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Protein

Mothers against decapentaplegic homolog 1

Gene

SMAD1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641ZincBy similarity
Metal bindingi109 – 1091ZincBy similarity
Metal bindingi121 – 1211ZincBy similarity
Metal bindingi126 – 1261ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-201451. Signaling by BMP.

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

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. Colocalizes with LEMD3 at the nucleus inner membrane (By similarity). Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Mothers against decapentaplegic homolog 1PRO_0000260256Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei322 – 3221Phosphothreonine; by MINK1, TNIK and MAP4K4By similarity
Modified residuei463 – 4631PhosphoserinePROSITE-ProRule annotationBy similarity
Modified residuei465 – 4651PhosphoserinePROSITE-ProRule annotationBy similarity

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
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.

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.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000003668.

Structurei

3D structure databases

ProteinModelPortaliQ1JQA2.
SMRiQ1JQA2. Positions 9-132, 268-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni418 – 42811L3 loopBy similarityAdd
BLAST

Compositional bias

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

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
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3701. Eukaryota.
ENOG410XQKU. LUCA.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiQ1JQA2.
KOiK04676.
OMAiRNIGQNE.
OrthoDBiEOG7W1540.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621S → G in ABI96185 (Ref. 1) Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ1JQA2.
SMRiQ1JQA2. Positions 9-132, 268-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000003668.

Proteomic databases

PaxDbiQ1JQA2.
PRIDEiQ1JQA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000003668; ENSBTAP00000003668; ENSBTAG00000002835.
GeneIDi540488.
KEGGibta:540488.

Organism-specific databases

CTDi4086.

Phylogenomic databases

eggNOGiKOG3701. Eukaryota.
ENOG410XQKU. LUCA.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiQ1JQA2.
KOiK04676.
OMAiRNIGQNE.
OrthoDBiEOG7W1540.
TreeFamiTF314923.

Enzyme and pathway databases

ReactomeiR-BTA-201451. Signaling by BMP.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and bioinformatic analysis of cDNA encoding cattle Smad1 gene."
    Zhang X., Xu S.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Ascending colon.

Entry informationi

Entry nameiSMAD1_BOVIN
AccessioniPrimary (citable) accession number: Q1JQA2
Secondary accession number(s): Q06AL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 13, 2006
Last modified: June 8, 2016
This is version 87 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.