OFD1
entrez
8481
canonical
uniprot
O75665
canonical
ensembl
ENSG00000046651
resolver
ensp
ENSP00000344314
resolver
ensp
ENSP00000369923
resolver
ensp
ENSP00000592768
resolver
ensp
ENSP00000592769
resolver
genesymbol
OFD1
resolver
genesymbol_syn
CXorf5
resolver
hgnc
HGNC:2567
resolver
uniprot
B9ZVU5
resolver
uniprot
E9KL37
resolver
uniprot
O75666
resolver
uniprot
Q4VAK4
resolver
uniprot_entry
E9KL37_HUMAN
resolver
uniprot_entry
OFD1_HUMAN
resolver
uniprot_sec
B9ZVU5
resolver
uniprot_sec
O75666
resolver
uniprot_sec
Q4VAK4
resolver
amino_acid_sequence
MMAQSNMFTVADVLSQDELRKKLYQTFKDRGILDTLKTQLRNQLIHELMHPVLSGELQPRSISVEGSSLLIGASNSLVADHLQRCGYEYSLSVFFPESGLAKEKVFTMQDLLQLIKINPTSSLYKSLVSGSDKENQKGFLMHFLKELAEYHQAKESCNMETQTSSTFNRDSLAEKLQLIDDQFADAYPQRIKFESLEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHKHQEIETKEIYAQRQLLLKDMDLLRGREAELKQRVEAFELNQKLQEEKHKSITEALRRQEQNIKSFEETYDRKLKNELLKYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKKEELNQSVNRVKELELELESVKAQSLAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQPAPELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQLKQTQTALENEVYCNPKQSVIDRSVNGLINGNVVPCNGEISGDFLNNPFKQENVLARMVASRITNYPTAWVEGSSPDSDLEFVANTKARVKELQQEAERLEKAFRSYHRRVIKNSAKSPLAAKSPPSLHLLEAFKNITSSSPERHIFGEDRVVSEQPQVGTLEERNDVVEALTGSAASRLRGGTSSRRLSSTPLPKAKRSLESEMYLEGLGRSHIASPSPCPDRMPLPSPTESRHSLSIPPVSSPPEQKVGLYRRQTELQDKSEFSDVDKLAFKDNEEFESSFESAGNMPRQLEMGGLSPAGDMSHVDAAAAAVPLSYQHPSVDQKQIEEQKEEEKIREQQVKERRQREERRQSNLQEVLERERRELEKLYQERKMIEESLKIKIKKELEMENELEMSNQEIKDKSAHSENPLEKYMKIIQQEQDQESADKSSKKMVQEGSLVDTLQSSDKVESLTGFSHEELDDSW
uniprot
proteins
disease_involvement
DISEASE: Orofaciodigital syndrome 1 (OFD1) [MIM:311200]: A form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by abnormalities in the oral cavity, face, and digits and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD1 is X-linked dominant syndrome, lethal in males. Craniofacial findings consist of facial asymmetry, hypertelorism, median cleft, or pseudocleft of the upper lip, hypoplasia of the alae nasi, oral clefts and abnormal frenulea, tongue anomalies (clefting, cysts, hamartoma), and anomalous dentition involving missing or extra teeth. Asymmetric brachydactyly and/or syndactyly of the fingers and toes occur frequently. Approximately 50% of OFD1 females have some degree of intellectual disability. Some patients have structural central nervous system anomalies such as agenesis of the corpus callosum, cerebellar agenesis, or a Dandy-Walker malformation. Patients with OFD1 can develop fibrocystic disease of the liver and pancreas, in addition to polycystic kidneys. {ECO:0000269|PubMed:11179005, ECO:0000269|PubMed:11950863, ECO:0000269|PubMed:12595504, ECO:0000269|PubMed:16397067, ECO:0000269|PubMed:23033313}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Simpson-Golabi-Behmel syndrome 2 (SGBS2) [MIM:300209]: A severe variant of Simpson-Golabi-Behmel syndrome, a condition characterized by pre- and postnatal overgrowth (gigantism), facial dysmorphism and a variety of inconstant visceral and skeletal malformations. {ECO:0000269|PubMed:16783569}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Joubert syndrome 10 (JBTS10) [MIM:300804]: 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:19800048, ECO:0000269|PubMed:26477546}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 23 (RP23) [MIM:300424]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:22619378}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164 (By similarity). Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis (PubMed:33934390). Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. Only OFD1 localized at the centriolar satellites is removed by autophagy, which is an important step in the ciliogenesis regulation (By similarity). {ECO:0000250|UniProtKB:Q80Z25, ECO:0000269|PubMed:33934390}.
uniprot
proteins
mass_dalton
116671
uniprot
proteins
mutagenesis
MUTAGEN 97; /note="E->G: Increased protein stability."; /evidence="ECO:0000269|PubMed:33934390"; MUTAGEN 735; /note="S->A: Loss of phosphorylation by PKA. Loss of cAMP-dependent interaction with TBC1D31. Loss of ubiquitin-mediated proteasomal degradation. Loss of function in cilium assembly. Dominant negative effect."; /evidence="ECO:0000269|PubMed:33934390
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation at Ser-735, by the cAMP-dependent protein kinase PKA, triggers ubiquitination and proteasomal degradation of OFD1. Also increases its interaction with TBC1D31 and regulates its function in ciliogenesis. {ECO:0000269|PubMed:33934390}.; PTM: Ubiquitinated by PJA2, upon phosphorylation at Ser-735 by PKA, leads to the proteasomal degradation of OFD1. {ECO:0000269|PubMed:33934390}.
uniprot
proteins
protein_family
OFD1 family
uniprot
proteins
pubmed
11179005
uniprot
proteins
pubmed
11950863
uniprot
proteins
pubmed
12595504
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16397067
uniprot
proteins
pubmed
16783569
uniprot
proteins
pubmed
17761535
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19800048
uniprot
proteins
pubmed
20230748
uniprot
proteins
pubmed
20835237
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22619378
uniprot
proteins
pubmed
23033313
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24089205
uniprot
proteins
pubmed
24121310
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24997988
uniprot
proteins
pubmed
26477546
uniprot
proteins
pubmed
26643951
uniprot
proteins
pubmed
33934390
uniprot
proteins
pubmed
38158857
uniprot
proteins
pubmed
9722947
uniprot
proteins
sequence_length
1012
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12595504, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20230748, ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17761535}. Nucleus {ECO:0000269|PubMed:17761535}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:26643951}. Note=Localizes to centriole distal ends and to centriolar satellites (PubMed:20230748, PubMed:24121310). Localization to centrioles and pericentriolar satellites may be mediated by KIAA0753/OFIP (PubMed:26643951). {ECO:0000269|PubMed:26643951}.
uniprot
proteins