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Protein

Mothers against decapentaplegic homolog 1

Gene

Smad1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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) (By similarity). May play a role in the initiation and maintenance of spermatogenesis. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By similarity). May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343).By similarity1 Publication

Sites

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

GO - Molecular functioni

GO - Biological processi

  • BMP signaling pathway Source: UniProtKB
  • bone development Source: MGI
  • cardiac muscle cell proliferation Source: MGI
  • cartilage development Source: MGI
  • cellular response to BMP stimulus Source: BHF-UCL
  • cellular response to organic cyclic compound Source: MGI
  • embryonic pattern specification Source: UniProtKB
  • gamete generation Source: MGI
  • hindbrain development Source: MGI
  • homeostatic process Source: MGI
  • inflammatory response Source: UniProtKB
  • MAPK cascade Source: MGI
  • mesodermal cell fate commitment Source: MGI
  • midbrain development Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of muscle cell apoptotic process Source: Ensembl
  • osteoblast fate commitment Source: MGI
  • positive regulation of cartilage development Source: MGI
  • positive regulation of dendrite morphogenesis Source: Ensembl
  • positive regulation of gene expression Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: BHF-UCL
  • protein phosphorylation Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to drug Source: Ensembl
  • response to organonitrogen compound Source: Ensembl
  • SMAD protein complex assembly Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: InterPro
  • ureteric bud development Source: UniProtKB
  • 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_334226. 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):
Dwarfin-A
Short name:
Dwf-A
Mothers-against-DPP-related 1
Short name:
Mad-related protein 1
Short name:
mMad1
SMAD family member 1
Short name:
SMAD 1
Short name:
Smad1
Gene namesi
Name:Smad1
Synonyms:Madh1, Madr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109452. Smad1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4. Colocalizes with LEMD3 at the nucleus inner membrane (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nuclear inner membrane Source: MGI
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Mothers against decapentaplegic homolog 1PRO_0000090848Add
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 annotation
Modified residuei465 – 4651PhosphoserinePROSITE-ProRule annotation

Post-translational modificationi

hosphorylation 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

MaxQBiP70340.
PaxDbiP70340.
PRIDEiP70340.

PTM databases

PhosphoSiteiP70340.

Expressioni

Tissue specificityi

Ubiquitous.

Developmental stagei

Ubiquitously expressed during embryogenesis. Expression starts in some seminiferous tubules at 2 weeks of age. After mid-puberty a stage-specific expression is established. During the cycling of the seminiferous epithelium, expression initiates in the pachytene spermatocytes of stage V seminiferous tubules, peaks at stage X, then decreases as pachytene spermatocytes differentiate into secondary spermatocytes and then round spermatids.

Gene expression databases

BgeeiP70340.
CleanExiMM_SMAD1.
ExpressionAtlasiP70340. baseline and differential.
GenevisibleiP70340. MM.

Interactioni

Subunit structurei

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 (By similarity). Also interacts with HGS, NANOG and ZCCHC12. Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity). Found in a complex with SMAD4 and YY1. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a SMAD4-independent manner.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Map3k7Q620733EBI-6992047,EBI-1775345

Protein-protein interaction databases

BioGridi201274. 35 interactions.
IntActiP70340. 7 interactions.
MINTiMINT-99213.
STRINGi10090.ENSMUSP00000071035.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 198Combined sources
Helixi25 – 4117Combined sources
Helixi47 – 5610Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 773Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 929Combined sources
Helixi100 – 1023Combined sources
Beta strandi103 – 1053Combined sources
Helixi113 – 1153Combined sources
Beta strandi118 – 1214Combined sources
Helixi124 – 1263Combined sources
Beta strandi127 – 1293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KMPX-ray2.70A/B9-132[»]
ProteinModelPortaliP70340.
SMRiP70340. Positions 9-132, 268-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70340.

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

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

eggNOGiNOG330956.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286018.
HOVERGENiHBG053353.
InParanoidiP70340.
KOiK04676.
OMAiMTHDTSQ.
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.

P70340-1 [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 SYPNSPGGSS
210 220 230 240 250
STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMAQDGSQ PMDTNMMAPP
260 270 280 290 300
LPAEISRGDV 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):52,157
Last modified:July 27, 2011 - v2
Checksum:i07A56FBEE79A1C2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951P → S in AAC52785 (PubMed:8799132).Curated
Sequence conflicti95 – 951P → S in AAG41407 (PubMed:11111041).Curated
Sequence conflicti142 – 1421R → K in AAC52785 (PubMed:8799132).Curated
Sequence conflicti142 – 1421R → K in AAG41407 (PubMed:11111041).Curated
Sequence conflicti199 – 2002SS → QG in AAB18256 (PubMed:9076678).Curated
Sequence conflicti393 – 3931A → E in AAB18256 (PubMed:9076678).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58992 mRNA. Translation: AAC52785.1.
U74359 mRNA. Translation: AAB18256.1.
AF295768
, AF295763, AF295764, AF295765, AF295766, AF295767 Genomic DNA. Translation: AAG41407.1.
AK017583 mRNA. Translation: BAB30820.1.
AK054104 mRNA. Translation: BAC35658.1.
BC058693 mRNA. Translation: AAH58693.1.
CCDSiCCDS22437.1.
RefSeqiNP_032565.2. NM_008539.3.
XP_006530809.1. XM_006530746.2.
UniGeneiMm.223717.

Genome annotation databases

EnsembliENSMUST00000066091; ENSMUSP00000071035; ENSMUSG00000031681.
GeneIDi17125.
KEGGimmu:17125.
UCSCiuc009mip.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58992 mRNA. Translation: AAC52785.1.
U74359 mRNA. Translation: AAB18256.1.
AF295768
, AF295763, AF295764, AF295765, AF295766, AF295767 Genomic DNA. Translation: AAG41407.1.
AK017583 mRNA. Translation: BAB30820.1.
AK054104 mRNA. Translation: BAC35658.1.
BC058693 mRNA. Translation: AAH58693.1.
CCDSiCCDS22437.1.
RefSeqiNP_032565.2. NM_008539.3.
XP_006530809.1. XM_006530746.2.
UniGeneiMm.223717.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KMPX-ray2.70A/B9-132[»]
ProteinModelPortaliP70340.
SMRiP70340. Positions 9-132, 268-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201274. 35 interactions.
IntActiP70340. 7 interactions.
MINTiMINT-99213.
STRINGi10090.ENSMUSP00000071035.

PTM databases

PhosphoSiteiP70340.

Proteomic databases

MaxQBiP70340.
PaxDbiP70340.
PRIDEiP70340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066091; ENSMUSP00000071035; ENSMUSG00000031681.
GeneIDi17125.
KEGGimmu:17125.
UCSCiuc009mip.2. mouse.

Organism-specific databases

CTDi4086.
MGIiMGI:109452. Smad1.

Phylogenomic databases

eggNOGiNOG330956.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286018.
HOVERGENiHBG053353.
InParanoidiP70340.
KOiK04676.
OMAiMTHDTSQ.
OrthoDBiEOG7W1540.
TreeFamiTF314923.

Enzyme and pathway databases

ReactomeiREACT_334226. Signaling by BMP.

Miscellaneous databases

ChiTaRSiSmad1. mouse.
EvolutionaryTraceiP70340.
NextBioi291304.
PROiP70340.
SOURCEiSearch...

Gene expression databases

BgeeiP70340.
CleanExiMM_SMAD1.
ExpressionAtlasiP70340. baseline and differential.
GenevisibleiP70340. MM.

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. "Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth."
    Yingling J.M., Das P., Savage C., Zhang M., Padgett R.W., Wang X.-F.
    Proc. Natl. Acad. Sci. U.S.A. 93:8940-8944(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Evidence that Mothers-against-dpp-related 1 (Madr1) plays a role in the initiation and maintenance of spermatogenesis in the mouse."
    Zhao G.-Q., Hogan B.L.M.
    Mech. Dev. 61:63-73(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryonic heart.
  3. "Characterization of the mouse Smad1 gene and its expression pattern in adult mouse tissues."
    Huang S., Flanders K.C., Roberts A.B.
    Gene 258:43-53(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Oviduct.
  5. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA."
    Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J., Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.
    Mol. Cell. Biol. 20:9346-9355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HGS.
  7. "SMAD-mediated modulation of YY1 activity regulates the BMP response and cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5 enhancer."
    Lee K.H., Evans S., Ruan T.Y., Lassar A.B.
    Development 131:4709-4723(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SMAD4 AND YY1.
  8. "Nanog binds to Smad1 and blocks bone morphogenetic protein-induced differentiation of embryonic stem cells."
    Suzuki A., Raya A., Kawakami Y., Morita M., Matsui T., Nakashima K., Gage F.H., Rodriguez-Esteban C., Izpisua Belmonte J.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10294-10299(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NANOG.
  9. "Sizn1 is a novel protein that functions as a transcriptional coactivator of bone morphogenic protein signaling."
    Cho G., Lim Y., Zand D., Golden J.A.
    Mol. Cell. Biol. 28:1565-1572(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZCCHC12.
  10. "Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of BMP and TGF-beta effectors."
    Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S., Jauch R., Kolatkar P.R.
    Nucleic Acids Res. 38:3477-3488(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 9-132 IN COMPLEX WITH DNA, ZINC_BINDING SITES, SUBUNIT.

Entry informationi

Entry nameiSMAD1_MOUSE
AccessioniPrimary (citable) accession number: P70340
Secondary accession number(s): P70442, Q6GT95, Q9CYK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.