Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)

 SMAD1_MOUSE             Reviewed;         465 AA.
 P70340; P70442; Q6GT95; Q9CYK6;
 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
 27-JUL-2011, sequence version 2.
 02-DEC-2020, entry version 196.
 RecName: Full=Mothers against decapentaplegic homolog 1;
          Short=MAD homolog 1;
          Short=Mothers against DPP homolog 1;
 AltName: Full=Dwarfin-A;
          Short=Dwf-A;
 AltName: Full=Mothers-against-DPP-related 1;
          Short=Mad-related protein 1;
          Short=mMad1;
 AltName: Full=SMAD family member 1;
          Short=SMAD 1;
          Short=Smad1;
 Name=Smad1; Synonyms=Madh1, Madr1;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
 Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Embryo;
 PubMed=8799132; DOI=10.1073/pnas.93.17.8940;
 Yingling J.M., Das P., Savage C., Zhang M., Padgett R.W., Wang X.-F.;
 "Mammalian dwarfins are phosphorylated in response to transforming growth
 factor beta and are implicated in control of cell growth.";
 Proc. Natl. Acad. Sci. U.S.A. 93:8940-8944(1996).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Embryonic heart;
 PubMed=9076678; DOI=10.1016/s0925-4773(96)00622-3;
 Zhao G.-Q., Hogan B.L.M.;
 "Evidence that Mothers-against-dpp-related 1 (Madr1) plays a role in the
 initiation and maintenance of spermatogenesis in the mouse.";
 Mech. Dev. 61:63-73(1997).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=129/Sv;
 PubMed=11111041; DOI=10.1016/s0378-1119(00)00396-6;
 Huang S., Flanders K.C., Roberts A.B.;
 "Characterization of the mouse Smad1 gene and its expression pattern in
 adult mouse tissues.";
 Gene 258:43-53(2000).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=C57BL/6J; TISSUE=Embryo, and Oviduct;
 PubMed=16141072; DOI=10.1126/science.1112014;
 Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
 Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
 Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
 Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
 Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
 Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
 Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
 Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
 Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
 Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
 Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
 Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
 Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
 Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
 Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
 Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
 Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
 Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
 Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
 Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
 Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
 Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
 Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
 Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
 Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
 van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
 Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
 Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
 Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
 Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
 Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
 Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
 Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
 Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
 "The transcriptional landscape of the mammalian genome.";
 Science 309:1559-1563(2005).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=C57BL/6J; TISSUE=Brain;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [6]
 INTERACTION WITH HGS.
 PubMed=11094085; DOI=10.1128/mcb.20.24.9346-9355.2000;
 Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J.,
 Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.;
 "Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through
 cooperation with SARA.";
 Mol. Cell. Biol. 20:9346-9355(2000).
 [7]
 INTERACTION WITH ZNF8.
 PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
 Jiao K., Zhou Y., Hogan B.L.M.;
 "Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
 as a novel nuclear interaction partner of Smad1.";
 Mol. Cell. Biol. 22:7633-7644(2002).
 [8]
 FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH SMAD4 AND YY1.
 PubMed=15329343; DOI=10.1242/dev.01344;
 Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
 "SMAD-mediated modulation of YY1 activity regulates the BMP response and
 cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
 enhancer.";
 Development 131:4709-4723(2004).
 [9]
 INTERACTION WITH ZC3H3.
 PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
 Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
 Schellens A., Van de Putte T., Pype S., Huylebroeck D., Verschueren K.;
 "Smicl is a novel Smad interacting protein and cleavage and polyadenylation
 specificity factor associated protein.";
 Genes Cells 10:897-906(2005).
 [10]
 INTERACTION WITH NANOG.
 PubMed=16801560; DOI=10.1073/pnas.0506945103;
 Suzuki A., Raya A., Kawakami Y., Morita M., Matsui T., Nakashima K.,
 Gage F.H., Rodriguez-Esteban C., Izpisua Belmonte J.C.;
 "Nanog binds to Smad1 and blocks bone morphogenetic protein-induced
 differentiation of embryonic stem cells.";
 Proc. Natl. Acad. Sci. U.S.A. 103:10294-10299(2006).
 [11]
 INTERACTION WITH ZCCHC12.
 PubMed=18160706; DOI=10.1128/mcb.01038-07;
 Cho G., Lim Y., Zand D., Golden J.A.;
 "Sizn1 is a novel protein that functions as a transcriptional coactivator
 of bone morphogenic protein signaling.";
 Mol. Cell. Biol. 28:1565-1572(2008).
 [12]
 INTERACTION WITH TMEM119.
 PubMed=21239498; DOI=10.1074/jbc.m110.179127;
 Hisa I., Inoue Y., Hendy G.N., Canaff L., Kitazawa R., Kitazawa S.,
 Komori T., Sugimoto T., Seino S., Kaji H.;
 "Parathyroid hormone-responsive Smad3-related factor, Tmem119, promotes
 osteoblast differentiation and interacts with the bone morphogenetic
 protein-Runx2 pathway.";
 J. Biol. Chem. 286:9787-9796(2011).
 [13]
 INTERACTION WITH RANBP3L, DEPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
 PubMed=25755279; DOI=10.1128/mcb.00121-15;
 Chen F., Lin X., Xu P., Zhang Z., Chen Y., Wang C., Han J., Zhao B.,
 Xiao M., Feng X.H.;
 "Nuclear export of Smads by RanBP3L regulates bone morphogenetic protein
 signaling and mesenchymal stem cell differentiation.";
 Mol. Cell. Biol. 35:1700-1711(2015).
 [14]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 9-132 IN COMPLEX WITH DNA,
 ZINC_BINDING SITES, AND SUBUNIT.
 PubMed=20147459; DOI=10.1093/nar/gkq046;
 Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S.,
 Jauch R., Kolatkar P.R.;
 "Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of
 BMP and TGF-beta effectors.";
 Nucleic Acids Res. 38:3477-3488(2010).
 -!- FUNCTION: Transcriptional modulator activated by BMP (bone
     morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-
     regulated SMAD (R-SMAD) (By similarity). May play a role in the
     initiation and maintenance of spermatogenesis. SMAD1/OAZ1/PSMB4 complex
     mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By
     similarity). May act synergistically with SMAD4 and YY1 in bone
     morphogenetic protein (BMP)-mediated cardiac-specific gene expression
     (PubMed:15329343). {ECO:0000250|UniProtKB:Q15797,
     ECO:0000269|PubMed:15329343}.
 -!- SUBUNIT: Upon C-terminus phosphorylation: forms trimers with another
     SMAD1 and the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit, CREB-
     binding protein (CBP), p300, SMURF1, SMURF2, USP15 and HOXC8.
     Associates with ZNF423 or ZNF521 in response to BMP2 leading to
     activate transcription of BMP target genes. Interacts with SKOR1.
     Interacts (via MH2 domain) with LEMD3. Binding to LEMD3 results in at
     least a partial reduction of receptor-mediated phosphorylation (By
     similarity). Also interacts with HGS, NANOG and ZCCHC12. Forms a
     ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into
     the 20S proteasome (By similarity). Found in a complex with SMAD4 and
     YY1. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a
     SMAD4-independent manner. Interacts with ZC3H3 (PubMed:16115198).
     Interacts with TMEM119 (PubMed:21239498). Interacts (via MH1 and MH2
     domains) with ZNF8 (PubMed:12370310). Interacts with RANBP3L; the
     interaction increases when SMAD1 is not phosphorylated and mediates
     SMAD1 nuclear export (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797,
     ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310,
     ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:16115198,
     ECO:0000269|PubMed:16801560, ECO:0000269|PubMed:18160706,
     ECO:0000269|PubMed:20147459, ECO:0000269|PubMed:21239498,
     ECO:0000269|PubMed:25755279}.
 -!- INTERACTION:
     P70340; Q62073: Map3k7; NbExp=3; IntAct=EBI-6992047, EBI-1775345;
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25755279}. Nucleus
     {ECO:0000269|PubMed:25755279}. Note=In the cytoplasm in the absence of
     ligand. Migration to the nucleus when complexed with SMAD4. Colocalizes
     with LEMD3 at the nucleus inner membrane. Exported from the nucleus to
     the cytoplasm when dephosphorylated (PubMed:25755279).
     {ECO:0000250|UniProtKB:Q15797, ECO:0000269|PubMed:25755279}.
 -!- TISSUE SPECIFICITY: Ubiquitous.
 -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during embryogenesis.
     Expression starts in some seminiferous tubules at 2 weeks of age. After
     mid-puberty a stage-specific expression is established. During the
     cycling of the seminiferous epithelium, expression initiates in the
     pachytene spermatocytes of stage V seminiferous tubules, peaks at stage
     X, then decreases as pachytene spermatocytes differentiate into
     secondary spermatocytes and then round spermatids.
 -!- DOMAIN: The MH2 domain mediates phosphorylation-dependent trimerization
     through L3 loop binding of phosphoserines in the adjacent subunit.
     {ECO:0000250|UniProtKB:Q15797}.
 -!- PTM: Phosphorylation of the C-terminal SVS motif by BMP type 1 receptor
     kinase activates SMAD1 by promoting dissociation from the receptor and
     trimerization with SMAD4 (By similarity). Dephosphorylation, probably
     by PPM1A, induces its export from the nucleus to the cytoplasm
     (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797,
     ECO:0000269|PubMed:25755279}.
 -!- PTM: Ubiquitinated by SMAD-specific E3 ubiquitin ligase SMURF1, leading
     to its degradation. Monoubiquitinated, leading to prevent DNA-binding.
     Deubiquitination by USP15 alleviates inhibition and promotes activation
     of TGF-beta target genes (By similarity). {ECO:0000250}.
 -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
 ---------------------------------------------------------------------------
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 EMBL; U58992; AAC52785.1; -; mRNA.
 EMBL; U74359; AAB18256.1; -; mRNA.
 EMBL; AF295768; AAG41407.1; -; Genomic_DNA.
 EMBL; AF295763; AAG41407.1; JOINED; Genomic_DNA.
 EMBL; AF295764; AAG41407.1; JOINED; Genomic_DNA.
 EMBL; AF295765; AAG41407.1; JOINED; Genomic_DNA.
 EMBL; AF295766; AAG41407.1; JOINED; Genomic_DNA.
 EMBL; AF295767; AAG41407.1; JOINED; Genomic_DNA.
 EMBL; AK017583; BAB30820.1; -; mRNA.
 EMBL; AK054104; BAC35658.1; -; mRNA.
 EMBL; BC058693; AAH58693.1; -; mRNA.
 CCDS; CCDS22437.1; -.
 RefSeq; NP_032565.2; NM_008539.3.
 RefSeq; XP_006530809.1; XM_006530746.3.
 PDB; 3KMP; X-ray; 2.70 A; A/B=9-132.
 PDBsum; 3KMP; -.
 SMR; P70340; -.
 BioGRID; 201274; 34.
 ComplexPortal; CPX-145; SMAD1 homotrimer.
 ComplexPortal; CPX-146; SMAD1-SMAD4 complex.
 CORUM; P70340; -.
 IntAct; P70340; 9.
 MINT; P70340; -.
 STRING; 10090.ENSMUSP00000071035; -.
 ChEMBL; CHEMBL3883282; -.
 iPTMnet; P70340; -.
 PhosphoSitePlus; P70340; -.
 EPD; P70340; -.
 MaxQB; P70340; -.
 PaxDb; P70340; -.
 PeptideAtlas; P70340; -.
 PRIDE; P70340; -.
 Antibodypedia; 3950; 1300 antibodies.
 Ensembl; ENSMUST00000066091; ENSMUSP00000071035; ENSMUSG00000031681.
 GeneID; 17125; -.
 KEGG; mmu:17125; -.
 UCSC; uc009mip.2; mouse.
 CTD; 4086; -.
 MGI; MGI:109452; Smad1.
 eggNOG; KOG3701; Eukaryota.
 GeneTree; ENSGT00940000154391; -.
 HOGENOM; CLU_026736_0_2_1; -.
 InParanoid; P70340; -.
 OMA; EVFHCNS; -.
 OrthoDB; 608001at2759; -.
 TreeFam; TF314923; -.
 Reactome; R-MMU-201451; Signaling by BMP.
 Reactome; R-MMU-5689880; Ub-specific processing proteases.
 Reactome; R-MMU-8941326; RUNX2 regulates bone development.
 BioGRID-ORCS; 17125; 2 hits in 19 CRISPR screens.
 ChiTaRS; Smad1; mouse.
 EvolutionaryTrace; P70340; -.
 PRO; PR:P70340; -.
 Proteomes; UP000000589; Chromosome 8.
 RNAct; P70340; protein.
 Bgee; ENSMUSG00000031681; Expressed in pineal body and 342 other tissues.
 ExpressionAtlas; P70340; baseline and differential.
 Genevisible; P70340; MM.
 GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
 GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0032991; C:protein-containing complex; ISO:MGI.
 GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
 GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
 GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
 GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
 GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
 GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
 GO; GO:0042802; F:identical protein binding; IPI:MGI.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
 GO; GO:0019901; F:protein kinase binding; ISO:MGI.
 GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
 GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
 GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
 GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
 GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
 GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
 GO; GO:0060348; P:bone development; IGI:MGI.
 GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
 GO; GO:0051216; P:cartilage development; IGI:MGI.
 GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
 GO; GO:0071773; P:cellular response to BMP stimulus; IGI:BHF-UCL.
 GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
 GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
 GO; GO:0007276; P:gamete generation; IMP:MGI.
 GO; GO:0030902; P:hindbrain development; IMP:MGI.
 GO; GO:0042592; P:homeostatic process; IMP:MGI.
 GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
 GO; GO:0000165; P:MAPK cascade; IMP:MGI.
 GO; GO:0001710; P:mesodermal cell fate commitment; IGI:MGI.
 GO; GO:0030901; P:midbrain development; IMP:MGI.
 GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
 GO; GO:0002051; P:osteoblast fate commitment; IGI:MGI.
 GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
 GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
 GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
 GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
 GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IMP:BHF-UCL.
 GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
 GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IGI:BHF-UCL.
 GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
 GO; GO:0042493; P:response to drug; ISO:MGI.
 GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
 GO; GO:0060395; P:SMAD protein signal transduction; IGI:BHF-UCL.
 GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
 GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
 Gene3D; 2.60.200.10; -; 1.
 Gene3D; 3.90.520.10; -; 1.
 InterPro; IPR013790; Dwarfin.
 InterPro; IPR003619; MAD_homology1_Dwarfin-type.
 InterPro; IPR013019; MAD_homology_MH1.
 InterPro; IPR017855; SMAD-like_dom_sf.
 InterPro; IPR001132; SMAD_dom_Dwarfin-type.
 InterPro; IPR008984; SMAD_FHA_dom_sf.
 InterPro; IPR036578; SMAD_MH1_sf.
 PANTHER; PTHR13703; PTHR13703; 1.
 Pfam; PF03165; MH1; 1.
 Pfam; PF03166; MH2; 1.
 SMART; SM00523; DWA; 1.
 SMART; SM00524; DWB; 1.
 SUPFAM; SSF49879; SSF49879; 1.
 SUPFAM; SSF56366; SSF56366; 1.
 PROSITE; PS51075; MH1; 1.
 PROSITE; PS51076; MH2; 1.
 1: Evidence at protein level;
 3D-structure; Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
 Phosphoprotein; Reference proteome; Transcription;
 Transcription regulation; Ubl conjugation; Zinc.
 CHAIN           1..465
                 /note="Mothers against decapentaplegic homolog 1"
                 /id="PRO_0000090848"
 DOMAIN          12..136
                 /note="MH1"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
 DOMAIN          271..465
                 /note="MH2"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
 REGION          418..428
                 /note="L3 loop"
                 /evidence="ECO:0000250|UniProtKB:Q15797"
 COMPBIAS        39..45
                 /note="Poly-Lys"
 METAL           64
                 /note="Zinc"
 METAL           109
                 /note="Zinc"
 METAL           121
                 /note="Zinc"
 METAL           126
                 /note="Zinc"
 MOD_RES         1
                 /note="N-acetylmethionine"
                 /evidence="ECO:0000250|UniProtKB:Q15797"
 MOD_RES         322
                 /note="Phosphothreonine; by MINK1, TNIK and MAP4K4"
                 /evidence="ECO:0000250|UniProtKB:Q15797"
 MOD_RES         463
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q15797,
                 ECO:0000255|PROSITE-ProRule:PRU00439"
 MOD_RES         465
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q15797,
                 ECO:0000255|PROSITE-ProRule:PRU00439"
 CONFLICT        95
                 /note="P -> S (in Ref. 1; AAC52785 and 3; AAG41407)"
                 /evidence="ECO:0000305"
 CONFLICT        142
                 /note="R -> K (in Ref. 1; AAC52785 and 3; AAG41407)"
                 /evidence="ECO:0000305"
 CONFLICT        199..200
                 /note="SS -> QG (in Ref. 2; AAB18256)"
                 /evidence="ECO:0000305"
 CONFLICT        393
                 /note="A -> E (in Ref. 2; AAB18256)"
                 /evidence="ECO:0000305"
 HELIX           12..19
                 /evidence="ECO:0000244|PDB:3KMP"
 HELIX           25..41
                 /evidence="ECO:0000244|PDB:3KMP"
 HELIX           47..56
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          66..68
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          71..73
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          75..77
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          80..82
                 /evidence="ECO:0000244|PDB:3KMP"
 HELIX           84..92
                 /evidence="ECO:0000244|PDB:3KMP"
 HELIX           100..102
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          103..105
                 /evidence="ECO:0000244|PDB:3KMP"
 HELIX           113..115
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          118..121
                 /evidence="ECO:0000244|PDB:3KMP"
 HELIX           124..126
                 /evidence="ECO:0000244|PDB:3KMP"
 STRAND          127..129
                 /evidence="ECO:0000244|PDB:3KMP"
 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

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