VP33B_HUMAN - dbPTM
VP33B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VP33B_HUMAN
UniProt AC Q9H267
Protein Name Vacuolar protein sorting-associated protein 33B
Gene Name VPS33B
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization Late endosome membrane
Peripheral membrane protein
Cytoplasmic side. Lysosome membrane
Peripheral membrane protein
Cytoplasmic side. Early endosome . Cytoplasmic vesicle, clathrin-coated vesicle . Recycling endosome . Colocalizes in clusters wi
Protein Description May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages. [PubMed: 18474358 Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity]
Protein Sequence MAFPHRPDAPELPDFSMLKRLARDQLIYLLEQLPGKKDLFIEADLMSPLDRIANVSILKQHEVDKLYKVENKPALSSNEQLCFLVRPRIKNMRYIASLVNADKLAGRTRKYKVIFSPQKFYACEMVLEEEGIYGDVSCDEWAFSLLPLDVDLLSMELPEFFRDYFLEGDQRWINTVAQALHLLSTLYGPFPNCYGIGRCAKMAYELWRNLEEEEDGETKGRRPEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVDFGPEVTSSDKSLKVLLNAEDKVFNEIRNEHFSNVFGFLSQKARNLQAQYDRRRGMDIKQMKNFVSQELKGLKQEHRLLSLHIGACESIMKKKTKQDFQELIKTEHALLEGFNIRESTSYIEEHIDRQVSPIESLRLMCLLSITENGLIPKDYRSLKTQYLQSYGPEHLLTFSNLRRAGLLTEQAPGDTLTAVESKVSKLVTDKAAGKITDAFSSLAKRSNFRAISKKLNLIPRVDGEYDLKVPRDMAYVFGGAYVPLSCRIIEQVLERRSWQGLDEVVRLLNCSDFAFTDMTKEDKASSESLRLILVVFLGGCTFSEISALRFLGREKGYRFIFLTTAVTNSARLMEAMSEVKA
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------MAFPHRPDA
------CCCCCCCCC		27.0319413330
12UbiquitinationHRPDAPELPDFSMLK
CCCCCCCCCCHHHHH		4.86-
19UbiquitinationLPDFSMLKRLARDQL
CCCHHHHHHHHHHHH		36.40-
36UbiquitinationLLEQLPGKKDLFIEA
HHHHCCCCCCEEEEH		40.9721890473
56PhosphorylationLDRIANVSILKQHEV
HHHHHCCHHHHHHHH		23.2421406692
65UbiquitinationLKQHEVDKLYKVENK
HHHHHHHHHEEECCC		59.91-
67PhosphorylationQHEVDKLYKVENKPA
HHHHHHHEEECCCCC		20.8020860994
103UbiquitinationASLVNADKLAGRTRK
HHHHCHHHHCCCCCE		37.51-
110UbiquitinationKLAGRTRKYKVIFSP
HHCCCCCEEEEEECC		49.13-
128UbiquitinationYACEMVLEEEGIYGD
EEEEEEEECCCCCCC		42.46-
167UbiquitinationFFRDYFLEGDQRWIN
HHHHHHHHCCHHHHH		51.31-
201UbiquitinationYGIGRCAKMAYELWR
CCHHHHHHHHHHHHH		27.91-
213UbiquitinationLWRNLEEEEDGETKG
HHHCCHHCCCCCCCC		52.60-
218PhosphorylationEEEEDGETKGRRPEI
HHCCCCCCCCCCCCC		44.3121406692
219UbiquitinationEEEDGETKGRRPEIG
HCCCCCCCCCCCCCC		46.2321890473
258UbiquitinationVDDTFRIKCGSVDFG
CCCEEEEEECCCCCC		28.43-
295PhosphorylationEIRNEHFSNVFGFLS
HHHHHHHHHHHHHHH		33.7120873877
302PhosphorylationSNVFGFLSQKARNLQ
HHHHHHHHHHHHHHH		27.6323403867
304UbiquitinationVFGFLSQKARNLQAQ
HHHHHHHHHHHHHHH		46.0321890473
304UbiquitinationVFGFLSQKARNLQAQ
HHHHHHHHHHHHHHH		46.0321890473
312PhosphorylationARNLQAQYDRRRGMD
HHHHHHHHHHHCCCC		17.90-
321UbiquitinationRRRGMDIKQMKNFVS
HHCCCCHHHHHHHHH		39.82-
321AcetylationRRRGMDIKQMKNFVS
HHCCCCHHHHHHHHH		39.8225953088
328PhosphorylationKQMKNFVSQELKGLK
HHHHHHHHHHHHHHH		17.5028102081
332UbiquitinationNFVSQELKGLKQEHR
HHHHHHHHHHHHHHH		62.54-
357UbiquitinationSIMKKKTKQDFQELI
HHHHHCCHHHHHHHH		57.67-
357MalonylationSIMKKKTKQDFQELI
HHHHHCCHHHHHHHH		57.6730639696
367UbiquitinationFQELIKTEHALLEGF
HHHHHHHHHHHHHCC		23.35-
370UbiquitinationLIKTEHALLEGFNIR
HHHHHHHHHHCCCCC		4.89-
375UbiquitinationHALLEGFNIRESTSY
HHHHHCCCCCCCCHH		43.17-
389UbiquitinationYIEEHIDRQVSPIES
HHHHHHHCCCCHHHH		37.89-
413UbiquitinationTENGLIPKDYRSLKT
HCCCCCCCCHHHHHH		61.47-
444PhosphorylationLRRAGLLTEQAPGDT
HHHCCCCCCCCCCCC		30.97-
451PhosphorylationTEQAPGDTLTAVESK
CCCCCCCCHHHHHHH		31.7424173317
453PhosphorylationQAPGDTLTAVESKVS
CCCCCCHHHHHHHHH		30.6522468782
458UbiquitinationTLTAVESKVSKLVTD
CHHHHHHHHHHHHHH		36.7021890473
461UbiquitinationAVESKVSKLVTDKAA
HHHHHHHHHHHHHHC		50.38-
466AcetylationVSKLVTDKAAGKITD
HHHHHHHHHCHHHHH		30.6725953088
466UbiquitinationVSKLVTDKAAGKITD
HHHHHHHHHCHHHHH		30.67-
470AcetylationVTDKAAGKITDAFSS
HHHHHCHHHHHHHHH		37.3925953088
470UbiquitinationVTDKAAGKITDAFSS
HHHHHCHHHHHHHHH		37.39-
476PhosphorylationGKITDAFSSLAKRSN
HHHHHHHHHHHHHHC		26.6028857561
477PhosphorylationKITDAFSSLAKRSNF
HHHHHHHHHHHHHCH		26.3728857561
480UbiquitinationDAFSSLAKRSNFRAI
HHHHHHHHHHCHHHH		62.7521890473
501PhosphorylationIPRVDGEYDLKVPRD
CCCCCCCCCCCCCCH		31.9127642862
504AcetylationVDGEYDLKVPRDMAY
CCCCCCCCCCCHHEE		47.5025953088
504UbiquitinationVDGEYDLKVPRDMAY
CCCCCCCCCCCHHEE		47.5021890473
525UbiquitinationVPLSCRIIEQVLERR
HHHHHHHHHHHHHHC		1.24-
547PhosphorylationVVRLLNCSDFAFTDM
HHHHHCCCHHCCCCC		34.3927251275
552PhosphorylationNCSDFAFTDMTKEDK
CCCHHCCCCCCHHHH		22.7927251275
554SulfoxidationSDFAFTDMTKEDKAS
CHHCCCCCCHHHHCC		5.3921406390
600PhosphorylationYRFIFLTTAVTNSAR
CEEEEEECCCCCHHH		22.6824425749
603PhosphorylationIFLTTAVTNSARLME
EEEECCCCCHHHHHH		22.4624425749
616UbiquitinationMEAMSEVKA------
HHHHHHHCC------		44.31-
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 VP33B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VP33B_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 VP33B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPE39_HUMANVIPAS39physical
16189514
UVRAG_HUMANUVRAGphysical
18552835
A4_HUMANAPPphysical
21832049
VPS35_HUMANVPS35physical
22939629
VPS29_HUMANVPS29physical
22939629
SPE39_HUMANVIPAS39physical
25416956
SPE39_HUMANVIPAS39physical
25783203
SPE39_HUMANVIPAS39physical
26463206
Drug and Disease Associations
Kegg Disease
H00950 Arthrogryposis, renal dysfunction, and cholestasis; ARC syndrome
OMIM Disease
208085Arthrogryposis, renal dysfunction and cholestasis syndrome 1 (ARCS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VP33B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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