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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)

 SMAD7_HUMAN             Reviewed;         426 AA.
O15105; B7Z773; K7EQ10; O14740; Q6DK23;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
30-AUG-2017, entry version 179.
RecName: Full=Mothers against decapentaplegic homolog 7;
Short=MAD homolog 7;
Short=Mothers against DPP homolog 7;
AltName: Full=Mothers against decapentaplegic homolog 8;
Short=MAD homolog 8;
Short=Mothers against DPP homolog 8;
AltName: Full=SMAD family member 7;
Short=SMAD 7;
Short=Smad7;
Short=hSMAD7;
Name=SMAD7; Synonyms=MADH7, MADH8;
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), AND MUTAGENESIS OF
409-ARG--ARG-426.
TISSUE=Umbilical vein endothelial cell;
PubMed=9215638; DOI=10.1016/S0092-8674(00)80303-7;
Hayashi H., Abdollah S., Qiu Y., Cai J., Xu Y.-Y., Grinnell B.W.,
Richardson M.A., Topper J.N., Gimbrone M.A. Jr., Wrana J.L., Falb D.;
"The MAD-related protein Smad7 associates with the TGFbeta receptor
and functions as an antagonist of TGFbeta signaling.";
Cell 89:1165-1173(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Umbilical vein endothelial cell;
PubMed=9256479; DOI=10.1073/pnas.94.17.9314;
Topper J.N., Cai J., Qui Y., Anderson K.R., Xu Y.-Y., Deeds J.D.,
Feeley R., Gimeno C.J., Woolf E.A., Tayber O., Mays G.G.,
Sampson B.A., Schoen F.J., Gimbrone M.A. Jr., Falb D.;
"Vascular MADs: two novel MAD-related genes selectively inducible by
flow in human vascular endothelium.";
Proc. Natl. Acad. Sci. U.S.A. 94:9314-9319(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9335507; DOI=10.1038/39369;
Nakao A., Afrakhte M., Moren A., Nakayama T., Christian J.L.,
Heuchel R., Itoh S., Kawabata M., Heldin N.-E., Heldin C.-H.,
ten Dijke P.;
"Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta
signalling.";
Nature 389:631-635(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hagiwara K., Yang K., McMenamin M.G., Freeman A.H., Bennett W.P.,
Nagashima M., Minter A.R., Miyazono K., Takenoshita S., Harris C.C.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 98-271 (ISOFORM 3).
TISSUE=Pulmonary artery;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[8]
REVIEW.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[9]
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).
[10]
INTERACTION WITH ACVR1B, AND FUNCTION.
PubMed=9892009; DOI=10.1210/mend.13.1.0218;
Lebrun J.J., Takabe K., Chen Y., Vale W.;
"Roles of pathway-specific and inhibitory Smads in activin receptor
signaling.";
Mol. Endocrinol. 13:15-23(1999).
[11]
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).
[12]
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).
[13]
FUNCTION, MUTAGENESIS OF TYR-211 AND 207-PRO--TYR-211, AND INTERACTION
WITH SMURF2 AND TGFBR1.
PubMed=11163210; DOI=10.1016/S1097-2765(00)00134-9;
Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H.,
Thomsen G.H., Wrana J.L.;
"Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the
TGF-beta receptor for degradation.";
Mol. Cell 6:1365-1375(2000).
[14]
INTERACTION WITH STAMBP.
PubMed=11483516; DOI=10.1093/emboj/20.15.4132;
Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.;
"Promoting bone morphogenetic protein signaling through negative
regulation of inhibitory Smads.";
EMBO J. 20:4132-4142(2001).
[15]
INTERACTION WITH SMURF1 AND TGFBR1, AND UBIQUITINATION.
PubMed=11278251; DOI=10.1074/jbc.C100008200;
Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T.,
Miyazono K.;
"Smurf1 interacts with transforming growth factor-beta type I receptor
through Smad7 and induces receptor degradation.";
J. Biol. Chem. 276:12477-12480(2001).
[16]
INTERACTION WITH ACVR1B, AND FUNCTION.
PubMed=12023024; DOI=10.1016/S0014-5793(02)02718-7;
Liu X., Nagarajan R.P., Vale W., Chen Y.;
"Phosphorylation regulation of the interaction between Smad7 and
activin type I receptor.";
FEBS Lett. 519:93-98(2002).
[17]
INTERACTION WITH EP300, ACETYLATION AT LYS-64 AND LYS-70,
UBIQUITINATION AT LYS-64 AND LYS-70, AND MUTAGENESIS OF LYS-64 AND
LYS-70.
PubMed=12408818; DOI=10.1016/S1097-2765(02)00639-1;
Gronroos E., Hellman U., Heldin C.H., Ericsson J.;
"Control of Smad7 stability by competition between acetylation and
ubiquitination.";
Mol. Cell 10:483-493(2002).
[18]
INTERACTION WITH RNF111, UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=14657019; DOI=10.1093/emboj/cdg632;
Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A.,
Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.;
"Arkadia amplifies TGF-beta superfamily signaling through degradation
of Smad7.";
EMBO J. 22:6458-6470(2003).
[19]
FUNCTION, AND INTERACTION WITH PPP1R15A.
PubMed=14718519; DOI=10.1083/jcb.200307151;
Shi W., Sun C., He B., Xiong W., Shi X., Yao D., Cao X.;
"GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I
receptor.";
J. Cell Biol. 164:291-300(2004).
[20]
INTERACTION WITH COPS5.
PubMed=14993265; DOI=10.1128/MCB.24.6.2251-2262.2004;
Kim B.-C., Lee H.-J., Park S.H., Lee S.R., Karpova T.S., McNally J.G.,
Felici A., Lee D.K., Kim S.-J.;
"Jab1/CSN5, a component of the COP9 signalosome, regulates
transforming growth factor beta signaling by binding to Smad7 and
promoting its degradation.";
Mol. Cell. Biol. 24:2251-2262(2004).
[21]
INTERACTION WITH SMURF2.
PubMed=16061177; DOI=10.1016/j.molcel.2005.06.028;
Ogunjimi A.A., Briant D.J., Pece-Barbara N., Le Roy C.,
Di Guglielmo G.M., Kavsak P., Rasmussen R.K., Seet B.T., Sicheri F.,
Wrana J.L.;
"Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to
the HECT domain.";
Mol. Cell 19:297-308(2005).
[22]
INTERACTION WITH AXIN1 AND AXIN2, UBIQUITINATION, AND SUBCELLULAR
LOCATION.
PubMed=16601693; DOI=10.1038/sj.emboj.7601057;
Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z.,
Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.;
"Axin is a scaffold protein in TGF-beta signaling that promotes
degradation of Smad7 by Arkadia.";
EMBO J. 25:1646-1658(2006).
[23]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PDPK1, AND
INTERACTION WITH PDPK1.
PubMed=17327236; DOI=10.1074/jbc.M609279200;
Seong H.A., Jung H., Kim K.T., Ha H.;
"3-Phosphoinositide-dependent PDK1 negatively regulates transforming
growth factor-beta-induced signaling in a kinase-dependent manner
through physical interaction with Smad proteins.";
J. Biol. Chem. 282:12272-12289(2007).
[24]
STRUCTURE BY NMR OF 203-217 IN COMPLEX WITH SMURF2.
PubMed=16641086; DOI=10.1074/jbc.M601493200;
Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D.;
"An expanded WW domain recognition motif revealed by the interaction
between Smad7 and the E3 ubiquitin ligase Smurf2.";
J. Biol. Chem. 281:17069-17075(2006).
[25]
INVOLVEMENT IN CRCS3.
PubMed=17934461; DOI=10.1038/ng.2007.18;
Members of the CORGI consortium;
Broderick P., Carvajal-Carmona L., Pittman A.M., Webb E., Howarth K.,
Rowan A., Lubbe S., Spain S., Sullivan K., Fielding S., Jaeger E.,
Vijayakrishnan J., Kemp Z., Gorman M., Chandler I., Papaemmanuil E.,
Penegar S., Wood W., Sellick G., Qureshi M., Teixeira A., Domingo E.,
Barclay E., Martin L., Sieber O., Kerr D., Gray R., Peto J.,
Cazier J.-B., Tomlinson I., Houlston R.S.;
"A genome-wide association study shows that common alleles of SMAD7
influence colorectal cancer risk.";
Nat. Genet. 39:1315-1317(2007).
-!- FUNCTION: Antagonist of signaling by TGF-beta (transforming growth
factor) type 1 receptor superfamily members; has been shown to
inhibit TGF-beta (Transforming growth factor) and activin
signaling by associating with their receptors thus preventing
SMAD2 access. Functions as an adapter to recruit SMURF2 to the
TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-
PP1 complex to TGFBR1, which promotes its dephosphorylation.
Positively regulates PDPK1 kinase activity by stimulating its
dissociation from the 14-3-3 protein YWHAQ which acts as a
negative regulator. {ECO:0000269|PubMed:11163210,
ECO:0000269|PubMed:12023024, ECO:0000269|PubMed:14718519,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:9892009}.
-!- SUBUNIT: Interacts with WWP1 (By similarity). Interacts with
COPS5. Interacts with NEDD4L. Interacts with STAMBP. Interacts
with RNF111, AXIN1 and AXIN2. Interacts with PPP1R15A. Interacts
(via MH2 domain) with EP300. Interacts with ACVR1B, SMURF1, SMURF2
and TGFBR1; SMAD7 recruits SMURF1 and SMURF2 to the TGF-beta
receptor and regulates its degradation. Interacts with PDPK1 (via
PH domain). {ECO:0000250, ECO:0000269|PubMed:11163210,
ECO:0000269|PubMed:11278251, ECO:0000269|PubMed:11483516,
ECO:0000269|PubMed:12023024, ECO:0000269|PubMed:12408818,
ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:14718519,
ECO:0000269|PubMed:14993265, ECO:0000269|PubMed:16061177,
ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:16641086,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:9892009}.
-!- INTERACTION:
P36896:ACVR1B; NbExp=2; IntAct=EBI-3861591, EBI-1384128;
O15169:AXIN1; NbExp=8; IntAct=EBI-3861591, EBI-710484;
Q92905:COPS5; NbExp=10; IntAct=EBI-3861591, EBI-594661;
P62942:FKBP1A; NbExp=3; IntAct=EBI-3861591, EBI-1027571;
Q99ML9:Rnf111 (xeno); NbExp=2; IntAct=EBI-3861591, EBI-646015;
O00308:WWP2; NbExp=5; IntAct=EBI-3861591, EBI-743923;
P46937:YAP1; NbExp=3; IntAct=EBI-3861591, EBI-1044059;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}.
Cytoplasm {ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}.
Note=Interaction with NEDD4L or RNF111 induces translocation from
the nucleus to the cytoplasm (PubMed:16601693). TGF-beta
stimulates its translocation from the nucleus to the cytoplasm.
PDPK1 inhibits its translocation from the nucleus to the cytoplasm
in response to TGF-beta (PubMed:17327236).
{ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O15105-1; Sequence=Displayed;
Name=2;
IsoId=O15105-2; Sequence=VSP_045197;
Note=No experimental confirmation available.;
Name=3;
IsoId=O15105-3; Sequence=VSP_047540;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous with higher expression in the lung
and vascular endothelium.
-!- INDUCTION: By TGFB1.
-!- PTM: Phosphorylation on Ser-249 does not affect its stability,
nuclear localization or inhibitory function in TGFB signaling;
however it affects its ability to regulate transcription (By
similarity). Phosphorylated by PDPK1.
{ECO:0000250|UniProtKB:O35253, ECO:0000269|PubMed:17327236}.
-!- PTM: Ubiquitinated by WWP1 (By similarity). Polyubiquitinated by
RNF111, which is enhanced by AXIN1 and promotes proteasomal
degradation (PubMed:14657019, PubMed:16601693). In response to
TGF-beta, ubiquitinated by SMURF1; which promotes its degradation
(PubMed:11278251). {ECO:0000250|UniProtKB:O35253,
ECO:0000269|PubMed:11278251, ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:16601693}.
-!- PTM: Acetylation prevents ubiquitination and degradation mediated
by SMURF1. {ECO:0000269|PubMed:12408818}.
-!- DISEASE: Colorectal cancer 3 (CRCS3) [MIM:612229]: A complex
disease characterized by malignant lesions arising from the inner
wall of the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000269|PubMed:17934461}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; AF010193; AAB81246.1; -; mRNA.
EMBL; AF015261; AAB81354.1; -; mRNA.
EMBL; AF026559; AAL68977.1; -; Genomic_DNA.
EMBL; AF026556; AAL68977.1; JOINED; Genomic_DNA.
EMBL; AF026557; AAL68977.1; JOINED; Genomic_DNA.
EMBL; AF026558; AAL68977.1; JOINED; Genomic_DNA.
EMBL; AK301535; BAH13509.1; -; mRNA.
EMBL; DA882147; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC114684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC074818; AAH74818.2; -; mRNA.
EMBL; BC074819; AAH74819.2; -; mRNA.
CCDS; CCDS11936.1; -. [O15105-1]
CCDS; CCDS54186.1; -. [O15105-2]
CCDS; CCDS59317.1; -. [O15105-3]
RefSeq; NP_001177750.1; NM_001190821.1. [O15105-3]
RefSeq; NP_001177751.1; NM_001190822.1. [O15105-2]
RefSeq; NP_001177752.1; NM_001190823.1.
RefSeq; NP_005895.1; NM_005904.3. [O15105-1]
UniGene; Hs.465087; -.
PDB; 2DJY; NMR; -; B=203-217.
PDB; 2KXQ; NMR; -; B=203-217.
PDB; 2LTV; NMR; -; B=206-217.
PDB; 2LTW; NMR; -; B=205-217.
PDB; 2LTX; NMR; -; B=203-217.
PDB; 2LTY; NMR; -; B=203-217.
PDB; 2LTZ; NMR; -; B=203-217.
PDBsum; 2DJY; -.
PDBsum; 2KXQ; -.
PDBsum; 2LTV; -.
PDBsum; 2LTW; -.
PDBsum; 2LTX; -.
PDBsum; 2LTY; -.
PDBsum; 2LTZ; -.
ProteinModelPortal; O15105; -.
SMR; O15105; -.
BioGrid; 110267; 95.
DIP; DIP-42252N; -.
IntAct; O15105; 27.
MINT; MINT-1179821; -.
STRING; 9606.ENSP00000262158; -.
iPTMnet; O15105; -.
PhosphoSitePlus; O15105; -.
BioMuta; SMAD7; -.
PaxDb; O15105; -.
PeptideAtlas; O15105; -.
PRIDE; O15105; -.
Ensembl; ENST00000262158; ENSP00000262158; ENSG00000101665. [O15105-1]
Ensembl; ENST00000589634; ENSP00000467621; ENSG00000101665. [O15105-3]
Ensembl; ENST00000591805; ENSP00000466902; ENSG00000101665. [O15105-2]
GeneID; 4092; -.
KEGG; hsa:4092; -.
UCSC; uc002ldg.3; human. [O15105-1]
CTD; 4092; -.
DisGeNET; 4092; -.
GeneCards; SMAD7; -.
HGNC; HGNC:6773; SMAD7.
HPA; CAB026212; -.
HPA; HPA028897; -.
MalaCards; SMAD7; -.
MIM; 602932; gene.
MIM; 612229; phenotype.
neXtProt; NX_O15105; -.
OpenTargets; ENSG00000101665; -.
PharmGKB; PA134875286; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000060106; -.
HOVERGEN; HBG053021; -.
InParanoid; O15105; -.
KO; K19631; -.
OMA; GQLCSEN; -.
OrthoDB; EOG091G0XBN; -.
PhylomeDB; O15105; -.
TreeFam; TF314923; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SignaLink; O15105; -.
SIGNOR; O15105; -.
ChiTaRS; SMAD7; human.
EvolutionaryTrace; O15105; -.
GeneWiki; Mothers_against_decapentaplegic_homolog_7; -.
GenomeRNAi; 4092; -.
PRO; PR:O15105; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000101665; -.
CleanEx; HS_SMAD7; -.
ExpressionAtlas; O15105; baseline and differential.
Genevisible; O15105; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0048185; F:activin binding; IPI:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0030617; F:transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity; IDA:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0034333; P:adherens junction assembly; IMP:BHF-UCL.
GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
GO; GO:0034629; P:cellular protein complex localization; IDA:BHF-UCL.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:BHF-UCL.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; TAS:BHF-UCL.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; TAS:BHF-UCL.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0002725; P:negative regulation of T cell cytokine production; ISS:BHF-UCL.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; ISS:BHF-UCL.
GO; GO:2000317; P:negative regulation of T-helper 17 type immune response; ISS:BHF-UCL.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:BHF-UCL.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; ISS:BHF-UCL.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IC:BHF-UCL.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IC:BHF-UCL.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
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_dom-like.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_domain.
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; 2.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 426 Mothers against decapentaplegic homolog
7.
/FTId=PRO_0000090872.
DOMAIN 64 207 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 261 426 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 208 217 Important for interaction with SMURF2.
MOTIF 208 211 PY-motif.
COMPBIAS 27 35 Poly-Gly.
COMPBIAS 49 56 Poly-Gly.
COMPBIAS 207 210 Poly-Pro.
METAL 125 125 Zinc. {ECO:0000250}.
METAL 180 180 Zinc. {ECO:0000250}.
METAL 192 192 Zinc. {ECO:0000250}.
METAL 197 197 Zinc. {ECO:0000250}.
MOD_RES 64 64 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12408818}.
MOD_RES 70 70 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12408818}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:O35253,
ECO:0000255|PROSITE-ProRule:PRU00439}.
CROSSLNK 64 64 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:12408818}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:12408818}.
VAR_SEQ 1 215 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045197.
VAR_SEQ 223 223 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047540.
MUTAGEN 64 64 K->A: Loss of acetylation, and of SMURF1-
dependent degradation; when associated
with A-70. {ECO:0000269|PubMed:12408818}.
MUTAGEN 70 70 K->A: Loss of acetylation, and of SMURF1-
dependent degradation; when associated
with A-64. {ECO:0000269|PubMed:12408818}.
MUTAGEN 207 211 Missing: Diminishes interaction with
SMURF2. {ECO:0000269|PubMed:11163210}.
MUTAGEN 211 211 Y->A: Diminishes interaction with SMURF2
and reduces inhibition of TGF-beta
signaling. {ECO:0000269|PubMed:11163210}.
MUTAGEN 409 426 Missing: 90% reduction in TGF-beta
receptor binding.
{ECO:0000269|PubMed:9215638}.
CONFLICT 71 71 G -> C (in Ref. 3; AAB81354).
{ECO:0000305}.
STRAND 204 206 {ECO:0000244|PDB:2DJY}.
STRAND 212 214 {ECO:0000244|PDB:2DJY}.
SEQUENCE 426 AA; 46426 MW; 5B76EC986776C102 CRC64;
MFRTKRSALV RRLWRSRAPG GEDEEEGAGG GGGGGELRGE GATDSRAHGA GGGGPGRAGC
CLGKAVRGAK GHHHPHPPAA GAGAAGGAEA DLKALTHSVL KKLKERQLEL LLQAVESRGG
TRTACLLLPG RLDCRLGPGA PAGAQPAQPP SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC
ESYGKINPEL VCCNPHHLSR LCELESPPPP YSRYPMDFLK PTADCPDAVP SSAETGGTNY
LAPGGLSDSQ LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ
LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP DSRTLLVHKV
FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV KGWGQCYTRQ FISSCPCWLE
VIFNSR


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