ARL13B
entrez
200894
canonical
uniprot
Q3SXY8
canonical
ensembl
ENSG00000169379
resolver
ensp
ENSP00000306225
resolver
ensp
ENSP00000377769
resolver
ensp
ENSP00000420780
resolver
ensp
ENSP00000445145
resolver
ensp
ENSP00000505036
resolver
ensp
ENSP00000505252
resolver
ensp
ENSP00000505366
resolver
ensp
ENSP00000505396
resolver
enst
ENST00000486562
resolver
enst
ENST00000679404
resolver
enst
ENST00000679587
resolver
enst
ENST00000681655
resolver
genesymbol
ARL13B
resolver
genesymbol_syn
ARL2L1
resolver
hgnc
HGNC:25419
resolver
uniprot
A0A7P0T892
resolver
uniprot
A0A7P0T933
resolver
uniprot
A0A7P0Z473
resolver
uniprot
D3DN29
resolver
uniprot
G3V1S8
resolver
uniprot
Q504W8
resolver
uniprot
Q8TCL5
resolver
uniprot_entry
A0A7P0T892_HUMAN
resolver
uniprot_entry
A0A7P0T933_HUMAN
resolver
uniprot_entry
A0A7P0Z473_HUMAN
resolver
uniprot_entry
AR13B_HUMAN
resolver
uniprot_sec
D3DN29
resolver
uniprot_sec
G3V1S8
resolver
uniprot_sec
Q504W8
resolver
uniprot_sec
Q8TCL5
resolver
amino_acid_sequence
MFSLMASCCGWFKRWREPVRKVTLLMVGLDNAGKTATAKGIQGEYPEDVAPTVGFSKINLRQGKFEVTIFDLGGGIRIRGIWKNYYAESYGVIFVVDSSDEERMEETKEAMSEMLRHPRISGKPILVLANKQDKEGALGEADVIECLSLEKLVNEHKCLCQIEPCSAISGYGKKIDKSIKKGLYWLLHVIARDFDALNERIQKETTEQRALEEQEKQERAERVRKLREERKQNEQEQAELDGTSGLAELDPEPTNPFQPIASVIIENEGKLEREKKNQKMEKDSDGCHLKHKMEHEQIETQGQVNHNGQKNNEFGLVENYKEALTQQLKNEDETDRPSLESANGKKKTKKLRMKRNHRVEPLNIDDCAPESPTPPPPPPPVGWGTPKVTRLPKLEPLGETHHNDFYRKPLPPLAVPQRPNSDAHDVIS
uniprot
proteins
disease_involvement
DISEASE: Joubert syndrome 8 (JBTS8) [MIM:612291]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. {ECO:0000269|PubMed:18674751, ECO:0000269|PubMed:25138100, ECO:0000269|PubMed:38219074}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze fit; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling. Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex. Plays a role in ciliar trafficking of phosphatidylinositol phosphatase INPP5E in ciliogenesis (PubMed:38219074). May regulate ARF6- and RAB22A-dependent endocytic recycling traffic (PubMed:23223633). {ECO:0000269|PubMed:23150559, ECO:0000269|PubMed:23223633, ECO:0000269|PubMed:38219074}.
uniprot
proteins
mass_dalton
48643
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="T->N: Does not affect localization to cilia."; /evidence="ECO:0000269|PubMed:18554500"; MUTAGEN 130; /note="N->I: Does not affect localization to cilia."; /evidence="ECO:0000269|PubMed:18554500"; MUTAGEN 231; /note="K->R: No effect. Abolishes sumoylation; when associated with R-270; R-275; R-276; R-279 and R-329."; /evidence="ECO:0000269|PubMed:23128241"; MUTAGEN 270; /note="K->R: No effect. Abolishes sumoylation; when associated with R-231; R-275; R-276; R-279 and R-329."; /evidence="ECO:0000269|PubMed:23128241"; MUTAGEN 275; /note="K->R: No effect. Abolishes sumoylation; when associated with R-231; R-270; R-276; R-279 and R-329."; /evidence="ECO:0000269|PubMed:23128241"; MUTAGEN 276; /note="K->R: No effect. Abolishes sumoylation; when associated with R-231; R-270; R-275; R-279 and R-329."; /evidence="ECO:0000269|PubMed:23128241"; MUTAGEN 279; /note="K->R: No effect. Abolishes sumoylation; when associated with R-231; R-270; R-275; R-276 and R-329."; /evidence="ECO:0000269|PubMed:23128241"; MUTAGEN 329; /note="K->R: Abolishes sumoylation. Abolishes sumoylation; when associated with R-231; R-270; R-275; R-276 and R-279."; /evidence="ECO:0000269|PubMed:23128241
uniprot
proteins
post_translational_modification
PTM: Sumoylation is required for PKD2 entry into cilium. {ECO:0000269|PubMed:23128241}.
uniprot
proteins
protein_family
Arf family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15314642
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18554500
uniprot
proteins
pubmed
18674751
uniprot
proteins
pubmed
20643351
uniprot
proteins
pubmed
21068128
uniprot
proteins
pubmed
23128241
uniprot
proteins
pubmed
23150559
uniprot
proteins
pubmed
23223633
uniprot
proteins
pubmed
24120134
uniprot
proteins
pubmed
24339792
uniprot
proteins
pubmed
25138100
uniprot
proteins
pubmed
38219074
uniprot
proteins
sequence_length
428
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}; Lipid-anchor {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}. Cell projection, cilium {ECO:0000269|PubMed:25138100, ECO:0000269|PubMed:38219074}. Cell membrane {ECO:0000269|PubMed:23223633}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23223633}. Note=Associates with the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone (PubMed:25138100, PubMed:38219074). Colocalizes with microtubules (PubMed:23223633). {ECO:0000269|PubMed:23223633, ECO:0000269|PubMed:25138100, ECO:0000269|PubMed:38219074}.
uniprot
proteins