ID WDR11_HUMAN Reviewed; 1224 AA. AC Q9BZH6; Q5VWA1; Q9P2J6; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JUL-2024, entry version 188. DE RecName: Full=WD repeat-containing protein 11; DE AltName: Full=Bromodomain and WD repeat-containing protein 2; DE AltName: Full=WD repeat-containing protein 15; GN Name=WDR11; Synonyms=BRWD2, KIAA1351, WDR15; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH ZNF320. RX PubMed=11536051; DOI=10.1038/sj.onc.1204694; RA Chernova O.B., Hunyadi A., Malaj E., Pan H., Crooks C., Roe B., RA Cowell J.K.; RT "A novel member of the WD-repeat gene family, WDR11, maps to the 10q26 RT region and is disrupted by a chromosome translocation in human glioblastoma RT cells."; RL Oncogene 20:5378-5392(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP SUBCELLULAR LOCATION, CHROMOSOMAL TRANSLOCATION, INTERACTION WITH EMX1, RP VARIANTS HH14 TRP-395; THR-435; GLN-448; GLN-690 AND LEU-1150, VARIANT RP GLN-978, AND CHARACTERIZATION OF VARIANTS HH14 TRP-395; THR-435; GLN-448; RP GLN-690 AND LEU-1150. RX PubMed=20887964; DOI=10.1016/j.ajhg.2010.08.018; RA Kim H.G., Ahn J.W., Kurth I., Ullmann R., Kim H.T., Kulharya A., Ha K.S., RA Itokawa Y., Meliciani I., Wenzel W., Lee D., Rosenberger G., Ozata M., RA Bick D.P., Sherins R.J., Nagase T., Tekin M., Kim S.H., Kim C.H., RA Ropers H.H., Gusella J.F., Kalscheuer V., Choi C.Y., Layman L.C.; RT "WDR11, a WD protein that interacts with transcription factor EMX1, is RT mutated in idiopathic hypogonadotropic hypogonadism and Kallmann RT syndrome."; RL Am. J. Hum. Genet. 87:465-479(2010). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP INTERACTION WITH TBC1D23. RX PubMed=29084197; DOI=10.1038/ncb3627; RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.; RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at RT the trans-Golgi."; RL Nat. Cell Biol. 19:1424-1432(2017). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EMX1 AND GLI3, VARIANT RP HH14 LEU-537, AND CHARACTERIZATION OF VARIANTS HH14 TRP-395; THR-435; RP GLN-448; LEU-537; GLN-690 AND LEU-1150. RX PubMed=29263200; DOI=10.15252/embr.201744632; RA Kim Y.J., Osborn D.P., Lee J.Y., Araki M., Araki K., Mohun T., RA Kaensaekoski J., Brandstack N., Kim H.T., Miralles F., Kim C.H., RA Brown N.A., Kim H.G., Martinez-Barbera J.P., Ataliotis P., Raivio T., RA Layman L.C., Kim S.H.; RT "WDR11-mediated Hedgehog signalling defects underlie a new ciliopathy RT related to Kallmann syndrome."; RL EMBO Rep. 19:269-289(2018). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH RP FAM91A1 AND C17ORF75. RX PubMed=29426865; DOI=10.1038/s41467-018-02919-4; RA Navarro Negredo P., Edgar J.R., Manna P.T., Antrobus R., Robinson M.S.; RT "The WDR11 complex facilitates the tethering of AP-1-derived vesicles."; RL Nat. Commun. 9:596-596(2018). RN [16] RP VARIANT MRT78 419-GLN--GLU-1224 DEL, CHARACTERIZATION OF VARIANT MRT78 RP 419-GLN--GLU-1224 DEL, INVOLVEMENT IN MRT78, AND SUBCELLULAR LOCATION. RX PubMed=34413497; DOI=10.1038/s41431-021-00943-5; RA Haag N., Tan E.C., Begemann M., Buschmann L., Kraft F., Holschbach P., RA Lai A.H.M., Brett M., Mochida G.H., DiTroia S., Pais L., Neil J.E., RA Al-Saffar M., Bastaki L., Walsh C.A., Kurth I., Knopp C.; RT "Biallelic loss-of-function variants in WDR11 are associated with RT microcephaly and intellectual disability."; RL Eur. J. Hum. Genet. 29:1663-1668(2021). CC -!- FUNCTION: Involved in the Hedgehog (Hh) signaling pathway, is essential CC for normal ciliogenesis (PubMed:29263200). Regulates the proteolytic CC processing of GLI3 and cooperates with the transcription factor EMX1 in CC the induction of downstream Hh pathway gene expression and CC gonadotropin-releasing hormone production (PubMed:29263200). WDR11 CC complex facilitates the tethering of Adaptor protein-1 complex (AP-1)- CC derived vesicles. WDR11 complex acts together with TBC1D23 to CC facilitate the golgin-mediated capture of vesicles generated using AP-1 CC (PubMed:29426865). {ECO:0000269|PubMed:29263200, CC ECO:0000269|PubMed:29426865}. CC -!- SUBUNIT: Component of the complex WDR11 composed of C17orf75, FAM91A1 CC and WDR11; FAM91A1 and WDR11 are required for proper location of the CC complex (PubMed:29426865). Interacts (via the N-terminal and the CC central portion of the protein) with EMX1 (PubMed:20887964). Interacts CC with GLI3; the interaction associateS EMX1 with GLI3 (PubMed:29263200). CC Interacts with TBC1D23; this interaction may be indirect and recruits CC TBC1D23 to AP-1-derived vesicles (PubMed:29084197, PubMed:29426865). CC {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29084197, CC ECO:0000269|PubMed:29263200, ECO:0000269|PubMed:29426865}. CC -!- INTERACTION: CC Q9BZH6; Q04741: EMX1; NbExp=2; IntAct=EBI-2009923, EBI-26568770; CC Q9BZH6; PRO_0000406137 [P10071]: GLI3; NbExp=3; IntAct=EBI-2009923, EBI-26568850; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000269|PubMed:29263200}. Cytoplasm {ECO:0000269|PubMed:20887964}. CC Nucleus {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29263200}. CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29263200}. CC Cytoplasmic vesicle {ECO:0000269|PubMed:29426865}. Golgi apparatus, CC trans-Golgi network {ECO:0000269|PubMed:29426865, CC ECO:0000269|PubMed:34413497}. Note=Shuttles from the cilium to the CC nucleus in response to Hh signaling (PubMed:29263200). Might be CC shuttling between the nucleus and the cytoplasm (PubMed:20887964). CC {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29263200}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DISEASE: Note=A chromosomal aberration involving WDR11 is found in a CC form of glioblastoma. Translocation t(10;19)(q26;q13.3) with ZNF320. CC {ECO:0000269|PubMed:11536051}. CC -!- DISEASE: Note=A chromosomal aberration involving WDR11 is found in a CC form of Kallmann syndrome. Translocation 46,XY,t(10;12)(q26.12;q13.11). CC {ECO:0000269|PubMed:20887964}. CC -!- DISEASE: Hypogonadotropic hypogonadism 14 with or without anosmia CC (HH14) [MIM:614858]: A disorder characterized by absent or incomplete CC sexual maturation by the age of 18 years, in conjunction with low CC levels of circulating gonadotropins and testosterone and no other CC abnormalities of the hypothalamic-pituitary axis. In some cases, it is CC associated with non-reproductive phenotypes, such as anosmia, cleft CC palate, and sensorineural hearing loss. Anosmia or hyposmia is related CC to the absence or hypoplasia of the olfactory bulbs and tracts. CC Hypogonadism is due to deficiency in gonadotropin-releasing hormone and CC probably results from a failure of embryonic migration of gonadotropin- CC releasing hormone-synthesizing neurons. In the presence of anosmia, CC idiopathic hypogonadotropic hypogonadism is referred to as Kallmann CC syndrome, whereas in the presence of a normal sense of smell, it has CC been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). CC {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29263200}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 78 CC (MRT78) [MIM:620237]: An autosomal recessive neurodevelopmental CC disorder characterized by usually mild intellectual disability, CC microcephaly, and short stature. Additional features may include ocular CC abnormalities and mild skeletal defects. {ECO:0000269|PubMed:34413497}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA92589.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF320223; AAK08064.1; -; mRNA. DR EMBL; AB037772; BAA92589.2; ALT_INIT; mRNA. DR EMBL; AC010998; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391425; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040469; AAH40469.1; -; mRNA. DR EMBL; BC071564; AAH71564.1; -; mRNA. DR CCDS; CCDS7619.1; -. DR RefSeq; NP_060587.8; NM_018117.11. DR AlphaFoldDB; Q9BZH6; -. DR BioGRID; 120839; 150. DR CORUM; Q9BZH6; -. DR IntAct; Q9BZH6; 29. DR MINT; Q9BZH6; -. DR STRING; 9606.ENSP00000263461; -. DR GlyGen; Q9BZH6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BZH6; -. DR PhosphoSitePlus; Q9BZH6; -. DR SwissPalm; Q9BZH6; -. DR BioMuta; WDR11; -. DR DMDM; 17368715; -. DR jPOST; Q9BZH6; -. DR MassIVE; Q9BZH6; -. DR PaxDb; 9606-ENSP00000263461; -. DR PeptideAtlas; Q9BZH6; -. DR ProteomicsDB; 79847; -. DR Pumba; Q9BZH6; -. DR Antibodypedia; 50226; 103 antibodies from 20 providers. DR DNASU; 55717; -. DR Ensembl; ENST00000263461.11; ENSP00000263461.5; ENSG00000120008.16. DR GeneID; 55717; -. DR KEGG; hsa:55717; -. DR MANE-Select; ENST00000263461.11; ENSP00000263461.5; NM_018117.12; NP_060587.8. DR UCSC; uc021pzt.2; human. DR AGR; HGNC:13831; -. DR CTD; 55717; -. DR DisGeNET; 55717; -. DR GeneCards; WDR11; -. DR GeneReviews; WDR11; -. DR HGNC; HGNC:13831; WDR11. DR HPA; ENSG00000120008; Low tissue specificity. DR MalaCards; WDR11; -. DR MIM; 606417; gene. DR MIM; 614858; phenotype. DR MIM; 620237; phenotype. DR neXtProt; NX_Q9BZH6; -. DR OpenTargets; ENSG00000120008; -. DR Orphanet; 478; Kallmann syndrome. DR Orphanet; 432; Normosmic congenital hypogonadotropic hypogonadism. DR Orphanet; 95496; Pituitary stalk interruption syndrome. DR PharmGKB; PA37818; -. DR VEuPathDB; HostDB:ENSG00000120008; -. DR eggNOG; KOG1912; Eukaryota. DR GeneTree; ENSGT00390000004068; -. DR HOGENOM; CLU_005717_1_0_1; -. DR InParanoid; Q9BZH6; -. DR OMA; VQWLWSQ; -. DR OrthoDB; 3107628at2759; -. DR PhylomeDB; Q9BZH6; -. DR TreeFam; TF314830; -. DR PathwayCommons; Q9BZH6; -. DR Reactome; R-HSA-9013407; RHOH GTPase cycle. DR SignaLink; Q9BZH6; -. DR BioGRID-ORCS; 55717; 12 hits in 1166 CRISPR screens. DR ChiTaRS; WDR11; human. DR GeneWiki; BRWD2; -. DR GenomeRNAi; 55717; -. DR Pharos; Q9BZH6; Tbio. DR PRO; PR:Q9BZH6; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9BZH6; Protein. DR Bgee; ENSG00000120008; Expressed in epithelium of nasopharynx and 198 other cell types or tissues. DR ExpressionAtlas; Q9BZH6; baseline and differential. DR GO; GO:0005930; C:axoneme; ISS:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0060322; P:head development; ISS:UniProtKB. DR GO; GO:0007507; P:heart development; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB. DR GO; GO:0035264; P:multicellular organism growth; ISS:UniProtKB. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB. DR GO; GO:0099041; P:vesicle tethering to Golgi; IDA:UniProtKB. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR InterPro; IPR039694; WDR11. DR PANTHER; PTHR14593; WD REPEAT-CONTAINING PROTEIN 11; 1. DR PANTHER; PTHR14593:SF5; WD REPEAT-CONTAINING PROTEIN 11; 1. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS00678; WD_REPEATS_1; 3. PE 1: Evidence at protein level; KW Cell projection; Chromosomal rearrangement; Cytoplasm; Cytoplasmic vesicle; KW Cytoskeleton; Disease variant; Golgi apparatus; KW Hypogonadotropic hypogonadism; Intellectual disability; Kallmann syndrome; KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; KW WD repeat. FT CHAIN 1..1224 FT /note="WD repeat-containing protein 11" FT /id="PRO_0000050889" FT REPEAT 59..108 FT /note="WD 1" FT REPEAT 111..154 FT /note="WD 2" FT REPEAT 354..393 FT /note="WD 3" FT REPEAT 471..510 FT /note="WD 4" FT REPEAT 566..605 FT /note="WD 5" FT REPEAT 708..745 FT /note="WD 6" FT REPEAT 747..787 FT /note="WD 7" FT REPEAT 793..831 FT /note="WD 8" FT REPEAT 893..940 FT /note="WD 9" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 402 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K1X1" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K1X1" FT VARIANT 395 FT /note="R -> W (in HH14; does not affect the interaction FT with EMX1; does not affect the subcellular location of the FT protein; decreases capacity to shuttle from cilium to FT nucleus; decreases GLI3 protein levels; dbSNP:rs201051480)" FT /evidence="ECO:0000269|PubMed:20887964, FT ECO:0000269|PubMed:29263200" FT /id="VAR_069194" FT VARIANT 419..1224 FT /note="Missing (in MRT78; no protein detected in homozygous FT patient cells)" FT /evidence="ECO:0000269|PubMed:34413497" FT /id="VAR_088097" FT VARIANT 435 FT /note="A -> T (in HH14; abolishes the interaction with FT EMX1; does not affect the subcellular location of the FT protein; decreases capacity to shuttle from cilium to FT nucleus; decreases interaction with EMX1; decreases GLI3 FT protein levels; dbSNP:rs318240760)" FT /evidence="ECO:0000269|PubMed:20887964, FT ECO:0000269|PubMed:29263200" FT /id="VAR_069195" FT VARIANT 448 FT /note="R -> Q (in HH14; reduces the interaction with EMX1; FT does not affect the subcellular location of the protein; FT decreases capacity to shuttle from cilium to nucleus; FT decreases GLI3 protein levels; dbSNP:rs144440500)" FT /evidence="ECO:0000269|PubMed:20887964, FT ECO:0000269|PubMed:29263200" FT /id="VAR_069196" FT VARIANT 537 FT /note="P -> L (in HH14; mild phenotype; decreases capacity FT to shuttle from cilium to nucleus; decreases interaction FT with EMX1; no effect on GLI3 protein levels; FT dbSNP:rs761599645)" FT /evidence="ECO:0000269|PubMed:29263200" FT /id="VAR_080856" FT VARIANT 690 FT /note="H -> Q (in HH14; abolishes the interaction with FT EMX1; decreases capacity to shuttle from cilium to nucleus; FT decreases interaction with EMX1; decreases GLI3 protein FT levels; dbSNP:rs318240761)" FT /evidence="ECO:0000269|PubMed:20887964, FT ECO:0000269|PubMed:29263200" FT /id="VAR_069197" FT VARIANT 978 FT /note="K -> Q (in dbSNP:rs144531702)" FT /evidence="ECO:0000269|PubMed:20887964" FT /id="VAR_069198" FT VARIANT 1150 FT /note="F -> L (in HH14; does not affect the subcellular FT location of the protein; decreases capacity to shuttle from FT cilium to nucleus; decreases GLI3 protein levels; FT dbSNP:rs139007744)" FT /evidence="ECO:0000269|PubMed:20887964, FT ECO:0000269|PubMed:29263200" FT /id="VAR_069199" SQ SEQUENCE 1224 AA; 136685 MW; 918221ABEAEFB4ED CRC64; MLPYTVNFKV SARTLTGALN AHNKAAVDWG WQGLIAYGCH SLVVVIDSIT AQTLQVLEKH KADVVKVKWA RENYHHNIGS PYCLRLASAD VNGKIIVWDV AAGVAQCEIQ EHAKPIQDVQ WLWNQDASRD LLLAIHPPNY IVLWNADTGT KLWKKSYADN ILSFSFDPFD PSHLTLLTSE GIVFISDFSP SKPPSGPGKK VYISSPHSSP AHNKLATATG AKKALNKVKI LITQEKPSAE FITLNDCLQL AYLPSKRNHM LLLYPREILI LDLEVNQTVG VIAIERTGVP FLQVIPCFQR DGLFCLHENG CITLRVRRSY NNIFTTSNEE PDPDPVQELT YDLRSQCDAI RVTKTVRPFS MVCCPVNENA AALVVSDGRV MIWELKSAVC NRNSRNSSSG VSPLYSPVSF CGIPVGVLQN KLPDLSLDNM IGQSAIAGEE HPRGSILREV HLKFLLTGLL SGLPAPQFAI RMCPPLTTKN IKMYQPLLAV GTSNGSVLVY HLTSGLLHKE LSIHSCEVKG IEWTSLTSFL SFATSTPNNM GLVRNELQLV DLPTGRSIAF RGERGNDESA IEMIKVSHLK QYLAVVFRDK PLELWDVRTC TLLREMSKNF PTITALEWSP SHNLKSLRKK QLATREAMAR QTVVSDTELS IVESSVISLL QEAESKSELS QNISAREHFV FTDIDGQVYH LTVEGNSVKD SARIPPDGSM GSITCIAWKG DTLVLGDMDG NLNFWDLKGR VSRGIPTHRS WVRKIRFAPG KGNQKLIAMY NDGAEVWDTK EVQMVSSLRS GRNVTFRILD VDWCTSDKVI LASDDGCIRV LEMSMKSACF RMDEQELTEP VWCPYLLVPR ASLALKAFLL HQPWNGQYSL DISHVDYPEN EEIKNLLQEQ LNSLSNDIKK LLLDPEFTLL QRCLLVSRLY GDESELHFWT VAAHYLHSLS QEKSASTTAP KEAAPRDKLS NPLDICYDVL CENAYFQKFQ LERVNLQEVK RSTYDHTRKC TDQLLLLGQT DRAVQLLLET SADNQHYYCD SLKACLVTTV TSSGPSQSTI KLVATNMIAN GKLAEGVQLL CLIDKAADAC RYLQTYGEWN RAAWLAKVRL NPEECADVLR RWVDHLCSPQ VNQKSKALLV LLSLGCFFSV AETLHSMRYF DRAALFVEAC LKYGAFEVTE DTEKLITAIY ADYARSLKNL GFKQGAVLFA SKAGAAGKDL LNELESPKEE PIEE //