SUFU_MOUSE
ID SUFU_MOUSE Reviewed; 484 AA.
AC Q9Z0P7; Q8C8B4; Q99JG0; Q9D521; Q9JLU1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Suppressor of fused homolog {ECO:0000303|PubMed:10531011};
GN Name=Sufu {ECO:0000303|PubMed:23034632, ECO:0000312|MGI:MGI:1345643};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH GLI1;
RP GLI2 AND GLI3, AND TISSUE SPECIFICITY.
RX PubMed=10531011; DOI=10.1016/s0960-9822(99)80482-5;
RA Ding Q., Fukami S., Meng X., Nishizaki Y., Zhang X., Sasaki H., Dlugosz A.,
RA Nakafuku M., Hui C.;
RT "Mouse suppressor of fused is a negative regulator of sonic hedgehog
RT signaling and alters the subcellular distribution of Gli1.";
RL Curr. Biol. 9:1119-1122(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Mammary gland, and Testis;
RX PubMed=11557033; DOI=10.1016/s0014-5793(01)02682-5;
RA Grimm T., Teglund S., Tackels D., Sangiorgi E., Gurrieri F., Schwartz C.,
RA Toftgaard R.;
RT "Genomic organization and embryonic expression of suppressor of fused, a
RT candidate gene for the split-hand/split-foot malformation type 3.";
RL FEBS Lett. 505:13-17(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH
RP CTNNB1.
RX PubMed=11477086; DOI=10.1074/jbc.m105317200;
RA Meng X., Poon R., Zhang X., Cheah A., Ding Q., Hui C.-C., Alman B.;
RT "Suppressor of fused negatively regulates beta-catenin signaling.";
RL J. Biol. Chem. 276:40113-40119(2001).
RN [7]
RP FUNCTION, INTERACTION WITH SAP18, AND IDENTIFICATION IN A DNA-BOUND SIN3
RP COREPRESSOR COMPLEX.
RX PubMed=11960000; DOI=10.1073/pnas.082096999;
RA Cheng S.Y., Bishop J.M.;
RT "Suppressor of fused represses Gli-mediated transcription by recruiting the
RT SAP18-mSin3 corepressor complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5442-5447(2002).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16155214; DOI=10.1242/dev.02021;
RA Cooper A.F., Yu K.P., Brueckner M., Brailey L.L., Johnson L., McGrath J.M.,
RA Bale A.E.;
RT "Cardiac and CNS defects in a mouse with targeted disruption of suppressor
RT of fused.";
RL Development 132:4407-4417(2005).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16459298; DOI=10.1016/j.devcel.2005.12.013;
RA Svard J., Heby-Henricson K., Henricson K.H., Persson-Lek M., Rozell B.,
RA Lauth M., Bergstrom A., Ericson J., Toftgard R., Teglund S.;
RT "Genetic elimination of Suppressor of fused reveals an essential repressor
RT function in the mammalian Hedgehog signaling pathway.";
RL Dev. Cell 10:187-197(2006).
RN [10]
RP INTERACTION WITH KIF7.
RX PubMed=19592253; DOI=10.1016/j.cub.2009.06.046;
RA Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W.,
RA Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J.,
RA Peterson A.S.;
RT "The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh
RT signal transduction during development.";
RL Curr. Biol. 19:1320-1326(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GLI3.
RX PubMed=20360384; DOI=10.1101/gad.1902910;
RA Humke E.W., Dorn K.V., Milenkovic L., Scott M.P., Rohatgi R.;
RT "The output of Hedgehog signaling is controlled by the dynamic association
RT between Suppressor of Fused and the Gli proteins.";
RL Genes Dev. 24:670-682(2010).
RN [13]
RP FUNCTION IN EPIDERMAL DIFFERENTIATION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GLI2.
RX PubMed=23034632; DOI=10.1242/dev.081190;
RA Li Z.J., Nieuwenhuis E., Nien W., Zhang X., Zhang J., Puviindran V.,
RA Wainwright B.J., Kim P.C., Hui C.C.;
RT "Kif7 regulates Gli2 through Sufu-dependent and -independent functions
RT during skin development and tumorigenesis.";
RL Development 139:4152-4161(2012).
CC -!- FUNCTION: Negative regulator in the hedgehog/smoothened signaling
CC pathway (PubMed:16155214, PubMed:16459298). Down-regulates GLI1-
CC mediated transactivation of target genes (PubMed:11960000). Part of a
CC corepressor complex that acts on DNA-bound GLI1 (PubMed:11960000). May
CC also act by linking GLI1 to BTRC and thereby targeting GLI1 to
CC degradation by the proteasome (By similarity). Sequesters GLI1, GLI2
CC and GLI3 in the cytoplasm, this effect is overcome by binding of STK36
CC to both SUFU and a GLI protein (PubMed:10531011, PubMed:16459298).
CC Negative regulator of beta-catenin signaling (PubMed:11477086).
CC Regulates the formation of either the repressor form (GLI3R) or the
CC activator form (GLI3A) of the full-length form of GLI3 (GLI3FL)
CC (PubMed:10531011, PubMed:20360384). GLI3FL is complexed with SUFU in
CC the cytoplasm and is maintained in a neutral state (PubMed:10531011,
CC PubMed:20360384). Without the Hh signal, the SUFU-GLI3 complex is
CC recruited to cilia, leading to the efficient processing of GLI3FL into
CC GLI3R (PubMed:10531011, PubMed:20360384). When Hh signaling is
CC initiated, SUFU dissociates from GLI3FL and the latter translocates to
CC the nucleus, where it is phosphorylated, destabilized, and converted to
CC a transcriptional activator (GLI3A) (PubMed:10531011, PubMed:20360384).
CC Required for normal embryonic development (PubMed:16155214,
CC PubMed:16459298). Required for the proper formation of hair follicles
CC and the control of epidermal differentiation (PubMed:16155214,
CC PubMed:16459298, PubMed:23034632). {ECO:0000250|UniProtKB:Q9UMX1,
CC ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:11477086,
CC ECO:0000269|PubMed:11960000, ECO:0000269|PubMed:16155214,
CC ECO:0000269|PubMed:16459298, ECO:0000269|PubMed:20360384,
CC ECO:0000269|PubMed:23034632}.
CC -!- SUBUNIT: May form homodimers (By similarity). Interacts with ULK3;
CC inactivating the protein kinase activity of ULK3. Interacts with RAB23
CC (By similarity). Part of a DNA-bound corepressor complex containing
CC SAP18, GLI1 and SIN3 (PubMed:11960000). Part of a complex containing
CC CTNNB1 (PubMed:11477086). Binds BTRC, GLI2, GLI3, SAP18 and STK36
CC (PubMed:20360384, PubMed:23034632). Binds both free and DNA-bound GLI1
CC (PubMed:10531011). Interacts with KIF7 (PubMed:19592253). Interacts
CC with GLI3FL and this interaction regulates the formation of either
CC repressor or activator forms of GLI3 (PubMed:20360384). Its association
CC with GLI3FL is regulated by Hh signaling and dissociation of the SUFU-
CC GLI3 interaction requires the presence of the ciliary motor KIF3A
CC (PubMed:20360384). {ECO:0000250|UniProtKB:Q9UMX1,
CC ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:11477086,
CC ECO:0000269|PubMed:11960000, ECO:0000269|PubMed:19592253,
CC ECO:0000269|PubMed:20360384, ECO:0000269|PubMed:23034632}.
CC -!- INTERACTION:
CC Q9Z0P7; P16110: Lgals3; NbExp=5; IntAct=EBI-3508336, EBI-3508325;
CC Q9Z0P7; O88907: Pias1; NbExp=3; IntAct=EBI-3508336, EBI-3508327;
CC Q9Z0P7; P50636: Rnf19a; NbExp=3; IntAct=EBI-3508336, EBI-3508340;
CC Q9Z0P7; O55128: Sap18; NbExp=6; IntAct=EBI-3508336, EBI-3508332;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10531011,
CC ECO:0000269|PubMed:16459298}. Nucleus {ECO:0000269|PubMed:10531011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Z0P7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0P7-2; Sequence=VSP_013281, VSP_013282;
CC Name=3;
CC IsoId=Q9Z0P7-3; Sequence=VSP_013282, VSP_013283;
CC Name=4; Synonyms=SU(FU)-XL;
CC IsoId=Q9Z0P7-4; Sequence=VSP_013282;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues.
CC {ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:11557033}.
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. Ubiquitination is
CC impaired by phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353.
CC {ECO:0000250|UniProtKB:Q9UMX1}.
CC -!- PTM: Phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353 prevents
CC ubiquitination by the SCF(FBXL17) complex.
CC {ECO:0000250|UniProtKB:Q9UMX1}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality at about 10.5 dpc
CC due to defects in neural tube closure, abnormal somites and abnormal
CC heart looping (PubMed:16155214, PubMed:16459298). Heterozygous mice are
CC born at the expected Mendelian rate and are fertile. After 1.5 years,
CC they develop a skin phenotype characterized by ventral alopecia,
CC increased pigmentation, with papules and nodules on paws and tail
CC (PubMed:16459298). {ECO:0000269|PubMed:16155214,
CC ECO:0000269|PubMed:16459298}.
CC -!- SIMILARITY: Belongs to the SUFU family. {ECO:0000305}.
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DR EMBL; AF134893; AAF61412.1; -; mRNA.
DR EMBL; AJ131692; CAB38081.1; -; mRNA.
DR EMBL; AJ308625; CAC34257.1; -; mRNA.
DR EMBL; AJ308626; CAC34258.1; -; mRNA.
DR EMBL; AJ308627; CAC34271.1; -; Genomic_DNA.
DR EMBL; AJ308628; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308629; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308630; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308632; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308634; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308635; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308633; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AJ308631; CAC34271.1; JOINED; Genomic_DNA.
DR EMBL; AK015885; BAB30017.1; -; mRNA.
DR EMBL; AK047603; BAC33095.1; -; mRNA.
DR EMBL; BC048168; AAH48168.1; -; mRNA.
DR EMBL; BC056997; AAH56997.1; -; mRNA.
DR CCDS; CCDS29879.1; -. [Q9Z0P7-1]
DR CCDS; CCDS38008.1; -. [Q9Z0P7-4]
DR RefSeq; NP_001020562.1; NM_001025391.2. [Q9Z0P7-1]
DR RefSeq; NP_056567.2; NM_015752.3. [Q9Z0P7-4]
DR AlphaFoldDB; Q9Z0P7; -.
DR SMR; Q9Z0P7; -.
DR BioGRID; 204881; 24.
DR ComplexPortal; CPX-147; GLI1-SUFU complex.
DR ComplexPortal; CPX-149; GLI2-SUFU complex.
DR ComplexPortal; CPX-151; GLI3-SUFU complex.
DR CORUM; Q9Z0P7; -.
DR IntAct; Q9Z0P7; 21.
DR STRING; 10090.ENSMUSP00000107498; -.
DR iPTMnet; Q9Z0P7; -.
DR PhosphoSitePlus; Q9Z0P7; -.
DR EPD; Q9Z0P7; -.
DR jPOST; Q9Z0P7; -.
DR MaxQB; Q9Z0P7; -.
DR PaxDb; Q9Z0P7; -.
DR PeptideAtlas; Q9Z0P7; -.
DR PRIDE; Q9Z0P7; -.
DR ProteomicsDB; 257101; -. [Q9Z0P7-1]
DR ProteomicsDB; 257102; -. [Q9Z0P7-2]
DR ProteomicsDB; 257103; -. [Q9Z0P7-3]
DR ProteomicsDB; 257104; -. [Q9Z0P7-4]
DR Antibodypedia; 1768; 298 antibodies from 38 providers.
DR DNASU; 24069; -.
DR Ensembl; ENSMUST00000039922; ENSMUSP00000049109; ENSMUSG00000025231. [Q9Z0P7-1]
DR Ensembl; ENSMUST00000111867; ENSMUSP00000107498; ENSMUSG00000025231. [Q9Z0P7-4]
DR GeneID; 24069; -.
DR KEGG; mmu:24069; -.
DR UCSC; uc008htn.2; mouse. [Q9Z0P7-2]
DR UCSC; uc008hto.2; mouse. [Q9Z0P7-3]
DR UCSC; uc008htq.2; mouse. [Q9Z0P7-1]
DR CTD; 51684; -.
DR MGI; MGI:1345643; Sufu.
DR VEuPathDB; HostDB:ENSMUSG00000025231; -.
DR eggNOG; ENOG502QT57; Eukaryota.
DR GeneTree; ENSGT00390000009747; -.
DR HOGENOM; CLU_033906_0_0_1; -.
DR InParanoid; Q9Z0P7; -.
DR OMA; LVPRMME; -.
DR PhylomeDB; Q9Z0P7; -.
DR TreeFam; TF324548; -.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 24069; 9 hits in 78 CRISPR screens.
DR ChiTaRS; Sufu; mouse.
DR PRO; PR:Q9Z0P7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z0P7; protein.
DR Bgee; ENSMUSG00000025231; Expressed in ear vesicle and 267 other tissues.
DR ExpressionAtlas; Q9Z0P7; baseline and differential.
DR Genevisible; Q9Z0P7; MM.
DR GO; GO:0005929; C:cilium; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1990788; C:GLI-SUFU complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IGI:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:1990787; P:negative regulation of hh target transcription factor activity; ISO:MGI.
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; IMP:MGI.
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; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IMP:MGI.
DR GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IMP:MGI.
DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR DisProt; DP01397; -.
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 Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..484
FT /note="Suppressor of fused homolog"
FT /id="PRO_0000072303"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..360
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT MOD_RES 303
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX1"
FT VAR_SEQ 62..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013281"
FT VAR_SEQ 252
FT /note="Q -> QQ (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10531011,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013282"
FT VAR_SEQ 433..484
FT /note="ILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH
FT -> VRRSLSSFSSSSCSSLAACPPLPHHPKDRPLWLPC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013283"
FT CONFLICT 79
FT /note="S -> C (in Ref. 1; AAF61412)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="L -> Q (in Ref. 1; AAF61412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53957 MW; 6ED5666BC4D4AFB5 CRC64;
MAELRPSVAP GPAAPPASGP SAPPAFASLF PPGLHAIYGE CRRLYPDQPN PLQVTAIVKY
WLGGPDPLDY VSMYRNMGSP SANIPEHWHY ISFGLSDLYG DNRVHEFTGT DGPSGFGFEL
TFRLKRETGE SAPPTWPAEL MQGLARYVFQ SENTFCSGDH VSWHSPLDNS ESRIQHMLLT
EDPQMQPVRT PFGVVTFLQI VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR
GETIFEIDPH LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDEEDSRS ICLGTQPRRL
SGKDTEQIRE TLRRGLEINS KPVLPPINSQ RQNGLTHDRA PSRKDSLGSD SSTAIIPHEL
IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI TGDMAITFVS TGVEGAFATE
EHPYAAHGPW LQILLTEEFV EKMLEDLEDL TSPEEFKLPK EYSWPEKKLK VSILPDVVFD
SPLH
