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Q15797

- SMAD1_HUMAN

UniProt

Q15797 - SMAD1_HUMAN

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Protein

Mothers against decapentaplegic homolog 1

Gene

SMAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641ZincBy similarity
Metal bindingi109 – 1091ZincBy similarity
Metal bindingi121 – 1211ZincBy similarity
Metal bindingi126 – 1261ZincBy similarity

GO - Molecular functioni

  1. co-SMAD binding Source: BHF-UCL
  2. identical protein binding Source: BHF-UCL
  3. I-SMAD binding Source: BHF-UCL
  4. metal ion binding Source: UniProtKB-KW
  5. protein kinase binding Source: UniProtKB
  6. receptor signaling protein activity Source: UniProtKB
  7. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  8. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  9. transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: BHF-UCL

GO - Biological processi

  1. BMP signaling pathway Source: UniProtKB
  2. bone development Source: Ensembl
  3. cardiac muscle cell proliferation Source: Ensembl
  4. cartilage development Source: Ensembl
  5. cellular response to BMP stimulus Source: BHF-UCL
  6. embryonic pattern specification Source: UniProtKB
  7. gamete generation Source: Ensembl
  8. hindbrain development Source: Ensembl
  9. homeostatic process Source: Ensembl
  10. inflammatory response Source: Ensembl
  11. MAPK cascade Source: Ensembl
  12. mesodermal cell fate commitment Source: Ensembl
  13. midbrain development Source: Ensembl
  14. negative regulation of cell proliferation Source: Ensembl
  15. negative regulation of muscle cell apoptotic process Source: Ensembl
  16. osteoblast fate commitment Source: Ensembl
  17. positive regulation of cartilage development Source: Ensembl
  18. positive regulation of dendrite morphogenesis Source: Ensembl
  19. positive regulation of gene expression Source: BHF-UCL
  20. positive regulation of osteoblast differentiation Source: Ensembl
  21. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  22. positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: BHF-UCL
  23. primary miRNA processing Source: BHF-UCL
  24. protein phosphorylation Source: Ensembl
  25. response to drug Source: Ensembl
  26. response to organonitrogen compound Source: Ensembl
  27. signal transduction Source: UniProtKB
  28. SMAD protein complex assembly Source: BHF-UCL
  29. transcription, DNA-templated Source: UniProtKB-KW
  30. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  31. ureteric bud development Source: Ensembl
  32. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.
SignaLinkiQ15797.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SMAD1
Synonyms:BSP1, MADH1, MADR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:6767. SMAD1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. integral component of membrane Source: UniProtKB
  4. intracellular Source: UniProtKB
  5. mitochondrion Source: HPA
  6. nuclear inner membrane Source: UniProtKB
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
  9. protein complex Source: MGI
  10. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi419 – 4191G → S: Loss of phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA30524.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Mothers against decapentaplegic homolog 1PRO_0000090847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei322 – 3221Phosphothreonine; by MINK1, TNIK and MAP4K41 Publication
Modified residuei463 – 4631Phosphoserine1 PublicationPROSITE-ProRule annotation
Modified residuei465 – 4651Phosphoserine1 PublicationPROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated on serine by BMP type 1 receptor kinase.2 Publications
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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15797.
PaxDbiQ15797.
PRIDEiQ15797.

PTM databases

PhosphoSiteiQ15797.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ15797.
CleanExiHS_SMAD1.
ExpressionAtlasiQ15797. baseline and differential.
GenevestigatoriQ15797.

Organism-specific databases

HPAiCAB005389.
HPA045647.

Interactioni

Subunit structurei

Found in a complex with SMAD4 and YY1. 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. Found in a macromolecular complex with FAM83G. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a SMAD4-independent manner.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP102756EBI-1567153,EBI-608057
GSK3BP498412EBI-1567153,EBI-373586
SMAD4Q134852EBI-1567153,EBI-347263
SMURF1Q9HCE74EBI-1567153,EBI-976466
UCHL3P153742EBI-1567153,EBI-954554
YAP1P469373EBI-1567153,EBI-1044059

Protein-protein interaction databases

BioGridi110261. 116 interactions.
DIPiDIP-38538N.
IntActiQ15797. 55 interactions.
MINTiMINT-244113.
STRINGi9606.ENSP00000305769.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi272 – 2787
Beta strandi291 – 2999
Beta strandi305 – 3106
Helixi321 – 3277
Beta strandi334 – 3385
Beta strandi340 – 3478
Beta strandi349 – 3513
Beta strandi353 – 3564
Helixi358 – 3636
Beta strandi372 – 3743
Beta strandi379 – 3846
Helixi385 – 3939
Turni394 – 3985
Helixi400 – 4045
Helixi405 – 4106
Beta strandi411 – 4177
Helixi429 – 4313
Beta strandi432 – 4409
Helixi441 – 45111
Beta strandi461 – 4633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3Q47X-ray1.70C456-464[»]
3Q4AX-ray1.54C456-465[»]
ProteinModelPortaliQ15797.
SMRiQ15797. Positions 9-132, 268-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 136125MH1PROSITE-ProRule annotationAdd
BLAST
Domaini271 – 465195MH2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 457Poly-Lys
Compositional biasi198 – 2014Poly-Ser

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG330956.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiQ15797.
KOiK04676.
OMAiPRNSEFN.
PhylomeDBiQ15797.
TreeFamiTF314923.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProiIPR013790. 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]
PANTHERiPTHR13703. PTHR13703. 1 hit.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 1 hit.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15797-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE
60 70 80 90 100
LEKALSCPGQ PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH
110 120 130 140 150
HELKPLECCE FPFGSKQKEV CINPYHYKRV ESPVLPPVLV PRHSEYNPQH
160 170 180 190 200
SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN SHPFPHSPNS SYPNSPGSSS
210 220 230 240 250
STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMTQDGSQ PMDTNMMAPP
260 270 280 290 300
LPSEINRGDV QAVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
310 320 330 340 350
DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD
360 370 380 390 400
SSIFVQSRNC NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF
410 420 430 440 450
ETVYELTKMC TIRMSFVKGW GAEYHRQDVT STPCWIEIHL HGPLQWLDKV
460
LTQMGSPHNP ISSVS
Length:465
Mass (Da):52,260
Last modified:November 1, 1996 - v1
Checksum:i2DD34B7F434DBC7E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31V → A Found in a patient with primary pulmonary hypertension; unknown pathological significance; affects SMAD-mediated signaling. 1 Publication
VAR_066869

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3765.1.
PIRiS68987.
RefSeqiNP_001003688.1. NM_001003688.1.
NP_005891.1. NM_005900.2.
XP_005263048.1. XM_005262991.1.
XP_005263049.1. XM_005262992.2.
XP_006714280.1. XM_006714217.1.
UniGeneiHs.604588.

Genome annotation databases

EnsembliENST00000302085; ENSP00000305769; ENSG00000170365.
ENST00000394092; ENSP00000377652; ENSG00000170365.
ENST00000515385; ENSP00000426568; ENSG00000170365.
GeneIDi4086.
KEGGihsa:4086.
UCSCiuc003ikc.3. human.

Polymorphism databases

DMDMi13633915.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3765.1.
PIRi S68987.
RefSeqi NP_001003688.1. NM_001003688.1.
NP_005891.1. NM_005900.2.
XP_005263048.1. XM_005262991.1.
XP_005263049.1. XM_005262992.2.
XP_006714280.1. XM_006714217.1.
UniGenei Hs.604588.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KHU X-ray 2.50 A/B/C/D 248-465 [» ]
2LAW NMR - B 222-233 [» ]
2LAX NMR - B 201-209 [» ]
2LAY NMR - B 201-209 [» ]
2LAZ NMR - B 210-217 [» ]
2LB0 NMR - B 208-217 [» ]
2LB1 NMR - B 221-233 [» ]
3Q47 X-ray 1.70 C 456-464 [» ]
3Q4A X-ray 1.54 C 456-465 [» ]
ProteinModelPortali Q15797.
SMRi Q15797. Positions 9-132, 268-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110261. 116 interactions.
DIPi DIP-38538N.
IntActi Q15797. 55 interactions.
MINTi MINT-244113.
STRINGi 9606.ENSP00000305769.

PTM databases

PhosphoSitei Q15797.

Polymorphism databases

DMDMi 13633915.

Proteomic databases

MaxQBi Q15797.
PaxDbi Q15797.
PRIDEi Q15797.

Protocols and materials databases

DNASUi 4086.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302085 ; ENSP00000305769 ; ENSG00000170365 .
ENST00000394092 ; ENSP00000377652 ; ENSG00000170365 .
ENST00000515385 ; ENSP00000426568 ; ENSG00000170365 .
GeneIDi 4086.
KEGGi hsa:4086.
UCSCi uc003ikc.3. human.

Organism-specific databases

CTDi 4086.
GeneCardsi GC04P146402.
HGNCi HGNC:6767. SMAD1.
HPAi CAB005389.
HPA045647.
MIMi 601595. gene.
neXtProti NX_Q15797.
PharmGKBi PA30524.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG330956.
GeneTreei ENSGT00760000119091.
HOGENOMi HOG000286019.
HOVERGENi HBG053353.
InParanoidi Q15797.
KOi K04676.
OMAi PRNSEFN.
PhylomeDBi Q15797.
TreeFami TF314923.

Enzyme and pathway databases

Reactomei REACT_12034. Signaling by BMP.
SignaLinki Q15797.

Miscellaneous databases

EvolutionaryTracei Q15797.
GeneWikii Mothers_against_decapentaplegic_homolog_1.
GenomeRNAii 4086.
NextBioi 16014.
PROi Q15797.
SOURCEi Search...

Gene expression databases

Bgeei Q15797.
CleanExi HS_SMAD1.
ExpressionAtlasi Q15797. baseline and differential.
Genevestigatori Q15797.

Family and domain databases

Gene3Di 2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR13703. PTHR13703. 1 hit.
Pfami PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view ]
SMARTi SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 1 hit.
PROSITEi PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. Cited for: REVIEW.
  16. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: PHOSPHORYLATION AT THR-322.
  23. 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. Cited for: POSSIBLE INVOLVEMENT IN PULMONARY HYPERTENSION, VARIANT ALA-3, CHARACTERIZATION OF VARIANT ALA-3.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Protein associated with SMAD1 (PAWS1/FAM83G) is a substrate for type I bone morphogenetic protein receptors and modulates bone morphogenetic protein signalling."
    Vogt J., Dingwell K.S., Herhaus L., Gourlay R., Macartney T., Campbell D., Smith J.C., Sapkota G.P.
    Open Biol. 4:130210-130210(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM83G.

Entry informationi

Entry nameiSMAD1_HUMAN
AccessioniPrimary (citable) accession number: Q15797
Secondary accession number(s): A8KAJ0, D3DNZ9, Q16636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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