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P97454

- SMAD5_MOUSE

UniProt

P97454 - SMAD5_MOUSE

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Protein
Mothers against decapentaplegic homolog 5
Gene
Smad5, Madh5, Msmad5
Organism
Mus musculus (Mouse)
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. SMAD5 is a receptor-regulated SMAD (R-SMAD) By similarity. Required for angiogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Zinc By similarity
Metal bindingi110 – 1101Zinc By similarity
Metal bindingi122 – 1221Zinc By similarity
Metal bindingi127 – 1271Zinc By similarity

GO - Molecular functioni

  1. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: MGI
  4. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. BMP signaling pathway Source: BHF-UCL
  2. Mullerian duct regression Source: Ensembl
  3. angiogenesis Source: UniProtKB-KW
  4. bone development Source: MGI
  5. cardiac muscle contraction Source: MGI
  6. cartilage development Source: MGI
  7. cellular response to BMP stimulus Source: BHF-UCL
  8. cellular response to organic cyclic compound Source: MGI
  9. embryonic pattern specification Source: UniProtKB
  10. erythrocyte differentiation Source: MGI
  11. germ cell development Source: MGI
  12. osteoblast fate commitment Source: MGI
  13. positive regulation of osteoblast differentiation Source: MGI
  14. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  15. positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: BHF-UCL
  16. protein phosphorylation Source: MGI
  17. transcription, DNA-templated Source: UniProtKB-KW
  18. transforming growth factor beta receptor signaling pathway Source: MGI
  19. ureteric bud development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_220505. Signaling by BMP.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Smad5
Synonyms:Madh5, Msmad5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1328787. Smad5.

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 By similarity.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: UniProtKB
  3. protein complex Source: MGI
  4. transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 465464Mothers against decapentaplegic homolog 5
PRO_0000090866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine By similarity
Modified residuei463 – 4631Phosphoserine By similarity
Modified residuei465 – 4651Phosphoserine By similarity

Post-translational modificationi

Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase.
Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin ligase SMURF1 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP97454.
PRIDEiP97454.

PTM databases

PhosphoSiteiP97454.

Expressioni

Gene expression databases

BgeeiP97454.
CleanExiMM_SMAD5.
GenevestigatoriP97454.

Interactioni

Subunit structurei

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 WWP1.1 Publication

Protein-protein interaction databases

BioGridi201278. 13 interactions.
IntActiP97454. 2 interactions.
MINTiMINT-99279.

Structurei

3D structure databases

ProteinModelPortaliP97454.
SMRiP97454. Positions 10-133, 270-453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 137125MH1
Add
BLAST
Domaini271 – 465195MH2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 467Poly-Lys

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.

Phylogenomic databases

eggNOGiNOG330956.
GeneTreeiENSGT00600000084186.
HOGENOMiHOG000286018.
HOVERGENiHBG053353.
InParanoidiP97454.
KOiK16790.
OMAiNRVGEAY.
OrthoDBiEOG7W1540.
PhylomeDBiP97454.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97454-1 [UniParc]FASTAAdd to Basket

« Hide

MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME    50
ELEKALSSPG QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS 100
HHELKPLDIC EFPFGSKQKE VCINPYHYKR VESPVLPPVL VPRHNEFNPQ 150
HSLLVQFRNL SHNEPHMPQN ATFPDSFHQP NNAPFPLSPN SPYPPSPASS 200
TYPNSPASSG PGSPFQLPAD TPPPAYMPPD DQMAPDNSQP MDTSSNMIPQ 250
TMPSISSRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT 300
DPSNNKSRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD 350
SSIFVQSRNC NFHHGFHPTT VCKIPSSCSL KIFNNQEFAQ LLAQSVNHGF 400
EAVYELTKMC TIRMSFVKGW GAEYHRQDVT STPCWIEIHL HGPLQWLDKV 450
LTQMGSPLNP ISSVS 465
Length:465
Mass (Da):52,172
Last modified:May 4, 2001 - v2
Checksum:iD66B638DA76BC20B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961S → P in AAB39737. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26565.1.
RefSeqiNP_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.
UniGeneiMm.272920.

Genome annotation databases

EnsembliENSMUST00000069557; ENSMUSP00000065798; ENSMUSG00000021540.
ENSMUST00000109874; ENSMUSP00000105500; ENSMUSG00000021540.
ENSMUST00000109876; ENSMUSP00000105502; ENSMUSG00000021540.
GeneIDi17129.
KEGGimmu:17129.
UCSCiuc007qsw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26565.1.
RefSeqi NP_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.
UniGenei Mm.272920.

3D structure databases

ProteinModelPortali P97454.
SMRi P97454. Positions 10-133, 270-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201278. 13 interactions.
IntActi P97454. 2 interactions.
MINTi MINT-99279.

PTM databases

PhosphoSitei P97454.

Proteomic databases

PaxDbi P97454.
PRIDEi P97454.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000069557 ; ENSMUSP00000065798 ; ENSMUSG00000021540 .
ENSMUST00000109874 ; ENSMUSP00000105500 ; ENSMUSG00000021540 .
ENSMUST00000109876 ; ENSMUSP00000105502 ; ENSMUSG00000021540 .
GeneIDi 17129.
KEGGi mmu:17129.
UCSCi uc007qsw.2. mouse.

Organism-specific databases

CTDi 4090.
MGIi MGI:1328787. Smad5.

Phylogenomic databases

eggNOGi NOG330956.
GeneTreei ENSGT00600000084186.
HOGENOMi HOG000286018.
HOVERGENi HBG053353.
InParanoidi P97454.
KOi K16790.
OMAi NRVGEAY.
OrthoDBi EOG7W1540.
PhylomeDBi P97454.
TreeFami TF314923.

Enzyme and pathway databases

Reactomei REACT_220505. Signaling by BMP.

Miscellaneous databases

NextBioi 291320.
PROi P97454.
SOURCEi Search...

Gene expression databases

Bgeei P97454.
CleanExi MM_SMAD5.
Genevestigatori P97454.

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. "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.
    , 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.

Entry informationi

Entry nameiSMAD5_MOUSE
AccessioniPrimary (citable) accession number: P97454
Secondary accession number(s): P70341, Q810K0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 4, 2001
Last modified: September 3, 2014
This is version 143 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi