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Protein

Mothers against decapentaplegic homolog 1

Gene

SMAD1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64ZincBy similarity1
Metal bindingi109ZincBy similarity1
Metal bindingi121ZincBy similarity1
Metal bindingi126ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-201451 Signaling by BMP
R-BTA-5689880 Ub-specific processing proteases
R-BTA-8941326 RUNX2 regulates bone development

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):
SMAD family member 1
Short name:
SMAD 1
Short name:
Smad1
Gene namesi
Name:SMAD1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 17

Organism-specific databases

VGNCiVGNC:34974 SMAD1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002602561 – 465Mothers against decapentaplegic homolog 1Add BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei322Phosphothreonine; by MINK1, TNIK and MAP4K4By similarity1
Modified residuei463PhosphoserinePROSITE-ProRule annotationBy similarity1
Modified residuei465PhosphoserinePROSITE-ProRule annotationBy similarity1

Post-translational modificationi

Phosphorylation of the C-terminal SVS motif by BMP type 1 receptor kinase activates SMAD1 by promoting dissociation from the receptor and trimerization with SMAD4 (By similarity). Dephosphorylation, probably by PPM1A, induces its export from the nucleus to the cytoplasm (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ1JQA2
PRIDEiQ1JQA2

Expressioni

Gene expression databases

BgeeiENSBTAG00000002835

Interactioni

Subunit structurei

Interacts with HGS, NANOG and ZCCHC12. Upon C-terminus phosphorylation: forms 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. Found in a complex with SMAD4 and YY1. Found in a macromolecular complex with FAM83G. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a SMAD4-independent manner. Interacts with ZC3H3. Interacts with TMEM119. Interacts (via MH1 and MH2 domains) with ZNF8 (By similarity). Interacts with RANBP3L; the interaction increases when SMAD1 is not phosphorylated and mediates SMAD1 nuclear export (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000003668

Structurei

3D structure databases

ProteinModelPortaliQ1JQA2
SMRiQ1JQA2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 136MH1PROSITE-ProRule annotationAdd BLAST125
Domaini271 – 465MH2PROSITE-ProRule annotationAdd BLAST195

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni418 – 428L3 loopBy similarityAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi39 – 45Poly-Lys7
Compositional biasi198 – 201Poly-Ser4

Domaini

The MH2 domain mediates phosphorylation-dependent trimerization through L3 loop binding of phosphoserines in the adjacent subunit.By similarity

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated

Phylogenomic databases

eggNOGiKOG3701 Eukaryota
ENOG410XQKU LUCA
GeneTreeiENSGT00760000119091
HOGENOMiHOG000286019
HOVERGENiHBG053353
InParanoidiQ1JQA2
KOiK04676
OMAiGTPSKCV
OrthoDBiEOG091G082C
TreeFamiTF314923

Family and domain databases

Gene3Di2.60.200.10, 1 hit
3.90.520.10, 1 hit
InterProiView protein in InterPro
IPR013790 Dwarfin
IPR003619 MAD_homology1_Dwarfin-type
IPR013019 MAD_homology_MH1
IPR017855 SMAD-like_dom_sf
IPR001132 SMAD_dom_Dwarfin-type
IPR008984 SMAD_FHA_dom_sf
IPR036578 SMAD_MH1_sf
PANTHERiPTHR13703 PTHR13703, 1 hit
PfamiView protein in Pfam
PF03165 MH1, 1 hit
PF03166 MH2, 1 hit
SMARTiView protein in SMART
SM00523 DWA, 1 hit
SM00524 DWB, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF56366 SSF56366, 1 hit
PROSITEiView protein in PROSITE
PS51075 MH1, 1 hit
PS51076 MH2, 1 hit

Sequencei

Sequence statusi: Complete.

Q1JQA2-1 [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 PMDTNMMAPS
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):52,250
Last modified:June 13, 2006 - v1
Checksum:i7C2E679F72B15C4F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti62S → G in ABI96185 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ922947 mRNA Translation: ABI96185.1
BC116117 mRNA Translation: AAI16118.1
RefSeqiNP_001069691.2, NM_001076223.2
XP_005217566.1, XM_005217509.2
XP_005217568.1, XM_005217511.2
XP_010812017.1, XM_010813715.2
XP_010812018.1, XM_010813716.2
UniGeneiBt.37151

Genome annotation databases

EnsembliENSBTAT00000003668; ENSBTAP00000003668; ENSBTAG00000002835
GeneIDi540488
KEGGibta:540488

Similar proteinsi

Entry informationi

Entry nameiSMAD1_BOVIN
AccessioniPrimary (citable) accession number: Q1JQA2
Secondary accession number(s): Q06AL6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 13, 2006
Last modified: March 28, 2018
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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