Reviewed, UniProtKB/Swiss-Prot P84022 (SMAD3_HUMAN)

Names and origin

Protein names

Recommended name:
    Mothers against decapentaplegic homolog 3
      Short name=Mad3
      Short name=hMAD-3
      Short name=Mothers against DPP homolog 3
Alternative name(s):
    SMAD 3
    hSMAD3
    JV15-2

Gene names

Name:	SMAD3
Synonyms:	MADH3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinase. SMAD3 is a receptor-regulated SMAD (R-SMAD) By similarity.
Subunit structure	Interacts with HGS. Interacts with NEDD4L in response to TGF-beta. Interacts with TTRAP By similarity. Interacts with SARA (SMAD anchor for receptor activation); form trimers with another SMAD3 and the co-SMAD SMAD4. Interacts with HDAC1, JUN/FOS, vitamin D receptor, homeobox protein TGIF and TGIF2, PEBP2-alpha C subunit, CREB-binding protein (CBP), p300, SKI, SNON, ATF2, SMURF2, AIP1, DACH1 and TGFB1I1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3. Found in a complex with SMAD2 and TRIM33 upon addition of TGF-beta. Interacts with SMAD2 and TRIM33. Found in a complex with SMAD3, Ran and XPO4. Interacts with XPO4. Interacts with LBXCOR1 and CORL2. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interaction with LEMD3 blocks the formation of heteromeric complex with SMAD4 and translocation to the nucleus. Interacts with RBPMS; the interaction is direct. Interacts with FOXL2 By similarity. Interacts (via MH2 domain) with MECOM; the interaction is direct. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.23 Ref.27
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 By similarity. Co-localizes with LEMD3 at the nucleus inner membrane. Ref.11
Domain	The MH2 domain is sufficient to carry protein nuclear export.
Post-translational modification	Phosphorylated on serine by TGF-beta and activin type 1 receptor kinases. Ref.1 Ref.24 Ref.26
Involvement in disease	Defects in SMAD3 may be a cause of colorectal cancer (CRC) [MIM:114500].
Sequence similarities	Belongs to the dwarfin/SMAD family. Contains 1 MH1 (MAD homology 1) domain. Contains 1 MH2 (MAD homology 2) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	SMAD protein complex assembly Inferred from direct assay. Source: UniProtKB activation of caspase activity Inferred from mutant phenotype. Source: UniProtKB cell cycle arrest Inferred from mutant phenotype. Source: UniProtKB cell-cell junction organization Inferred from mutant phenotype. Source: UniProtKB evasion of host defenses by virus Inferred from direct assay. Source: UniProtKB immune response Inferred from mutant phenotype. Source: UniProtKB induction of apoptosis Inferred from mutant phenotype. Source: UniProtKB negative regulation of cell growth Ref.1 Inferred from direct assay. Source: UniProtKB negative regulation of mitotic cell cycle Inferred from mutant phenotype. Source: UniProtKB positive regulation of epithelial to mesenchymal transition Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription factor import into nucleus Inferred from direct assay. Source: UniProtKB primary microRNA processing Traceable author statement. Source: UniProtKB regulation of transforming growth factor beta receptor signaling pathway Ref.1 Inferred from mutant phenotype. Source: UniProtKB regulation of transforming growth factor-beta2 production Inferred from mutant phenotype. Source: UniProtKB response to hypoxia Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: UniProtKB transport Inferred from direct assay. Source: UniProtKB wound healing Traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome nuclear inner membrane Ref.13 Inferred from direct assay. Source: UniProtKB receptor complex Ref.1 Inferred from mutant phenotype. Source: UniProtKB transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	R-SMAD binding Inferred from physical interaction. Source: UniProtKB co-SMAD binding Ref.1 Inferred from physical interaction. Source: UniProtKB promoter binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.1 Inferred from physical interaction. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: UniProtKB transcription factor activity Inferred from direct assay. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB transforming growth factor beta receptor binding Inferred from physical interaction. Source: UniProtKB transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Inferred from direct assay. Source: UniProtKB ubiquitin protein ligase binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTB	P60709	1	EBI-347161,EBI-353944
DACH1	Q9UI36	1	EBI-347161,EBI-347111
GRB2	P62993	1	EBI-347161,EBI-401755
PRTN3	P24158	1	EBI-347161,EBI-465028
SKI	P12755	1	EBI-347161,EBI-347281
SMAD4	Q13485	1	EBI-347161,EBI-347263
SREBF2	Q12772	1	EBI-347161,EBI-465059
SRY	Q05066	1	EBI-347161,EBI-464987
Tp63	O88898-2	1	EBI-347161,EBI-2338228	From a different organism.
Tp63	O88898-5	1	EBI-347161,EBI-2338240	From a different organism.
ZFYVE9	O95405	1	EBI-347161,EBI-296817

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 425

425

Mothers against decapentaplegic homolog 3

PRO_0000090856

Regions

Domain

10 – 136

127

MH1

Domain

232 – 425

194

MH2

Region

271 – 324

54

Sufficient for interaction with XPO4

Amino acid modifications

Modified residue

8

1

Phosphothreonine Ref.26

Modified residue

378

1

N6-acetyllysine Ref.28

Modified residue

416

1

Phosphoserine Ref.24

Modified residue

423

1

Phosphoserine By similarity

Modified residue

425

1

Phosphoserine By similarity

Natural variations

Natural variant

170

1

I → V: dbSNP rs35874463.

VAR_052021

Natural variant

393

1

P → L in a colorectal cancer sample; somatic mutation. Ref.31

VAR_036474

Experimental info

Mutagenesis

422 – 425

4

SSVS → AAVA: Does not abolish protein nuclear export. Ref.17

Mutagenesis

422 – 425

4

SSVS → RRVR: Diminishes cargo protein export. Ref.17

Sequence conflict

178

1

E → EVGTWAAQAGL in BAA22032. Ref.3

Secondary structure

1

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425

Helix Strand Turn

Details...

Helix

10 – 16

7

Helix

25 – 44

20

Helix

48 – 57

10

Beta strand

66 – 68

3

Beta strand

75 – 77

3

Beta strand

80 – 82

3

Helix

84 – 92

9

Helix

100 – 102

3

Beta strand

103 – 105

3

Helix

113 – 115

3

Beta strand

118 – 121

4

Helix

124 – 126

3

Beta strand

127 – 129

3

Beta strand

221 – 225

5

Beta strand

231 – 239

9

Beta strand

242 – 250

9

Beta strand

252 – 258

7

Beta strand

268 – 270

3

Helix

281 – 290

10

Beta strand

294 – 299

6

Beta strand

302 – 307

6

Beta strand

309 – 311

3

Beta strand

313 – 316

4

Helix

318 – 321

4

Beta strand

332 – 334

3

Beta strand

339 – 343

5

Helix

345 – 358

14

Helix

360 – 364

5

Helix

365 – 370

6

Beta strand

371 – 377

7

Beta strand

392 – 400

9

Helix

401 – 413

13

Sequences

	Sequence		Length	Mass (Da)
	P84022-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 46DF5E8B371321AC	FASTA	425	48,081
	10 20 30 40 50 60 MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNV 70 80 90 100 110 120 NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMELCE FAFNMKKDEV 130 140 150 160 170 180 CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNIPETP 190 200 210 220 230 240 PPGYLSEDGE TSDHQMNHSM DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL 250 260 270 280 290 300 NQRVGETFHA SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG 310 320 330 340 350 360 GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA LLAQSVNQGF 370 380 390 400 410 420 EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL NGPLQWLDKV LTQMGSPSIR CSSVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Receptor-associated Mad homologues synergize as effectors of the TGF-beta response." Zhang Y., Feng X.-H., Wu R.-Y., Derynck R. Nature 383:168-172(1996) [PubMed: 8774881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION. Tissue: Placenta.
[2]	"Mad-related genes in the human." 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. Nat. Genet. 13:347-349(1996) [PubMed: 8673135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Genomic structure of the human Smad3 gene and its infrequent alterations in colorectal cancers." Arai T., Akiyama Y., Okabe S., Ando M., Endo M., Yuasa Y. Cancer Lett. 122:157-163(1998) [PubMed: 9464505] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Colon carcinoma.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[8]	"The oncoprotein Evi-1 represses TGF-beta signalling by inhibiting Smad3." Kurokawa M., Mitani K., Irie K., Matsuyama T., Takahashi T., Chiba S., Yazaki Y., Matsumoto K., Hirai H. Nature 394:92-96(1998) [PubMed: 9665135] [Abstract] Cited for: INTERACTION WITH MECOM.
[9]	"TGIF2 interacts with histone deacetylase 1 and represses transcription." Melhuish T.A., Gallo C.M., Wotton D. J. Biol. Chem. 276:32109-32114(2001) [PubMed: 11427533] [Abstract] Cited for: INTERACTION WITH TGIF2.
[10]	"DACH1 inhibits transforming growth factor-beta signaling through binding Smad4." Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K., Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G. J. Biol. Chem. 278:51673-51684(2003) [PubMed: 14525983] [Abstract] Cited for: INTERACTION WITH DACH1.
[11]	"MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling." Lin F., Morrison J.M., Wu W., Worman H.J. Hum. Mol. Genet. 14:437-445(2005) [PubMed: 15601644] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LEMD3.
[12]	"Novel function of androgen receptor-associated protein 55/Hic-5 as a negative regulator of Smad3 signaling." Wang H., Song K., Sponseller T.L., Danielpour D. J. Biol. Chem. 280:5154-5162(2005) [PubMed: 15561701] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[13]	"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." Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K. J. Biol. Chem. 280:15992-16001(2005) [PubMed: 15647271] [Abstract] Cited for: INTERACTION WITH LEMD3.
[14]	"Cloning and functional characterization of a new Ski homolog, Fussel-18, specifically expressed in neuronal tissues." Arndt S., Poser I., Schubert T., Moser M., Bosserhoff A.-K. Lab. Invest. 85:1330-1341(2005) [PubMed: 16200078] [Abstract] Cited for: INTERACTION WITH CORL2.
[15]	"Oligomerization of Evi-1 regulated by the PR domain contributes to recruitment of corepressor CtBP." Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S., Kurokawa M., Hirai H. Oncogene 24:6165-6173(2005) [PubMed: 15897867] [Abstract] Cited for: INTERACTION WITH MECOM.
[16]	"Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway." He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J. Cell 125:929-941(2006) [PubMed: 16751102] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD2 AND TRIM33, INTERACTION WITH SMAD2 AND TRIM33.
[17]	"The mechanism of nuclear export of Smad3 involves exportin 4 and Ran." Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y., Heldin C.-H., Moustakas A. Mol. Cell. Biol. 26:1318-1332(2006) [PubMed: 16449645] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RAN AND XPO4, INTERACTION WITH XPO4, MUTAGENESIS OF 422-SER--SER-425.
[18]	"Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS." Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q. Nucleic Acids Res. 34:6314-6326(2006) [PubMed: 17099224] [Abstract] Cited for: INTERACTION WITH RBPMS.
[19]	"TGF-beta signal transduction." Massague J. Annu. Rev. Biochem. 67:753-791(1998) [PubMed: 9759503] [Abstract] Cited for: REVIEW.
[20]	"Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells." Verschueren K., Huylebroeck D. Cytokine Growth Factor Rev. 10:187-199(1999) [PubMed: 10647776] [Abstract] Cited for: REVIEW.
[21]	"The Smad pathway." Wrana J.L., Attisano L. Cytokine Growth Factor Rev. 11:5-13(2000) [PubMed: 10708948] [Abstract] Cited for: REVIEW.
[22]	"TGF-beta signaling by Smad proteins." Miyazono K. Cytokine Growth Factor Rev. 11:15-22(2000) [PubMed: 10708949] [Abstract] Cited for: REVIEW.
[23]	"Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling." Arndt S., Poser I., Moser M., Bosserhoff A.-K. Mol. Cell. Neurosci. 34:603-611(2007) [PubMed: 17292623] [Abstract] Cited for: INTERACTION WITH LBXCOR1.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, MASS SPECTROMETRY.
[25]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, MASS SPECTROMETRY.
[27]	"SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells." Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T. J. Biol. Chem. 284:3334-3344(2009) [PubMed: 19049980] [Abstract] Cited for: INTERACTION WITH PRDM16; SKI AND HDAC1.
[28]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, MASS SPECTROMETRY.
[29]	"Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling." Shi Y., Wang Y.-F., Jayaraman L., Yang H., Massague J., Pavletich N.P. Cell 94:585-594(1998) [PubMed: 9741623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-144.
[30]	"Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control." Qin B.Y., Lam S.S., Correia J.J., Lin K. Genes Dev. 16:1950-1963(2002) [PubMed: 12154125] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 220-425 IN COMPLEX WITH ZFYVE9.
[31]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-393.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U68019 mRNA. Translation: AAB80960.1.
U76622 mRNA. Translation: AAB18967.1.
AB004930 Genomic DNA. Translation: BAA22032.1.
AF025300 , AF025293, AF025294, AF025295, AF025296, AF025297, AF025298, AF025299 Genomic DNA. Translation: AAL68976.1.
AK290881 mRNA. Translation: BAF83570.1.
CH471082 Genomic DNA. Translation: EAW77788.1.
BC050743 mRNA. Translation: AAH50743.1.

IPI

IPI00024305.

PIR

S71798.

RefSeq

NP_001138574.1.
NP_001138575.1.
NP_005893.1.

UniGene

Hs.718953

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MHD	X-ray	2.80	A/B	1-132	[»]
1MJS	X-ray	1.91	A	229-425	[»]
1MK2	X-ray	2.74	A	220-425	[»]
1OZJ	X-ray	2.40	A/B	1-144	[»]
1U7F	X-ray	2.60	A/C	228-424	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29720N.

IntAct

P84022. 18 interactions.

STRING

P84022.

PTM databases

PhosphoSite

P84022.

Proteomic databases

PRIDE

P84022.

Genome annotation databases

Ensembl

ENST00000327367; ENSP00000332973; ENSG00000166949; Homo sapiens. [Genome view]

GeneID

4088.

KEGG

hsa:4088.

UCSC

uc002aqj.1. human.

Organism-specific databases

CTD

4088.

GeneCards

GC15P065145.

H-InvDB

HIX0012370.

HGNC

HGNC:6769. SMAD3.

HPA

CAB008094.

MIM

114500. phenotype.
603109. gene.

PharmGKB

PA30526.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14839.

HOVERGEN

P84022.

InParanoid

P84022.

OMA

AMEMCEF.

PhylomeDB

P84022.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.
smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_6844. Signaling by TGF beta.

Gene expression databases

ArrayExpress

P84022.

Bgee

P84022.

CleanEx

HS_SMAD3.

Genevestigator

P84022.

GermOnline

ENSG00000166949. Homo sapiens.

Family and domain databases

InterPro

IPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]

Gene3D

G3DSA:3.90.520.10. MAD_MH1. 1 hit.
G3DSA:2.60.200.10. MH2_Dwarfin-type. 1 hit.

PANTHER

PTHR13703. Dwarfin. 1 hit.

Pfam

PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]

SMART

SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]

PROSITE

PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

16026.

SOURCE

Search...

Entry information

Entry name

SMAD3_HUMAN

Accession

Primary (citable) accession number: P84022
Secondary accession number(s): A8K4B6 , O09064, O09144, O14510, O35273, Q92940, Q93002, Q9GKR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.