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Protein Page:
RAB9A (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RAB9A Involved in the transport of proteins between the endosomes and the trans Golgi network. Interacts (preferentially in its GTP-bound form) with GCC2 (via its GRIP domain). Belongs to the small GTPase superfamily. Rab family. Note: This description may include information from UniProtKB.
Protein type: G protein; G protein, monomeric; G protein, monomeric, Rab
Cellular Component: Golgi membrane; endoplasmic reticulum membrane; phagocytic vesicle membrane; lysosome; late endosome; plasma membrane; phagocytic vesicle
Molecular Function: GTPase activity; protein binding; GDP binding; GTP binding
Biological Process: protein transport; GTP catabolic process; small GTPase mediated signal transduction; positive regulation of exocytosis
Reference #:  P51151 (UniProtKB)
Alt. Names/Synonyms: RAB9; RAB9, member RAS oncogene family; RAB9A; RAB9A, member RAS oncogene family; Ras-related protein Rab-9A
Gene Symbols: RAB9A
Molecular weight: 22,838 Da
Basal Isoelectric point: 5.26  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RAB9A

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 T34 YVTNKFDTQLFHTIG
0 2 K103-u QNLSNWKkEFIyyAD
0 36 Y107-p NWKkEFIyyADVKEP
0 3 Y108-p WKkEFIyyADVKEPE
0 2 K112 FIyyADVKEPESFPF
0 4 S179-p VLATEDRsDHLIQTD
  mouse

 
S34-p YVTNKFDsQLFHTIG
K103-u QNLSNWKkEFIYYAD
Y107 NWKkEFIYYADVkEP
Y108 WKkEFIYYADVkEPE
K112-u FIYYADVkEPESFPF
S179-p ILATEDRsEHLIQTD
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