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Oral-facial-digital syndrome 1 protein (Protein 71-7A)

 OFD1_HUMAN              Reviewed;        1012 AA.
O75665; B9ZVU5; O75666; Q4VAK4;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 166.
RecName: Full=Oral-facial-digital syndrome 1 protein;
AltName: Full=Protein 71-7A;
Name=OFD1; Synonyms=CXorf5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=9722947; DOI=10.1006/geno.1998.5348;
de Conciliis L., Marchitiello A., Wapenaar M.C., Borsani G.,
Giglio S., Mariani M., Consalez G.G., Zuffardi O., Franco B.,
Ballabio A., Banfi S.;
"Characterization of Cxorf5 (71-7A), a novel human cDNA mapping to
Xp22 and encoding a protein containing coiled-coil alpha-helical
domains.";
Genomics 51:243-250(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT OFD1 PHE-74.
PubMed=12595504; DOI=10.1097/01.ASN.0000054497.48394.D2;
Romio L., Wright V., Price K., Winyard P.J., Donnai D., Porteous M.E.,
Franco B., Giorgio G., Malcolm S., Woolf A.S., Feather S.A.;
"OFD1, the gene mutated in oral-facial-digital syndrome type 1, is
expressed in the metanephros and in human embryonic renal mesenchymal
cells.";
J. Am. Soc. Nephrol. 14:680-689(2003).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[6]
INVOLVEMENT IN SGBS2.
PubMed=16783569; DOI=10.1007/s00439-006-0210-5;
Budny B., Chen W., Omran H., Fliegauf M., Tzschach A., Wisniewska M.,
Jensen L.R., Raynaud M., Shoichet S.A., Badura M., Lenzner S.,
Latos-Bielenska A., Ropers H.-H.;
"A novel X-linked recessive mental retardation syndrome comprising
macrocephaly and ciliary dysfunction is allelic to oral-facial-digital
type I syndrome.";
Hum. Genet. 120:171-178(2006).
[7]
SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION, AND INTERACTION WITH
RUVBL1.
PubMed=17761535; DOI=10.1091/mbc.E07-03-0198;
Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S.,
Franco B.;
"Functional characterization of the OFD1 protein reveals a nuclear
localization and physical interaction with subunits of a chromatin
remodeling complex.";
Mol. Biol. Cell 18:4397-4404(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
INVOLVEMENT IN JBTS10, AND INTERACTION WITH LCA5.
PubMed=19800048; DOI=10.1016/j.ajhg.2009.09.002;
Coene K.L., Roepman R., Doherty D., Afroze B., Kroes H.Y.,
Letteboer S.J., Ngu L.H., Budny B., van Wijk E., Gorden N.T.,
Azhimi M., Thauvin-Robinet C., Veltman J.A., Boink M., Kleefstra T.,
Cremers F.P., van Bokhoven H., de Brouwer A.P.;
"OFD1 is mutated in X-linked Joubert syndrome and interacts with LCA5-
encoded lebercilin.";
Am. J. Hum. Genet. 85:465-481(2009).
[10]
SUBCELLULAR LOCATION.
PubMed=20230748; DOI=10.1016/j.devcel.2009.12.022;
Singla V., Romaguera-Ros M., Garcia-Verdugo J.M., Reiter J.F.;
"Ofd1, a human disease gene, regulates the length and distal structure
of centrioles.";
Dev. Cell 18:410-424(2010).
[11]
INTERACTION WITH SDCCAG8.
PubMed=20835237; DOI=10.1038/ng.662;
Otto E.A., Hurd T.W., Airik R., Chaki M., Zhou W., Stoetzel C.,
Patil S.B., Levy S., Ghosh A.K., Murga-Zamalloa C.A., van Reeuwijk J.,
Letteboer S.J., Sang L., Giles R.H., Liu Q., Coene K.L.,
Estrada-Cuzcano A., Collin R.W., McLaughlin H.M., Held S.,
Kasanuki J.M., Ramaswami G., Conte J., Lopez I., Washburn J.,
Macdonald J., Hu J., Yamashita Y., Maher E.R., Guay-Woodford L.M.,
Neumann H.P., Obermuller N., Koenekoop R.K., Bergmann C., Bei X.,
Lewis R.A., Katsanis N., Lopes V., Williams D.S., Lyons R.H.,
Dang C.V., Brito D.A., Dias M.B., Zhang X., Cavalcoli J.D.,
Nurnberg G., Nurnberg P., Pierce E.A., Jackson P.K., Antignac C.,
Saunier S., Roepman R., Dollfus H., Khanna H., Hildebrandt F.;
"Candidate exome capture identifies mutation of SDCCAG8 as the cause
of a retinal-renal ciliopathy.";
Nat. Genet. 42:840-850(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND SER-669, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
INVOLVEMENT IN RP23.
PubMed=22619378; DOI=10.1093/hmg/dds194;
Webb T.R., Parfitt D.A., Gardner J.C., Martinez A., Bevilacqua D.,
Davidson A.E., Zito I., Thiselton D.L., Ressa J.H., Apergi M.,
Schwarz N., Kanuga N., Michaelides M., Cheetham M.E., Gorin M.B.,
Hardcastle A.J.;
"Deep intronic mutation in OFD1, identified by targeted genomic next-
generation sequencing, causes a severe form of X-linked retinitis
pigmentosa (RP23).";
Hum. Mol. Genet. 21:3647-3654(2012).
[14]
SUBCELLULAR LOCATION.
PubMed=24121310; DOI=10.1038/emboj.2013.223;
Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B.,
Merdes A., Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N.,
Bekker-Jensen S.;
"A new cellular stress response that triggers centriolar satellite
reorganization and ciliogenesis.";
EMBO J. 32:3029-3040(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663; SER-669; SER-686;
SER-720; SER-745; SER-774; SER-789 AND SER-811, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
INTERACTION WITH MAP1LC3B.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from
centriolar satellites.";
Nature 502:254-257(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INTERACTION WITH C2CD3.
PubMed=24997988; DOI=10.1038/ng.3031;
Thauvin-Robinet C., Lee J.S., Lopez E., Herranz-Perez V., Shida T.,
Franco B., Jego L., Ye F., Pasquier L., Loget P., Gigot N., Aral B.,
Lopes C.A., St-Onge J., Bruel A.L., Thevenon J., Gonzalez-Granero S.,
Alby C., Munnich A., Vekemans M., Huet F., Fry A.M., Saunier S.,
Riviere J.B., Attie-Bitach T., Garcia-Verdugo J.M., Faivre L.,
Megarbane A., Nachury M.V.;
"The oral-facial-digital syndrome gene C2CD3 encodes a positive
regulator of centriole elongation.";
Nat. Genet. 46:905-911(2014).
[19]
INTERACTION WITH FOPNL; KIAA0753 AND PCM1, AND SUBCELLULAR LOCATION.
PubMed=26643951; DOI=10.1093/hmg/ddv488;
Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M.,
Lembo F., Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P.,
Kuentz P., Thevenon J., Burglen L., Faivre L., Riviere J.B.,
Huynen M.A., Birnbaum D., Rosnet O., Thauvin-Robinet C.;
"OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
satellites and centrosomes and is mutated in one individual with oral-
facial-digital syndrome.";
Hum. Mol. Genet. 25:497-513(2016).
[20]
VARIANTS OFD1 358-PHE--TYR-360 AND ARG-435.
PubMed=11179005; DOI=10.1086/318802;
Ferrante M.I., Giorgio G., Feather S.A., Bulfone A., Wright V.,
Ghiani M., Selicorni A., Gammaro L., Scolari F., Woolf A.S.,
Sylvie O., Le Marec B., Malcolm S., Winter R., Ballabio A., Franco B.;
"Identification of the gene for oral-facial-digital type I syndrome.";
Am. J. Hum. Genet. 68:569-576(2001).
[21]
VARIANT OFD1 THR-79.
PubMed=11950863; DOI=10.1136/jmg.39.4.292;
Rakkolainen A., Ala-Mello S., Kristo P., Orpana A., Jaervelae I.;
"Four novel mutations in the OFD1 (Cxorf5) gene in Finnish patients
with oral-facial-digital syndrome 1.";
J. Med. Genet. 39:292-296(2002).
[22]
VARIANT OFD1 SER-138.
PubMed=16397067; DOI=10.1136/jmg.2004.027672;
Thauvin-Robinet C., Cossee M., Cormier-Daire V., Van Maldergem L.,
Toutain A., Alembik Y., Bieth E., Layet V., Parent P., David A.,
Goldenberg A., Mortier G., Heron D., Sagot P., Bouvier A.M., Huet F.,
Cusin V., Donzel A., Devys D., Teyssier J.R., Faivre L.;
"Clinical, molecular, and genotype-phenotype correlation studies from
25 cases of oral-facial-digital syndrome type 1: a French and Belgian
collaborative study.";
J. Med. Genet. 43:54-61(2006).
[23]
VARIANT OFD1 ARG-141.
PubMed=23033313; DOI=10.1002/humu.22224;
Bisschoff I.J., Zeschnigk C., Horn D., Wellek B., Riess A.,
Wessels M., Willems P., Jensen P., Busche A., Bekkebraten J.,
Chopra M., Hove H.D., Evers C., Heimdal K., Kaiser A.S., Kunstmann E.,
Robinson K.L., Linne M., Martin P., McGrath J., Pradel W.,
Prescott K.E., Roesler B., Rudolf G., Siebers-Renelt U.,
Tyshchenko N., Wieczorek D., Wolff G., Dobyns W.B.,
Morris-Rosendahl D.J.;
"Novel mutations including deletions of the entire OFD1 gene in 30
families with type 1 orofaciodigital syndrome: A study of the
extensive clinical variability.";
Hum. Mutat. 34:237-247(2013).
[24]
VARIANT JBTS10 ASP-307.
PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
Care4Rare Canada Consortium;
Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
Schwartzentruber J., Martin B., Patry L., Nassif C.,
Dionne-Laporte A., Ospina L.H., Lemyre E., Massicotte C.,
Laframboise R., Maranda B., Labuda D., Decarie J.C., Rypens F.,
Goldsher D., Fallet-Bianco C., Soucy J.F., Laberge A.M., Maftei C.,
Boycott K., Brais B., Boucher R.M., Rouleau G.A., Katsanis N.,
Majewski J., Elpeleg O., Kukolich M.K., Shalev S., Michaud J.L.;
"Joubert Syndrome in French Canadians and Identification of Mutations
in CEP104.";
Am. J. Hum. Genet. 97:744-753(2015).
-!- FUNCTION: Component of the centrioles controlling mother and
daughter centrioles length. Recruits to the centriole IFT88 and
centriole distal appendage-specific proteins including CEP164.
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. 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}.
-!- SUBUNIT: Homooligomer. Interacts with LCA5. Interacts with RUVBL1;
the interaction is direct and may mediate interaction with the
NuA4 histone acetyltransferase complex. Interacts with SDCCAG8;
the interaction is direct. Interacts with MAP1LC3B. Interacts with
C2CD3; OFD1 may act as a egative regulator of C2CD3. Forms a
complex with KIAA0753/OFIP and FOPNL/FOR20; the interaction with
FOPNL is detected only in the presence of KIAA0753. Interacts with
PCM1; this interaction may be mediated by KIAA0753/OFIP
(PubMed:26643951). {ECO:0000269|PubMed:17761535,
ECO:0000269|PubMed:19800048, ECO:0000269|PubMed:20835237,
ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24997988,
ECO:0000269|PubMed:26643951}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-716327, EBI-716327;
Q4AC94:C2CD3; NbExp=3; IntAct=EBI-716327, EBI-10897521;
Q9GZQ8:MAP1LC3B; NbExp=4; IntAct=EBI-716327, EBI-373144;
Q9Y5B8:NME7; NbExp=3; IntAct=EBI-716327, EBI-744782;
Q15154:PCM1; NbExp=8; IntAct=EBI-716327, EBI-741421;
P53350:PLK1; NbExp=4; IntAct=EBI-716327, EBI-476768;
Q9Y265:RUVBL1; NbExp=3; IntAct=EBI-716327, EBI-353675;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ODF1a;
IsoId=O75665-1; Sequence=Displayed;
Name=2; Synonyms=ODF1b;
IsoId=O75665-2; Sequence=VSP_004177, VSP_004178;
Name=3;
IsoId=O75665-3; Sequence=VSP_023334;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in 9 and 14 weeks
old embryos in metanephric mesenchyme, oral mucosa, lung, heart,
nasal and cranial cartilage, and brain. Expressed in metanephros,
brain, tongue, and limb. {ECO:0000269|PubMed:12595504}.
-!- 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 mutations 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 mutations 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
mutations 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 mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the OFD1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name= Oral-facial-digital syndrome 1 (OFD1);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/OFD1";
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EMBL; Y15164; CAA75436.1; -; mRNA.
EMBL; Y16355; CAA76185.1; -; mRNA.
EMBL; AC003037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC096344; AAH96344.1; -; mRNA.
CCDS; CCDS14157.1; -. [O75665-1]
CCDS; CCDS83454.1; -. [O75665-3]
RefSeq; NP_001317138.1; NM_001330209.1. [O75665-3]
RefSeq; NP_003602.1; NM_003611.2. [O75665-1]
UniGene; Hs.6483; -.
ProteinModelPortal; O75665; -.
SMR; O75665; -.
BioGrid; 114055; 288.
CORUM; O75665; -.
DIP; DIP-60601N; -.
IntAct; O75665; 265.
STRING; 9606.ENSP00000344314; -.
iPTMnet; O75665; -.
PhosphoSitePlus; O75665; -.
SwissPalm; O75665; -.
BioMuta; OFD1; -.
EPD; O75665; -.
MaxQB; O75665; -.
PaxDb; O75665; -.
PeptideAtlas; O75665; -.
PRIDE; O75665; -.
Ensembl; ENST00000340096; ENSP00000344314; ENSG00000046651. [O75665-1]
Ensembl; ENST00000380550; ENSP00000369923; ENSG00000046651. [O75665-3]
GeneID; 8481; -.
KEGG; hsa:8481; -.
UCSC; uc004cvp.5; human. [O75665-1]
CTD; 8481; -.
DisGeNET; 8481; -.
EuPathDB; HostDB:ENSG00000046651.14; -.
GeneCards; OFD1; -.
GeneReviews; OFD1; -.
HGNC; HGNC:2567; OFD1.
HPA; HPA031102; -.
HPA; HPA031103; -.
HPA; HPA031104; -.
MalaCards; OFD1; -.
MIM; 300170; gene.
MIM; 300209; phenotype.
MIM; 300424; phenotype.
MIM; 300804; phenotype.
MIM; 311200; phenotype.
neXtProt; NX_O75665; -.
OpenTargets; ENSG00000046651; -.
Orphanet; 2754; Joubert syndrome with orofaciodigital defect.
Orphanet; 2750; Orofaciodigital syndrome type 1.
Orphanet; 244; Primary ciliary dyskinesia.
Orphanet; 791; Retinitis pigmentosa.
Orphanet; 79022; Simpson-Golabi-Behmel syndrome type 2.
PharmGKB; PA31909; -.
eggNOG; ENOG410IJF2; Eukaryota.
eggNOG; ENOG41112K2; LUCA.
GeneTree; ENSGT00390000001798; -.
HOGENOM; HOG000231349; -.
HOVERGEN; HBG080238; -.
InParanoid; O75665; -.
KO; K16480; -.
OMA; PAGDMPH; -.
OrthoDB; EOG091G01ST; -.
PhylomeDB; O75665; -.
TreeFam; TF331230; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; O75665; -.
ChiTaRS; OFD1; human.
GeneWiki; OFD1; -.
GenomeRNAi; 8481; -.
PRO; PR:O75665; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000046651; -.
CleanEx; HS_OFD1; -.
ExpressionAtlas; O75665; baseline and differential.
Genevisible; O75665; HS.
GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
InterPro; IPR006594; LisH.
Pfam; PF16045; LisH_2; 1.
SMART; SM00667; LisH; 1.
PROSITE; PS50896; LISH; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Ciliopathy; Cilium;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Joubert syndrome; Nucleus;
Phosphoprotein; Reference proteome; Retinitis pigmentosa.
CHAIN 1 1012 Oral-facial-digital syndrome 1 protein.
/FTId=PRO_0000058029.
DOMAIN 70 102 LisH. {ECO:0000255|PROSITE-
ProRule:PRU00126}.
REGION 609 665 Mediates homooligomerization.
REGION 615 1012 Mediates the interaction with SDCCAG8.
{ECO:0000269|PubMed:20835237}.
COILED 189 557 {ECO:0000255}.
COILED 622 662 {ECO:0000255}.
COILED 867 956 {ECO:0000255}.
MOD_RES 663 663 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 789 789 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 811 811 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 313 352 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023334.
VAR_SEQ 352 367 KYQLELKDDYIIRTNR -> NFHRLHGVCLALGILI (in
isoform 2). {ECO:0000303|PubMed:9722947}.
/FTId=VSP_004177.
VAR_SEQ 368 1012 Missing (in isoform 2).
{ECO:0000303|PubMed:9722947}.
/FTId=VSP_004178.
VARIANT 74 74 S -> F (in OFD1; dbSNP:rs312262812).
{ECO:0000269|PubMed:12595504}.
/FTId=VAR_015574.
VARIANT 79 79 A -> T (in OFD1; dbSNP:rs312262814).
{ECO:0000269|PubMed:11950863}.
/FTId=VAR_030789.
VARIANT 138 138 G -> S (in OFD1; dbSNP:rs312262827).
{ECO:0000269|PubMed:16397067}.
/FTId=VAR_058758.
VARIANT 141 141 M -> R (in OFD1; dbSNP:rs886039860).
{ECO:0000269|PubMed:23033313}.
/FTId=VAR_069100.
VARIANT 307 307 V -> D (in JBTS10; unknown pathological
significance).
{ECO:0000269|PubMed:26477546}.
/FTId=VAR_075701.
VARIANT 358 360 KDD -> FSY (in OFD1).
/FTId=VAR_013753.
VARIANT 435 435 S -> R (in OFD1; dbSNP:rs122460150).
{ECO:0000269|PubMed:11179005}.
/FTId=VAR_013754.
SEQUENCE 1012 AA; 116671 MW; C2BF4376F89E6738 CRC64;
MMAQSNMFTV ADVLSQDELR KKLYQTFKDR GILDTLKTQL RNQLIHELMH PVLSGELQPR
SISVEGSSLL IGASNSLVAD HLQRCGYEYS LSVFFPESGL AKEKVFTMQD LLQLIKINPT
SSLYKSLVSG SDKENQKGFL MHFLKELAEY HQAKESCNME TQTSSTFNRD SLAEKLQLID
DQFADAYPQR IKFESLEIKL NEYKREIEEQ LRAEMCQKLK FFKDTEIAKI KMEAKKKYEK
ELTMFQNDFE KACQAKSEAL VLREKSTLER IHKHQEIETK EIYAQRQLLL KDMDLLRGRE
AELKQRVEAF ELNQKLQEEK HKSITEALRR QEQNIKSFEE TYDRKLKNEL LKYQLELKDD
YIIRTNRLIE DERKNKEKAV HLQEELIAIN SKKEELNQSV NRVKELELEL ESVKAQSLAI
TKQNHMLNEK VKEMSDYSLL KEEKLELLAQ NKLLKQQLEE SRNENLRLLN RLAQPAPELA
VFQKELRKAE KAIVVEHEEF ESCRQALHKQ LQDEIEHSAQ LKAQILGYKA SVKSLTTQVA
DLKLQLKQTQ TALENEVYCN PKQSVIDRSV NGLINGNVVP CNGEISGDFL NNPFKQENVL
ARMVASRITN YPTAWVEGSS PDSDLEFVAN TKARVKELQQ EAERLEKAFR SYHRRVIKNS
AKSPLAAKSP PSLHLLEAFK NITSSSPERH IFGEDRVVSE QPQVGTLEER NDVVEALTGS
AASRLRGGTS SRRLSSTPLP KAKRSLESEM YLEGLGRSHI ASPSPCPDRM PLPSPTESRH
SLSIPPVSSP PEQKVGLYRR QTELQDKSEF SDVDKLAFKD NEEFESSFES AGNMPRQLEM
GGLSPAGDMS HVDAAAAAVP LSYQHPSVDQ KQIEEQKEEE KIREQQVKER RQREERRQSN
LQEVLERERR ELEKLYQERK MIEESLKIKI KKELEMENEL EMSNQEIKDK SAHSENPLEK
YMKIIQQEQD QESADKSSKK MVQEGSLVDT LQSSDKVESL TGFSHEELDD SW


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