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Protein Page:
Rab4 (human)

Overview
Rab4 a member of the RAB family of RAS-related GTP-binding proteins, important regulators of vesicular transport and are located in specific intracellular compartments. RAB7 has been localized to late endosomes and shown to be important in the late endocytic pathway. In addition, it has been shown to have a fundamental role in the cellular vacuolation induced by the cytotoxin VacA of Helicobacter pylori. Mutations in this protein cause Charcot-Marie-Tooth type 2B neuropathy. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric; G protein, monomeric, Rab; G protein
Chromosomal Location of Human Ortholog: 1q42-q43
Cellular Component: cytosol; endosome; perinuclear region of cytoplasm; plasma membrane; recycling endosome; vesicle
Molecular Function: ATPase activator activity; ATPase binding; GDP binding; GTP binding; GTPase activity; ionotropic glutamate receptor binding; protein binding; protein transporter activity; syntaxin binding
Biological Process: antigen processing and presentation; intracellular protein transport; metabolic process; nucleocytoplasmic transport; positive regulation of ATPase activity; Rab protein signal transduction; regulation of endocytosis
Reference #:  P20338 (UniProtKB)
Gene Symbols: RAB4A
Molecular weight: 24,390 Da
Basal Isoelectric point: 5.82  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Rab4

Protein Structure Not Found.
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Sites Implicated In
intracellular localization: S204‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 2 T24‑p LVIGNAGtGKSCLLH
0 1 T137‑p LDADREVtFLEAsRF
0 1 S142‑p EVtFLEAsRFAQENE
0 4 S190‑p LDPERMGsGIQyGDA
0 1 Y194‑p RMGsGIQyGDAALRQ
2 0 S204‑p AALRQLRsPRRAQAP
  mouse

 
T24 LVIGNAGTGKSCLLH
T137 LDADREVTFLEASRF
S142 EVTFLEASRFAQENE
S190 LDPERMGSGIQYGDA
Y194 RMGSGIQYGDAALRQ
S204 AALRQLRSPRRTQAP
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