Molecular Target Synopsis
Domains and Structures
Drugs and Clinical Candidates
Ligand Efficiency Plot
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
Germline Genetics

RAB13 (P51153) - Overview - Molecular Target Synopsis


RAB13, Ras-related protein Rab-13
UniProt P51153

Also Known as RAB13_HUMAN, RAB13

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis. Interacts (GTP-bound form) with MICALL2; competes with RAB8A and is involved in tight junctions assembly. Interacts (GTP-bound form) with MICALL1. Interacts (GTP-bound form) with MICAL1, MICAL3, MICALCL, EHBP1 and EHBP1L1; ternary complexes of RAB8A, RAB13 and either MICAL1 or EHBP1L1 are possible. Interacts with PRKACA; downstream effector of RAB13 involved in tight junction assembly. Interacts with GRB2; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA. Interacts (isoprenylated form) with PDE6D; dissociates RAB13 from membranes. Interacts with BICDL2/BICDR2. Interacts with LEPROT and LEPROTL1.

Isoforms / Transcripts (Protein Coding)

Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform

Sub-cellular localization

UniProt: RAB13 is active in the following subcellular-locations: cell junction, cell membrane, cell projection, cytoplasmic vesicle membrane, golgi apparatus, lamellipodium, recycling endosome membrane, tight junction, trans-golgi network membrane.
GO terms: RAB13 is active in the following subcellular-locations: bicellular tight junction, cell junction, cytoplasmic vesicle, cytoplasmic vesicle membrane, cytosol, endocytic vesicle, extracellular exosome, insulin-responsive compartment, lamellipodium, lateral plasma membrane, neuron projection, plasma membrane, recycling endosome, recycling endosome membrane, trans-Golgi network.

GO terms

Gene Copy Number Variation

In COSMIC - Cell Lines Project RAB13 has gain in 15 cell-lines, loss in 0 cell-lines and no signal in 990 cell-lines. (see details)

Gene Expression

In NCI60, the highest expressing cell lines are: SNB_75, OVCAR_4, MCF7

In Array Express (RNA-seq of 675 commonly used human cancer cell lines), the highest expressing cell lines are: COV644, Caki-1, COLO-818

In Array Express (RNA-seq of long poly adenylated RNA and long non poly adenylated RNA from ENCODE cell lines), the highest expressing cell lines are: IMR-90, NHLF, AG445

(see details)

3D Structures

At greater than 50% identity similarity to RAB13 there are:
56 structures (108 chains) solved
47 are solved in complex with at least one small molecule ligand
1 are solved with an approved drug

RAB13 is solved in complex with the approved drug(s):


(see details)
Molecular Target 3D Synopsis

Screening and Chemistry

RAB13 has been screened with compounds ( bioactivities). (see details)