SMAD1_MOUSE
ID SMAD1_MOUSE Reviewed; 465 AA.
AC P70340; P70442; Q6GT95; Q9CYK6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Mothers against decapentaplegic homolog 1;
DE Short=MAD homolog 1;
DE Short=Mothers against DPP homolog 1;
DE AltName: Full=Dwarfin-A;
DE Short=Dwf-A;
DE AltName: Full=Mothers-against-DPP-related 1;
DE Short=Mad-related protein 1;
DE Short=mMad1;
DE AltName: Full=SMAD family member 1;
DE Short=SMAD 1;
DE Short=Smad1;
GN Name=Smad1; Synonyms=Madh1, Madr1;
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].
RC TISSUE=Embryo;
RX PubMed=8799132; DOI=10.1073/pnas.93.17.8940;
RA Yingling J.M., Das P., Savage C., Zhang M., Padgett R.W., Wang X.-F.;
RT "Mammalian dwarfins are phosphorylated in response to transforming growth
RT factor beta and are implicated in control of cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8940-8944(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic heart;
RX PubMed=9076678; DOI=10.1016/s0925-4773(96)00622-3;
RA Zhao G.-Q., Hogan B.L.M.;
RT "Evidence that Mothers-against-dpp-related 1 (Madr1) plays a role in the
RT initiation and maintenance of spermatogenesis in the mouse.";
RL Mech. Dev. 61:63-73(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11111041; DOI=10.1016/s0378-1119(00)00396-6;
RA Huang S., Flanders K.C., Roberts A.B.;
RT "Characterization of the mouse Smad1 gene and its expression pattern in
RT adult mouse tissues.";
RL Gene 258:43-53(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Oviduct;
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].
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 INTERACTION WITH HGS.
RX PubMed=11094085; DOI=10.1128/mcb.20.24.9346-9355.2000;
RA Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J.,
RA Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.;
RT "Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through
RT cooperation with SARA.";
RL Mol. Cell. Biol. 20:9346-9355(2000).
RN [7]
RP INTERACTION WITH ZNF8.
RX PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
RA Jiao K., Zhou Y., Hogan B.L.M.;
RT "Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
RT as a novel nuclear interaction partner of Smad1.";
RL Mol. Cell. Biol. 22:7633-7644(2002).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH SMAD4 AND YY1.
RX PubMed=15329343; DOI=10.1242/dev.01344;
RA Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
RT "SMAD-mediated modulation of YY1 activity regulates the BMP response and
RT cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
RT enhancer.";
RL Development 131:4709-4723(2004).
RN [9]
RP INTERACTION WITH ZC3H3.
RX PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
RA Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
RA Schellens A., Van de Putte T., Pype S., Huylebroeck D., Verschueren K.;
RT "Smicl is a novel Smad interacting protein and cleavage and polyadenylation
RT specificity factor associated protein.";
RL Genes Cells 10:897-906(2005).
RN [10]
RP INTERACTION WITH NANOG.
RX PubMed=16801560; DOI=10.1073/pnas.0506945103;
RA Suzuki A., Raya A., Kawakami Y., Morita M., Matsui T., Nakashima K.,
RA Gage F.H., Rodriguez-Esteban C., Izpisua Belmonte J.C.;
RT "Nanog binds to Smad1 and blocks bone morphogenetic protein-induced
RT differentiation of embryonic stem cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10294-10299(2006).
RN [11]
RP INTERACTION WITH ZCCHC12.
RX PubMed=18160706; DOI=10.1128/mcb.01038-07;
RA Cho G., Lim Y., Zand D., Golden J.A.;
RT "Sizn1 is a novel protein that functions as a transcriptional coactivator
RT of bone morphogenic protein signaling.";
RL Mol. Cell. Biol. 28:1565-1572(2008).
RN [12]
RP INTERACTION WITH TMEM119.
RX PubMed=21239498; DOI=10.1074/jbc.m110.179127;
RA Hisa I., Inoue Y., Hendy G.N., Canaff L., Kitazawa R., Kitazawa S.,
RA Komori T., Sugimoto T., Seino S., Kaji H.;
RT "Parathyroid hormone-responsive Smad3-related factor, Tmem119, promotes
RT osteoblast differentiation and interacts with the bone morphogenetic
RT protein-Runx2 pathway.";
RL J. Biol. Chem. 286:9787-9796(2011).
RN [13]
RP INTERACTION WITH RANBP3L, DEPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=25755279; DOI=10.1128/mcb.00121-15;
RA Chen F., Lin X., Xu P., Zhang Z., Chen Y., Wang C., Han J., Zhao B.,
RA Xiao M., Feng X.H.;
RT "Nuclear export of Smads by RanBP3L regulates bone morphogenetic protein
RT signaling and mesenchymal stem cell differentiation.";
RL Mol. Cell. Biol. 35:1700-1711(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 9-132 IN COMPLEX WITH DNA,
RP ZINC_BINDING SITES, AND SUBUNIT.
RX PubMed=20147459; DOI=10.1093/nar/gkq046;
RA Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S.,
RA Jauch R., Kolatkar P.R.;
RT "Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of
RT BMP and TGF-beta effectors.";
RL Nucleic Acids Res. 38:3477-3488(2010).
CC -!- FUNCTION: Transcriptional modulator activated by BMP (bone
CC morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-
CC regulated SMAD (R-SMAD) (By similarity). May play a role in the
CC initiation and maintenance of spermatogenesis. SMAD1/OAZ1/PSMB4 complex
CC mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By
CC similarity). May act synergistically with SMAD4 and YY1 in bone
CC morphogenetic protein (BMP)-mediated cardiac-specific gene expression
CC (PubMed:15329343). {ECO:0000250|UniProtKB:Q15797,
CC ECO:0000269|PubMed:15329343}.
CC -!- SUBUNIT: Upon C-terminus phosphorylation: forms trimers with another
CC SMAD1 and the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit, CREB-
CC binding protein (CBP), p300, SMURF1, SMURF2, USP15 and HOXC8.
CC Associates with ZNF423 or ZNF521 in response to BMP2 leading to
CC activate transcription of BMP target genes. Interacts with SKOR1.
CC Interacts (via MH2 domain) with LEMD3. Binding to LEMD3 results in at
CC least a partial reduction of receptor-mediated phosphorylation (By
CC similarity). Also interacts with HGS, NANOG and ZCCHC12. Forms a
CC ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into
CC the 20S proteasome (By similarity). Found in a complex with SMAD4 and
CC YY1. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a
CC SMAD4-independent manner. Interacts with ZC3H3 (PubMed:16115198).
CC Interacts with TMEM119 (PubMed:21239498). Interacts (via MH1 and MH2
CC domains) with ZNF8 (PubMed:12370310). Interacts with RANBP3L; the
CC interaction increases when SMAD1 is not phosphorylated and mediates
CC SMAD1 nuclear export (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797,
CC ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310,
CC ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:16115198,
CC ECO:0000269|PubMed:16801560, ECO:0000269|PubMed:18160706,
CC ECO:0000269|PubMed:20147459, ECO:0000269|PubMed:21239498,
CC ECO:0000269|PubMed:25755279}.
CC -!- INTERACTION:
CC P70340; Q62073: Map3k7; NbExp=3; IntAct=EBI-6992047, EBI-1775345;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25755279}. Nucleus
CC {ECO:0000269|PubMed:25755279}. Note=In the cytoplasm in the absence of
CC ligand. Migration to the nucleus when complexed with SMAD4. Colocalizes
CC with LEMD3 at the nucleus inner membrane. Exported from the nucleus to
CC the cytoplasm when dephosphorylated (PubMed:25755279).
CC {ECO:0000250|UniProtKB:Q15797, ECO:0000269|PubMed:25755279}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during embryogenesis.
CC Expression starts in some seminiferous tubules at 2 weeks of age. After
CC mid-puberty a stage-specific expression is established. During the
CC cycling of the seminiferous epithelium, expression initiates in the
CC pachytene spermatocytes of stage V seminiferous tubules, peaks at stage
CC X, then decreases as pachytene spermatocytes differentiate into
CC secondary spermatocytes and then round spermatids.
CC -!- DOMAIN: The MH2 domain mediates phosphorylation-dependent trimerization
CC through L3 loop binding of phosphoserines in the adjacent subunit.
CC {ECO:0000250|UniProtKB:Q15797}.
CC -!- PTM: Phosphorylation of the C-terminal SVS motif by BMP type 1 receptor
CC kinase activates SMAD1 by promoting dissociation from the receptor and
CC trimerization with SMAD4 (By similarity). Dephosphorylation, probably
CC by PPM1A, induces its export from the nucleus to the cytoplasm
CC (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797,
CC ECO:0000269|PubMed:25755279}.
CC -!- PTM: Ubiquitinated by SMAD-specific E3 ubiquitin ligase SMURF1, leading
CC to its degradation. Monoubiquitinated, leading to prevent DNA-binding.
CC Deubiquitination by USP15 alleviates inhibition and promotes activation
CC of TGF-beta target genes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; U58992; AAC52785.1; -; mRNA.
DR EMBL; U74359; AAB18256.1; -; mRNA.
DR EMBL; AF295768; AAG41407.1; -; Genomic_DNA.
DR EMBL; AF295763; AAG41407.1; JOINED; Genomic_DNA.
DR EMBL; AF295764; AAG41407.1; JOINED; Genomic_DNA.
DR EMBL; AF295765; AAG41407.1; JOINED; Genomic_DNA.
DR EMBL; AF295766; AAG41407.1; JOINED; Genomic_DNA.
DR EMBL; AF295767; AAG41407.1; JOINED; Genomic_DNA.
DR EMBL; AK017583; BAB30820.1; -; mRNA.
DR EMBL; AK054104; BAC35658.1; -; mRNA.
DR EMBL; BC058693; AAH58693.1; -; mRNA.
DR CCDS; CCDS22437.1; -.
DR RefSeq; NP_032565.2; NM_008539.3.
DR RefSeq; XP_006530809.1; XM_006530746.3.
DR PDB; 3KMP; X-ray; 2.70 A; A/B=9-132.
DR PDBsum; 3KMP; -.
DR AlphaFoldDB; P70340; -.
DR SMR; P70340; -.
DR BioGRID; 201274; 34.
DR ComplexPortal; CPX-145; SMAD1 homotrimer.
DR ComplexPortal; CPX-146; SMAD1-SMAD4 complex.
DR CORUM; P70340; -.
DR IntAct; P70340; 9.
DR MINT; P70340; -.
DR STRING; 10090.ENSMUSP00000071035; -.
DR ChEMBL; CHEMBL3883282; -.
DR iPTMnet; P70340; -.
DR PhosphoSitePlus; P70340; -.
DR EPD; P70340; -.
DR MaxQB; P70340; -.
DR PaxDb; P70340; -.
DR PeptideAtlas; P70340; -.
DR PRIDE; P70340; -.
DR ProteomicsDB; 261254; -.
DR Antibodypedia; 3950; 1394 antibodies from 43 providers.
DR DNASU; 17125; -.
DR Ensembl; ENSMUST00000066091; ENSMUSP00000071035; ENSMUSG00000031681.
DR GeneID; 17125; -.
DR KEGG; mmu:17125; -.
DR UCSC; uc009mip.2; mouse.
DR CTD; 4086; -.
DR MGI; MGI:109452; Smad1.
DR VEuPathDB; HostDB:ENSMUSG00000031681; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000154391; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; P70340; -.
DR OMA; GTPSKCV; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; P70340; -.
DR TreeFam; TF314923; -.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8941326; RUNX2 regulates bone development.
DR BioGRID-ORCS; 17125; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Smad1; mouse.
DR EvolutionaryTrace; P70340; -.
DR PRO; PR:P70340; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P70340; protein.
DR Bgee; ENSMUSG00000031681; Expressed in ileal epithelium and 296 other tissues.
DR ExpressionAtlas; P70340; baseline and differential.
DR Genevisible; P70340; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; ISO:MGI.
DR GO; GO:0071142; C:homomeric SMAD protein complex; IPI:ComplexPortal.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0060348; P:bone development; IGI:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IGI:BHF-UCL.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0042592; P:homeostatic process; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0001710; P:mesodermal cell fate commitment; IGI:MGI.
DR GO; GO:0030901; P:midbrain development; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0002051; P:osteoblast fate commitment; IGI:MGI.
DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IGI:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IGI:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..465
FT /note="Mothers against decapentaplegic homolog 1"
FT /id="PRO_0000090848"
FT DOMAIN 12..136
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 271..465
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 162..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..428
FT /note="L3 loop"
FT /evidence="ECO:0000250|UniProtKB:Q15797"
FT COMPBIAS 171..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15797"
FT MOD_RES 322
FT /note="Phosphothreonine; by MINK1, TNIK and MAP4K4"
FT /evidence="ECO:0000250|UniProtKB:Q15797"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15797,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15797,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT CONFLICT 95
FT /note="P -> S (in Ref. 1; AAC52785 and 3; AAG41407)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="R -> K (in Ref. 1; AAC52785 and 3; AAG41407)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..200
FT /note="SS -> QG (in Ref. 2; AAB18256)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> E (in Ref. 2; AAB18256)"
FT /evidence="ECO:0000305"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:3KMP"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:3KMP"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3KMP"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3KMP"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3KMP"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3KMP"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3KMP"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3KMP"
SQ SEQUENCE 465 AA; 52157 MW; 07A56FBEE79A1C2A CRC64;
MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE LEKALSCPGQ
PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH HELKPLECCE FPFGSKQKEV
CINPYHYKRV ESPVLPPVLV PRHSEYNPQH SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN
SHPFPHSPNS SYPNSPGGSS STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMAQDGSQ
PMDTNMMAPP LPAEISRGDV QAVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF ETVYELTKMC TIRMSFVKGW
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPHNP ISSVS
