P18075 (BMP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bone morphogenetic protein 7
Short name=BMP-7

Alternative name(s):
Osteogenic protein 1
Short name=OP-1
INN=Eptotermin alfa

Gene names

Name:	BMP7
Synonyms:	OP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis.
Subunit structure	Homodimer; disulfide-linked. Interacts with SOSTDC1. Interacts with TWSG1 By similarity. Ref.6
Subcellular location	Secreted.
Tissue specificity	Expressed in the kidney and bladder. Lower levels seen in the brain.
Developmental stage	Expressed in the developing eye, brain and ear during embryogenesis. Ref.7
Post-translational modification	Several N-termini starting at positions 293, 300, 315 and 316 have been identified by direct sequencing resulting in secretion of different mature forms (Ref.5).
Pharmaceutical use	Available under the name Osigraft (Stryker). Its use is indicated in the treatment of tibial non-union of at least 9 months duration, secondary to trauma, in skeletally mature patients, in cases where autograft has failed or is unfeasible.
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Biological process	Chondrogenesis Differentiation Osteogenesis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Cytokine Developmental protein Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from direct assay PubMed 16049014PubMed 18436533. Source: BHF-UCL SMAD protein signal transduction Inferred from direct assay PubMed 17244894. Source: UniProtKB axon guidance Inferred from electronic annotation. Source: Compara branching involved in salivary gland morphogenesis Inferred from electronic annotation. Source: Compara branching morphogenesis of an epithelial tube Inferred from electronic annotation. Source: Compara cartilage development Inferred from electronic annotation. Source: UniProtKB-KW cellular response to hypoxia Inferred from sequence or structural similarity. Source: BHF-UCL dendrite development Traceable author statement PubMed 11580864. Source: BHF-UCL embryonic camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara embryonic limb morphogenesis Inferred from electronic annotation. Source: Compara embryonic pattern specification Inferred from electronic annotation. Source: Compara embryonic skeletal joint morphogenesis Inferred from electronic annotation. Source: Compara epithelial cell differentiation Inferred from electronic annotation. Source: Compara epithelial to mesenchymal transition Traceable author statement PubMed 14679171. Source: HGNC growth Inferred from electronic annotation. Source: InterPro mesoderm formation Inferred from electronic annotation. Source: Compara mesonephros development Inferred from expression pattern PubMed 18437684. Source: UniProtKB metanephric mesenchymal cell proliferation involved in metanephros development Inferred from electronic annotation. Source: Compara metanephric mesenchyme morphogenesis Inferred from electronic annotation. Source: Compara metanephros development Inferred from expression pattern PubMed 18437684. Source: UniProtKB monocyte aggregation Inferred from direct assay PubMed 15100360. Source: UniProtKB negative regulation of MAP kinase activity Inferred from direct assay PubMed 17244894. Source: UniProtKB negative regulation of NF-kappaB import into nucleus Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of Notch signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of glomerular mesangial cell proliferation Inferred from direct assay PubMed 17244894. Source: UniProtKB negative regulation of mesenchymal cell apoptotic process involved in nephron morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of mitosis Inferred from direct assay PubMed 17244894. Source: UniProtKB negative regulation of neurogenesis Inferred from electronic annotation. Source: Compara negative regulation of neuron differentiation Inferred from direct assay PubMed 16325379. Source: MGI negative regulation of prostatic bud formation Inferred from electronic annotation. Source: Compara negative regulation of striated muscle cell apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 15100360PubMed 17244894. Source: UniProtKB nephrogenic mesenchyme morphogenesis Inferred from electronic annotation. Source: Compara neuron projection morphogenesis Inferred from direct assay PubMed 16325379. Source: MGI odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara ossification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of bone mineralization Inferred from direct assay PubMed 18436533. Source: BHF-UCL positive regulation of dendrite development Inferred from direct assay PubMed 11580864. Source: BHF-UCL positive regulation of heterotypic cell-cell adhesion Inferred from direct assay PubMed 15100360. Source: UniProtKB positive regulation of hyaluranon cable assembly Inferred from direct assay PubMed 15100360. Source: UniProtKB positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from direct assay PubMed 18436533. Source: BHF-UCL positive regulation of pathway-restricted SMAD protein phosphorylation Inferred from direct assay PubMed 17244894. Source: UniProtKB positive regulation of peptidyl-threonine phosphorylation Inferred from direct assay PubMed 19736306. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 15100360. Source: UniProtKB protein localization to nucleus Inferred from direct assay PubMed 17244894. Source: UniProtKB regulation of branching involved in prostate gland morphogenesis Inferred from electronic annotation. Source: Compara regulation of removal of superoxide radicals Inferred from sequence or structural similarity. Source: BHF-UCL skeletal system development Traceable author statement Ref.1. Source: ProtInc steroid hormone mediated signaling pathway Inferred from mutant phenotype PubMed 17244894. Source: UniProtKB ureteric bud development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular space Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Propeptide

30 – 292

263

PRO_0000033876

Chain

293 – 431

139

Bone morphogenetic protein 7

PRO_0000033877

Amino acid modifications

Glycosylation

187

1

N-linked (GlcNAc...) Potential

Glycosylation

302

1

N-linked (GlcNAc...) Potential

Glycosylation

321

1

N-linked (GlcNAc...) Potential

Glycosylation

372

1

N-linked (GlcNAc...) Potential

Disulfide bond

330 ↔ 396

Disulfide bond

359 ↔ 428

Disulfide bond

363 ↔ 430

Disulfide bond

395

Interchain

Natural variations

Natural variant

198

1

L → P Found in a patient with unilateral microphthalmia, optic disk and chorioretinal coloboma, mild learning difficulties. Ref.7

VAR_064058

Natural variant

321

1

N → S. Ref.7

VAR_064059

Secondary structure

1

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431

Helix Strand Turn

Details...

Beta strand

329 – 333

5

Beta strand

336 – 338

3

Helix

339 – 342

4

Turn

345 – 347

3

Beta strand

348 – 350

3

Beta strand

352 – 355

4

Beta strand

358 – 362

5

Beta strand

365 – 368

4

Helix

369 – 371

3

Helix

375 – 386

12

Turn

388 – 390

3

Beta strand

396 – 409

14

Helix

411 – 413

3

Beta strand

415 – 430

16

Sequences

	Sequence		Length	Mass (Da)
	P18075 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 47A05E45C6815F8A	FASTA	431	49,313
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"OP-1 cDNA encodes an osteogenic protein in the TGF-beta family." Oezkaynak E., Rueger D.C., Drier E.A., Corbett C., Ridge R.J., Sampath T.K., Oppermann H. EMBO J. 9:2085-2093(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Placenta.
[2]	"Identification of transforming growth factor beta family members present in bone-inductive protein purified from bovine bone." Celeste A.J., Iannazzi J.A., Taylor R.C., Hewick R.M., Rosen V., Wang E.A., Wozney J.M. Proc. Natl. Acad. Sci. U.S.A. 87:9843-9847(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Brain.
[5]	"Expression and characterization of a human BMP-7 variant with improved biochemical properties." Swencki-Underwood B., Mills J.K., Vennarini J., Boakye K., Luo J., Pomerantz S., Cunningham M.R., Farrell F.X., Naso M.F., Amegadzie B. Protein Expr. Purif. 57:312-319(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 293-302.
[6]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SOSTDC1.
[7]	"Bone morphogenetic protein 7 (BMP7) mutations are associated with variable ocular, brain, ear, palate, and skeletal anomalies." Wyatt A.W., Osborne R.J., Stewart H., Ragge N.K. Hum. Mutat. 31:781-787(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, VARIANTS PRO-198 AND SER-321, ASSOCIATION WITH DEVELOPMENTAL EYE ANOMALIES.
[8]	"Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily." Griffith D.L., Keck P.C., Sampath T.K., Rueger D.C., Carlson W.D. Proc. Natl. Acad. Sci. U.S.A. 93:878-883(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 293-431.
+	Additional computationally mapped references.

Web resources

Wikipedia

Bone morphogenetic protein 7 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X51801 mRNA. Translation: CAA36100.1.
M60316 mRNA. Translation: AAA36738.1.
AL122058, AL157414 Genomic DNA. Translation: CAB90273.2.
AL157414, AL122058 Genomic DNA. Translation: CAC08434.2.
BC008584 mRNA. Translation: AAH08584.1.

IPI

IPI00550949.

PIR

BMHU7. C39263.

RefSeq

NP_001710.1. NM_001719.2.

UniGene

Hs.473163.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BMP	X-ray	2.80	A	293-431	[»]
1LX5	X-ray	3.30	A	293-431	[»]
1LXI	X-ray	2.00	A	293-431	[»]
1M4U	X-ray	2.42	L	293-431	[»]

ProteinModelPortal

P18075.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5800N.

IntAct

P18075. 2 interactions.

MINT

MINT-263199.

STRING

9606.ENSP00000379204.

PTM databases

PhosphoSite

P18075.

Polymorphism databases

DMDM

115078.

Proteomic databases

PaxDb

P18075.

PRIDE

P18075.

Protocols and materials databases

DNASU

655.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000395863; ENSP00000379204; ENSG00000101144.

GeneID

655.

KEGG

hsa:655.

UCSC

uc010gip.1. human.

Organism-specific databases

CTD

655.

GeneCards

GC20M055743.

HGNC

HGNC:1074. BMP7.

MIM

112267. gene.

neXtProt

NX_P18075.

PharmGKB

PA25384.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG272883.

HOGENOM

HOG000249476.

HOVERGEN

HBG004860.

InParanoid

P18075.

KO

K16621.

OMA

GKHNAAP.

OrthoDB

EOG4GB76H.

PhylomeDB

P18075.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.

Reactome

REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P18075.

Bgee

P18075.

CleanEx

HS_BMP7.

Genevestigator

P18075.

GermOnline

ENSG00000101144. Homo sapiens.

Family and domain databases

InterPro

IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]

PANTHER

PTHR11848. PTHR11848. 1 hit.

Pfam

PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]

SMART

SM00204. TGFB. 1 hit.
[Graphical view]

PROSITE

PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

BMP7. human.

EvolutionaryTrace

P18075.

GenomeRNAi

655.

NextBio

2664.

SOURCE

Search...

Entry information

Entry name

BMP7_HUMAN

Accession

Primary (citable) accession number: P18075
Secondary accession number(s): Q9H512, Q9NTQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 151 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.