WDR11_HUMAN
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 03-AUG-2022, entry version 177.
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).
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}. Note=Shuttles from
CC the cilium to the nucleus in response to Hh signaling
CC (PubMed:29263200). Might be shuttling between the nucleus and the
CC cytoplasm (PubMed:20887964). {ECO:0000269|PubMed:20887964,
CC 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 -!- 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; 112.
DR CORUM; Q9BZH6; -.
DR IntAct; Q9BZH6; 27.
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 EPD; Q9BZH6; -.
DR jPOST; Q9BZH6; -.
DR MassIVE; Q9BZH6; -.
DR MaxQB; Q9BZH6; -.
DR PaxDb; Q9BZH6; -.
DR PeptideAtlas; Q9BZH6; -.
DR PRIDE; Q9BZH6; -.
DR ProteomicsDB; 79847; -.
DR Antibodypedia; 50226; 97 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 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 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; KGIEWIS; -.
DR OrthoDB; 617629at2759; -.
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 1089 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 196 other tissues.
DR ExpressionAtlas; Q9BZH6; baseline and differential.
DR Genevisible; Q9BZH6; HS.
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; -; 3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR039694; WDR11.
DR PANTHER; PTHR14593; PTHR14593; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 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; Kallmann syndrome; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; 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 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
