UniProt ID | RAB3A_HUMAN | |
---|---|---|
UniProt AC | P20336 | |
Protein Name | Ras-related protein Rab-3A | |
Gene Name | RAB3A | |
Organism | Homo sapiens (Human). | |
Sequence Length | 220 | |
Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . |
|
Protein Description | Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.. | |
Protein Sequence | MASATDSRYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLSDQQVPPHQDCAC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
42 | Phosphorylation | KTSFLFRYADDSFTP CEEEEEEECCCCCCC | 13.67 | 22817900 | |
65 | Phosphorylation | DFKVKTIYRNDKRIK CEEEEEEEECCCEEE | 14.48 | - | |
78 | Phosphorylation | IKLQIWDTAGQERYR EEEEEECCCCHHHHH | 20.07 | 28857561 | |
84 | Phosphorylation | DTAGQERYRTITTAY CCCCHHHHHHHHHHH | 16.03 | 19060867 | |
86 | Phosphorylation | AGQERYRTITTAYYR CCHHHHHHHHHHHHH | 17.46 | 26824392 | |
88 | Phosphorylation | QERYRTITTAYYRGA HHHHHHHHHHHHHCC | 12.54 | - | |
89 | Phosphorylation | ERYRTITTAYYRGAM HHHHHHHHHHHHCCC | 14.60 | 24961811 | |
91 | Phosphorylation | YRTITTAYYRGAMGF HHHHHHHHHHCCCEE | 7.51 | 21951684 | |
92 | Phosphorylation | RTITTAYYRGAMGFI HHHHHHHHHCCCEEE | 10.50 | 21951684 | |
102 | Phosphorylation | AMGFILMYDITNEES CCEEEEEEECCCHHH | 10.76 | 21951684 | |
123 | Phosphorylation | WSTQIKTYSWDNAQV CCCEEEEEEECCCEE | 11.63 | - | |
173 | Ubiquitination | AKDNINVKQTFERLV HCCCCCHHHHHHHHH | 38.85 | - | |
188 | Phosphorylation | DVICEKMSESLDTAD HHHHHHHHHCCCCCC | 34.79 | 25850435 | |
190 | Phosphorylation | ICEKMSESLDTADPA HHHHHHHCCCCCCCC | 25.00 | 25159151 | |
193 | Phosphorylation | KMSESLDTADPAVTG HHHHCCCCCCCCCCC | 37.95 | 29514088 | |
218 | Geranylgeranylation | QVPPHQDCAC----- CCCCCCCCCC----- | 3.15 | 1648736 | |
218 | Geranylgeranylation | QVPPHQDCAC----- CCCCCCCCCC----- | 3.15 | 1648736 | |
220 | Methylation | PPHQDCAC------- CCCCCCCC------- | 7.82 | 1648736 | |
220 | Geranylgeranylation | PPHQDCAC------- CCCCCCCC------- | 7.82 | 1648736 | |
220 | Geranylgeranylation | PPHQDCAC------- CCCCCCCC------- | 7.82 | 1648736 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
86 | T | Phosphorylation | Kinase | LRRK2 | Q5S007 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
86 | T | Phosphorylation |
| 26824392 |
* 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 RAB3A_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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Prenylation | |
Reference | PubMed |
"Rab geranylgeranyl transferase catalyzes the geranylgeranylation ofadjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."; Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.; Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994). Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220, AND MASS SPECTROMETRY. | |
"Isoprenoid modification of rab proteins terminating in CC or CXCmotifs."; Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R.,Sinensky M., Balch W.E., Buss J.E., Der C.J.; Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991). Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220. |