RAB3A_HUMAN - dbPTM
RAB3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
42PhosphorylationKTSFLFRYADDSFTP
CEEEEEEECCCCCCC
13.6722817900
65PhosphorylationDFKVKTIYRNDKRIK
CEEEEEEEECCCEEE
14.48-
78PhosphorylationIKLQIWDTAGQERYR
EEEEEECCCCHHHHH
20.0728857561
84PhosphorylationDTAGQERYRTITTAY
CCCCHHHHHHHHHHH
16.0319060867
86PhosphorylationAGQERYRTITTAYYR
CCHHHHHHHHHHHHH
17.4626824392
88PhosphorylationQERYRTITTAYYRGA
HHHHHHHHHHHHHCC
12.54-
89PhosphorylationERYRTITTAYYRGAM
HHHHHHHHHHHHCCC
14.6024961811
91PhosphorylationYRTITTAYYRGAMGF
HHHHHHHHHHCCCEE
7.5121951684
92PhosphorylationRTITTAYYRGAMGFI
HHHHHHHHHCCCEEE
10.5021951684
102PhosphorylationAMGFILMYDITNEES
CCEEEEEEECCCHHH
10.7621951684
123PhosphorylationWSTQIKTYSWDNAQV
CCCEEEEEEECCCEE
11.63-
173UbiquitinationAKDNINVKQTFERLV
HCCCCCHHHHHHHHH
38.85-
188PhosphorylationDVICEKMSESLDTAD
HHHHHHHHHCCCCCC
34.7925850435
190PhosphorylationICEKMSESLDTADPA
HHHHHHHCCCCCCCC
25.0025159151
193PhosphorylationKMSESLDTADPAVTG
HHHHCCCCCCCCCCC
37.9529514088
218GeranylgeranylationQVPPHQDCAC-----
CCCCCCCCCC-----
3.151648736
218GeranylgeranylationQVPPHQDCAC-----
CCCCCCCCCC-----
3.151648736
220MethylationPPHQDCAC-------
CCCCCCCC-------
7.821648736
220GeranylgeranylationPPHQDCAC-------
CCCCCCCC-------
7.821648736
220GeranylgeranylationPPHQDCAC-------
CCCCCCCC-------
7.821648736

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
86TPhosphorylationKinaseLRRK2Q5S007
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
86TPhosphorylation

26824392

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 RAB3A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RP3A_HUMANRPH3Aphysical
10025402
SYTL4_HUMANSYTL4physical
11773082
RAE1_HUMANCHMphysical
12535645
SYTL4_HUMANSYTL4physical
11865063
SYUA_HUMANSNCAphysical
15207266
SYUA_HUMANSNCAphysical
15854772
BICL2_MOUSECcdc64bphysical
20360680
MSS4_HUMANRABIFphysical
25416956
RAB3I_HUMANRAB3IPphysical
25416956
RAE2_HUMANCHMLphysical
26186194
RAE1_HUMANCHMphysical
26186194
SYTL4_HUMANSYTL4physical
26186194
RAB3B_HUMANRAB3Bphysical
26186194
MOCOS_HUMANMOCOSphysical
26186194
RB33B_HUMANRAB33Bphysical
26186194
PGTA_HUMANRABGGTAphysical
26186194
VW5B2_HUMANVWA5B2physical
26186194
MOG1_HUMANRANGRFphysical
26186194
CAF17_HUMANIBA57physical
26186194
WIPI3_HUMANWDR45Bphysical
26186194
RAB3B_HUMANRAB3Bphysical
28514442
SYTL4_HUMANSYTL4physical
28514442
RAE1_HUMANCHMphysical
28514442
RAE2_HUMANCHMLphysical
28514442
MOG1_HUMANRANGRFphysical
28514442
RB33B_HUMANRAB33Bphysical
28514442
GDIA_HUMANGDI1physical
28514442
MOCOS_HUMANMOCOSphysical
28514442
VW5B2_HUMANVWA5B2physical
28514442
GDIB_HUMANGDI2physical
28514442

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 RAB3A_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"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.

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