MAN1_HUMAN
ID MAN1_HUMAN Reviewed; 911 AA.
AC Q9Y2U8; Q9NT47; Q9NYA5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Inner nuclear membrane protein Man1;
DE AltName: Full=LEM domain-containing protein 3;
GN Name=LEMD3; Synonyms=MAN1;
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 [GENOMIC DNA / MRNA].
RX PubMed=10671519; DOI=10.1074/jbc.275.7.4840;
RA Lin F., Blake D.L., Callebaut I., Skerjanc I.S., Holmer L., McBurney M.W.,
RA Paulin-Levasseur M., Worman H.J.;
RT "MAN1, an inner nuclear membrane protein that shares the LEM domain with
RT lamina-associated polypeptide 2 and emerin.";
RL J. Biol. Chem. 275:4840-4847(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-911.
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 [3]
RP INVOLVEMENT IN BOS.
RX PubMed=15489854; DOI=10.1038/ng1453;
RA Hellemans J., Preobrazhenska O., Willaert A., Debeer P., Verdonk P.C.M.,
RA Costa T., Janssens K., Menten B., Van Roy N., Vermeulen S.J.T.,
RA Savarirayan R., Van Hul W., Vanhoenacker F., Huylebroeck D., De Paepe A.,
RA Naeyaert J.-M., Vandesompele J., Speleman F., Verschueren K., Coucke P.J.,
RA Mortier G.R.;
RT "Loss-of-function mutations in LEMD3 result in osteopoikilosis, Buschke-
RT Ollendorff syndrome and melorheostosis.";
RL Nat. Genet. 36:1213-1218(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3.
RX PubMed=15601644; DOI=10.1093/hmg/ddi040;
RA Lin F., Morrison J.M., Wu W., Worman H.J.;
RT "MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and
RT Smad3 and antagonizes transforming growth factor-beta signaling.";
RL Hum. Mol. Genet. 14:437-445(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMAD1; SMAD2; SMAD3 AND
RP SMAD5, AND MUTAGENESIS OF 703-LEU-ILE-704 AND 835-TYR-VAL-836.
RX PubMed=15647271; DOI=10.1074/jbc.m411234200;
RA Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S.,
RA Luo K.;
RT "The integral inner nuclear membrane protein MAN1 physically interacts with
RT the R-Smad proteins to repress signaling by the transforming growth
RT factor-{beta} superfamily of cytokines.";
RL J. Biol. Chem. 280:15992-16001(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-187; SER-259;
RP SER-261; SER-280; SER-352; THR-365; SER-402; SER-777 AND SER-911, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-141; SER-144 AND
RP SER-261, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-187 AND THR-883, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-144; SER-187;
RP THR-209; SER-261; SER-402 AND THR-883, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP STRUCTURE BY NMR OF 655-775, AND DNA-BINDING.
RX PubMed=16648637; DOI=10.1074/jbc.m601980200;
RA Caputo S., Couprie J., Duband-Goulet I., Konde E., Lin F., Braud S.,
RA Gondry M., Gilquin B., Worman H.J., Zinn-Justin S.;
RT "The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding
RT winged helix domain.";
RL J. Biol. Chem. 281:18208-18215(2006).
RN [17]
RP VARIANTS BOS 655-ARG--SER-911 DEL AND 855-TRP--SER-911 DEL.
RX PubMed=19438932; DOI=10.1111/j.1399-0004.2009.01177.x;
RA Zhang Y., Castori M., Ferranti G., Paradisi M., Wordsworth B.P.;
RT "Novel and recurrent germline LEMD3 mutations causing Buschke-Ollendorff
RT syndrome and osteopoikilosis but not isolated melorheostosis.";
RL Clin. Genet. 75:556-561(2009).
RN [18]
RP ERRATUM OF PUBMED:19438932.
RA Zhang Y., Castori M., Ferranti G., Paradisi M., Wordsworth B.P.;
RL Clin. Genet. 79:401-401(2011).
CC -!- FUNCTION: Can function as a specific repressor of TGF-beta, activin,
CC and BMP signaling through its interaction with the R-SMAD proteins.
CC Antagonizes TGF-beta-induced cell proliferation arrest.
CC {ECO:0000269|PubMed:15601644, ECO:0000269|PubMed:15647271}.
CC -!- SUBUNIT: Interacts with SMAD1, SMAD2, SMAD3 and SMAD5. Binds to both
CC phosphorylated and unphosphorylated R-SMADS.
CC {ECO:0000269|PubMed:15601644, ECO:0000269|PubMed:15647271}.
CC -!- INTERACTION:
CC Q9Y2U8; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-2561428, EBI-712367;
CC Q9Y2U8; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-2561428, EBI-7545592;
CC Q9Y2U8; Q15797: SMAD1; NbExp=4; IntAct=EBI-2561428, EBI-1567153;
CC Q9Y2U8; O15198-2: SMAD9; NbExp=4; IntAct=EBI-2561428, EBI-12273450;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:15647271}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15647271}.
CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver and skeletal
CC muscle.
CC -!- DISEASE: Buschke-Ollendorff syndrome (BOS) [MIM:166700]: A disease
CC characterized by osteopoikilosis and disseminated connective-tissue
CC nevi. Osteopoikilosis is a skeletal dysplasia characterized by a
CC symmetric but unequal distribution of multiple hyperostotic areas in
CC different parts of the skeleton. Elastic-type nevi (juvenile elastoma)
CC and collagen-type nevi (dermatofibrosis lenticularis disseminata) have
CC been described in BOS. Skin or bony lesions can be absent in some
CC family members, whereas other relatives may have both.
CC {ECO:0000269|PubMed:15489854, ECO:0000269|PubMed:19438932}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AF112299; AAD31593.2; -; mRNA.
DR EMBL; AF263918; AAF73293.1; -; Genomic_DNA.
DR EMBL; AF180135; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180136; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180137; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180138; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180139; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180140; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180141; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AF180142; AAF73293.1; JOINED; Genomic_DNA.
DR EMBL; AL137533; CAB70796.1; ALT_SEQ; mRNA.
DR CCDS; CCDS8972.1; -.
DR PIR; T46377; T46377.
DR RefSeq; NP_001161086.1; NM_001167614.1.
DR RefSeq; NP_055134.2; NM_014319.4.
DR PDB; 2CH0; NMR; -; A=655-775.
DR PDB; 5ZOJ; X-ray; 2.79 A; D/E=762-890.
DR PDB; 5ZOK; X-ray; 2.85 A; B/D=762-890.
DR PDBsum; 2CH0; -.
DR PDBsum; 5ZOJ; -.
DR PDBsum; 5ZOK; -.
DR AlphaFoldDB; Q9Y2U8; -.
DR SMR; Q9Y2U8; -.
DR BioGRID; 117127; 247.
DR CORUM; Q9Y2U8; -.
DR IntAct; Q9Y2U8; 61.
DR MINT; Q9Y2U8; -.
DR STRING; 9606.ENSP00000308369; -.
DR GlyGen; Q9Y2U8; 1 site.
DR iPTMnet; Q9Y2U8; -.
DR PhosphoSitePlus; Q9Y2U8; -.
DR BioMuta; LEMD3; -.
DR DMDM; 13629600; -.
DR EPD; Q9Y2U8; -.
DR jPOST; Q9Y2U8; -.
DR MassIVE; Q9Y2U8; -.
DR MaxQB; Q9Y2U8; -.
DR PaxDb; Q9Y2U8; -.
DR PeptideAtlas; Q9Y2U8; -.
DR PRIDE; Q9Y2U8; -.
DR ProteomicsDB; 85904; -.
DR Antibodypedia; 29213; 159 antibodies from 22 providers.
DR DNASU; 23592; -.
DR Ensembl; ENST00000308330.3; ENSP00000308369.2; ENSG00000174106.3.
DR GeneID; 23592; -.
DR KEGG; hsa:23592; -.
DR MANE-Select; ENST00000308330.3; ENSP00000308369.2; NM_014319.5; NP_055134.2.
DR UCSC; uc001ssl.3; human.
DR CTD; 23592; -.
DR DisGeNET; 23592; -.
DR GeneCards; LEMD3; -.
DR HGNC; HGNC:28887; LEMD3.
DR HPA; ENSG00000174106; Low tissue specificity.
DR MalaCards; LEMD3; -.
DR MIM; 166700; phenotype.
DR MIM; 607844; gene.
DR neXtProt; NX_Q9Y2U8; -.
DR OpenTargets; ENSG00000174106; -.
DR Orphanet; 94063; 12q14 microdeletion syndrome.
DR Orphanet; 1306; Buschke-Ollendorff syndrome.
DR Orphanet; 166119; Isolated osteopoikilosis.
DR Orphanet; 1879; Melorheostosis with osteopoikilosis.
DR PharmGKB; PA134907442; -.
DR VEuPathDB; HostDB:ENSG00000174106; -.
DR eggNOG; KOG0147; Eukaryota.
DR GeneTree; ENSGT00940000157643; -.
DR HOGENOM; CLU_017040_0_0_1; -.
DR InParanoid; Q9Y2U8; -.
DR OMA; NAYSKPK; -.
DR OrthoDB; 817293at2759; -.
DR PhylomeDB; Q9Y2U8; -.
DR TreeFam; TF315385; -.
DR PathwayCommons; Q9Y2U8; -.
DR Reactome; R-HSA-2980766; Nuclear Envelope Breakdown.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q9Y2U8; -.
DR BioGRID-ORCS; 23592; 32 hits in 1094 CRISPR screens.
DR ChiTaRS; LEMD3; human.
DR EvolutionaryTrace; Q9Y2U8; -.
DR GenomeRNAi; 23592; -.
DR Pharos; Q9Y2U8; Tbio.
DR PRO; PR:Q9Y2U8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y2U8; protein.
DR Bgee; ENSG00000174106; Expressed in endothelial cell and 207 other tissues.
DR ExpressionAtlas; Q9Y2U8; baseline and differential.
DR Genevisible; Q9Y2U8; HS.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; IEA:InterPro.
DR CDD; cd12286; RRM_Man1; 1.
DR Gene3D; 1.10.10.1180; -; 1.
DR Gene3D; 1.10.720.40; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR InterPro; IPR034997; Man1.
DR InterPro; IPR034394; Man1_RRM.
DR InterPro; IPR041885; MAN1_winged_helix_dom.
DR InterPro; IPR018996; MSC.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR13428:SF10; PTHR13428:SF10; 1.
DR Pfam; PF03020; LEM; 1.
DR Pfam; PF09402; MSC; 1.
DR SMART; SM00540; LEM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; DNA-binding; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..911
FT /note="Inner nuclear membrane protein Man1"
FT /id="PRO_0000206149"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..50
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT DNA_BIND 707..726
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..911
FT /note="Interaction with SMAD1, SMAD2, SMAD3 and SMAD5"
FT /evidence="ECO:0000269|PubMed:15647271"
FT REGION 879..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 365
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 883
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 260
FT /note="D -> Y (in dbSNP:rs7487311)"
FT /id="VAR_034605"
FT VARIANT 655..911
FT /note="Missing (in BOS; patient does not show
FT osteopoikilosis)"
FT /evidence="ECO:0000269|PubMed:19438932"
FT /id="VAR_080412"
FT VARIANT 855..911
FT /note="Missing (in BOS)"
FT /evidence="ECO:0000269|PubMed:19438932"
FT /id="VAR_080413"
FT MUTAGEN 703..704
FT /note="LI->ED: Impairs binding to SMAD1. Loss of ability to
FT repress transcriptional activation in response to TGF-beta,
FT BMP2 and activin signaling."
FT /evidence="ECO:0000269|PubMed:15647271"
FT MUTAGEN 835..836
FT /note="YV->DD: Impairs binding to SMAD1."
FT /evidence="ECO:0000269|PubMed:15647271"
FT CONFLICT 508..509
FT /note="IE -> K (in Ref. 1; AAF73293)"
FT /evidence="ECO:0000305"
FT HELIX 659..663
FT /evidence="ECO:0007829|PDB:2CH0"
FT TURN 664..669
FT /evidence="ECO:0007829|PDB:2CH0"
FT HELIX 670..684
FT /evidence="ECO:0007829|PDB:2CH0"
FT HELIX 696..701
FT /evidence="ECO:0007829|PDB:2CH0"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:2CH0"
FT HELIX 713..723
FT /evidence="ECO:0007829|PDB:2CH0"
FT TURN 724..726
FT /evidence="ECO:0007829|PDB:2CH0"
FT STRAND 730..737
FT /evidence="ECO:0007829|PDB:2CH0"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:2CH0"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:2CH0"
FT STRAND 765..770
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT TURN 774..776
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT STRAND 784..791
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT HELIX 794..796
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT HELIX 803..813
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT TURN 814..816
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT STRAND 820..825
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT STRAND 834..840
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT HELIX 841..851
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT STRAND 859..865
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT HELIX 868..874
FT /evidence="ECO:0007829|PDB:5ZOJ"
FT HELIX 876..880
FT /evidence="ECO:0007829|PDB:5ZOJ"
SQ SEQUENCE 911 AA; 99997 MW; 21D1E6BB0D499131 CRC64;
MAAAAASAPQ QLSDEELFSQ LRRYGLSPGP VTESTRPVYL KKLKKLREEE QQQHRSGGRG
NKTRNSNNNN TAAATVAAAG PAAAAAAGMG VRPVSGDLSY LRTPGGLCRI SASGPESLLG
GPGGASAAPA AGSKVLLGFS SDESDVEASP RDQAGGGGRK DRASLQYRGL KAPPAPLAAS
EVTNSNSAER RKPHSWWGAR RPAGPELQTP PGKDGAVEDE EGEGEDGEER DPETEEPLWA
SRTVNGSRLV PYSCRENYSD SEEEDDDDVA SSRQVLKDDS LSRHRPRRTH SKPLPPLTAK
SAGGRLETSV QGGGGLAMND RAAAAGSLDR SRNLEEAAAA EQGGGCDQVD SSPVPRYRVN
AKKLTPLLPP PLTDMDSTLD SSTGSLLKTN NHIGGGAFSV DSPRIYSNSL PPSAAVAASS
SLRINHANHT GSNHTYLKNT YNKPKLSEPE EELLQQFKRE EVSPTGSFSA HYLSMFLLTA
ACLFFLILGL TYLGMRGTGV SEDGELSIEN PFGETFGKIQ ESEKTLMMNT LYKLHDRLAQ
LAGDHECGSS SQRTLSVQEA AAYLKDLGPE YEGIFNTSLQ WILENGKDVG IRCVGFGPEE
ELTNITDVQF LQSTRPLMSF WCRFRRAFVT VTHRLLLLCL GVVMVCVVLR YMKYRWTKEE
EETRQMYDMV VKIIDVLRSH NEACQENKDL QPYMPIPHVR DSLIQPHDRK KMKKVWDRAV
DFLAANESRV RTETRRIGGA DFLVWRWIQP SASCDKILVI PSKVWQGQAF HLDRRNSPPN
SLTPCLKIRN MFDPVMEIGD QWHLAIQEAI LEKCSDNDGI VHIAVDKNSR EGCVYVKCLS
PEYAGKAFKA LHGSWFDGKL VTVKYLRLDR YHHRFPQALT SNTPLKPSNK HMNSMSHLRL
RTGLTNSQGS S
