VTI1B_HUMAN - dbPTM
VTI1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTI1B_HUMAN
UniProt AC Q9UEU0
Protein Name Vesicle transport through interaction with t-SNAREs homolog 1B
Gene Name VTI1B
Organism Homo sapiens (Human).
Sequence Length 232
Subcellular Localization Early endosome membrane
Single-pass type IV membrane protein . Late endosome membrane
Single-pass type IV membrane protein . Lysosome membrane . Cytoplasmic granule . Recycling endosome 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. May be concerned with increased secretion of cytokines associated with cellular senescence..
Protein Sequence MASSAASSEHFEKLHEIFRGLHEDLQGVPERLLGTAGTEEKKKLIRDFDEKQQEANETLAEMEEELRYAPLSFRNPMMSKLRNYRKDLAKLHREVRSTPLTATPGGRGDMKYGIYAVENEHMNRLQSQRAMLLQGTESLNRATQSIERSHRIATETDQIGSEIIEELGEQRDQLERTKSRLVNTSENLSKSRKILRSMSRKVTTNKLLLSIIILLELAILGGLVYYKFFRSH
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------MASSAASSE
------CCCCHHCHH
16.5222223895
3Phosphorylation-----MASSAASSEH
-----CCCCHHCHHH
21.1524173317
4Phosphorylation----MASSAASSEHF
----CCCCHHCHHHH
20.5124173317
13 (in isoform 1)Ubiquitination-54.9521890473
13MalonylationASSEHFEKLHEIFRG
HCHHHHHHHHHHHHH
54.9526320211
13UbiquitinationASSEHFEKLHEIFRG
HCHHHHHHHHHHHHH
54.9523000965
38PhosphorylationRLLGTAGTEEKKKLI
HHHCCCCCHHHHHHH
38.2121815630
412-HydroxyisobutyrylationGTAGTEEKKKLIRDF
CCCCCHHHHHHHHCH
49.31-
51UbiquitinationLIRDFDEKQQEANET
HHHCHHHHHHHHHHH
60.1629967540
72PhosphorylationELRYAPLSFRNPMMS
HHHHCCCCCCCHHHH
22.5429523821
79PhosphorylationSFRNPMMSKLRNYRK
CCCCHHHHHHHHHHH
23.4529523821
80MalonylationFRNPMMSKLRNYRKD
CCCHHHHHHHHHHHH
33.3030639696
84PhosphorylationMMSKLRNYRKDLAKL
HHHHHHHHHHHHHHH
16.7722817900
90UbiquitinationNYRKDLAKLHREVRS
HHHHHHHHHHHHHHC
52.7229967540
97PhosphorylationKLHREVRSTPLTATP
HHHHHHHCCCCCCCC
39.2824719451
98PhosphorylationLHREVRSTPLTATPG
HHHHHHCCCCCCCCC
16.2627251275
101PhosphorylationEVRSTPLTATPGGRG
HHHCCCCCCCCCCCC
29.6829396449
103PhosphorylationRSTPLTATPGGRGDM
HCCCCCCCCCCCCCC
19.7525159151
107MethylationLTATPGGRGDMKYGI
CCCCCCCCCCCCCEE
43.8024129315
111UbiquitinationPGGRGDMKYGIYAVE
CCCCCCCCCEEEEEC
45.1033845483
112PhosphorylationGGRGDMKYGIYAVEN
CCCCCCCCEEEEECC
11.3421945579
115PhosphorylationGDMKYGIYAVENEHM
CCCCCEEEEECCHHH
10.5521945579
127PhosphorylationEHMNRLQSQRAMLLQ
HHHHHHHHHHHHHHH
26.6528509920
136PhosphorylationRAMLLQGTESLNRAT
HHHHHHCHHHHHHHH
14.9430266825
138PhosphorylationMLLQGTESLNRATQS
HHHHCHHHHHHHHHH
30.6830266825
143PhosphorylationTESLNRATQSIERSH
HHHHHHHHHHHHHHH
21.4429978859
145PhosphorylationSLNRATQSIERSHRI
HHHHHHHHHHHHHCC
23.2824719451
149PhosphorylationATQSIERSHRIATET
HHHHHHHHHCCCCCH
12.3424706070
154PhosphorylationERSHRIATETDQIGS
HHHHCCCCCHHHHHH
36.7320873877
156PhosphorylationSHRIATETDQIGSEI
HHCCCCCHHHHHHHH
28.9320873877
161PhosphorylationTETDQIGSEIIEELG
CCHHHHHHHHHHHHH
27.5329116813
177O-linked_GlycosylationQRDQLERTKSRLVNT
HHHHHHHHHHHHHCC
24.8129237092
179PhosphorylationDQLERTKSRLVNTSE
HHHHHHHHHHHCCCH
30.1825159151
179O-linked_GlycosylationDQLERTKSRLVNTSE
HHHHHHHHHHHCCCH
30.1829237092
184PhosphorylationTKSRLVNTSENLSKS
HHHHHHCCCHHHHHH
29.9125262027
185PhosphorylationKSRLVNTSENLSKSR
HHHHHCCCHHHHHHH
21.2030266825
189PhosphorylationVNTSENLSKSRKILR
HCCCHHHHHHHHHHH
39.9219664995
190UbiquitinationNTSENLSKSRKILRS
CCCHHHHHHHHHHHH
58.4023000965
193UbiquitinationENLSKSRKILRSMSR
HHHHHHHHHHHHHCC
53.8623000965
203PhosphorylationRSMSRKVTTNKLLLS
HHHCCCHHHHHHHHH
27.90-
210PhosphorylationTTNKLLLSIIILLEL
HHHHHHHHHHHHHHH
16.23-
225PhosphorylationAILGGLVYYKFFRSH
HHHHHHHHHHHHCCC
13.14-

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 VTI1B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTI1B_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 VTI1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN5_HUMANPTPN5physical
25416956
SYNE4_HUMANSYNE4physical
25416956
TRI59_HUMANTRIM59physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
LRAD1_HUMANLDLRAD1physical
25416956
CAND2_HUMANCAND2physical
26186194
EI2BE_HUMANEIF2B5physical
26186194
RNF13_HUMANRNF13physical
26186194
EI2BA_HUMANEIF2B1physical
26186194
CCDC9_HUMANCCDC9physical
26186194
EI2BD_HUMANEIF2B4physical
26186194
IPO7_HUMANIPO7physical
26186194
SNAA_HUMANNAPAphysical
26186194
IPO9_HUMANIPO9physical
26186194
STX18_HUMANSTX18physical
26186194
IF4A3_HUMANEIF4A3physical
26186194
NBAS_HUMANNBASphysical
26186194
SNAG_HUMANNAPGphysical
26186194
CWC27_HUMANCWC27physical
26186194
CWC22_HUMANCWC22physical
26186194
STX6_HUMANSTX6physical
26186194
HPHL1_HUMANHEPHL1physical
26186194
CALL3_HUMANCALML3physical
26186194
STX7_HUMANSTX7physical
26186194
ACINU_HUMANACIN1physical
26186194
ECD_HUMANECDphysical
26186194
AP3B1_HUMANAP3B1physical
26186194
S10A3_HUMANS100A3physical
26186194
STX12_HUMANSTX12physical
26186194
AP3M1_HUMANAP3M1physical
26186194
VPS45_HUMANVPS45physical
26186194
SESD1_HUMANSESTD1physical
26186194
UBF1_HUMANUBTFphysical
26186194
EI2BB_HUMANEIF2B2physical
26186194
STXB5_HUMANSTXBP5physical
26186194
EI2BG_HUMANEIF2B3physical
26186194
STX8_HUMANSTX8physical
26186194
DSG4_HUMANDSG4physical
26186194
FHL2_HUMANFHL2physical
26186194
ARL10_HUMANARL10physical
26186194
STX10_HUMANSTX10physical
26186194
VAMP3_HUMANVAMP3physical
26186194
CASC3_HUMANCASC3physical
26186194
PPAL_HUMANACP2physical
26186194
CS025_HUMANC19orf25physical
26186194
2A5E_HUMANPPP2R5Ephysical
26186194
STX8_HUMANSTX8physical
21516116
SNAG_HUMANNAPGphysical
28514442
STX12_HUMANSTX12physical
28514442
STX7_HUMANSTX7physical
28514442
CWC22_HUMANCWC22physical
28514442
STX6_HUMANSTX6physical
28514442
SESD1_HUMANSESTD1physical
28514442
STX18_HUMANSTX18physical
28514442
EI2BG_HUMANEIF2B3physical
28514442
EPN4_HUMANCLINT1physical
28514442
STXB5_HUMANSTXBP5physical
28514442
SNAA_HUMANNAPAphysical
28514442
CCDC9_HUMANCCDC9physical
28514442
CWC27_HUMANCWC27physical
28514442
STX8_HUMANSTX8physical
28514442
IPO9_HUMANIPO9physical
28514442
FHL2_HUMANFHL2physical
28514442
EI2BA_HUMANEIF2B1physical
28514442
EI2BB_HUMANEIF2B2physical
28514442
RNF13_HUMANRNF13physical
28514442
EI2BE_HUMANEIF2B5physical
28514442
EI2BD_HUMANEIF2B4physical
28514442
AP3B1_HUMANAP3B1physical
28514442
VAMP3_HUMANVAMP3physical
28514442
ARL10_HUMANARL10physical
28514442
VPS45_HUMANVPS45physical
28514442
ACINU_HUMANACIN1physical
28514442
UBF1_HUMANUBTFphysical
28514442
HPHL1_HUMANHEPHL1physical
28514442
ASPH_HUMANASPHphysical
28514442
DSG4_HUMANDSG4physical
28514442
TBC15_HUMANTBC1D15physical
28514442
2A5E_HUMANPPP2R5Ephysical
28514442
AP3M1_HUMANAP3M1physical
28514442
CAND2_HUMANCAND2physical
28514442
STX10_HUMANSTX10physical
28514442
PPAL_HUMANACP2physical
28514442
NBAS_HUMANNBASphysical
28514442
IF4A3_HUMANEIF4A3physical
28514442
IPO7_HUMANIPO7physical
28514442
ECD_HUMANECDphysical
28514442
CASC3_HUMANCASC3physical
28514442
EXOC1_HUMANEXOC1physical
27173435
DCTN2_HUMANDCTN2physical
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 VTI1B_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.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103, AND MASSSPECTROMETRY.

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