Reviewed, UniProtKB/Swiss-Prot P12643 (BMP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Bone morphogenetic protein 2
      Short name=BMP-2
Alternative name(s):
    BMP-2A

Gene names

Name:	BMP2
Synonyms:	BMP2A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	396 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.
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 process	Chondrogenesis Differentiation Osteogenesis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Cytokine Developmental protein Growth factor
PTM	Cleavage on pair of basic residues Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	BMP 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 component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytokine 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Propeptide

24 – 282

259

PRO_0000033824

Chain

283 – 396

114

Bone morphogenetic protein 2

PRO_0000033825

Amino acid modifications

Glycosylation

135

1

N-linked (GlcNAc...) Potential

Glycosylation

163

1

N-linked (GlcNAc...) Potential

Glycosylation

164

1

N-linked (GlcNAc...) Potential

Glycosylation

200

1

N-linked (GlcNAc...) Potential

Disulfide bond

296 ↔ 361

Disulfide bond

325 ↔ 393

Disulfide bond

329 ↔ 395

Disulfide bond

360

Interchain

Natural variations

Natural variant

37

1

S → A: dbSNP rs2273073.

VAR_020061

Natural variant

106

1

A → T: dbSNP rs2273074.

VAR_020062

Natural variant

190

1

R → S: dbSNP rs235768.

VAR_024232

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

396

Helix Strand Turn

Details...

Beta strand

295 – 299

5

Beta strand

302 – 304

3

Helix

305 – 308

4

Turn

311 – 313

3

Beta strand

314 – 316

3

Beta strand

318 – 321

4

Beta strand

324 – 326

3

Helix

335 – 337

3

Helix

341 – 352

12

Beta strand

360 – 374

15

Beta strand

380 – 396

17

Sequences

	Sequence		Length	Mass (Da)
	P12643-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 20653A3987B25E60	FASTA	396	44,702
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

M22489 mRNA. Translation: AAA51834.1.
AF040249 Genomic DNA. Translation: AAF21646.1.
AL035668 Genomic DNA. Translation: CAB82007.1.

PIR

BMHU2. B37278.

RefSeq

NP_001191.1.

UniGene

Hs.73853

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ES7	X-ray	2.90	A/C	283-396	[»]
1REU	X-ray	2.65	A	294-396	[»]
1REW	X-ray	1.86	A/B	283-396	[»]
2GOO	X-ray	2.20	A/D	283-396	[»]
2H62	X-ray	1.85	A/B	283-396	[»]
2H64	X-ray	1.92	A	283-396	[»]
2QJ9	X-ray	2.44	A/B	283-396	[»]
2QJA	X-ray	2.60	A/B	283-396	[»]
2QJB	X-ray	2.50	A/B	283-396	[»]
3BK3	X-ray	2.70	A/B	283-396	[»]
3BMP	X-ray	2.70	A	283-396	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5792N.

Genome annotation databases

Ensembl

ENSG00000125845. Homo sapiens. [Contig view]

GeneID

650.

KEGG

hsa:650.

Organism-specific databases

H-InvDB

HIX0040599.

HGNC

HGNC:1069. BMP2.

MIM

112261. gene.

PharmGKB

PA25379.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P12643.

HOVERGEN

P12643.

Gene expression databases

ArrayExpress

P12643.

CleanEx

HS_BMP2.

GermOnline

ENSG00000125845. Homo sapiens.

Family and domain databases

InterPro

IPR002405. Inhibin_asu.
IPR001839. TGFb.
IPR001111. TGFb_N.
IPR015615. TGFbeta.
[Graphical view]

PANTHER

PTHR11848. TGFbeta. 1 hit.

Pfam

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

PRINTS

PR00669. INHIBINA.

ProDom

PD000357. TGFb. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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 Resources

DrugBank

DB00641. Simvastatin.

NextBio

2640.

SOURCE

Search...

Entry information

Entry name

BMP2_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)