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UniProtKB/Swiss-Prot entry P18075


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BMP7_HUMAN
Primary accession number P18075
Secondary accession numbers Q9H512 Q9NTQ7
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1990 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 101)
Name and origin of the protein
Protein name Bone morphogenetic protein 7 [Precursor]
Synonyms BMP-7
Osteogenic protein 1
OP-1
Eptotermin alfa
Gene name
Name: BMP7
Synonyms: OP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=2357959 [NCBI, ExPASy, EBI, Israel, Japan]
Oezkaynak E., Rueger D.C., Drier E.A., Corbett C., Ridge R.J., Sampath T.K., Oppermann H.;
"OP-1 cDNA encodes an osteogenic protein in the TGF-beta family.";
EMBO J. 9:2085-2093(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2263636 [NCBI, ExPASy, EBI, Israel, Japan]
Celeste A.J., Iannazzi J.A., Taylor R.C., Hewick R.M., Rosen V., Wang E.A., Wozney J.M.;
"Identification of transforming growth factor beta family members present in bone-inductive protein purified from bovine bone.";
Proc. Natl. Acad. Sci. U.S.A. 87:9843-9847(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SOSTDC1.
DOI=10.1016/j.bbrc.2004.02.075; PubMed=15020244 [NCBI, ExPASy, EBI, Israel, Japan]
Yanagita M., Oka M., Watabe T., Iguchi H., Niida A., Takahashi S., Akiyama T., Miyazono K., Yanagisawa M., Sakurai T.;
"USAG-1: a bone morphogenetic protein antagonist abundantly expressed in the kidney.";
Biochem. Biophys. Res. Commun. 316:490-500(2004).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 293-431.
DOI=10.1073/pnas.93.2.878; PubMed=8570652 [NCBI, ExPASy, EBI, Israel, Japan]
Griffith D.L., Keck P.C., Sampath T.K., Rueger D.C., Carlson W.D.;
"Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 93:878-883(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X51801; CAA36100.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60316; AAA36738.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL122058; CAB90273.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL157414; CAB90273.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL157414; CAC08434.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL122058; CAC08434.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008584; AAH08584.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C39263; BMHU7.
RefSeq NP_001710.1; -.
UniGene Hs.473163
3D structure databases
PDB
1BMP; X-ray; 2.80 A; A=293-431.[ExPASy / RCSB / EBI]
1LX5; X-ray; 3.30 A; A=293-431.[ExPASy / RCSB / EBI]
1LXI; X-ray; 2.00 A; A=293-431.[ExPASy / RCSB / EBI]
1M4U; X-ray; 2.42 A; L=293-431.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BMP; -.
1LX5; -.
1LXI; -.
1M4U; -.
ModBase P18075.
Protein-protein interaction databases
DIP DIP:5800N; -.
IntAct P18075; -.
Organism-specific databases
H-InvDB HIX0015936; -.
HGNC HGNC:1074; BMP7.
GenAtlas BMP7.
MIM 112267; gene. [NCBI / EBI]
PharmGKB PA25384; -.
GeneCards P18075.
Gene expression databases
ArrayExpress P18075; -.
CleanEx HS_BMP7; -.
GermOnline ENSG00000101144; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030509; Biological process: BMP signaling pathway (inferred from direct assay from UniProtKB).
GO:0001837; Biological process: epithelial to mesenchymal transition (traceable author statement from HGNC).
GO:0045786; Biological process: negative regulation of cell cycle (inferred from direct assay from HGNC).
GO:0030501; Biological process: positive regulation of bone mineralization (inferred from direct assay from UniProtKB).
GO:0045669; Biological process: positive regulation of osteoblast differentiation (inferred from direct assay from UniProtKB).
GO:0045941; Biological process: positive regulation of transcription (inferred from direct assay from HGNC).
GO:0001501; Biological process: skeletal development (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001839; TGFb.
IPR001111; TGFb_N.
IPR015615; TGFbeta.
Graphical view of domain structure.
PANTHER PTHR11848; TGFbeta; 1.
Pfam PF00019; TGF_beta; 1.
PF00688; TGFb_propeptide; 1.
Pfam graphical view of domain structure.
ProDom PD000357; TGFb; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00204; TGFB; 1.
SMART graphical view of domain structure.
PROSITE PS00250; TGF_BETA_1; 1.
PS51362; TGF_BETA_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P18075.
Genome annotation databases
Ensembl ENSG00000101144; Homo sapiens. [Contig view]
GeneID 655; -.
KEGG hsa:655; -.
Phylogenomic databases
HOGENOM P18075; -.
HOVERGEN P18075; -.
Other
LinkHub P18075; -.
SOURCE BMP7; Homo sapiens.
ProtoNet P18075.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chondrogenesis; Cytokine; Developmental protein; Differentiation; Direct protein sequencing; Glycoprotein; Growth factor; Osteogenesis; Pharmaceutical; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    29  29     Potential. 
PROPEP   30   292  263     Potential. PRO_0000033876
CHAIN   293   431  139     Bone morphogenetic protein 7. PRO_0000033877
CARBOHYD   187   187        N-linked (GlcNAc...) (Potential). 
CARBOHYD   302   302        N-linked (GlcNAc...) (Potential). 
CARBOHYD   321   321        N-linked (GlcNAc...) (Potential). 
CARBOHYD   372   372        N-linked (GlcNAc...) (Potential). 
DISULFID   330   396         
DISULFID   359   428         
DISULFID   363   430         
DISULFID   395   395        Interchain. 
STRAND   329   333  5      
STRAND   336   338  3      
HELIX   339   342  4      
TURN   345   347  3      
STRAND   348   350  3      
STRAND   352   355  4      
STRAND   358   362  5      
HELIX   369   371  3      
HELIX   375   386  12      
TURN   388   390  3      
STRAND   396   409  14      
STRAND   415   430  16      
Sequence information
Length: 431 AA [This is the length of the unprocessed precursor] Molecular weight: 49313 Da [This is the MW of the unprocessed precursor] CRC64: 47A05E45C6815F8A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHVRSLRAAA PHSFVALWAP LFLLRSALAD FSLDNEVHSS FIHRRLRSQE RREMQREILS 

        70         80         90        100        110        120 
ILGLPHRPRP HLQGKHNSAP MFMLDLYNAM AVEEGGGPGG QGFSYPYKAV FSTQGPPLAS 

       130        140        150        160        170        180 
LQDSHFLTDA DMVMSFVNLV EHDKEFFHPR YHHREFRFDL SKIPEGEAVT AAEFRIYKDY 

       190        200        210        220        230        240 
IRERFDNETF RISVYQVLQE HLGRESDLFL LDSRTLWASE EGWLVFDITA TSNHWVVNPR 

       250        260        270        280        290        300 
HNLGLQLSVE TLDGQSINPK LAGLIGRHGP QNKQPFMVAF FKATEVHFRS IRSTGSKQRS 

       310        320        330        340        350        360 
QNRSKTPKNQ EALRMANVAE NSSSDQRQAC KKHELYVSFR DLGWQDWIIA PEGYAAYYCE 

       370        380        390        400        410        420 
GECAFPLNSY MNATNHAIVQ TLVHFINPET VPKPCCAPTQ LNAISVLYFD DSSNVILKKY 

       430 
RNMVVRACGC H 

P18075 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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