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Reviewed, UniProtKB/Swiss-Prot P84022 (SMAD3_HUMAN)

Last modified February 9, 2010. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processSMAD 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 componentcytosol

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 functionR-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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Mothers against decapentaplegic homolog 3
PRO_0000090856

Regions

Domain10 – 136127MH1
Domain232 – 425194MH2
Region271 – 32454Sufficient for interaction with XPO4

Amino acid modifications

Modified residue81Phosphothreonine Ref.26
Modified residue3781N6-acetyllysine Ref.28
Modified residue4161Phosphoserine Ref.24
Modified residue4231Phosphoserine By similarity
Modified residue4251Phosphoserine By similarity

Natural variations

Natural variant1701I → V: dbSNP rs35874463.
VAR_052021
Natural variant3931P → L in a colorectal cancer sample; somatic mutation. Ref.31
VAR_036474

Experimental info

Mutagenesis422 – 4254SSVS → AAVA: Does not abolish protein nuclear export. Ref.17
Mutagenesis422 – 4254SSVS → RRVR: Diminishes cargo protein export. Ref.17
Sequence conflict1781E → EVGTWAAQAGL in BAA22032. Ref.3

Secondary structure

............................................................ 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84022-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 46DF5E8B371321AC

FASTA42548,081
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
IPIIPI00024305.
PIRS71798.
RefSeqNP_001138574.1.
NP_001138575.1.
NP_005893.1.
UniGeneHs.718953

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHDX-ray2.80A/B1-132[»]
1MJSX-ray1.91A229-425[»]
1MK2X-ray2.74A220-425[»]
1OZJX-ray2.40A/B1-144[»]
1U7FX-ray2.60A/C228-424[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29720N.
IntActP84022. 18 interactions.
STRINGP84022.

PTM databases

PhosphoSiteP84022.

Proteomic databases

PRIDEP84022.

Genome annotation databases

EnsemblENST00000327367; ENSP00000332973; ENSG00000166949; Homo sapiens. [Genome view]
GeneID4088.
KEGGhsa:4088.
UCSCuc002aqj.1. human.

Organism-specific databases

CTD4088.
GeneCardsGC15P065145.
H-InvDBHIX0012370.
HGNCHGNC:6769. SMAD3.
HPACAB008094.
MIM114500. phenotype.
603109. gene.
PharmGKBPA30526.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14839.
HOVERGENP84022.
InParanoidP84022.
OMAAMEMCEF.
PhylomeDBP84022.

Enzyme and pathway databases

Pathway_Interaction_DBhif1_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.
ReactomeREACT_6844. Signaling by TGF beta.

Gene expression databases

ArrayExpressP84022.
BgeeP84022.
CleanExHS_SMAD3.
GenevestigatorP84022.
GermOnlineENSG00000166949. Homo sapiens.

Family and domain databases

InterProIPR013790. 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]
Gene3DG3DSA:3.90.520.10. MAD_MH1. 1 hit.
G3DSA:2.60.200.10. MH2_Dwarfin-type. 1 hit.
PANTHERPTHR13703. Dwarfin. 1 hit.
PfamPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
PROSITEPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio16026.
SOURCESearch...

Entry information

Entry nameSMAD3_HUMAN
AccessionPrimary (citable) accession number: P84022
Secondary accession number(s): A8K4B6 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents