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Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)

 SMAD1_HUMAN             Reviewed;         465 AA.
Q15797; A8KAJ0; D3DNZ9; Q16636; Q9UFT8;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-APR-2020, entry version 219.
RecName: Full=Mothers against decapentaplegic homolog 1;
Short=MAD homolog 1;
Short=Mothers against DPP homolog 1;
AltName: Full=JV4-1;
AltName: Full=Mad-related protein 1;
AltName: Full=SMAD family member 1;
Short=SMAD 1;
Short=Smad1;
Short=hSMAD1;
AltName: Full=Transforming growth factor-beta-signaling protein 1;
Short=BSP-1;
Name=SMAD1; Synonyms=BSP1, MADH1, MADR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8673135; DOI=10.1038/ng0796-347;
Riggins G.J., Thiagalingam S., Rosenblum E., Weinstein C.L., Kern S.E.,
Hamilton S.R., Willson J.K.V., Markowitz S.D., Kinzler K.W.,
Vogelstein B.V.;
"Mad-related genes in the human.";
Nat. Genet. 13:347-349(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=8637600; DOI=10.1038/381620a0;
Liu F., Hata A., Baker J.C., Doody J., Carcamo J., Harland R.M.,
Massague J.;
"A human Mad protein acting as a BMP-regulated transcriptional activator.";
Nature 381:620-623(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF GLY-419.
PubMed=8653785; DOI=10.1016/s0092-8674(00)81250-7;
Hoodless P.A., Haerry T., Abdollah S., Stapleton M., O'Connor M.B.,
Attisano L., Wrana J.L.;
"MADR1, a MAD-related protein that functions in BMP2 signaling pathways.";
Cell 85:489-500(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary carcinoma;
PubMed=8663601; DOI=10.1074/jbc.271.30.17617;
Lechleider R.J., de Caestecker M.P., Dehejia A., Polymeropoulos M.H.,
Roberts A.B.;
"Serine phosphorylation, chromosomal localization, and transforming growth
factor-beta signal transduction by human bsp-1.";
J. Biol. Chem. 271:17617-17620(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8774881; DOI=10.1038/383168a0;
Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.;
"Receptor-associated Mad homologues synergize as effectors of the TGF-beta
response.";
Nature 383:168-172(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[11]
PROTEIN SEQUENCE OF 1-15; 33-39; 129-157; 283-306 AND 309-319, ACETYLATION
AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lempens A., Norman J.C.;
Submitted (OCT-2009) to UniProtKB.
[12]
PHOSPHORYLATION AT SER-463 AND SER-465.
PubMed=9136927; DOI=10.1101/gad.11.8.984;
Kretzschmar M., Liu F., Hata A., Doody J., Massague J.;
"The TGF-beta family mediator Smad1 is phosphorylated directly and
activated functionally by the BMP receptor kinase.";
Genes Dev. 11:984-995(1997).
[13]
REVIEW.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[14]
REVIEW.
PubMed=10647776; DOI=10.1016/s1359-6101(99)00012-x;
Verschueren K., Huylebroeck D.;
"Remarkable versatility of Smad proteins in the nucleus of transforming
growth factor-beta activated cells.";
Cytokine Growth Factor Rev. 10:187-199(1999).
[15]
INTERACTION WITH ZNF423.
PubMed=10660046; DOI=10.1016/s0092-8674(00)81561-5;
Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A.,
Massague J.;
"OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-
Smad and Olf signaling pathways.";
Cell 100:229-240(2000).
[16]
REVIEW.
PubMed=10708948; DOI=10.1016/s1359-6101(99)00024-6;
Wrana J.L., Attisano L.;
"The Smad pathway.";
Cytokine Growth Factor Rev. 11:5-13(2000).
[17]
REVIEW.
PubMed=10708949; DOI=10.1016/s1359-6101(99)00025-8;
Miyazono K.;
"TGF-beta signaling by Smad proteins.";
Cytokine Growth Factor Rev. 11:15-22(2000).
[18]
IDENTIFICATION IN A COMPLEX WITH PSMB4 AND OAZ1, AND FUNCTION.
PubMed=12097147; DOI=10.1186/1471-2121-3-15;
Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y.,
Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.;
"A novel link between the proteasome pathway and the signal transduction
pathway of the bone morphogenetic proteins (BMPs).";
BMC Cell Biol. 3:15-15(2002).
[19]
INTERACTION WITH ZNF521.
PubMed=14630787; DOI=10.1182/blood-2003-07-2388;
Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N.,
De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M.,
Morrone G., Venuta S.;
"Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse
Evi3, is highly expressed in primitive human hematopoietic cells.";
Blood 103:2062-2070(2004).
[20]
SUBCELLULAR LOCATION, AND INTERACTION WITH LEMD3.
PubMed=15647271; DOI=10.1074/jbc.m411234200;
Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S.,
Luo K.;
"The integral inner nuclear membrane protein MAN1 physically interacts with
the R-Smad proteins to repress signaling by the transforming growth
factor-{beta} superfamily of cytokines.";
J. Biol. Chem. 280:15992-16001(2005).
[21]
INTERACTION WITH SKOR1.
PubMed=17292623; DOI=10.1016/j.mcn.2007.01.002;
Arndt S., Poser I., Moser M., Bosserhoff A.-K.;
"Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling.";
Mol. Cell. Neurosci. 34:603-611(2007).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION AT THR-322.
PubMed=21690388; DOI=10.1073/pnas.1104128108;
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K.,
Mao J., Ip Y.T., Xu L.;
"Smad inhibition by the Ste20 kinase Misshapen.";
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011).
[24]
UBIQUITINATION, DEUBIQUITINATION BY USP15, DNA-BINDING, AND INTERACTION
WITH USP15.
PubMed=21947082; DOI=10.1038/ncb2346;
Inui M., Manfrin A., Mamidi A., Martello G., Morsut L., Soligo S., Enzo E.,
Moro S., Polo S., Dupont S., Cordenonsi M., Piccolo S.;
"USP15 is a deubiquitylating enzyme for receptor-activated SMADs.";
Nat. Cell Biol. 13:1368-1375(2011).
[25]
SUBCELLULAR LOCATION.
PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
"Protein phosphatase 5 modulates SMAD3 function in the transforming growth
factor-beta pathway.";
Cell. Signal. 24:1999-2006(2012).
[26]
POSSIBLE INVOLVEMENT IN PULMONARY HYPERTENSION, VARIANT ALA-3, AND
CHARACTERIZATION OF VARIANT ALA-3.
PubMed=21898662; DOI=10.1002/humu.21605;
Nasim M.T., Ogo T., Ahmed M., Randall R., Chowdhury H.M., Snape K.M.,
Bradshaw T.Y., Southgate L., Lee G.J., Jackson I., Lord G.M., Gibbs J.S.,
Wilkins M.R., Ohta-Ogo K., Nakamura K., Girerd B., Coulet F., Soubrier F.,
Humbert M., Morrell N.W., Trembath R.C., Machado R.D.;
"Molecular genetic characterization of SMAD signaling molecules in
pulmonary arterial hypertension.";
Hum. Mutat. 32:1385-1389(2011).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[28]
INTERACTION WITH FAM83G.
PubMed=24554596; DOI=10.1098/rsob.130210;
Vogt J., Dingwell K.S., Herhaus L., Gourlay R., Macartney T., Campbell D.,
Smith J.C., Sapkota G.P.;
"Protein associated with SMAD1 (PAWS1/FAM83G) is a substrate for type I
bone morphogenetic protein receptors and modulates bone morphogenetic
protein signalling.";
Open Biol. 4:130210-130210(2014).
[29]
INTERACTION WITH RANBP3L, AND MUTAGENESIS OF 463-SER--SER-465.
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).
[30]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 248-465, PHOSPHORYLATION AT
SER-463 AND SER-465, SUBUNIT, AND MUTAGENESIS OF ASP-297; VAL-317; LYS-373;
LYS-418; TYR-424; ARG-426 AND ASP-448.
PubMed=11779505; DOI=10.1016/s1097-2765(01)00417-8;
Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K.;
"Structural basis of Smad1 activation by receptor kinase phosphorylation.";
Mol. Cell 8:1303-1312(2001).
-!- FUNCTION: Transcriptional modulator activated by BMP (bone
morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-
regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the
degradation of the CREBBP/EP300 repressor SNIP1. May act
synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-
mediated cardiac-specific gene expression.
{ECO:0000269|PubMed:12097147}.
-!- SUBUNIT: Found in a complex with SMAD4 and YY1. Interacts with HGS,
NANOG and ZCCHC12 (By similarity). 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.
Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is
incorporated into the 20S proteasome. Found in a macromolecular complex
with FAM83G. Interacts (via MH2 domain) with FAM83G (via MH2 domain);
in a SMAD4-independent manner. Interacts with ZC3H3 (By similarity).
Interacts with TMEM119 (By similarity). Interacts (via MH1 and MH2
domains) with ZNF8 (By similarity). Interacts with RANBP3L; the
interaction increases when SMAD1 is not phosphorylated and mediates
SMAD1 nuclear export (PubMed:25755279). {ECO:0000250|UniProtKB:P70340,
ECO:0000269|PubMed:10660046, ECO:0000269|PubMed:11779505,
ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:14630787,
ECO:0000269|PubMed:15647271, ECO:0000269|PubMed:17292623,
ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:24554596,
ECO:0000269|PubMed:25755279}.
-!- INTERACTION:
Q15797; Q15797; NbExp=5; IntAct=EBI-1567153, EBI-1567153;
Q15797; P10275: AR; NbExp=6; IntAct=EBI-1567153, EBI-608057;
Q15797; Q9GZU7: CTDSP1; NbExp=2; IntAct=EBI-1567153, EBI-751587;
Q15797; O14595: CTDSP2; NbExp=2; IntAct=EBI-1567153, EBI-2802973;
Q15797; O15194: CTDSPL; NbExp=2; IntAct=EBI-1567153, EBI-12544034;
Q15797; P17844: DDX5; NbExp=4; IntAct=EBI-1567153, EBI-351962;
Q15797; Q9NRR4: DROSHA; NbExp=3; IntAct=EBI-1567153, EBI-528367;
Q15797; O95208-2: EPN2; NbExp=3; IntAct=EBI-1567153, EBI-12135243;
Q15797; P49841: GSK3B; NbExp=2; IntAct=EBI-1567153, EBI-373586;
Q15797; O15397: IPO8; NbExp=2; IntAct=EBI-1567153, EBI-358808;
Q15797; Q9Y2U8: LEMD3; NbExp=4; IntAct=EBI-1567153, EBI-2561428;
Q15797; P28070: PSMB4; NbExp=4; IntAct=EBI-1567153, EBI-603350;
Q15797; Q13485: SMAD4; NbExp=12; IntAct=EBI-1567153, EBI-347263;
Q15797; O43541: SMAD6; NbExp=4; IntAct=EBI-1567153, EBI-976374;
Q15797; Q9HCE7: SMURF1; NbExp=2; IntAct=EBI-1567153, EBI-976466;
Q15797; Q9HCE7-2: SMURF1; NbExp=2; IntAct=EBI-1567153, EBI-9845742;
Q15797; Q9HAU4: SMURF2; NbExp=6; IntAct=EBI-1567153, EBI-396727;
Q15797; P15374: UCHL3; NbExp=2; IntAct=EBI-1567153, EBI-954554;
Q15797; P46937: YAP1; NbExp=3; IntAct=EBI-1567153, EBI-1044059;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15647271}. Nucleus
{ECO:0000269|PubMed:15647271, ECO:0000269|PubMed:22781750}.
Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when
complexed with SMAD4 (PubMed:15647271). Co-localizes with LEMD3 at the
nucleus inner membrane (PubMed:15647271). Exported from the nucleus to
the cytoplasm when dephosphorylated (By similarity).
{ECO:0000250|UniProtKB:P70340, ECO:0000269|PubMed:15647271}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15797-1; Sequence=Displayed;
Name=2;
IsoId=Q15797-2; Sequence=VSP_057163, VSP_057164, VSP_057165,
VSP_057166;
-!- TISSUE SPECIFICITY: Ubiquitous. Highest expression seen in the heart
and skeletal muscle.
-!- DOMAIN: The MH2 domain mediates phosphorylation-dependent trimerization
through L3 loop binding of phosphoserines in the adjacent subunit.
{ECO:0000269|PubMed:11779505}.
-!- 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. {ECO:0000269|PubMed:11779505,
ECO:0000269|PubMed:21690388, ECO:0000269|PubMed:9136927}.
-!- 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. Dephosphorylation, probably by PPM1A, induces
its export from the nucleus to the cytoplasm (By similarity).
{ECO:0000250|UniProtKB:P70340, ECO:0000269|PubMed:21947082}.
-!- DISEASE: Note=SMAD1 variants may be associated with susceptibility to
pulmonary hypertension, a disorder characterized by plexiform lesions
of proliferating endothelial cells in pulmonary arterioles. The lesions
lead to elevated pulmonary arterial pression, right ventricular
failure, and death. The disease can occur from infancy throughout life
and it has a mean age at onset of 36 years. Penetrance is reduced.
Although familial pulmonary hypertension is rare, cases secondary to
known etiologies are more common and include those associated with the
appetite-suppressant drugs. {ECO:0000269|PubMed:21898662}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U59912; AAC50790.1; -; mRNA.
EMBL; U59423; AAB06852.1; -; mRNA.
EMBL; U54826; AAC50493.1; -; mRNA.
EMBL; U57456; AAC50621.1; -; mRNA.
EMBL; BT007386; AAP36050.1; -; mRNA.
EMBL; AK293055; BAF85744.1; -; mRNA.
EMBL; AL117396; CAB55898.1; -; Genomic_DNA.
EMBL; CH471056; EAX05037.1; -; Genomic_DNA.
EMBL; CH471056; EAX05038.1; -; Genomic_DNA.
EMBL; CH471056; EAX05039.1; -; Genomic_DNA.
EMBL; CH471056; EAX05040.1; -; Genomic_DNA.
EMBL; BC001878; AAH01878.1; -; mRNA.
CCDS; CCDS3765.1; -. [Q15797-1]
PIR; S68987; S68987.
RefSeq; NP_001003688.1; NM_001003688.1. [Q15797-1]
RefSeq; NP_005891.1; NM_005900.2. [Q15797-1]
RefSeq; XP_005263049.1; XM_005262992.3.
RefSeq; XP_006714280.1; XM_006714217.2.
RefSeq; XP_011530263.1; XM_011531961.1.
RefSeq; XP_011530264.1; XM_011531962.1. [Q15797-1]
RefSeq; XP_011530265.1; XM_011531963.1.
RefSeq; XP_011530266.1; XM_011531964.1. [Q15797-1]
PDB; 1KHU; X-ray; 2.50 A; A/B/C/D=248-465.
PDB; 2LAW; NMR; -; B=222-233.
PDB; 2LAX; NMR; -; B=201-209.
PDB; 2LAY; NMR; -; B=201-209.
PDB; 2LAZ; NMR; -; B=210-217.
PDB; 2LB0; NMR; -; B=208-217.
PDB; 2LB1; NMR; -; B=220-233.
PDB; 3Q47; X-ray; 1.70 A; C=456-464.
PDB; 3Q4A; X-ray; 1.54 A; C=456-465.
PDB; 5ZOK; X-ray; 2.85 A; A/C=259-462.
PDBsum; 1KHU; -.
PDBsum; 2LAW; -.
PDBsum; 2LAX; -.
PDBsum; 2LAY; -.
PDBsum; 2LAZ; -.
PDBsum; 2LB0; -.
PDBsum; 2LB1; -.
PDBsum; 3Q47; -.
PDBsum; 3Q4A; -.
PDBsum; 5ZOK; -.
SMR; Q15797; -.
BioGrid; 110261; 126.
ComplexPortal; CPX-144; SMAD1 homotrimer.
ComplexPortal; CPX-54; SMAD1-SMAD4 complex.
CORUM; Q15797; -.
DIP; DIP-38538N; -.
IntAct; Q15797; 82.
MINT; Q15797; -.
STRING; 9606.ENSP00000426568; -.
MoonDB; Q15797; Predicted.
iPTMnet; Q15797; -.
PhosphoSitePlus; Q15797; -.
SwissPalm; Q15797; -.
BioMuta; SMAD1; -.
DMDM; 13633915; -.
EPD; Q15797; -.
jPOST; Q15797; -.
MassIVE; Q15797; -.
MaxQB; Q15797; -.
PaxDb; Q15797; -.
PeptideAtlas; Q15797; -.
PRIDE; Q15797; -.
ProteomicsDB; 60766; -. [Q15797-1]
Antibodypedia; 3950; 1277 antibodies.
DNASU; 4086; -.
Ensembl; ENST00000302085; ENSP00000305769; ENSG00000170365. [Q15797-1]
Ensembl; ENST00000394092; ENSP00000377652; ENSG00000170365. [Q15797-1]
Ensembl; ENST00000515385; ENSP00000426568; ENSG00000170365. [Q15797-1]
GeneID; 4086; -.
KEGG; hsa:4086; -.
UCSC; uc003ikc.4; human. [Q15797-1]
CTD; 4086; -.
DisGeNET; 4086; -.
GeneCards; SMAD1; -.
HGNC; HGNC:6767; SMAD1.
HPA; ENSG00000170365; Low tissue specificity.
MIM; 601595; gene.
neXtProt; NX_Q15797; -.
OpenTargets; ENSG00000170365; -.
PharmGKB; PA30524; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000154391; -.
HOGENOM; CLU_026736_0_2_1; -.
InParanoid; Q15797; -.
KO; K04676; -.
OMA; EVFHCNS; -.
PhylomeDB; Q15797; -.
TreeFam; TF314923; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8941326; RUNX2 regulates bone development.
SignaLink; Q15797; -.
SIGNOR; Q15797; -.
ChiTaRS; SMAD1; human.
EvolutionaryTrace; Q15797; -.
GeneWiki; Mothers_against_decapentaplegic_homolog_1; -.
GenomeRNAi; 4086; -.
Pharos; Q15797; Tbio.
PRO; PR:Q15797; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; Q15797; protein.
Bgee; ENSG00000170365; Expressed in visceral pleura and 240 other tissues.
ExpressionAtlas; Q15797; baseline and differential.
Genevisible; Q15797; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0071141; C:SMAD protein complex; NAS:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070878; F:primary miRNA binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; TAS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
GO; GO:0007276; P:gamete generation; IEA:Ensembl.
GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
GO; GO:0042592; P:homeostatic process; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
GO; GO:0001710; P:mesodermal cell fate commitment; IEA:Ensembl.
GO; GO:0030901; P:midbrain development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0002051; P:osteoblast fate commitment; IEA:Ensembl.
GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISS:BHF-UCL.
GO; GO:0031053; P:primary miRNA processing; TAS:BHF-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; ISS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; NAS:UniProtKB.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DisProt; DP01206; -.
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; Alternative splicing; Cytoplasm;
Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1..465
/note="Mothers against decapentaplegic homolog 1"
/id="PRO_0000090847"
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:0000269|PubMed:11779505"
COMPBIAS 39..45
/note="Poly-Lys"
COMPBIAS 198..201
/note="Poly-Ser"
METAL 64
/note="Zinc"
/evidence="ECO:0000250"
METAL 109
/note="Zinc"
/evidence="ECO:0000250"
METAL 121
/note="Zinc"
/evidence="ECO:0000250"
METAL 126
/note="Zinc"
/evidence="ECO:0000250"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000269|Ref.11"
MOD_RES 322
/note="Phosphothreonine; by MINK1, TNIK and MAP4K4"
/evidence="ECO:0000269|PubMed:21690388"
MOD_RES 463
/note="Phosphoserine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:11779505, ECO:0000269|PubMed:9136927"
MOD_RES 465
/note="Phosphoserine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:11779505, ECO:0000269|PubMed:9136927"
VAR_SEQ 1..12
/note="MNVTSLFSFTSP -> MFVLLFFPFLFL (in isoform 2)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_057163"
VAR_SEQ 13..133
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_057164"
VAR_SEQ 220..258
/note="ADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRG -> GRLECSVMF
CSHIRQCYHSVTEKLGQPAVEGGFQPWYMT (in isoform 2)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_057165"
VAR_SEQ 259..465
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_057166"
VARIANT 3
/note="V -> A (found in a patient with primary pulmonary
hypertension; unknown pathological significance; affects
SMAD-mediated signaling; dbSNP:rs587777018)"
/evidence="ECO:0000269|PubMed:21898662"
/id="VAR_066869"
MUTAGEN 297
/note="D->H: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 317
/note="V->D: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 373
/note="K->S: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 418
/note="K->S: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 419
/note="G->S: Loss of phosphorylation."
/evidence="ECO:0000269|PubMed:8653785"
MUTAGEN 424
/note="Y->F: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 426
/note="R->S: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 448
/note="D->H: Reduced trimerization."
/evidence="ECO:0000269|PubMed:11779505"
MUTAGEN 463..465
/note="SVS->AVA: Increases interaction with RANBPL3."
/evidence="ECO:0000269|PubMed:25755279"
MUTAGEN 463..465
/note="SVS->DVD: Decreases interaction with RANBPL3."
/evidence="ECO:0000269|PubMed:25755279"
STRAND 272..278
/evidence="ECO:0000244|PDB:1KHU"
STRAND 281..288
/evidence="ECO:0000244|PDB:5ZOK"
STRAND 291..299
/evidence="ECO:0000244|PDB:1KHU"
STRAND 305..310
/evidence="ECO:0000244|PDB:1KHU"
HELIX 321..327
/evidence="ECO:0000244|PDB:1KHU"
TURN 328..332
/evidence="ECO:0000244|PDB:5ZOK"
STRAND 334..338
/evidence="ECO:0000244|PDB:1KHU"
STRAND 340..347
/evidence="ECO:0000244|PDB:1KHU"
STRAND 349..351
/evidence="ECO:0000244|PDB:1KHU"
STRAND 353..356
/evidence="ECO:0000244|PDB:1KHU"
HELIX 358..363
/evidence="ECO:0000244|PDB:1KHU"
STRAND 372..374
/evidence="ECO:0000244|PDB:1KHU"
STRAND 379..384
/evidence="ECO:0000244|PDB:1KHU"
HELIX 385..393
/evidence="ECO:0000244|PDB:1KHU"
TURN 394..398
/evidence="ECO:0000244|PDB:1KHU"
HELIX 400..404
/evidence="ECO:0000244|PDB:1KHU"
HELIX 405..410
/evidence="ECO:0000244|PDB:1KHU"
STRAND 411..417
/evidence="ECO:0000244|PDB:1KHU"
STRAND 421..425
/evidence="ECO:0000244|PDB:5ZOK"
HELIX 429..431
/evidence="ECO:0000244|PDB:1KHU"
STRAND 432..440
/evidence="ECO:0000244|PDB:1KHU"
HELIX 441..451
/evidence="ECO:0000244|PDB:1KHU"
STRAND 461..463
/evidence="ECO:0000244|PDB:3Q47"
SEQUENCE 465 AA; 52260 MW; 2DD34B7F434DBC7E CRC64;
MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE LEKALSCPGQ
PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH HELKPLECCE FPFGSKQKEV
CINPYHYKRV ESPVLPPVLV PRHSEYNPQH SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN
SHPFPHSPNS SYPNSPGSSS STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMTQDGSQ
PMDTNMMAPP LPSEINRGDV 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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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP32: Translation Factors
WP211: BMP signaling pathway
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP731: Sterol regulatory element binding protein related
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP813: G Protein Signaling Pathways
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1566: Citrate cycle (TCA cycle)
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP210: Cytoplasmic Ribosomal Proteins
WP35: G Protein Signaling Pathways
WP505: TGF Beta Signaling Pathway
WP1370: TGF Beta Signaling Pathway
WP930: TGF Beta Signaling Pathway
WP1165: G Protein Signaling Pathways
WP230: TGF Beta Signaling Pathway
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP313: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[Smad1 Madh1 Madr1] 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 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[SMAD7 MADH7 MADH8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) (hSMAD7)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[Smox Dmel\CG2262 DSMAD2 DSmad2 dSMAD2 dSmad2 dsmad2 l(1)G0348 Sad sad Smad SMAD2 Smad2 smad2 SMOX SmoX smox ted tmp CG2262 Dmel_CG2262] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[MAD1L1 MAD1 TXBP181] Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181)
[Mad CG12399] Protein mothers against dpp
[TSC22D1 KIAA1994 TGFB1I4 TSC22 hucep-2] TSC22 domain family protein 1 (Cerebral protein 2) (Regulatory protein TSC-22) (TGFB-stimulated clone 22 homolog) (Transforming growth factor beta-1-induced transcript 4 protein)
[ZFYVE9 MADHIP SARA SMADIP] Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)

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