VPS11_HUMAN - dbPTM
VPS11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS11_HUMAN
UniProt AC Q9H270
Protein Name Vacuolar protein sorting-associated protein 11 homolog
Gene Name VPS11
Organism Homo sapiens (Human).
Sequence Length 941
Subcellular Localization Endosome . Late endosome membrane
Peripheral membrane protein
Cytoplasmic side . Lysosome membrane
Peripheral membrane protein
Cytoplasmic side . Early endosome . Cytoplasmic vesicle . Cytoplasmic vesicle, autophagosome . Cytoplasmic vesicle, clat
Protein Description Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are 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 HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. [PubMed: 11382755]
Protein Sequence MAAYLQWRRFVFFDKELVKEPLSNDGAAPGATPASGSAASKFLCLPPGITVCDSGRGSLVFGDMEGQIWFLPRSLQLTGFQAYKLRVTHLYQLKQHNILASVGEDEEGINPLVKIWNLEKRDGGNPLCTRIFPAIPGTEPTVVSCLTVHENLNFMAIGFTDGSVTLNKGDITRDRHSKTQILHKGNYPVTGLAFRQAGKTTHLFVVTTENVQSYIVSGKDYPRVELDTHGCGLRCSALSDPSQDLQFIVAGDECVYLYQPDERGPCFAFEGHKLIAHWFRGYLIIVSRDRKVSPKSEFTSRDSQSSDKQILNIYDLCNKFIAYSTVFEDVVDVLAEWGSLYVLTRDGRVHALQEKDTQTKLEMLFKKNLFEMAINLAKSQHLDSDGLAQIFMQYGDHLYSKGNHDGAVQQYIRTIGKLEPSYVIRKFLDAQRIHNLTAYLQTLHRQSLANADHTTLLLNCYTKLKDSSKLEEFIKKKSESEVHFDVETAIKVLRQAGYYSHALYLAENHAHHEWYLKIQLEDIKNYQEALRYIGKLPFEQAESNMKRYGKILMHHIPEQTTQLLKGLCTDYRPSLEGRSDREAPGCRANSEEFIPIFANNPRELKAFLEHMSEVQPDSPQGIYDTLLELRLQNWAHEKDPQVKEKLHAEAISLLKSGRFCDVFDKALVLCQMHDFQDGVLYLYEQGKLFQQIMHYHMQHEQYRQVISVCERHGEQDPSLWEQALSYFARKEEDCKEYVAAVLKHIENKNLMPPLLVVQTLAHNSTATLSVIRDYLVQKLQKQSQQIAQDELRVRRYREETTRIRQEIQELKASPKIFQKTKCSICNSALELPSVHFLCGHSFHQHCFESYSESDADCPTCLPENRKVMDMIRAQEQKRDLHDQFQHQLRCSNDSFSVIADYFGRGVFNKLTLLTDPPTARLTSSLEAGLQRDLLMHSRRGT
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
2Acetylation------MAAYLQWRR
------CCHHHCHHE		12.5722223895
19UbiquitinationFFDKELVKEPLSNDG
ECCHHHHCCCCCCCC		67.2621890473
32PhosphorylationDGAAPGATPASGSAA
CCCCCCCCCCCCCCC		25.8825159151
84UbiquitinationLTGFQAYKLRVTHLY
CCCCEEEEEEEEEHH		32.6021890473
91PhosphorylationKLRVTHLYQLKQHNI
EEEEEEHHHHHHCCC		12.2818083107
120UbiquitinationVKIWNLEKRDGGNPL
HHHHCCCCCCCCCCC		59.98-
184UbiquitinationSKTQILHKGNYPVTG
CCCEEEECCCCCCCE		45.46-
200PhosphorylationAFRQAGKTTHLFVVT
EEEECCCEEEEEEEE		20.6629759185
201PhosphorylationFRQAGKTTHLFVVTT
EEECCCEEEEEEEEC		21.7729759185
213PhosphorylationVTTENVQSYIVSGKD
EECCCEEEEECCCCC		16.7329759185
214PhosphorylationTTENVQSYIVSGKDY
ECCCEEEEECCCCCC		6.5629759185
217PhosphorylationNVQSYIVSGKDYPRV
CEEEEECCCCCCCCE		30.4829759185
293PhosphorylationVSRDRKVSPKSEFTS
EECCCCCCCCCCCCC		29.6423312004
303PhosphorylationSEFTSRDSQSSDKQI
CCCCCCCCCCCCHHH		30.7425159151
305PhosphorylationFTSRDSQSSDKQILN
CCCCCCCCCCHHHHH		44.4425159151
366AcetylationTKLEMLFKKNLFEMA
HHHHHHHHHHHHHHH		36.4725953088
366MalonylationTKLEMLFKKNLFEMA
HHHHHHHHHHHHHHH		36.4726320211
400PhosphorylationQYGDHLYSKGNHDGA
HHCCCCEECCCCHHH		40.2124719451
417UbiquitinationQYIRTIGKLEPSYVI
HHHHHHCCCCCHHHH		45.91-
426UbiquitinationEPSYVIRKFLDAQRI
CCHHHHHHHHCHHHH		38.87-
465AcetylationLNCYTKLKDSSKLEE
HHHHHHHCCCHHHHH		58.0612436855
475AcetylationSKLEEFIKKKSESEV
HHHHHHHHHCCCCCC		60.5125953088
475UbiquitinationSKLEEFIKKKSESEV
HHHHHHHHHCCCCCC		60.51-
560PhosphorylationMHHIPEQTTQLLKGL
HHHCCHHHHHHHHHH		18.1728857561
561PhosphorylationHHIPEQTTQLLKGLC
HHCCHHHHHHHHHHC		19.5328857561
565UbiquitinationEQTTQLLKGLCTDYR
HHHHHHHHHHCCCCC		59.43-
574PhosphorylationLCTDYRPSLEGRSDR
HCCCCCHHCCCCCCC		30.0127251275
590PhosphorylationAPGCRANSEEFIPIF
CCCCCCCCCCCCHHH		37.2028857561
623PhosphorylationPDSPQGIYDTLLELR
CCCCCCHHHHHHHHH		15.0827642862
638UbiquitinationLQNWAHEKDPQVKEK
HHHHHHCCCHHHHHH		65.91-
652PhosphorylationKLHAEAISLLKSGRF
HHHHHHHHHHHCCCC		34.4024719451
737PhosphorylationKEEDCKEYVAAVLKH
CHHHHHHHHHHHHHH		4.8529496907
781MalonylationYLVQKLQKQSQQIAQ
HHHHHHHHHHHHHHH		63.4526320211
800O-linked_GlycosylationVRRYREETTRIRQEI
HHHHHHHHHHHHHHH		19.3430379171
813PhosphorylationEIQELKASPKIFQKT
HHHHHHCCCCHHHHC		25.7423401153
866UbiquitinationTCLPENRKVMDMIRA
CCCCCCHHHHHHHHH		54.19-
891PhosphorylationFQHQLRCSNDSFSVI
HHHHHHCCCCCCHHH		36.9228857561
894PhosphorylationQLRCSNDSFSVIADY
HHHCCCCCCHHHHHH		24.5428857561
896PhosphorylationRCSNDSFSVIADYFG
HCCCCCCHHHHHHHC		19.3028857561
904MethylationVIADYFGRGVFNKLT
HHHHHHCCCCCCHHE		28.36-
909UbiquitinationFGRGVFNKLTLLTDP
HCCCCCCHHEEECCC		31.2421890473
918PhosphorylationTLLTDPPTARLTSSL
EEECCCCCCCHHHHH		29.7828857561
922PhosphorylationDPPTARLTSSLEAGL
CCCCCCHHHHHHHHH		15.6623403867
923PhosphorylationPPTARLTSSLEAGLQ
CCCCCHHHHHHHHHH		37.2023401153
924PhosphorylationPTARLTSSLEAGLQR
CCCCHHHHHHHHHHH		25.6223401153
937PhosphorylationQRDLLMHSRRGT---
HHHHHHHHCCCC---		15.0923186163
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 VPS11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS11_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 VPS11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS18_HUMANVPS18physical
11382755
VPS16_HUMANVPS16physical
11382755
VP33A_HUMANVPS33Aphysical
11382755
STX7_HUMANSTX7physical
11382755
GGA3_HUMANGGA3physical
16996030
PLK2_RATPlk2physical
16203730
ECM29_HUMANKIAA0368physical
20682791
UVRAG_HUMANUVRAGphysical
18552835
VPS39_HUMANVPS39physical
22939629
WWP2_HUMANWWP2physical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
VPS39_HUMANVPS39physical
26186194
TGFA1_HUMANTGFBRAP1physical
26186194
VPS18_HUMANVPS18physical
26186194
GTF2I_HUMANGTF2Iphysical
26496610
TGFA1_HUMANTGFBRAP1physical
26496610
VPS8_HUMANVPS8physical
26496610
SCRIB_HUMANSCRIBphysical
26496610
VPS18_HUMANVPS18physical
26496610
CAMP3_HUMANCAMSAP3physical
26496610
VPS16_HUMANVPS16physical
26496610
VP33A_HUMANVPS33Aphysical
26496610
VPS16_HUMANVPS16physical
26463206
VP33A_HUMANVPS33Aphysical
26463206
VPS8_HUMANVPS8physical
26463206
TGFA1_HUMANTGFBRAP1physical
26463206
VPS41_HUMANVPS41physical
26463206
VPS39_HUMANVPS39physical
26463206
TGFA1_HUMANTGFBRAP1physical
28514442
VPS18_HUMANVPS18physical
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 VPS11_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-924, AND MASSSPECTROMETRY.

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