VTI1A_HUMAN - dbPTM
VTI1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTI1A_HUMAN
UniProt AC Q96AJ9
Protein Name Vesicle transport through interaction with t-SNAREs homolog 1A
Gene Name VTI1A
Organism Homo sapiens (Human).
Sequence Length 217
Subcellular Localization Cytoplasmic vesicle . Golgi apparatus membrane
Single-pass type IV membrane protein.
Protein Description V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be involved in increased cytokine secretion associated with cellular senescence..
Protein Sequence MSSDFEGYEQDFAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEAKELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDDGNSSENQRAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARERLRETDANLGKSSRILTGMLRRIIQNRILLVILGIIVVITILMAITFSVRRH
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
2Phosphorylation------MSSDFEGYE
------CCCCCCCHH
38.3223663014
3Phosphorylation-----MSSDFEGYEQ
-----CCCCCCCHHH
45.0523663014
8PhosphorylationMSSDFEGYEQDFAVL
CCCCCCCHHHHHHHH
11.8328464451
16PhosphorylationEQDFAVLTAEITSKI
HHHHHHHHHHHHHHH
18.6924719451
35UbiquitinationRLPPDEKKQMVANVE
CCCCHHHHHHHHHHH
41.39-
43UbiquitinationQMVANVEKQLEEAKE
HHHHHHHHHHHHHHH
56.7723000965
49UbiquitinationEKQLEEAKELLEQMD
HHHHHHHHHHHHHCC
52.7723000965
55SulfoxidationAKELLEQMDLEVREI
HHHHHHHCCCHHHHC
4.6621406390
66PhosphorylationVREIPPQSRGMYSNR
HHHCCCCCCCCCHHH
36.25-
76PhosphorylationMYSNRMRSYKQEMGK
CCHHHHHHHHHHHCC
27.60-
78UbiquitinationSNRMRSYKQEMGKLE
HHHHHHHHHHHCCCC
40.8224816145
86PhosphorylationQEMGKLETDFKRSRI
HHHCCCCCHHHHHHC
58.1129083192
89UbiquitinationGKLETDFKRSRIAYS
CCCCCHHHHHHCCCC
52.88-
91PhosphorylationLETDFKRSRIAYSDE
CCCHHHHHHCCCCHH
28.73-
95PhosphorylationFKRSRIAYSDEVRNE
HHHHHCCCCHHHHHH
17.8125884760
96PhosphorylationKRSRIAYSDEVRNEL
HHHHCCCCHHHHHHH
20.4827486199
110PhosphorylationLLGDDGNSSENQRAH
HCCCCCCCCHHHHHH
44.5528450419
111PhosphorylationLGDDGNSSENQRAHL
CCCCCCCCHHHHHHH
44.5628450419
122PhosphorylationRAHLLDNTERLERSS
HHHHHCHHHHHHHHH
23.3428555341
136PhosphorylationSRRLEAGYQIAVETE
HHHHHHHHHHEHHHH
12.0928796482
142PhosphorylationGYQIAVETEQIGQEM
HHHHEHHHHHHHHHH
26.9627732954
154PhosphorylationQEMLENLSHDREKIQ
HHHHHCCCCCHHHHH
34.6227732954
170PhosphorylationARERLRETDANLGKS
HHHHHHHHHCCCCHH
33.7029083192
176UbiquitinationETDANLGKSSRILTG
HHHCCCCHHHHHHHH
48.7221906983
178PhosphorylationDANLGKSSRILTGML
HCCCCHHHHHHHHHH
27.1628348404
183UbiquitinationKSSRILTGMLRRIIQ
HHHHHHHHHHHHHHH
15.0727667366
213PhosphorylationILMAITFSVRRH---
HHHHHHHHHHCC---
13.18-

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 VTI1A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTI1A_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 VTI1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STX7_HUMANSTX7physical
11101518
STX8_HUMANSTX8physical
11101518
VAMP8_HUMANVAMP8physical
11101518

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 VTI1A_HUMAN

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Related Literatures of Post-Translational Modification

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