Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O75665 (OFD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oral-facial-digital syndrome 1 protein
Alternative name(s):
Protein 71-7A
Gene names
Name:OFD1
Synonyms:CXorf5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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. Ref.7 Ref.9 Ref.11 Ref.14

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Cytoplasmcytoskeletoncilium basal body. Nucleus. Note: Localizes to centriole distal ends and to centriolar satellites By similarity. Ref.4 Ref.5 Ref.7 Ref.10

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. Ref.4

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.15 Ref.16 Ref.17 Ref.18

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the OFD1 family.

Contains 1 LisH domain.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseCiliopathy
Disease mutation
Joubert syndrome
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial cilium movement involved in determination of left/right asymmetry

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcentriolar satellite

Inferred from sequence or structural similarity. Source: UniProtKB

centriole

Inferred from direct assay Ref.10. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

ciliary basal body

Inferred from direct assay Ref.10. Source: UniProtKB

cilium

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

gamma-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PLK1P533502EBI-716327,EBI-476768

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75665-1)

Also known as: ODF1a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75665-2)

Also known as: ODF1b;

The sequence of this isoform differs from the canonical sequence as follows:
     352-367: KYQLELKDDYIIRTNR → NFHRLHGVCLALGILI
     368-1012: Missing.
Isoform 3 (identifier: O75665-3)

The sequence of this isoform differs from the canonical sequence as follows:
     313-352: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10121012Oral-facial-digital syndrome 1 protein
PRO_0000058029

Regions

Domain70 – 10233LisH
Region609 – 66557Mediates homooligomerization
Region615 – 1012398Mediates the interaction with SDCCAG8
Coiled coil189 – 557369 Potential
Coiled coil622 – 66241 Potential
Coiled coil867 – 95690 Potential

Amino acid modifications

Modified residue6631Phosphoserine Ref.12
Modified residue6691Phosphoserine Ref.12
Modified residue6861Phosphoserine Ref.8

Natural variations

Alternative sequence313 – 35240Missing in isoform 3.
VSP_023334
Alternative sequence352 – 36716KYQLE…IRTNR → NFHRLHGVCLALGILI in isoform 2.
VSP_004177
Alternative sequence368 – 1012645Missing in isoform 2.
VSP_004178
Natural variant741S → F in OFD1. Ref.4
VAR_015574
Natural variant791A → T in OFD1. Ref.16
VAR_030789
Natural variant1381G → S in OFD1. Ref.17
VAR_058758
Natural variant1411M → R in OFD1. Ref.18
VAR_069100
Natural variant358 – 3603KDD → FSY in OFD1.
VAR_013753
Natural variant4351S → R in OFD1. Ref.15
VAR_013754

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ODF1a) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C2BF4376F89E6738

FASTA1,012116,671
        10         20         30         40         50         60 
MMAQSNMFTV ADVLSQDELR KKLYQTFKDR GILDTLKTQL RNQLIHELMH PVLSGELQPR 

        70         80         90        100        110        120 
SISVEGSSLL IGASNSLVAD HLQRCGYEYS LSVFFPESGL AKEKVFTMQD LLQLIKINPT 

       130        140        150        160        170        180 
SSLYKSLVSG SDKENQKGFL MHFLKELAEY HQAKESCNME TQTSSTFNRD SLAEKLQLID 

       190        200        210        220        230        240 
DQFADAYPQR IKFESLEIKL NEYKREIEEQ LRAEMCQKLK FFKDTEIAKI KMEAKKKYEK 

       250        260        270        280        290        300 
ELTMFQNDFE KACQAKSEAL VLREKSTLER IHKHQEIETK EIYAQRQLLL KDMDLLRGRE 

       310        320        330        340        350        360 
AELKQRVEAF ELNQKLQEEK HKSITEALRR QEQNIKSFEE TYDRKLKNEL LKYQLELKDD 

       370        380        390        400        410        420 
YIIRTNRLIE DERKNKEKAV HLQEELIAIN SKKEELNQSV NRVKELELEL ESVKAQSLAI 

       430        440        450        460        470        480 
TKQNHMLNEK VKEMSDYSLL KEEKLELLAQ NKLLKQQLEE SRNENLRLLN RLAQPAPELA 

       490        500        510        520        530        540 
VFQKELRKAE KAIVVEHEEF ESCRQALHKQ LQDEIEHSAQ LKAQILGYKA SVKSLTTQVA 

       550        560        570        580        590        600 
DLKLQLKQTQ TALENEVYCN PKQSVIDRSV NGLINGNVVP CNGEISGDFL NNPFKQENVL 

       610        620        630        640        650        660 
ARMVASRITN YPTAWVEGSS PDSDLEFVAN TKARVKELQQ EAERLEKAFR SYHRRVIKNS 

       670        680        690        700        710        720 
AKSPLAAKSP PSLHLLEAFK NITSSSPERH IFGEDRVVSE QPQVGTLEER NDVVEALTGS 

       730        740        750        760        770        780 
AASRLRGGTS SRRLSSTPLP KAKRSLESEM YLEGLGRSHI ASPSPCPDRM PLPSPTESRH 

       790        800        810        820        830        840 
SLSIPPVSSP PEQKVGLYRR QTELQDKSEF SDVDKLAFKD NEEFESSFES AGNMPRQLEM 

       850        860        870        880        890        900 
GGLSPAGDMS HVDAAAAAVP LSYQHPSVDQ KQIEEQKEEE KIREQQVKER RQREERRQSN 

       910        920        930        940        950        960 
LQEVLERERR ELEKLYQERK MIEESLKIKI KKELEMENEL EMSNQEIKDK SAHSENPLEK 

       970        980        990       1000       1010 
YMKIIQQEQD QESADKSSKK MVQEGSLVDT LQSSDKVESL TGFSHEELDD SW 

« Hide

Isoform 2 (ODF1b) [UniParc].

Checksum: F68CBB8EF28B5D2D
Show »

FASTA36742,925
Isoform 3 [UniParc].

Checksum: A5D2A7ECACB02E21
Show »

FASTA972111,745

References

« Hide 'large scale' references
[1]"Characterization of Cxorf5 (71-7A), a novel human cDNA mapping to Xp22 and encoding a protein containing coiled-coil alpha-helical domains."
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.
Genomics 51:243-250(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"OFD1, the gene mutated in oral-facial-digital syndrome type 1, is expressed in the metanephros and in human embryonic renal mesenchymal cells."
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.
J. Am. Soc. Nephrol. 14:680-689(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT OFD1 PHE-74.
[5]"Proteomic characterization of the human centrosome by protein correlation profiling."
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Lymphoblast.
[6]"A novel X-linked recessive mental retardation syndrome comprising macrocephaly and ciliary dysfunction is allelic to oral-facial-digital type I syndrome."
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.
Hum. Genet. 120:171-178(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SIMPSON-GOLABI-BEHMEL SYNDROME.
[7]"Functional characterization of the OFD1 protein reveals a nuclear localization and physical interaction with subunits of a chromatin remodeling complex."
Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S., Franco B.
Mol. Biol. Cell 18:4397-4404(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION, INTERACTION WITH RUVBL1.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"OFD1 is mutated in X-linked Joubert syndrome and interacts with LCA5-encoded lebercilin."
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.
Am. J. Hum. Genet. 85:465-481(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN JBTS10, INTERACTION WITH LCA5.
[10]"Ofd1, a human disease gene, regulates the length and distal structure of centrioles."
Singla V., Romaguera-Ros M., Garcia-Verdugo J.M., Reiter J.F.
Dev. Cell 18:410-424(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Candidate exome capture identifies mutation of SDCCAG8 as the cause of a retinal-renal ciliopathy."
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. expand/collapse author list , 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.
Nat. Genet. 42:840-850(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SDCCAG8.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND SER-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3B.
[15]"Identification of the gene for oral-facial-digital type I syndrome."
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.
Am. J. Hum. Genet. 68:569-576(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OFD1 358-PHE--TYR-360 AND ARG-435.
[16]"Four novel mutations in the OFD1 (Cxorf5) gene in Finnish patients with oral-facial-digital syndrome 1."
Rakkolainen A., Ala-Mello S., Kristo P., Orpana A., Jaervelae I.
J. Med. Genet. 39:292-296(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OFD1 THR-79.
[17]"Clinical, molecular, and genotype-phenotype correlation studies from 25 cases of oral-facial-digital syndrome type 1: a French and Belgian collaborative study."
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. expand/collapse author list , Devys D., Teyssier J.R., Faivre L.
J. Med. Genet. 43:54-61(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OFD1 SER-138.
[18]"Novel mutations including deletions of the entire OFD1 gene in 30 families with type 1 orofaciodigital syndrome: A study of the extensive clinical variability."
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. expand/collapse author list , 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.
Hum. Mutat. 34:237-247(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OFD1 ARG-141.
+Additional computationally mapped references.

Web resources

GeneReviews
Oral-facial-digital syndrome 1 (OFD1)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15164 mRNA. Translation: CAA75436.1.
Y16355 mRNA. Translation: CAA76185.1.
AC003037 Genomic DNA. No translation available.
BC096344 mRNA. Translation: AAH96344.1.
RefSeqNP_003602.1. NM_003611.2.
XP_005274661.1. XM_005274604.1.
UniGeneHs.6483.

3D structure databases

ProteinModelPortalO75665.
SMRO75665. Positions 72-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114055. 19 interactions.
DIPDIP-60601N.
IntActO75665. 15 interactions.
MINTMINT-1369849.
STRING9606.ENSP00000344314.

PTM databases

PhosphoSiteO75665.

Proteomic databases

PaxDbO75665.
PRIDEO75665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340096; ENSP00000344314; ENSG00000046651. [O75665-1]
ENST00000380550; ENSP00000369923; ENSG00000046651. [O75665-3]
ENST00000398395; ENSP00000381432; ENSG00000046651. [O75665-2]
GeneID8481.
KEGGhsa:8481.
UCSCuc004cvp.4. human. [O75665-1]
uc004cvu.4. human. [O75665-3]

Organism-specific databases

CTD8481.
GeneCardsGC0XP013752.
HGNCHGNC:2567. OFD1.
HPAHPA031102.
HPA031103.
HPA031104.
MIM300170. gene.
300209. phenotype.
300804. phenotype.
311200. phenotype.
neXtProtNX_O75665.
Orphanet2754. Joubert syndrome with orofaciodigital defect.
2750. Orofaciodigital syndrome type 1.
244. Primary ciliary dyskinesia.
791. Retinitis pigmentosa.
79022. Simpson-Golabi-Behmel syndrome type 2.
PharmGKBPA31909.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68802.
HOGENOMHOG000231349.
HOVERGENHBG080238.
InParanoidO75665.
KOK16480.
OMAERHIFGE.
OrthoDBEOG7D59MR.
PhylomeDBO75665.
TreeFamTF331230.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO75665.
BgeeO75665.
CleanExHS_OFD1.
GenevestigatorO75665.

Family and domain databases

InterProIPR006594. LisH_dimerisation.
[Graphical view]
SMARTSM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOFD1. human.
GeneWikiOFD1.
GenomeRNAi8481.
NextBio31735.
PROO75665.
SOURCESearch...

Entry information

Entry nameOFD1_HUMAN
AccessionPrimary (citable) accession number: O75665
Secondary accession number(s): B9ZVU5, O75666, Q4VAK4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM