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 . |
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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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MASSAASSE ------CCCCHHCHH | 16.52 | 22223895 | |
3 | Phosphorylation | -----MASSAASSEH -----CCCCHHCHHH | 21.15 | 24173317 | |
4 | Phosphorylation | ----MASSAASSEHF ----CCCCHHCHHHH | 20.51 | 24173317 | |
13 (in isoform 1) | Ubiquitination | - | 54.95 | 21890473 | |
13 | Malonylation | ASSEHFEKLHEIFRG HCHHHHHHHHHHHHH | 54.95 | 26320211 | |
13 | Ubiquitination | ASSEHFEKLHEIFRG HCHHHHHHHHHHHHH | 54.95 | 23000965 | |
38 | Phosphorylation | RLLGTAGTEEKKKLI HHHCCCCCHHHHHHH | 38.21 | 21815630 | |
41 | 2-Hydroxyisobutyrylation | GTAGTEEKKKLIRDF CCCCCHHHHHHHHCH | 49.31 | - | |
51 | Ubiquitination | LIRDFDEKQQEANET HHHCHHHHHHHHHHH | 60.16 | 29967540 | |
72 | Phosphorylation | ELRYAPLSFRNPMMS HHHHCCCCCCCHHHH | 22.54 | 29523821 | |
79 | Phosphorylation | SFRNPMMSKLRNYRK CCCCHHHHHHHHHHH | 23.45 | 29523821 | |
80 | Malonylation | FRNPMMSKLRNYRKD CCCHHHHHHHHHHHH | 33.30 | 30639696 | |
84 | Phosphorylation | MMSKLRNYRKDLAKL HHHHHHHHHHHHHHH | 16.77 | 22817900 | |
90 | Ubiquitination | NYRKDLAKLHREVRS HHHHHHHHHHHHHHC | 52.72 | 29967540 | |
97 | Phosphorylation | KLHREVRSTPLTATP HHHHHHHCCCCCCCC | 39.28 | 24719451 | |
98 | Phosphorylation | LHREVRSTPLTATPG HHHHHHCCCCCCCCC | 16.26 | 27251275 | |
101 | Phosphorylation | EVRSTPLTATPGGRG HHHCCCCCCCCCCCC | 29.68 | 29396449 | |
103 | Phosphorylation | RSTPLTATPGGRGDM HCCCCCCCCCCCCCC | 19.75 | 25159151 | |
107 | Methylation | LTATPGGRGDMKYGI CCCCCCCCCCCCCEE | 43.80 | 24129315 | |
111 | Ubiquitination | PGGRGDMKYGIYAVE CCCCCCCCCEEEEEC | 45.10 | 33845483 | |
112 | Phosphorylation | GGRGDMKYGIYAVEN CCCCCCCCEEEEECC | 11.34 | 21945579 | |
115 | Phosphorylation | GDMKYGIYAVENEHM CCCCCEEEEECCHHH | 10.55 | 21945579 | |
127 | Phosphorylation | EHMNRLQSQRAMLLQ HHHHHHHHHHHHHHH | 26.65 | 28509920 | |
136 | Phosphorylation | RAMLLQGTESLNRAT HHHHHHCHHHHHHHH | 14.94 | 30266825 | |
138 | Phosphorylation | MLLQGTESLNRATQS HHHHCHHHHHHHHHH | 30.68 | 30266825 | |
143 | Phosphorylation | TESLNRATQSIERSH HHHHHHHHHHHHHHH | 21.44 | 29978859 | |
145 | Phosphorylation | SLNRATQSIERSHRI HHHHHHHHHHHHHCC | 23.28 | 24719451 | |
149 | Phosphorylation | ATQSIERSHRIATET HHHHHHHHHCCCCCH | 12.34 | 24706070 | |
154 | Phosphorylation | ERSHRIATETDQIGS HHHHCCCCCHHHHHH | 36.73 | 20873877 | |
156 | Phosphorylation | SHRIATETDQIGSEI HHCCCCCHHHHHHHH | 28.93 | 20873877 | |
161 | Phosphorylation | TETDQIGSEIIEELG CCHHHHHHHHHHHHH | 27.53 | 29116813 | |
177 | O-linked_Glycosylation | QRDQLERTKSRLVNT HHHHHHHHHHHHHCC | 24.81 | 29237092 | |
179 | Phosphorylation | DQLERTKSRLVNTSE HHHHHHHHHHHCCCH | 30.18 | 25159151 | |
179 | O-linked_Glycosylation | DQLERTKSRLVNTSE HHHHHHHHHHHCCCH | 30.18 | 29237092 | |
184 | Phosphorylation | TKSRLVNTSENLSKS HHHHHHCCCHHHHHH | 29.91 | 25262027 | |
185 | Phosphorylation | KSRLVNTSENLSKSR HHHHHCCCHHHHHHH | 21.20 | 30266825 | |
189 | Phosphorylation | VNTSENLSKSRKILR HCCCHHHHHHHHHHH | 39.92 | 19664995 | |
190 | Ubiquitination | NTSENLSKSRKILRS CCCHHHHHHHHHHHH | 58.40 | 23000965 | |
193 | Ubiquitination | ENLSKSRKILRSMSR HHHHHHHHHHHHHCC | 53.86 | 23000965 | |
203 | Phosphorylation | RSMSRKVTTNKLLLS HHHCCCHHHHHHHHH | 27.90 | - | |
210 | Phosphorylation | TTNKLLLSIIILLEL HHHHHHHHHHHHHHH | 16.23 | - | |
225 | Phosphorylation | AILGGLVYYKFFRSH HHHHHHHHHHHHCCC | 13.14 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of VTI1B_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VTI1B_HUMAN !! |
* 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 !! |
Kegg Disease | ||||||
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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. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |