VAMP7_HUMAN - dbPTM
VAMP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAMP7_HUMAN
UniProt AC P51809
Protein Name Vesicle-associated membrane protein 7
Gene Name VAMP7
Organism Homo sapiens (Human).
Sequence Length 220
Subcellular Localization Cytoplasmic vesicle, secretory vesicle membrane
Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane
Single-pass type IV membrane protein. Late endosome membrane
Single-pass type IV membrane protein. Lysosome membrane
S
Protein Description Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation..
Protein Sequence MAILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENKGLDKVMETQAQVDELKGIMVRNIDLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCMKNLKLTIIIIIVSIVFIYIIVSPLCGGFTWPSCVKK
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------MAILFAVVA
------CCHHHHHHC
13.75-
12PhosphorylationFAVVARGTTILAKHA
HHHHCCCCEEHHCCC
12.7119413330
13PhosphorylationAVVARGTTILAKHAW
HHHCCCCEEHHCCCC
19.4719413330
38PhosphorylationQILAKIPSENNKLTY
HHHHHCCCCCCCEEE
57.3319845377
42MalonylationKIPSENNKLTYSHGN
HCCCCCCCEEEECCC
54.5126320211
45PhosphorylationSENNKLTYSHGNYLF
CCCCCEEEECCCCHH
14.76-
50PhosphorylationLTYSHGNYLFHYICQ
EEEECCCCHHEEEEC
18.4819845377
62PhosphorylationICQDRIVYLCITDDD
EECCCEEEEEEECCH
8.0920068231
84 (in isoform 3)Ubiquitination-65.2021890473
96 (in isoform 3)Ubiquitination-29.2221890473
119 (in isoform 3)Ubiquitination-59.6121890473
121UbiquitinationLKHHSENKGLDKVME
HHHHHCCCCHHHHHH
57.72-
125UbiquitinationSENKGLDKVMETQAQ
HCCCCHHHHHHHHHH
48.8221890473
125 (in isoform 2)Ubiquitination-48.8221890473
125 (in isoform 1)Ubiquitination-48.8221890473
127SulfoxidationNKGLDKVMETQAQVD
CCCHHHHHHHHHHHH
5.9321406390
131 (in isoform 3)Ubiquitination-20.8421890473
137 (in isoform 1)Ubiquitination-44.3221890473
137 (in isoform 2)Ubiquitination-44.3221890473
137UbiquitinationQAQVDELKGIMVRNI
HHHHHHHHCCEEECC
44.3221906983
160 (in isoform 1)Ubiquitination-51.2321890473
160UbiquitinationRLELLIDKTENLVDS
EEEEEEECCCCCCCC
51.2321906983
161PhosphorylationLELLIDKTENLVDSS
EEEEEECCCCCCCCC
26.7620068231
167PhosphorylationKTENLVDSSVTFKTT
CCCCCCCCCCCCCCC
21.1623401153
168PhosphorylationTENLVDSSVTFKTTS
CCCCCCCCCCCCCCC
22.2529255136
170PhosphorylationNLVDSSVTFKTTSRN
CCCCCCCCCCCCCHH
22.7429255136
172UbiquitinationVDSSVTFKTTSRNLA
CCCCCCCCCCCHHHH
41.3421890473
172 (in isoform 1)Ubiquitination-41.3421890473

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
45YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAMP7_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 VAMP7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP3D1_HUMANAP3D1physical
12853575
SNP29_HUMANSNAP29physical
12853575
AP3M1_HUMANAP3M1physical
12853575
SNP25_HUMANSNAP25physical
12853575
STX1A_HUMANSTX1Aphysical
12853575
SNP23_HUMANSNAP23physical
12853575
STX4_HUMANSTX4physical
12853575
SNP23_HUMANSNAP23physical
9614185
ANR27_HUMANANKRD27physical
19745841
STX6_HUMANSTX6physical
19557002
STX7_HUMANSTX7physical
19557002
STX8_HUMANSTX8physical
19557002
2AAA_HUMANPPP2R1Aphysical
27173435

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 VAMP7_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-168, AND MASSSPECTROMETRY.

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