHCCCCCCCCC		25.5621815630
38PhosphorylationASLSKFSYIDMDKEL
HHHHHCCCCCCCCCC		12.2228796482
64PhosphorylationFDIPQVDTPPTLESI
CCCCCCCCCCCHHHH		32.1024275569
75PhosphorylationLESILNETDDEDESF
HHHHHCCCCCCCCCC		47.9129759185
125PhosphorylationRKKKLPDSFSLHGSV
CCCCCCCCCCCCHHH		18.1326074081
127PhosphorylationKKLPDSFSLHGSVMR
CCCCCCCCCCHHHHH		24.3314702039
131PhosphorylationDSFSLHGSVMRHSLL
CCCCCCHHHHHHHHH		11.2926074081
136PhosphorylationHGSVMRHSLLKGISA
CHHHHHHHHHHHCHH		25.6526074081
142PhosphorylationHSLLKGISAQIVSAA
HHHHHHCHHHHHCHH		23.84-
232UbiquitinationMWDLASGKLLRSITD
EECCCCCCCHHHHHC		41.68-
284PhosphorylationMGVRTCESRCLFSGS
HCCEEECCEEEEECC		30.3628258704
334PhosphorylationLVIGLKPSLKVWMTF
HHCCCCCCCEEEEEE		38.95-
491O-linked_GlycosylationIFYLGTKSVYVMMLR
EEEECCCHHHHHHHH		20.6530379171
527AcetylationAWSFHEGKAKAVVGL
HHHHHCCCCEEEEEE		43.6719811869
529AcetylationSFHEGKAKAVVGLSG
HHHCCCCEEEEEECC		45.2419811877
535PhosphorylationAKAVVGLSGDASKRK
CEEEEEECCCHHHHH		28.7922210691
539PhosphorylationVGLSGDASKRKAIVA
EEECCCHHHHHHHHH		37.42-
540AcetylationGLSGDASKRKAIVAD
EECCCHHHHHHHHHH		60.6925953088
540UbiquitinationGLSGDASKRKAIVAD
EECCCHHHHHHHHHH		60.69-
594UbiquitinationYCLLLQRKDLLFSQM
HHHHHHHHHHHHHHH		39.50-
599PhosphorylationQRKDLLFSQMYDKLS
HHHHHHHHHHHHHHC		17.6321406692
602PhosphorylationDLLFSQMYDKLSENS
HHHHHHHHHHHCCCH		11.4221406692
636SulfoxidationVGITPQVMKDLIVHF
CCCCHHHHHHHHHHH		2.0521406390
972UbiquitinationIEELVSLKPCKAAEL
HHHHHCCCCCCHHHH		40.64-
972AcetylationIEELVSLKPCKAAEL
HHHHHCCCCCCHHHH		40.6425953088
1007PhosphorylationLLFKFLRSLLDPREG
HHHHHHHHHCCCCCC		35.1227174698
1131PhosphorylationIALCQRNSHNLNQQQ
HHHHHHCCCCCCHHH		18.88-
1155 (in isoform 3)Phosphorylation-49.64-
1156 (in isoform 3)Phosphorylation-5.17-
1157 (in isoform 3)Phosphorylation-29.31-
1157PhosphorylationMMAPQKLSSSAIPHL
HHCCHHCCCCCCCHH		29.3118491316
1158PhosphorylationMAPQKLSSSAIPHLH
HCCHHCCCCCCCHHC		33.9418491316
1159PhosphorylationAPQKLSSSAIPHLHS
CCHHCCCCCCCHHCH		27.1718491316
1171PhosphorylationLHSEALKSLTMQVLN
HCHHHHHHHHHHHHH		29.8922210691
1173PhosphorylationSEALKSLTMQVLNSM
HHHHHHHHHHHHHHH		16.7922210691
1179PhosphorylationLTMQVLNSMAAFIAL
HHHHHHHHHHHHHHH		12.9722210691
1188PhosphorylationAAFIALPSILQRILQ
HHHHHHHHHHHHHHC		36.4622210691
1257PhosphorylationGLNPKQDYCSICLQQ
CCCCCCCCHHHHHHH		5.8926356563
1265PhosphorylationCSICLQQYKRRQEMA
HHHHHHHHHHHHHHC		8.1026356563
1317UbiquitinationSSSNKVGKLSENSSE
CCCCCCEEECCCCCH		52.40-
1319PhosphorylationSNKVGKLSENSSEIK
CCCCEEECCCCCHHH		37.9118187866
1322PhosphorylationVGKLSENSSEIKKGR
CEEECCCCCHHHCCC		25.8727422710
1323PhosphorylationGKLSENSSEIKKGRI
EEECCCCCHHHCCCC		55.7225627689
1331PhosphorylationEIKKGRITPSQVKMS
HHHCCCCCHHHCCCC		18.6125159151
1333PhosphorylationKKGRITPSQVKMSPS
HCCCCCHHHCCCCCC		38.6730576142
1336UbiquitinationRITPSQVKMSPSYHQ
CCCHHHCCCCCCCCC		26.48-
1338PhosphorylationTPSQVKMSPSYHQSK
CHHHCCCCCCCCCCC		12.6525159151
1340PhosphorylationSQVKMSPSYHQSKGD
HHCCCCCCCCCCCCC		28.1330576142
1341PhosphorylationQVKMSPSYHQSKGDP
HCCCCCCCCCCCCCC		13.7829396449
1344PhosphorylationMSPSYHQSKGDPTAK
CCCCCCCCCCCCCCC		25.8726074081
1349PhosphorylationHQSKGDPTAKKGTSE
CCCCCCCCCCCCCCC		56.7126074081
1374PhosphorylationFDQLCRLYRGSSRLA
HHHHHHHHCCCHHHH		8.1224719451
1377PhosphorylationLCRLYRGSSRLALLT
HHHHHCCCHHHHHHH		11.8624719451
1378PhosphorylationCRLYRGSSRLALLTE
HHHHCCCHHHHHHHH		33.8527282143
1387PhosphorylationLALLTELSQNRSSES
HHHHHHHHCCCCCCC		21.1228857561
1392PhosphorylationELSQNRSSESYRPFS
HHHCCCCCCCCCCCC		27.5924719451
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 VPS8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS8_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 VPS8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS11_HUMANVPS11physical
26463206
VPS16_HUMANVPS16physical
26463206
TGFA1_HUMANTGFBRAP1physical
26463206
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 VPS8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-26, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1319 AND SER-1322, ANDMASS SPECTROMETRY.

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