RAB23
entrez
51715
canonical
uniprot
Q9ULC3
canonical
ensembl
ENSG00000112210
resolver
ensp
ENSP00000320413
resolver
ensp
ENSP00000417610
resolver
ensp
ENSP00000545585
resolver
ensp
ENSP00000545586
resolver
ensp
ENSP00000545587
resolver
ensp
ENSP00000545588
resolver
ensp
ENSP00000545589
resolver
ensp
ENSP00000545590
resolver
ensp
ENSP00000545591
resolver
ensp
ENSP00000545592
resolver
ensp
ENSP00000545593
resolver
ensp
ENSP00000608894
resolver
ensp
ENSP00000608895
resolver
ensp
ENSP00000608896
resolver
ensp
ENSP00000608897
resolver
ensp
ENSP00000608898
resolver
ensp
ENSP00000634733
resolver
ensp
ENSP00000634734
resolver
enst
ENST00000317483
resolver
enst
ENST00000468148
resolver
enst
ENST00000875526
resolver
enst
ENST00000875527
resolver
enst
ENST00000875528
resolver
enst
ENST00000875529
resolver
enst
ENST00000875530
resolver
enst
ENST00000875531
resolver
enst
ENST00000875532
resolver
enst
ENST00000875533
resolver
enst
ENST00000875534
resolver
enst
ENST00000938835
resolver
enst
ENST00000938836
resolver
enst
ENST00000938837
resolver
enst
ENST00000938838
resolver
enst
ENST00000938839
resolver
enst
ENST00000964674
resolver
enst
ENST00000964675
resolver
genesymbol
RAB23
resolver
hgnc
HGNC:14263
resolver
uniprot
B2R9I5
resolver
uniprot
Q68DJ6
resolver
uniprot
Q8NI06
resolver
uniprot
Q9P023
resolver
uniprot_entry
RAB23_HUMAN
resolver
uniprot_sec
B2R9I5
resolver
uniprot_sec
Q68DJ6
resolver
uniprot_sec
Q8NI06
resolver
uniprot_sec
Q9P023
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP (Probable). Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity (Probable). Inhibited by GDP dissociation inhibitors (GDIs) (Probable). {ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYLAEKYLQKLKQQIAEDPELTHSSSNKIGVFNTSGGSHSGQNSGTLNGGDVINLRPNKQRTKKNRNPFSSCSIP
uniprot
proteins
disease_involvement
DISEASE: Carpenter syndrome 1 (CRPT1) [MIM:201000]: A rare autosomal recessive disorder characterized by acrocephaly with variable synostosis of the sagittal, lambdoid, and coronal sutures; peculiar facies; brachydactyly of the hands with syndactyly; preaxial polydactyly and syndactyly of the feet; congenital heart defects; growth retardation; intellectual disability; hypogenitalism; and obesity. In addition, cerebral malformations, oral and dental abnormalities, coxa valga, genu valgum, hydronephrosis, precocious puberty, and hearing loss may be observed. {ECO:0000269|PubMed:17503333, ECO:0000269|PubMed:21412941, ECO:0000269|PubMed:40825043}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. In conjunction with IFT57 and KIF17, it drives the localization of specific G protein-coupled receptors, such as the dopamime receptor DRD1, to primary cilia (PubMed:26182404). Has a critical role in the formation and elongation of neuronal primary cilia, thereby impacting the activation of sonic hedgehog (Shh) signaling (PubMed:40825043). Additionally, it is involved in the down-regulation of Shh signaling by cooperating with SUFU to prevent the nuclear import of GLI1 transcription factor, thus suppressing its transcriptional activity (PubMed:22365972) (PubMed:39615683). Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes (PubMed:22452336). {ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:22452336, ECO:0000269|PubMed:26182404, ECO:0000269|PubMed:39615683, ECO:0000269|PubMed:40825043}.
uniprot
proteins
mass_dalton
26659
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17503333
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21255211
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21412941
uniprot
proteins
pubmed
22365972
uniprot
proteins
pubmed
22452336
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26182404
uniprot
proteins
pubmed
39615683
uniprot
proteins
pubmed
40825043
uniprot
proteins
sequence_length
237
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35288}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:P35288}. Cytoplasm {ECO:0000269|PubMed:22365972}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:22452336}. Endosome membrane {ECO:0000250, ECO:0000250|UniProtKB:P35288}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000269|PubMed:21255211}.
uniprot
proteins