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Q15797 (SMAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mothers against decapentaplegic homolog 1

Short name=MAD homolog 1
Short name=Mothers against DPP homolog 1
Alternative name(s):
JV4-1
Mad-related protein 1
SMAD family member 1
Short name=SMAD 1
Short name=Smad1
Short name=hSMAD1
Transforming growth factor-beta-signaling protein 1
Short name=BSP-1
Gene names
Name:SMAD1
Synonyms:BSP1, MADH1, MADR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.17

Subunit structure

Interacts with HGS, NANOG and ZCCHC12 By similarity. May form 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. Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. Co-localizes with LEMD3 at the nucleus inner membrane. Ref.19 Ref.24

Tissue specificity

Ubiquitous. Highest expression seen in the heart and skeletal muscle.

Post-translational modification

Phosphorylated on serine by BMP type 1 receptor kinase. Ref.11 Ref.22

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. Ref.23

Involvement in disease

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.

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
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

MAPK cascade

Inferred from electronic annotation. Source: Ensembl

SMAD protein complex assembly

Inferred from direct assay PubMed 9111321. Source: BHF-UCL

bone development

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

cellular response to BMP stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic pattern specification

Inferred from sequence or structural similarity. Source: UniProtKB

gamete generation

Inferred from electronic annotation. Source: Ensembl

hindbrain development

Inferred from electronic annotation. Source: Ensembl

homeostatic process

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

mesodermal cell fate commitment

Inferred from electronic annotation. Source: Ensembl

midbrain development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

osteoblast fate commitment

Inferred from electronic annotation. Source: Ensembl

positive regulation of cartilage development

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from direct assay PubMed 19664780. Source: BHF-UCL

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred by curator PubMed 19664780. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

primary miRNA processing

Traceable author statement PubMed 19018011. Source: BHF-UCL

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement Ref.12. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Non-traceable author statement Ref.4. Source: UniProtKB

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 9389648. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

integral component of membrane

Non-traceable author statement Ref.4. Source: UniProtKB

intracellular

Non-traceable author statement Ref.13. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nuclear inner membrane

Inferred from direct assay Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.12. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 23610558. Source: MGI

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionI-SMAD binding

Inferred from physical interaction PubMed 9436979. Source: BHF-UCL

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

co-SMAD binding

Inferred from physical interaction PubMed 9111321. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 9111321. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase binding

Inferred from physical interaction PubMed 12874272. Source: UniProtKB

receptor signaling protein activity

Non-traceable author statement Ref.16Ref.3. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 9389648. Source: BHF-UCL

transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity

Traceable author statement PubMed 19018011. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Mothers against decapentaplegic homolog 1
PRO_0000090847

Regions

Domain12 – 136125MH1
Domain271 – 465195MH2
Compositional bias39 – 457Poly-Lys
Compositional bias198 – 2014Poly-Ser

Sites

Metal binding641Zinc By similarity
Metal binding1091Zinc By similarity
Metal binding1211Zinc By similarity
Metal binding1261Zinc By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue3221Phosphothreonine; by MINK1, TNIK and MAP4K4 Ref.22
Modified residue4631Phosphoserine Ref.11
Modified residue4651Phosphoserine Ref.11

Natural variations

Natural variant31V → A Found in a patient with primary pulmonary hypertension; unknown pathological significance; affects SMAD-mediated signaling. Ref.25
VAR_066869

Experimental info

Mutagenesis4191G → S: Loss of phosphorylation. Ref.3

Secondary structure

................................. 465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15797 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2DD34B7F434DBC7E

FASTA46552,260
        10         20         30         40         50         60 
MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE LEKALSCPGQ 

        70         80         90        100        110        120 
PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH HELKPLECCE FPFGSKQKEV 

       130        140        150        160        170        180 
CINPYHYKRV ESPVLPPVLV PRHSEYNPQH SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN 

       190        200        210        220        230        240 
SHPFPHSPNS SYPNSPGSSS STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMTQDGSQ 

       250        260        270        280        290        300 
PMDTNMMAPP LPSEINRGDV QAVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT 

       310        320        330        340        350        360 
DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC 

       370        380        390        400        410        420 
NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF ETVYELTKMC TIRMSFVKGW 

       430        440        450        460 
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPHNP ISSVS 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A human Mad protein acting as a BMP-regulated transcriptional activator."
Liu F., Hata A., Baker J.C., Doody J., Carcamo J., Harland R.M., Massague J.
Nature 381:620-623(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"MADR1, a MAD-related protein that functions in BMP2 signaling pathways."
Hoodless P.A., Haerry T., Abdollah S., Stapleton M., O'Connor M.B., Attisano L., Wrana J.L.
Cell 85:489-500(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLY-419.
[4]"Serine phosphorylation, chromosomal localization, and transforming growth factor-beta signal transduction by human bsp-1."
Lechleider R.J., de Caestecker M.P., Dehejia A., Polymeropoulos M.H., Roberts A.B.
J. Biol. Chem. 271:17617-17620(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[10]Bienvenut W.V., Lempens A., Norman J.C.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-15; 33-39; 129-157; 283-306 AND 309-319, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[11]"The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase."
Kretzschmar M., Liu F., Hata A., Doody J., Massague J.
Genes Dev. 11:984-995(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-463 AND SER-465.
[12]"TGF-beta signal transduction."
Massague J.
Annu. Rev. Biochem. 67:753-791(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"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] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-Smad and Olf signaling pathways."
Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A., Massague J.
Cell 100:229-240(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF423.
[15]"The Smad pathway."
Wrana J.L., Attisano L.
Cytokine Growth Factor Rev. 11:5-13(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"TGF-beta signaling by Smad proteins."
Miyazono K.
Cytokine Growth Factor Rev. 11:15-22(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
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.
BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PSMB4 AND OAZ1, FUNCTION.
[18]"Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse Evi3, is highly expressed in primitive human hematopoietic cells."
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.
Blood 103:2062-2070(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF521.
[19]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LEMD3.
[20]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKOR1.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Smad inhibition by the Ste20 kinase Misshapen."
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K., Mao J., Ip Y.T., Xu L.
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-322.
[23]"USP15 is a deubiquitylating enzyme for receptor-activated SMADs."
Inui M., Manfrin A., Mamidi A., Martello G., Morsut L., Soligo S., Enzo E., Moro S., Polo S., Dupont S., Cordenonsi M., Piccolo S.
Nat. Cell Biol. 13:1368-1375(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15, DNA-BINDING, INTERACTION WITH USP15.
[24]"Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[25]"Molecular genetic characterization of SMAD signaling molecules in pulmonary arterial hypertension."
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. expand/collapse author list , Humbert M., Morrell N.W., Trembath R.C., Machado R.D.
Hum. Mutat. 32:1385-1389(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN PULMONARY HYPERTENSION, VARIANT ALA-3, CHARACTERIZATION OF VARIANT ALA-3.
[26]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59912 mRNA. Translation: AAC50790.1.
U59423 mRNA. Translation: AAB06852.1.
U54826 mRNA. Translation: AAC50493.1.
U57456 mRNA. Translation: AAC50621.1.
BT007386 mRNA. Translation: AAP36050.1.
AK293055 mRNA. Translation: BAF85744.1.
CH471056 Genomic DNA. Translation: EAX05037.1.
CH471056 Genomic DNA. Translation: EAX05038.1.
CH471056 Genomic DNA. Translation: EAX05040.1.
BC001878 mRNA. Translation: AAH01878.1.
PIRS68987.
RefSeqNP_001003688.1. NM_001003688.1.
NP_005891.1. NM_005900.2.
XP_005263048.1. XM_005262991.1.
XP_005263049.1. XM_005262992.2.
UniGeneHs.604588.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KHUX-ray2.50A/B/C/D248-465[»]
2LAWNMR-B222-233[»]
2LAXNMR-B201-209[»]
2LAYNMR-B201-209[»]
2LAZNMR-B210-217[»]
2LB0NMR-B208-217[»]
2LB1NMR-B221-233[»]
ProteinModelPortalQ15797.
SMRQ15797. Positions 9-132, 268-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110261. 117 interactions.
DIPDIP-38538N.
IntActQ15797. 54 interactions.
MINTMINT-244113.
STRING9606.ENSP00000305769.

PTM databases

PhosphoSiteQ15797.

Polymorphism databases

DMDM13633915.

Proteomic databases

PaxDbQ15797.
PRIDEQ15797.

Protocols and materials databases

DNASU4086.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302085; ENSP00000305769; ENSG00000170365.
ENST00000394092; ENSP00000377652; ENSG00000170365.
ENST00000515385; ENSP00000426568; ENSG00000170365.
GeneID4086.
KEGGhsa:4086.
UCSCuc003ikc.3. human.

Organism-specific databases

CTD4086.
GeneCardsGC04P146402.
HGNCHGNC:6767. SMAD1.
HPACAB005389.
HPA045647.
MIM601595. gene.
neXtProtNX_Q15797.
PharmGKBPA30524.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG330956.
HOGENOMHOG000286019.
HOVERGENHBG053353.
InParanoidQ15797.
KOK04676.
OMAPRNSEFN.
PhylomeDBQ15797.
TreeFamTF314923.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ15797.

Gene expression databases

ArrayExpressQ15797.
BgeeQ15797.
CleanExHS_SMAD1.
GenevestigatorQ15797.

Family and domain databases

Gene3D2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
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]
PANTHERPTHR13703. PTHR13703. 1 hit.
PfamPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 1 hit.
PROSITEPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15797.
GeneWikiMothers_against_decapentaplegic_homolog_1.
GenomeRNAi4086.
NextBio16014.
PROQ15797.
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Entry information

Entry nameSMAD1_HUMAN
AccessionPrimary (citable) accession number: Q15797
Secondary accession number(s): A8KAJ0, D3DNZ9, Q16636
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM