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Database: UniProt
Entry: Q9UMX1
LinkDB: Q9UMX1
Original site: Q9UMX1 
ID   SUFU_HUMAN              Reviewed;         484 AA.
AC   Q9UMX1; Q7LCP7; Q9NT90; Q9NZ07; Q9UHK2; Q9UHM8; Q9UMY0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   07-OCT-2020, entry version 176.
DE   RecName: Full=Suppressor of fused homolog {ECO:0000303|PubMed:10559945, ECO:0000303|PubMed:10564661};
DE            Short=SUFUH {ECO:0000303|PubMed:10559945};
GN   Name=SUFU {ECO:0000303|PubMed:12068298, ECO:0000312|HGNC:HGNC:16466};
GN   ORFNames=UNQ650/PRO1280 {ECO:0000303|PubMed:12975309};
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] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION
RP   WITH GLI1; GLI2; GLI3 AND BTRC, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Fetal kidney, Fetal lung, and Fetal testis;
RX   PubMed=10564661;
RA   Stone D.M., Murone M., Luoh S.-M., Ye W., Armanini M.P., Gurney A.,
RA   Phillips H., Brush J., Goddard A., deSauvage F.J., Rosenthal A.;
RT   "Characterization of the human suppressor of fused, a negative regulator of
RT   the zinc-finger transcription factor Gli.";
RL   J. Cell Sci. 112:4437-4448(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GLI1,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10559945; DOI=10.1038/13031;
RA   Kogerman P., Grimm T., Kogerman L., Krause D., Unden A.B., Sandstedt B.,
RA   Toftgaard R., Zaphiropoulos P.G.;
RT   "Mammalian suppressor-of-fused modulates nuclear-cytoplasmic shuttling of
RT   Gli-1.";
RL   Nat. Cell Biol. 1:312-319(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, VARIANTS LEU-15 AND SER-340,
RP   AND INVOLVEMENT IN MDB.
RX   PubMed=12068298; DOI=10.1038/ng916;
RA   Taylor M.D., Liu L., Raffel C., Hui C.-C., Mainprize T.G., Zhang X.,
RA   Agatep R., Chiappa S., Gao L., Lowrance A., Hao A., Goldstein A.M.,
RA   Stavrou T., Scherer S.W., Dura W.T., Wainwright B., Squire J.A.,
RA   Rutka J.T., Hogg D.;
RT   "Mutations in SUFU predispose to medulloblastoma.";
RL   Nat. Genet. 31:306-310(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-484 (ISOFORM 1).
RC   TISSUE=Neuron;
RX   PubMed=11252182; DOI=10.1007/s004270050255;
RA   Delattre M., Briand S., Paces-Fessy M., Blanchet-Tournier M.-F.;
RT   "Suppressor of fused gene involved in hedgehog signal transduction in
RT   Drosophila melanogaster is conserved in mammals.";
RL   Dev. Genes Evol. 209:294-300(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-484 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH STK36.
RX   PubMed=10806483; DOI=10.1038/35010610;
RA   Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M., Grey C.,
RA   Rosenthal A., de Sauvage F.J.;
RT   "Gli regulation by the opposing activities of fused and suppressor of
RT   fused.";
RL   Nat. Cell Biol. 2:310-312(2000).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP   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   [11]
RP   INVOLVEMENT IN BCNS.
RX   PubMed=19533801; DOI=10.1002/ajmg.a.32944;
RA   Pastorino L., Ghiorzo P., Nasti S., Battistuzzi L., Cusano R.,
RA   Marzocchi C., Garre M.L., Clementi M., Scarra G.B.;
RT   "Identification of a SUFU germline mutation in a family with Gorlin
RT   syndrome.";
RL   Am. J. Med. Genet. A 149A:1539-1543(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-303, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   INTERACTION WITH ULK3.
RX   PubMed=20643644; DOI=10.1074/jbc.m110.133991;
RA   Maloverjan A., Piirsoo M., Kasak L., Peil L., Osterlund T., Kogerman P.;
RT   "Dual function of UNC-51-like kinase 3 (Ulk3) in the Sonic hedgehog
RT   signaling pathway.";
RL   J. Biol. Chem. 285:30079-30090(2010).
RN   [14]
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   [15]
RP   INTERACTION WITH RAB23, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22365972; DOI=10.1016/j.cellsig.2012.02.004;
RA   Chi S., Xie G., Liu H., Chen K., Zhang X., Li C., Xie J.;
RT   "Rab23 negatively regulates Gli1 transcriptional factor in a Su(Fu)-
RT   dependent manner.";
RL   Cell. Signal. 24:1222-1228(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-342 AND SER-346, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [17]
RP   FUNCTION, UBIQUITINATION AT LYS-257, PHOSPHORYLATION AT SER-342; SER-346;
RP   SER-352 AND THR-353, AND MUTAGENESIS OF LYS-257 AND 342-SER--SER-346.
RX   PubMed=27234298; DOI=10.15252/embj.201593374;
RA   Raducu M., Fung E., Serres S., Infante P., Barberis A., Fischer R.,
RA   Bristow C., Thezenas M.L., Finta C., Christianson J.C., Buffa F.M.,
RA   Kessler B.M., Sibson N.R., Di Marcotullio L., Toftgaard R.,
RA   D'Angiolella V.;
RT   "SCF (Fbxl17) ubiquitylation of Sufu regulates Hedgehog signaling and
RT   medulloblastoma development.";
RL   EMBO J. 35:1400-1416(2016).
RN   [18]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLI1 AND GLI3, INVOLVEMENT
RP   IN JBTS32, VARIANTS JBTS32 ARG-176 AND THR-406, CHARACTERIZATION OF
RP   VARIANTS JBTS32 ARG-176 AND THR-406, AND VARIANTS VAL-19; VAL-37; MET-77;
RP   GLN-289; VAL-293; 299-ARG--HIS-484 DEL; LEU-382; ARG-442 AND ASN-481.
RX   PubMed=28965847; DOI=10.1016/j.ajhg.2017.08.017;
RA   De Mori R., Romani M., D'Arrigo S., Zaki M.S., Lorefice E., Tardivo S.,
RA   Biagini T., Stanley V., Musaev D., Fluss J., Micalizzi A., Nuovo S.,
RA   Illi B., Chiapparini L., Di Marcotullio L., Issa M.Y., Anello D.,
RA   Casella A., Ginevrino M., Leggins A.S., Roosing S., Alfonsi R., Rosati J.,
RA   Schot R., Mancini G.M.S., Bertini E., Dobyns W.B., Mazza T., Gleeson J.G.,
RA   Valente E.M.;
RT   "Hypomorphic Recessive Variants in SUFU Impair the Sonic Hedgehog Pathway
RT   and Cause Joubert Syndrome with Cranio-facial and Skeletal Defects.";
RL   Am. J. Hum. Genet. 101:552-563(2017).
RN   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 27-268, FUNCTION, INTERACTION
RP   WITH GLI1, AND MUTAGENESIS OF GLU-106; ASP-111; THR-128; GLU-152; ASP-159;
RP   GLU-181; GLU-221 AND ASP-262.
RX   PubMed=15367681; DOI=10.1128/mcb.24.19.8627-8641.2004;
RA   Merchant M., Vajdos F.F., Ultsch M., Maun H.R., Wendt U., Cannon J.,
RA   Desmarais W., Lazarus R.A., de Vos A.M., de Sauvage F.J.;
RT   "Suppressor of fused regulates Gli activity through a dual binding
RT   mechanism.";
RL   Mol. Cell. Biol. 24:8627-8641(2004).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 32-278 AND 361-483 IN COMPLEXES
RP   WITH GLI1 AND GLI3, INTRINSICALLY DISORDERED REGION, FUNCTION, AND
RP   INTERACTION WITH GLI1 AND GLI3.
RX   PubMed=24311597; DOI=10.1107/s0907444913028473;
RA   Cherry A.L., Finta C., Karlstrom M., Jin Q., Schwend T., Astorga-Wells J.,
RA   Zubarev R.A., Del Campo M., Criswell A.R., de Sanctis D., Jovine L.,
RA   Toftgard R.;
RT   "Structural basis of SUFU-GLI interaction in human Hedgehog signalling
RT   regulation.";
RL   Acta Crystallogr. D 69:2563-2579(2013).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH GLI1, INTERACTION
RP   WITH GLI1 AND GLI2, FUNCTION, AND MUTAGENESIS OF TYR-147; ASP-159 AND
RP   LEU-380.
RX   PubMed=24217340; DOI=10.1038/ncomms3608;
RA   Zhang Y., Fu L., Qi X., Zhang Z., Xia Y., Jia J., Jiang J., Zhao Y., Wu G.;
RT   "Structural insight into the mutual recognition and regulation between
RT   Suppressor of Fused and Gli/Ci.";
RL   Nat. Commun. 4:2608-2608(2013).
CC   -!- FUNCTION: Negative regulator in the hedgehog/smoothened signaling
CC       pathway (PubMed:10559945, PubMed:10564661, PubMed:10806483,
CC       PubMed:12068298, PubMed:12975309, PubMed:27234298, PubMed:15367681,
CC       PubMed:22365972, PubMed:24217340, PubMed:24311597, PubMed:28965847).
CC       Down-regulates GLI1-mediated transactivation of target genes
CC       (PubMed:15367681, PubMed:24217340, PubMed:24311597). Down-regulates
CC       GLI2-mediated transactivation of target genes (PubMed:24311597,
CC       PubMed:24217340). Part of a corepressor complex that acts on DNA-bound
CC       GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1
CC       to degradation by the proteasome (PubMed:10559945, PubMed:10564661,
CC       PubMed:10806483, PubMed:24217340). Sequesters GLI1, GLI2 and GLI3 in
CC       the cytoplasm, this effect is overcome by binding of STK36 to both SUFU
CC       and a GLI protein (PubMed:10559945, PubMed:10564661, PubMed:10806483,
CC       PubMed:24217340). Negative regulator of beta-catenin signaling (By
CC       similarity). Regulates the formation of either the repressor form
CC       (GLI3R) or the activator form (GLI3A) of the full-length form of GLI3
CC       (GLI3FL) (PubMed:24311597, PubMed:28965847). GLI3FL is complexed with
CC       SUFU in the cytoplasm and is maintained in a neutral state
CC       (PubMed:24311597, PubMed:28965847). Without the Hh signal, the SUFU-
CC       GLI3 complex is recruited to cilia, leading to the efficient processing
CC       of GLI3FL into GLI3R (PubMed:24311597, PubMed:28965847). When Hh
CC       signaling is initiated, SUFU dissociates from GLI3FL and the latter
CC       translocates to the nucleus, where it is phosphorylated, destabilized,
CC       and converted to a transcriptional activator (GLI3A) (PubMed:24311597,
CC       PubMed:28965847). Required for normal embryonic development (By
CC       similarity). Required for the proper formation of hair follicles and
CC       the control of epidermal differentiation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Z0P7, ECO:0000269|PubMed:10559945,
CC       ECO:0000269|PubMed:10564661, ECO:0000269|PubMed:10806483,
CC       ECO:0000269|PubMed:12068298, ECO:0000269|PubMed:12975309,
CC       ECO:0000269|PubMed:15367681, ECO:0000269|PubMed:22365972,
CC       ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597,
CC       ECO:0000269|PubMed:27234298, ECO:0000269|PubMed:28965847}.
CC   -!- SUBUNIT: May form homodimers (PubMed:10564661). Part of a DNA-bound
CC       corepressor complex containing SAP18, GLI1 and SIN3 (By similarity).
CC       Part of a complex containing CTNNB1 (By similarity). Binds BTRC, GLI2,
CC       GLI3, SAP18 and STK36 (PubMed:10564661, PubMed:10806483). Binds both
CC       free and DNA-bound GLI1 (PubMed:10559945, PubMed:15367681,
CC       PubMed:24217340, PubMed:24311597, PubMed:28965847). Interacts with KIF7
CC       (By similarity). Interacts with GLI3FL and this interaction regulates
CC       the formation of either repressor or activator forms of GLI3
CC       (PubMed:24311597, PubMed:28965847). Its association with GLI3FL is
CC       regulated by Hh signaling and dissociation of the SUFU-GLI3 interaction
CC       requires the presence of the ciliary motor KIF3A (PubMed:24311597,
CC       PubMed:28965847). Interacts with ULK3; inactivating the protein kinase
CC       activity of ULK3 (PubMed:20643644). Interacts with RAB23
CC       (PubMed:22365972). {ECO:0000250|UniProtKB:Q9Z0P7,
CC       ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:10564661,
CC       ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:15367681,
CC       ECO:0000269|PubMed:20643644, ECO:0000269|PubMed:22365972,
CC       ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597,
CC       ECO:0000269|PubMed:28965847}.
CC   -!- INTERACTION:
CC       Q9UMX1; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-740595, EBI-742038;
CC       Q9UMX1; Q13515: BFSP2; NbExp=4; IntAct=EBI-740595, EBI-10229433;
CC       Q9UMX1; Q53ET0: CRTC2; NbExp=5; IntAct=EBI-740595, EBI-1181987;
CC       Q9UMX1; O43186: CRX; NbExp=3; IntAct=EBI-740595, EBI-748171;
CC       Q9UMX1; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-740595, EBI-11988027;
CC       Q9UMX1; P51114-2: FXR1; NbExp=3; IntAct=EBI-740595, EBI-11022345;
CC       Q9UMX1; P08151: GLI1; NbExp=26; IntAct=EBI-740595, EBI-308084;
CC       Q9UMX1; P10071: GLI3; NbExp=3; IntAct=EBI-740595, EBI-308055;
CC       Q9UMX1; Q7Z353: HDX; NbExp=3; IntAct=EBI-740595, EBI-1052734;
CC       Q9UMX1; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-740595, EBI-3044087;
CC       Q9UMX1; O95678: KRT75; NbExp=3; IntAct=EBI-740595, EBI-2949715;
CC       Q9UMX1; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-740595, EBI-11985629;
CC       Q9UMX1; Q86VQ0: LCA5; NbExp=3; IntAct=EBI-740595, EBI-6658186;
CC       Q9UMX1; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-740595, EBI-1216080;
CC       Q9UMX1; Q9UJ55: MAGEL2; NbExp=3; IntAct=EBI-740595, EBI-5668174;
CC       Q9UMX1; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-740595, EBI-16439278;
CC       Q9UMX1; O00746: NME4; NbExp=3; IntAct=EBI-740595, EBI-744871;
CC       Q9UMX1; Q7Z412: PEX26; NbExp=2; IntAct=EBI-740595, EBI-752057;
CC       Q9UMX1; Q96D15: RCN3; NbExp=5; IntAct=EBI-740595, EBI-746283;
CC       Q9UMX1; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-740595, EBI-7225508;
CC       Q9UMX1; Q9NRP7: STK36; NbExp=3; IntAct=EBI-740595, EBI-863797;
CC       Q9UMX1; Q8N4C7: STX19; NbExp=3; IntAct=EBI-740595, EBI-8484990;
CC       Q9UMX1; Q08117-2: TLE5; NbExp=3; IntAct=EBI-740595, EBI-11741437;
CC       Q9UMX1; Q15915: ZIC1; NbExp=3; IntAct=EBI-740595, EBI-11963196;
CC       Q9UMX1; Q8NC26: ZNF114; NbExp=3; IntAct=EBI-740595, EBI-10265237;
CC       Q9UMX1; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-740595, EBI-373456;
CC       Q9UMX1; Q9NWS9-2: ZNF446; NbExp=4; IntAct=EBI-740595, EBI-740232;
CC       Q9UMX1; Q9BV97: ZNF747; NbExp=4; IntAct=EBI-740595, EBI-4395497;
CC       Q9UMX1; Q0D2J5: ZNF763; NbExp=3; IntAct=EBI-740595, EBI-10226414;
CC       Q9UMX1; Q96H86: ZNF764; NbExp=5; IntAct=EBI-740595, EBI-745775;
CC       Q9UMX1; Q8TBC5: ZSCAN18; NbExp=3; IntAct=EBI-740595, EBI-3919096;
CC       Q9UMX1; Q0VGT2: Gli2; Xeno; NbExp=3; IntAct=EBI-740595, EBI-9344284;
CC       Q9UMX1-1; P08151: GLI1; NbExp=2; IntAct=EBI-740615, EBI-308084;
CC       Q9UMX1-2; P08151: GLI1; NbExp=4; IntAct=EBI-740621, EBI-308084;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10559945,
CC       ECO:0000269|PubMed:28965847}. Nucleus {ECO:0000269|PubMed:10559945,
CC       ECO:0000269|PubMed:28965847}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Su(fu)484;
CC         IsoId=Q9UMX1-1; Sequence=Displayed;
CC       Name=2; Synonyms=Su(fu)433;
CC         IsoId=Q9UMX1-2; Sequence=VSP_013278, VSP_013279;
CC       Name=3;
CC         IsoId=Q9UMX1-3; Sequence=VSP_013280;
CC   -!- TISSUE SPECIFICITY: Ubiquitous in adult tissues. Detected in
CC       osteoblasts of the perichondrium in the developing limb of 12-week old
CC       embryos. Isoform 1 is detected in fetal brain, lung, kidney and testis.
CC       Isoform 2 is detected in fetal testis, and at much lower levels in
CC       fetal brain, lung and kidney. {ECO:0000269|PubMed:10559945,
CC       ECO:0000269|PubMed:10564661}.
CC   -!- PTM: Polyubiquitinated at Lys-257 by the SCF(FBXL17) complex, leading
CC       to its subsequent degradation and allowing the release of GLI1 for
CC       proper hedgehog/smoothened signal transduction (PubMed:27234298).
CC       Ubiquitination is impaired by phosphorylation at Ser-342, Ser-346, Ser-
CC       352 and Thr-353 (PubMed:27234298). {ECO:0000269|PubMed:27234298}.
CC   -!- PTM: Phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353 prevents
CC       ubiquitination by the SCF(FBXL17) complex.
CC       {ECO:0000269|PubMed:27234298}.
CC   -!- DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive
CC       embryonal tumor of the cerebellum with a preferential manifestation in
CC       children. {ECO:0000269|PubMed:12068298}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Joubert syndrome 32 (JBTS32) [MIM:617757]: A form of Joubert
CC       syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC       apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC       delay. Neuroradiologically, it is characterized by cerebellar vermian
CC       hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC       peduncles, and an abnormally large interpeduncular fossa, giving the
CC       appearance of a molar tooth on transaxial slices (molar tooth sign).
CC       Additional variable features include retinal dystrophy, renal disease,
CC       liver fibrosis, and polydactyly. JBTS32 inheritance is autosomal
CC       recessive. {ECO:0000269|PubMed:28965847}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Basal cell nevus syndrome (BCNS) [MIM:109400]: An autosomal
CC       dominant disease characterized by nevoid basal cell carcinomas and
CC       developmental abnormalities such as rib and craniofacial alterations,
CC       polydactyly, syndactyly, and spina bifida. In addition, the patients
CC       suffer from a multitude of tumors like basal cell carcinomas, fibromas
CC       of the ovaries and heart, cysts of the skin, jaws and mesentery, as
CC       well as medulloblastomas and meningiomas.
CC       {ECO:0000269|PubMed:19533801}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC   -!- SIMILARITY: Belongs to the SUFU family. {ECO:0000305}.
DR   EMBL; AF144231; AAF23890.1; -; mRNA.
DR   EMBL; AF159447; AAF23893.1; -; mRNA.
DR   EMBL; AF222345; AAF35866.1; -; mRNA.
DR   EMBL; AF175770; AAD50501.1; -; mRNA.
DR   EMBL; AY081829; AAM08947.1; -; Genomic_DNA.
DR   EMBL; AY081818; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081819; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081820; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081822; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081824; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081825; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081821; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081823; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081826; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081828; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY081827; AAM08947.1; JOINED; Genomic_DNA.
DR   EMBL; AY358550; AAQ88914.1; -; mRNA.
DR   EMBL; AL121928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013291; AAH13291.1; -; mRNA.
DR   EMBL; AF172319; AAD51655.1; -; mRNA.
DR   EMBL; AL137465; CAB70752.1; -; mRNA.
DR   CCDS; CCDS53571.1; -. [Q9UMX1-2]
DR   CCDS; CCDS7537.1; -. [Q9UMX1-1]
DR   PIR; T46409; T46409.
DR   RefSeq; NP_001171604.1; NM_001178133.1. [Q9UMX1-2]
DR   RefSeq; NP_057253.2; NM_016169.3. [Q9UMX1-1]
DR   PDB; 1M1L; X-ray; 2.65 A; A/B/C/D=27-262.
DR   PDB; 4BL8; X-ray; 3.04 A; A/B=32-483.
DR   PDB; 4BL9; X-ray; 2.80 A; A/B/C/D=32-278, A/B/C/D=361-483.
DR   PDB; 4BLA; X-ray; 3.50 A; A/B/C/D=32-278, A/B/C/D=361-483.
DR   PDB; 4BLB; X-ray; 2.80 A; A/B/C/D=32-278, A/B/C/D=361-483.
DR   PDB; 4BLD; X-ray; 2.80 A; A/B/C/D=32-278, A/B/C/D=361-483.
DR   PDB; 4KM8; X-ray; 2.26 A; A=1-484.
DR   PDB; 4KM9; X-ray; 3.19 A; A=1-484.
DR   PDB; 4KMD; X-ray; 1.70 A; A=1-484.
DR   PDB; 4KMH; X-ray; 3.04 A; A/B=1-484.
DR   PDBsum; 1M1L; -.
DR   PDBsum; 4BL8; -.
DR   PDBsum; 4BL9; -.
DR   PDBsum; 4BLA; -.
DR   PDBsum; 4BLB; -.
DR   PDBsum; 4BLD; -.
DR   PDBsum; 4KM8; -.
DR   PDBsum; 4KM9; -.
DR   PDBsum; 4KMD; -.
DR   PDBsum; 4KMH; -.
DR   SMR; Q9UMX1; -.
DR   BioGRID; 119676; 73.
DR   ComplexPortal; CPX-148; GLI2-SUFU complex.
DR   ComplexPortal; CPX-150; GLI3-SUFU complex.
DR   ComplexPortal; CPX-56; GLI1-SUFU complex.
DR   CORUM; Q9UMX1; -.
DR   ELM; Q9UMX1; -.
DR   IntAct; Q9UMX1; 64.
DR   MINT; Q9UMX1; -.
DR   STRING; 9606.ENSP00000358918; -.
DR   ChEMBL; CHEMBL5390; -.
DR   iPTMnet; Q9UMX1; -.
DR   PhosphoSitePlus; Q9UMX1; -.
DR   BioMuta; SUFU; -.
DR   DMDM; 62511179; -.
DR   CPTAC; CPTAC-1329; -.
DR   EPD; Q9UMX1; -.
DR   jPOST; Q9UMX1; -.
DR   MassIVE; Q9UMX1; -.
DR   PaxDb; Q9UMX1; -.
DR   PeptideAtlas; Q9UMX1; -.
DR   PRIDE; Q9UMX1; -.
DR   ProteomicsDB; 85217; -. [Q9UMX1-1]
DR   ProteomicsDB; 85218; -. [Q9UMX1-2]
DR   ProteomicsDB; 85219; -. [Q9UMX1-3]
DR   Antibodypedia; 1768; 276 antibodies.
DR   DNASU; 51684; -.
DR   Ensembl; ENST00000369899; ENSP00000358915; ENSG00000107882. [Q9UMX1-2]
DR   Ensembl; ENST00000369902; ENSP00000358918; ENSG00000107882. [Q9UMX1-1]
DR   Ensembl; ENST00000423559; ENSP00000411597; ENSG00000107882. [Q9UMX1-3]
DR   GeneID; 51684; -.
DR   KEGG; hsa:51684; -.
DR   UCSC; uc001kvw.3; human. [Q9UMX1-1]
DR   CTD; 51684; -.
DR   DisGeNET; 51684; -.
DR   EuPathDB; HostDB:ENSG00000107882.11; -.
DR   GeneCards; SUFU; -.
DR   GeneReviews; SUFU; -.
DR   HGNC; HGNC:16466; SUFU.
DR   HPA; ENSG00000107882; Low tissue specificity.
DR   MalaCards; SUFU; -.
DR   MIM; 109400; phenotype.
DR   MIM; 155255; phenotype.
DR   MIM; 607035; gene.
DR   MIM; 617757; phenotype.
DR   neXtProt; NX_Q9UMX1; -.
DR   OpenTargets; ENSG00000107882; -.
DR   Orphanet; 36; Acrocallosal syndrome.
DR   Orphanet; 251863; Desmoplastic/nodular medulloblastoma.
DR   Orphanet; 263662; Familial multiple meningioma.
DR   Orphanet; 377; Gorlin syndrome.
DR   Orphanet; 251858; Medulloblastoma with extensive nodularity.
DR   Orphanet; 2495; Meningioma.
DR   Orphanet; 280200; Microform holoprosencephaly.
DR   PharmGKB; PA38146; -.
DR   eggNOG; ENOG502QT57; Eukaryota.
DR   GeneTree; ENSGT00390000009747; -.
DR   HOGENOM; CLU_033906_0_0_1; -.
DR   InParanoid; Q9UMX1; -.
DR   KO; K06229; -.
DR   OMA; GDNIPWR; -.
DR   OrthoDB; 1248959at2759; -.
DR   PhylomeDB; Q9UMX1; -.
DR   TreeFam; TF324548; -.
DR   PathwayCommons; Q9UMX1; -.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   SignaLink; Q9UMX1; -.
DR   SIGNOR; Q9UMX1; -.
DR   BioGRID-ORCS; 51684; 13 hits in 890 CRISPR screens.
DR   ChiTaRS; SUFU; human.
DR   EvolutionaryTrace; Q9UMX1; -.
DR   GeneWiki; SUFU; -.
DR   GenomeRNAi; 51684; -.
DR   Pharos; Q9UMX1; Tbio.
DR   PRO; PR:Q9UMX1; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9UMX1; protein.
DR   Bgee; ENSG00000107882; Expressed in layer of synovial tissue and 203 other tissues.
DR   Genevisible; Q9UMX1; HS.
DR   GO; GO:0097546; C:ciliary base; TAS:Reactome.
DR   GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IDA:MGI.
DR   GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR   GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR   GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IBA:GO_Central.
DR   GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; TAS:BHF-UCL.
DR   GO; GO:0042308; P:negative regulation of protein import into nucleus; TAS:BHF-UCL.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:UniProtKB.
DR   GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   GO; GO:0043588; P:skin development; IEA:Ensembl.
DR   GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IEA:Ensembl.
DR   GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IEA:Ensembl.
DR   GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR   DisProt; DP01312; -.
DR   Gene3D; 3.30.1360.230; -; 1.
DR   InterPro; IPR020941; SUFU-like_domain.
DR   InterPro; IPR024314; SUFU_C.
DR   InterPro; IPR038489; SUFU_C_sf.
DR   InterPro; IPR037181; SUFU_N.
DR   InterPro; IPR007768; Suppressor_of_fused.
DR   InterPro; IPR016591; Suppressor_of_fused_euk.
DR   PANTHER; PTHR10928; PTHR10928; 1.
DR   Pfam; PF05076; SUFU; 1.
DR   Pfam; PF12470; SUFU_C; 1.
DR   PIRSF; PIRSF011844; Suppressor_of_fused_protein; 1.
DR   SUPFAM; SSF103359; SSF103359; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Ciliopathy; Cytoplasm;
KW   Developmental protein; Disease mutation; Isopeptide bond; Joubert syndrome;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Tumor suppressor; Ubl conjugation.
FT   CHAIN           1..484
FT                   /note="Suppressor of fused homolog"
FT                   /id="PRO_0000072302"
FT   REGION          279..360
FT                   /note="Intrinsically disordered"
FT                   /evidence="ECO:0000269|PubMed:24311597"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         303
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:27234298"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:27234298"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:27234298"
FT   MOD_RES         353
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:27234298"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   CROSSLNK        257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:27234298"
FT   CROSSLNK        321
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         433..484
FT                   /note="ILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH
FT                   -> VRRPFFFSLLPFIDFLAHPSSSPLAALDGTPSWGAGHECLMDSGPGACV (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10564661"
FT                   /id="VSP_013280"
FT   VAR_SEQ         433
FT                   /note="I -> L (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10564661,
FT                   ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013278"
FT   VAR_SEQ         434..484
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10564661,
FT                   ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013279"
FT   VARIANT         15
FT                   /note="P -> L (in dbSNP:rs28942088)"
FT                   /evidence="ECO:0000269|PubMed:12068298"
FT                   /id="VAR_021566"
FT   VARIANT         19
FT                   /note="G -> V"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080418"
FT   VARIANT         37
FT                   /note="I -> V (in dbSNP:rs745793517)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080419"
FT   VARIANT         77
FT                   /note="V -> M"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080420"
FT   VARIANT         176
FT                   /note="H -> R (in JBTS32; decreased stability; no effect on
FT                   nuclear and cytoplasmic localization; decreased interaction
FT                   with GLI3; no effect on interaction with GLI1; decreased
FT                   repression of the hedgehog/smoothened signaling pathway;
FT                   dbSNP:rs1554852272)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080421"
FT   VARIANT         289
FT                   /note="R -> Q (in dbSNP:rs149016373)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080422"
FT   VARIANT         293
FT                   /note="I -> V (in dbSNP:rs574002050)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080423"
FT   VARIANT         299..484
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080424"
FT   VARIANT         340
FT                   /note="A -> S (in dbSNP:rs34135067)"
FT                   /evidence="ECO:0000269|PubMed:12068298"
FT                   /id="VAR_021567"
FT   VARIANT         382
FT                   /note="P -> L (in dbSNP:rs1401882800)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080425"
FT   VARIANT         406
FT                   /note="I -> T (in JBTS32; decreased stability; forms
FT                   cytoplasmic aggregates; decreased interaction with GLI3; no
FT                   effect on interaction with GLI1; decreased repression of
FT                   the hedgehog/smoothened signaling pathway;
FT                   dbSNP:rs1554854758)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080426"
FT   VARIANT         442
FT                   /note="K -> R (in dbSNP:rs772598739)"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080427"
FT   VARIANT         481
FT                   /note="S -> N"
FT                   /evidence="ECO:0000269|PubMed:28965847"
FT                   /id="VAR_080428"
FT   MUTAGEN         106
FT                   /note="E->A: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         111
FT                   /note="D->A: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         128
FT                   /note="T->A,D: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         147
FT                   /note="Y->R: Impairs interaction with GLI1 and GLI2.
FT                   Abolishes interaction with GLI1 and GLI2; when associated
FT                   with R-159 and R-380."
FT                   /evidence="ECO:0000269|PubMed:24217340"
FT   MUTAGEN         152
FT                   /note="E->A: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         159
FT                   /note="D->A: Abolishes down-regulation of GLI1 activity.
FT                   Has only slight effect on GLI1 binding."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         159
FT                   /note="D->R: Impairs interaction with GLI1 and GLI2.
FT                   Abolishes interaction with GLI1 and GLI2; when associated
FT                   with R-147 and R-380."
FT                   /evidence="ECO:0000269|PubMed:24217340"
FT   MUTAGEN         181
FT                   /note="E->A: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         221
FT                   /note="E->A: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         257
FT                   /note="K->R: Abolishes ubiquitination by the SCF(FBXL17)
FT                   complex."
FT                   /evidence="ECO:0000269|PubMed:27234298"
FT   MUTAGEN         262
FT                   /note="D->A: No effect on down-regulation of GLI1
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15367681"
FT   MUTAGEN         342..346
FT                   /note="SRKDS->ARKDA: Increased interaction with FBXL17 and
FT                   ubiquitination by the SCF(FBXL17) complex."
FT                   /evidence="ECO:0000269|PubMed:27234298"
FT   MUTAGEN         342..346
FT                   /note="SRKDS->DRKDD: Phosphomimetic mutant; decreased
FT                   interaction with FBXL17 and ubiquitination by the
FT                   SCF(FBXL17) complex."
FT                   /evidence="ECO:0000269|PubMed:27234298"
FT   MUTAGEN         380
FT                   /note="L->R: Impairs interaction with GLI1 and GLI2.
FT                   Abolishes interaction with GLI1 and GLI2; when associated
FT                   with R-147 and R-159."
FT                   /evidence="ECO:0000269|PubMed:24217340"
FT   CONFLICT        336
FT                   /note="A -> P (in Ref. 2; AAD50501)"
FT                   /evidence="ECO:0000305"
FT   HELIX           27..29
FT                   /evidence="ECO:0000244|PDB:4KM8"
FT   HELIX           32..44
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          52..55
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           60..62
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          69..76
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           80..82
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          87..96
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          101..105
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          110..125
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           136..151
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          160..162
FT                   /evidence="ECO:0000244|PDB:4BLB"
FT   STRAND          169..171
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          176..181
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          188..190
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          193..203
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           205..213
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           216..224
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           227..229
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   TURN            230..234
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           244..247
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           250..262
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          266..276
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          363..367
FT                   /evidence="ECO:0000244|PDB:4BL9"
FT   STRAND          369..373
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           375..378
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           381..387
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           389..391
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          395..403
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          405..409
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          420..422
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          424..427
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          430..434
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           437..446
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   TURN            447..449
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          460..464
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           465..467
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   STRAND          469..473
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           476..479
FT                   /evidence="ECO:0000244|PDB:4KMD"
SQ   SEQUENCE   484 AA;  53947 MW;  4A9CD1CF75FC179A CRC64;
     MAELRPSGAP GPTAPPAPGP TAPPAFASLF PPGLHAIYGE CRRLYPDQPN PLQVTAIVKY
     WLGGPDPLDY VSMYRNVGSP SANIPEHWHY ISFGLSDLYG DNRVHEFTGT DGPSGFGFEL
     TFRLKRETGE SAPPTWPAEL MQGLARYVFQ SENTFCSGDH VSWHSPLDNS ESRIQHMLLT
     EDPQMQPVQT PFGVVTFLQI VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR
     GETIFEIDPH LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDDEDSRS ICIGTQPRRL
     SGKDTEQIRE TLRRGLEINS KPVLPPINPQ RQNGLAHDRA PSRKDSLESD SSTAIIPHEL
     IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI TGDMAITFVS TGVEGAFATE
     EHPYAAHGPW LQILLTEEFV EKMLEDLEDL TSPEEFKLPK EYSWPEKKLK VSILPDVVFD
     SPLH
//
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