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P97454 (SMAD5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mothers against decapentaplegic homolog 5

Short name=MAD homolog 5
Short name=Mothers against DPP homolog 5
Alternative name(s):
Dwarfin-C
Short name=Dwf-C
SMAD family member 5
Short name=SMAD 5
Short name=Smad5
Short name=mSmad5
Gene names
Name:Smad5
Synonyms:Madh5, Msmad5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) By similarity. Required for angiogenesis.

Subunit structure

May form trimers with the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit and SMURF1. Interacts with SUV39H1 and SUV39H2. Interacts (via MH2 domain) with LEMD3 By similarity. Interacts with WWP1. Ref.7

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 By similarity.

Post-translational modification

Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase.

Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin ligase SMURF1 By similarity.

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 processAngiogenesis
Differentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from genetic interaction PubMed 20843790. Source: BHF-UCL

Mullerian duct regression

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

bone development

Inferred from genetic interaction PubMed 19224984. Source: MGI

cardiac muscle contraction

Inferred from mutant phenotype PubMed 17456754. Source: MGI

cartilage development

Inferred from genetic interaction PubMed 19224984. Source: MGI

cellular response to BMP stimulus

Inferred from genetic interaction PubMed 20843790. Source: BHF-UCL

cellular response to organic cyclic compound

Inferred from direct assay PubMed 19103752. Source: MGI

embryonic pattern specification

Inferred from sequence or structural similarity. Source: UniProtKB

erythrocyte differentiation

Inferred from mutant phenotype PubMed 15591122. Source: MGI

germ cell development

Inferred from mutant phenotype PubMed 11404080. Source: MGI

osteoblast fate commitment

Inferred from genetic interaction PubMed 15150273. Source: MGI

positive regulation of osteoblast differentiation

Inferred from genetic interaction PubMed 15150273. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15557274. Source: MGI

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

Inferred from genetic interaction PubMed 20843790. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay PubMed 18776146. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 11376112. Source: MGI

ureteric bud development

Inferred from expression pattern PubMed 14656760. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19103752. Source: MGI

nucleus

Inferred from direct assay PubMed 12151307. Source: UniProtKB

protein complex

Inferred from sequence orthology PubMed 23610558. Source: MGI

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 18692037. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 12370310PubMed 15150273PubMed 16115198PubMed 21239498. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 465464Mothers against decapentaplegic homolog 5
PRO_0000090866

Regions

Domain13 – 137125MH1
Domain271 – 465195MH2
Compositional bias40 – 467Poly-Lys

Sites

Metal binding651Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1221Zinc By similarity
Metal binding1271Zinc By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue4631Phosphoserine By similarity
Modified residue4651Phosphoserine By similarity

Experimental info

Sequence conflict1961S → P in AAB39737. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P97454 [UniParc].

Last modified May 4, 2001. Version 2.
Checksum: D66B638DA76BC20B

FASTA46552,172
        10         20         30         40         50         60 
MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME ELEKALSSPG 

        70         80         90        100        110        120 
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLDIC EFPFGSKQKE 

       130        140        150        160        170        180 
VCINPYHYKR VESPVLPPVL VPRHNEFNPQ HSLLVQFRNL SHNEPHMPQN ATFPDSFHQP 

       190        200        210        220        230        240 
NNAPFPLSPN SPYPPSPASS TYPNSPASSG PGSPFQLPAD TPPPAYMPPD DQMAPDNSQP 

       250        260        270        280        290        300 
MDTSSNMIPQ TMPSISSRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT 

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

       370        380        390        400        410        420 
NFHHGFHPTT VCKIPSSCSL KIFNNQEFAQ LLAQSVNHGF EAVYELTKMC TIRMSFVKGW 

       430        440        450        460 
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPLNP ISSVS 

« Hide

References

« Hide 'large scale' references
[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].
[2]"The C-terminal domain of Mad-like signal transducers is sufficient for biological activity in the Xenopus embryo and transcriptional activation."
Meersseman G., Verschueren K., Nelles L., Blumenstock C., Kraft H., Wuytens G., Remacle J., Kozak C.A., Tylzanowski P., Niehrs C., Huylebroeck D.
Mech. Dev. 61:127-140(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic organization and expression of mouse Smad5."
Chang H., Kraft H., Verschueren K., Wang P., Huylebroeck D., Matzuk M.M.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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. expand/collapse author list , 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: Spinal cord.
[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].
Tissue: Eye.
[6]"Functions of mammalian Smad genes as revealed by targeted gene disruption in mice."
Weinstein M., Yang X., Deng C.-X.
Cytokine Growth Factor Rev. 11:49-58(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)."
Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., Miyazawa K.
Oncogene 23:6914-6923(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WWP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58993 mRNA. Translation: AAB07871.1.
U77638 mRNA. Translation: AAB39737.1.
AF063006 mRNA. Translation: AAC83580.1.
AK082997 mRNA. Translation: BAC38724.1.
BC050001 mRNA. Translation: AAH50001.2.
CCDSCCDS26565.1.
RefSeqNP_001157513.1. NM_001164041.1.
NP_001157514.1. NM_001164042.1.
NP_032567.1. NM_008541.3.
XP_006517180.1. XM_006517117.1.
XP_006517181.1. XM_006517118.1.
UniGeneMm.272920.

3D structure databases

ProteinModelPortalP97454.
SMRP97454. Positions 10-133, 270-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201278. 13 interactions.
IntActP97454. 2 interactions.
MINTMINT-99279.

PTM databases

PhosphoSiteP97454.

Proteomic databases

PaxDbP97454.
PRIDEP97454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069557; ENSMUSP00000065798; ENSMUSG00000021540.
ENSMUST00000109874; ENSMUSP00000105500; ENSMUSG00000021540.
ENSMUST00000109876; ENSMUSP00000105502; ENSMUSG00000021540.
GeneID17129.
KEGGmmu:17129.
UCSCuc007qsw.2. mouse.

Organism-specific databases

CTD4090.
MGIMGI:1328787. Smad5.

Phylogenomic databases

eggNOGNOG330956.
GeneTreeENSGT00600000084186.
HOGENOMHOG000286018.
HOVERGENHBG053353.
InParanoidP97454.
KOK16790.
OMANRVGEAY.
OrthoDBEOG7W1540.
PhylomeDBP97454.
TreeFamTF314923.

Gene expression databases

BgeeP97454.
CleanExMM_SMAD5.
GenevestigatorP97454.

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

NextBio291320.
PROP97454.
SOURCESearch...

Entry information

Entry nameSMAD5_MOUSE
AccessionPrimary (citable) accession number: P97454
Secondary accession number(s): P70341, Q810K0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 4, 2001
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot