RAB13
entrez
5872
canonical
uniprot
P51153
canonical
ensembl
ENSG00000143545
resolver
ensembl
ENSG00000285641
resolver
ensp
ENSP00000357564
resolver
ensp
ENSP00000480103
resolver
ensp
ENSP00000497071
resolver
enst
ENST00000368575
resolver
enst
ENST00000614713
resolver
enst
ENST00000648869
resolver
genesymbol
RAB13
resolver
hgnc
HGNC:9762
resolver
uniprot
A0A087WWB9
resolver
uniprot
A8K6B5
resolver
uniprot
D3DV67
resolver
uniprot
Q504R6
resolver
uniprot
Q5U0A6
resolver
uniprot
Q6GPG6
resolver
uniprot
Q96GU4
resolver
uniprot_entry
A0A087WWB9_HUMAN
resolver
uniprot_entry
Q504R6_HUMAN
resolver
uniprot_entry
RAB13_HUMAN
resolver
uniprot_sec
A8K6B5
resolver
uniprot_sec
D3DV67
resolver
uniprot_sec
Q5U0A6
resolver
uniprot_sec
Q6GPG6
resolver
uniprot_sec
Q96GU4
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) including DENND1C, which promote the exchange of bound GDP for free GTP (PubMed:20937701). Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors (GDIs) (Probable). Activated in response to insulin (By similarity). {ECO:0000250|UniProtKB:P35286, ECO:0000269|PubMed:20937701, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDNFNNTYISTIGIDFKIRTVDIEGKKIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRKVQKEQADKLAREHGIRFFETSAKSSMNVDEAFSSLARDILLKSGGRRSGNGNKPPSTDLKTCDKKNTNKCSLG
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: 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. RAB13 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. {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:15096524, ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:18779367, ECO:0000269|PubMed:20008558, ECO:0000269|PubMed:35343654}.
uniprot
proteins
mass_dalton
22774
uniprot
proteins
mutagenesis
MUTAGEN 22; /note="T->N: Dominant negative."; /evidence="ECO:0000269|PubMed:18779367"; MUTAGEN 67; /note="Q->L: Constitutively active mutant locked in the active GTP-bound form. Impairs transports of cargo from the trans-Golgi network to the recycling endosomes and alters the assembly of functional tight junctions."; /evidence="ECO:0000269|PubMed:18779367"; MUTAGEN 194..199; /note="KKNTNK->RRNTNR: In 3KR mutant; abolished stearoylation in response to S.flexneri infection."; /evidence="ECO:0000269|PubMed:30061757
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty acyltransferase IcsB, thereby disrupting the host actin cytoskeleton. {ECO:0000269|PubMed:30061757}.; PTM: Ubiquitinated via 'Lys-11'-linked ubiquitination on Lys-46 and Lys-58; impairing the recruitment of guanosine diphosphate (GDP) dissociation inhibitor 1/GDI1. {ECO:0000269|PubMed:35343654}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
12058051
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15096524
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15528189
uniprot
proteins
pubmed
16525024
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18779367
uniprot
proteins
pubmed
20008558
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20937701
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21795389
uniprot
proteins
pubmed
22562557
uniprot
proteins
pubmed
27552051
uniprot
proteins
pubmed
30061757
uniprot
proteins
pubmed
35343654
uniprot
proteins
pubmed
8294494
uniprot
proteins
pubmed
8375503
uniprot
proteins
pubmed
9712853
uniprot
proteins
sequence_length
203
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15528189}; Lipid-anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side {ECO:0000305|PubMed:8375503}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:8294494}; Lipid-anchor {ECO:0000305|PubMed:8375503}; Cytoplasmic side {ECO:0000305|PubMed:8375503}. Cell junction, tight junction {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:8294494}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18779367}. Recycling endosome membrane {ECO:0000269|PubMed:18779367}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions (PubMed:8294494). Relocalizes to the leading edge of lamellipodia in migrating endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q9DD03, ECO:0000269|PubMed:8294494}.
uniprot
proteins