VP33A_HUMAN - dbPTM
VP33A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VP33A_HUMAN
UniProt AC Q96AX1
Protein Name Vacuolar protein sorting-associated protein 33A
Gene Name VPS33A
Organism Homo sapiens (Human).
Sequence Length 596
Subcellular Localization Cytoplasmic vesicle . Late endosome membrane
Peripheral membrane protein
Cytoplasmic side . Lysosome membrane
Peripheral membrane protein
Cytoplasmic side . Early endosome . Cytoplasmic vesicle, autophagosome . Cytoplasmic vesicle, clathrin-coated
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: 23351085]
Protein Sequence MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF
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
7Phosphorylation-MAAHLSYGRVNLNV
-CCCCCCCCCCCHHH		18.4729496907
52PhosphorylationPFGLIAQYSLLKEHE
HHHHHHHHHHHHHHC		7.7124719451
53PhosphorylationFGLIAQYSLLKEHEV
HHHHHHHHHHHHHCE		18.3624719451
62UbiquitinationLKEHEVEKMFTLKGN
HHHHCEEECEEECCC		44.4829967540
67UbiquitinationVEKMFTLKGNRLPAA
EEECEEECCCCCCHH		51.5929967540
77UbiquitinationRLPAADVKNIIFFVR
CCCHHHHCCEEEEEC		42.8721963094
99PhosphorylationIIAENVLSEDRRGPT
HHHHHCCCCCCCCCC		32.9226503514
110UbiquitinationRGPTRDFHILFVPRR
CCCCCCEEEEEEECH		21.8233845483
115UbiquitinationDFHILFVPRRSLLCE
CEEEEEEECHHHHHH		20.7333845483
126UbiquitinationLLCEQRLKDLGVLGS
HHHHHHHHHHCCCHH		53.7721906983
133PhosphorylationKDLGVLGSFIHREEY
HHHCCCHHHHCCCCC		19.5020873877
195UbiquitinationTIPQIFGKGECARQV
CHHHHHCCHHHHHHH		40.56-
251UbiquitinationLTYEGLIDEIYGIQN
CCHHHHHHHHHCCCC		41.0833845483
256UbiquitinationLIDEIYGIQNSYVKL
HHHHHHCCCCCEECC		1.6533845483
262UbiquitinationGIQNSYVKLPPEKFA
CCCCCEECCCHHHCC		47.2233845483
267UbiquitinationYVKLPPEKFAPKKQG
EECCCHHHCCCCCCC		53.2333845483
278UbiquitinationKKQGDGGKDLPTEAK
CCCCCCCCCCCHHHH		62.7233845483
286UbiquitinationDLPTEAKKLQLNSAE
CCCHHHHHHCCCCHH		48.8133845483
291UbiquitinationAKKLQLNSAEELYAE
HHHHCCCCHHHHHHH		45.7233845483
297UbiquitinationNSAEELYAEIRDKNF
CCHHHHHHHHHCCCC		20.5432015554
300UbiquitinationEELYAEIRDKNFNAV
HHHHHHHHCCCCCHH		40.1133845483
302UbiquitinationLYAEIRDKNFNAVGS
HHHHHHCCCCCHHHH		54.3032015554
302AcetylationLYAEIRDKNFNAVGS
HHHHHHCCCCCHHHH		54.30164115
305UbiquitinationEIRDKNFNAVGSVLS
HHHCCCCCHHHHHHH		43.0133845483
309PhosphorylationKNFNAVGSVLSKKAK
CCCCHHHHHHHHHHH		17.1828857561
313AcetylationAVGSVLSKKAKIISA
HHHHHHHHHHHHHHH		53.22164119
313UbiquitinationAVGSVLSKKAKIISA
HHHHHHHHHHHHHHH		53.2232015554
314UbiquitinationVGSVLSKKAKIISAA
HHHHHHHHHHHHHHH		52.0822817900
314AcetylationVGSVLSKKAKIISAA
HHHHHHHHHHHHHHH		52.08164123
316UbiquitinationSVLSKKAKIISAAFE
HHHHHHHHHHHHHHH		49.8321906983
316AcetylationSVLSKKAKIISAAFE
HHHHHHHHHHHHHHH		49.83164127
319UbiquitinationSKKAKIISAAFEERH
HHHHHHHHHHHHHHH		19.6132015554
324UbiquitinationIISAAFEERHNAKTV
HHHHHHHHHHCCCCH		53.4332015554
329UbiquitinationFEERHNAKTVGEIKQ
HHHHHCCCCHHHHHH		49.4023000965
335UbiquitinationAKTVGEIKQFVSQLP
CCCHHHHHHHHHHCH		33.1223000965
346UbiquitinationSQLPHMQAARGSLAN
HHCHHHHHHCCHHCC		7.4932015554
350PhosphorylationHMQAARGSLANHTSI
HHHHHCCHHCCCCCH		20.8228857561
351UbiquitinationMQAARGSLANHTSIA
HHHHCCHHCCCCCHH		6.5232015554
362UbiquitinationTSIAELIKDVTTSED
CCHHHHHHCCCCCHH		59.7932015554
400UbiquitinationIEDCIAQKHSLIKVL
HHHHHHHHHHHHHHH		26.5829967540
402PhosphorylationDCIAQKHSLIKVLRL
HHHHHHHHHHHHHHH		38.5324719451
414PhosphorylationLRLVCLQSVCNSGLK
HHHHHHHHHHCCCHH		18.71-
418PhosphorylationCLQSVCNSGLKQKVL
HHHHHHCCCHHHHHH		40.14-
421UbiquitinationSVCNSGLKQKVLDYY
HHHCCCHHHHHHHHH		52.1529967540
423UbiquitinationCNSGLKQKVLDYYKR
HCCCHHHHHHHHHHH		43.0829967540
429UbiquitinationQKVLDYYKREILQTY
HHHHHHHHHHHHHHH		37.0129967540
4292-HydroxyisobutyrylationQKVLDYYKREILQTY
HHHHHHHHHHHHHHH		37.01-
454UbiquitinationLEKAGLLKPQTGGRN
HHHCCCCCCCCCCCC		39.8729967540
463PhosphorylationQTGGRNNYPTIRKTL
CCCCCCCCHHHHHHH		12.8024719451
465PhosphorylationGGRNNYPTIRKTLRL
CCCCCCHHHHHHHHH		24.0524719451
531PhosphorylationEERQPLPTGLQKKRQ
CCCCCCCCCHHHCCC		59.20-
535UbiquitinationPLPTGLQKKRQPGEN
CCCCCHHHCCCCCCC		55.7727667366
536UbiquitinationLPTGLQKKRQPGENR
CCCCHHHCCCCCCCC		43.2224816145
574PhosphorylationLEDGGTEYVIATTKL
CCCCCEEEEEEEEEC		9.3027307780
578PhosphorylationGTEYVIATTKLMNGT
CEEEEEEEEECCCCC		17.2227307780
579PhosphorylationTEYVIATTKLMNGTS
EEEEEEEEECCCCCH		17.1027307780
594UbiquitinationWIEALMEKPF-----
HHHHHHCCCC-----		37.45-
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 VP33A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VP33A_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 VP33A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS11_HUMANVPS11physical
11382755
VPS18_HUMANVPS18physical
11382755
PLK2_RATPlk2physical
16203730
UVRAG_HUMANUVRAGphysical
18552835
VPS16_HUMANVPS16physical
22939629
VPS18_HUMANVPS18physical
22939629
VPS41_HUMANVPS41physical
22939629
VPS18_HUMANVPS18physical
26344197
VPS18_HUMANVPS18physical
25783203
VPS16_HUMANVPS16physical
23901104
VPS11_HUMANVPS11physical
26463206
VPS16_HUMANVPS16physical
26463206
TGFA1_HUMANTGFBRAP1physical
26463206
VPS41_HUMANVPS41physical
26463206
VPS18_HUMANVPS18physical
26463206
UVRAG_HUMANUVRAGphysical
24554770
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 VP33A_HUMAN

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Related Literatures of Post-Translational Modification

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