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Reviewed, UniProtKB/Swiss-Prot P12643 (BMP2_HUMAN)

Last modified November 25, 2008. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bone morphogenetic protein 2
      Short name=BMP-2
Alternative name(s):
    BMP-2A
Gene names
Name: BMP2
Synonyms: BMP2A
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Induces cartilage and bone formation.

Subunit structure

Homodimer; disulfide-linked. Interacts with GREM2 By similarity and SOSTDC1.

Subcellular location

Secreted.

Tissue specificity

Particularly abundant in lung, spleen and colon and in low but significant levels in heart, brain, placenta, liver, skeletal muscle, kidney, pancreas, prostate, ovary and small intestine.

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords

   Biological processChondrogenesis
Differentiation
Osteogenesis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionCytokine
Developmental protein
Growth factor
   PTMCleavage on pair of basic residues
Glycoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processBMP signaling pathway

Inferred from direct assay. Source: UniProtKB

cardiac cell differentiation

Inferred from direct assay. Source: MGI

cardiac epithelial to mesenchymal transition

Inferred from direct assay. Source: UniProtKB

cartilage development

Inferred from electronic annotation. Source: UniProtKB-KW

cell-cell signaling

Traceable author statement. Source: ProtInc

growth

Inferred from electronic annotation. Source: InterPro

negative regulation of cell cycle

Inferred from direct assay. Source: HGNC

negative regulation of gene-specific transcription

Inferred from direct assay. Source: UniProtKB

positive regulation of bone mineralization

Inferred from direct assay. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from direct assay. Source: UniProtKB

positive regulation of transcription

Inferred from direct assay. Source: UniProtKB

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncytokine activity

Inferred from electronic annotation. Source: UniProtKB-KW

growth factor activity

Inferred from electronic annotation. Source: InterPro

specific transcriptional repressor activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 282259
PRO_0000033824
Chain283 – 396114Bone morphogenetic protein 2
PRO_0000033825

Amino acid modifications

Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Disulfide bond296 ↔ 361
Disulfide bond325 ↔ 393
Disulfide bond329 ↔ 395
Disulfide bond360Interchain

Natural variations

Natural variant371S → A: dbSNP rs2273073.
VAR_020061
Natural variant1061A → T: dbSNP rs2273074.
VAR_020062
Natural variant1901R → S: dbSNP rs235768.
VAR_024232

Secondary structure

.................... 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12643-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 20653A3987B25E60

FASTA39644,702
        10         20         30         40         50         60 
MVAGTRCLLA LLLPQVLLGG AAGLVPELGR RKFAAASSGR PSSQPSDEVL SEFELRLLSM 

        70         80         90        100        110        120 
FGLKQRPTPS RDAVVPPYML DLYRRHSGQP GSPAPDHRLE RAASRANTVR SFHHEESLEE 

       130        140        150        160        170        180 
LPETSGKTTR RFFFNLSSIP TEEFITSAEL QVFREQMQDA LGNNSSFHHR INIYEIIKPA 

       190        200        210        220        230        240 
TANSKFPVTR LLDTRLVNQN ASRWESFDVT PAVMRWTAQG HANHGFVVEV AHLEEKQGVS 

       250        260        270        280        290        300 
KRHVRISRSL HQDEHSWSQI RPLLVTFGHD GKGHPLHKRE KRQAKHKQRK RLKSSCKRHP 

       310        320        330        340        350        360 
LYVDFSDVGW NDWIVAPPGY HAFYCHGECP FPLADHLNST NHAIVQTLVN SVNSKIPKAC 

       370        380        390 
CVPTELSAIS MLYLDENEKV VLKNYQDMVV EGCGCR 

« Hide

References

« Hide 'large scale' references
[1]"Novel regulators of bone formation: molecular clones and activities."
Wozney J.M., Rosen V., Celeste A.J., Mitsock L.M., Whitters M.J., Kriz R.W., Hewick R.M., Wang E.A.
Science 242:1528-1534(1988) [PubMed: 3201241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human bone morphogenetic protein 2 (BMP-2) genomic DNA sequence."
Shore E.M., Xu M.-Q., Calvert G., Moriatis J., Kaplan F.S.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"USAG-1: a bone morphogenetic protein antagonist abundantly expressed in the kidney."
Yanagita M., Oka M., Watabe T., Iguchi H., Niida A., Takahashi S., Akiyama T., Miyazono K., Yanagisawa M., Sakurai T.
Biochem. Biophys. Res. Commun. 316:490-500(2004) [PubMed: 15020244] [Abstract]
Cited for: INTERACTION WITH SOSTDC1.
[5]"Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution."
Scheufler C., Sebald W., Huelsmeyer M.
J. Mol. Biol. 287:103-115(1999) [PubMed: 10074410] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 292-396.
+Additional computationally mapped references.

Web resources

Wikipedia

Bone morphogenetic protein 2 entry

Cross-references

Sequence databases

M22489 mRNA. Translation: AAA51834.1.
AF040249 Genomic DNA. Translation: AAF21646.1.
AL035668 Genomic DNA. Translation: CAB82007.1.
PIRBMHU2. B37278.
RefSeqNP_001191.1.
UniGeneHs.73853

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ES7X-ray2.90A/C283-396[»]
1REUX-ray2.65A294-396[»]
1REWX-ray1.86A/B283-396[»]
2GOOX-ray2.20A/D283-396[»]
2H62X-ray1.85A/B283-396[»]
2H64X-ray1.92A283-396[»]
2QJ9X-ray2.44A/B283-396[»]
2QJAX-ray2.60A/B283-396[»]
2QJBX-ray2.50A/B283-396[»]
3BK3X-ray2.70A/B283-396[»]
3BMPX-ray2.70A283-396[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5792N.

Genome annotation databases

EnsemblENSG00000125845. Homo sapiens. [Contig view]
GeneID650.
KEGGhsa:650.

Organism-specific databases

H-InvDBHIX0040599.
HGNCHGNC:1069. BMP2.
MIM112261. gene.
PharmGKBPA25379.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP12643.
HOVERGENP12643.

Gene expression databases

ArrayExpressP12643.
CleanExHS_BMP2.
GermOnlineENSG00000125845. Homo sapiens.

Family and domain databases

InterProIPR002405. Inhibin_asu.
IPR001839. TGFb.
IPR001111. TGFb_N.
IPR015615. TGFbeta.
[Graphical view]
PANTHERPTHR11848. TGFbeta. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSPR00669. INHIBINA.
ProDomPD000357. TGFb. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00641. Simvastatin.
NextBio2640.
SOURCESearch...

Entry information

Entry nameBMP2_HUMAN
AccessionPrimary (citable) accession number: P12643
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 25, 2008
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents