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P12645 (BMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone morphogenetic protein 3

Short name=BMP-3
Alternative name(s):
Bone morphogenetic protein 3A
Short name=BMP-3A
Osteogenin
Gene names
Name:BMP3
Synonyms:BMP3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Negatively regulates bone density. Antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentitation and ossification. Ref.4 Ref.6

Subunit structure

Homodimer; disulfide-linked By similarity. Ref.8

Subcellular location

Secreted.

Tissue specificity

Expressed in adult and fetal cartilage. Ref.7

Induction

Highly expressed in fracture tissue, particularly in osteoblasts, osteoclasts and chondroblasts. Ref.5

Sequence similarities

Belongs to the TGF-beta family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 362340 By similarity
PRO_0000033836
Chain363 – 472110Bone morphogenetic protein 3
PRO_0000033837

Amino acid modifications

Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation1751N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Disulfide bond370 ↔ 437 Ref.8
Disulfide bond399 ↔ 469 Ref.8
Disulfide bond403 ↔ 471 Ref.8
Disulfide bond436Interchain Ref.8

Natural variations

Natural variant1761Q → K.
Corresponds to variant rs34213771 [ dbSNP | Ensembl ].
VAR_047418
Natural variant1761Q → L.
Corresponds to variant rs34847147 [ dbSNP | Ensembl ].
VAR_047419
Natural variant1921R → Q.
Corresponds to variant rs3733549 [ dbSNP | Ensembl ].
VAR_020063
Natural variant2051L → F. Ref.1 Ref.2 Ref.3
Corresponds to variant rs6831040 [ dbSNP | Ensembl ].
VAR_047420
Natural variant2221T → M.
Corresponds to variant rs34505126 [ dbSNP | Ensembl ].
VAR_047421

Secondary structure

......................... 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12645 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 2809B7EF5E37596A

FASTA47253,372
        10         20         30         40         50         60 
MAGASRLLFL WLGCFCVSLA QGERPKPPFP ELRKAVPGDR TAGGGPDSEL QPQDKVSEHM 

        70         80         90        100        110        120 
LRLYDRYSTV QAARTPGSLE GGSQPWRPRL LREGNTVRSF RAAAAETLER KGLYIFNLTS 

       130        140        150        160        170        180 
LTKSENILSA TLYFCIGELG NISLSCPVSG GCSHHAQRKH IQIDLSAWTL KFSRNQSQLL 

       190        200        210        220        230        240 
GHLSVDMAKS HRDIMSWLSK DITQLLRKAK ENEEFLIGFN ITSKGRQLPK RRLPFPEPYI 

       250        260        270        280        290        300 
LVYANDAAIS EPESVVSSLQ GHRNFPTGTV PKWDSHIRAA LSIERRKKRS TGVLLPLQNN 

       310        320        330        340        350        360 
ELPGAEYQYK KDEVWEERKP YKTLQAQAPE KSKNKKKQRK GPHRKSQTLQ FDEQTLKKAR 

       370        380        390        400        410        420 
RKQWIEPRNC ARRYLKVDFA DIGWSEWIIS PKSFDAYYCS GACQFPMPKS LKPSNHATIQ 

       430        440        450        460        470 
SIVRAVGVVP GIPEPCCVPE KMSSLSILFF DENKNVVLKV YPNMTVESCA CR 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-205.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-205.
[3]"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], VARIANT PHE-205.
[4]"Bone morphogenetic protein-3 is a negative regulator of bone density."
Daluiski A., Engstrand T., Bahamonde M.E., Gamer L.W., Agius E., Stevenson S.L., Cox K., Rosen V., Lyons K.M.
Nat. Genet. 27:84-88(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"BMP signaling components are expressed in human fracture callus."
Kloen P., Di Paola M., Borens O., Richmond J., Perino G., Helfet D.L., Goumans M.J.
Bone 33:362-371(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Characterization of the distinct orthotopic bone-forming activity of 14 BMPs using recombinant adenovirus-mediated gene delivery."
Kang Q., Sun M.H., Cheng H., Peng Y., Montag A.G., Deyrup A.T., Jiang W., Luu H.H., Luo J., Szatkowski J.P., Vanichakarn P., Park J.Y., Li Y., Haydon R.C., He T.-C.
Gene Ther. 11:1312-1320(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Expression of bone morphogenetic proteins, receptors, and tissue inhibitors in human fetal, adult, and osteoarthritic articular cartilage."
Chen A.L., Fang C., Liu C., Leslie M.P., Chang E., Di Cesare P.E.
J. Orthop. Res. 22:1188-1192(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"BMP-3 and BMP-6 structures illuminate the nature of binding specificity with receptors."
Allendorph G.P., Isaacs M.J., Kawakami Y., Izpisua Belmonte J.C., Choe S.
Biochemistry 46:12238-12247(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 363-472, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Wikipedia

Bone morphogenetic protein 3 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22491 mRNA. Translation: AAA51836.1.
AC093883 Genomic DNA. No translation available.
BC096269 mRNA. Translation: AAH96269.1.
BC096270 mRNA. Translation: AAH96270.1.
BC096271 mRNA. Translation: AAH96271.1.
BC117514 mRNA. Translation: AAI17515.1.
CCDSCCDS3588.1.
PIRBMHU3. D37278.
RefSeqNP_001192.2. NM_001201.2.
UniGeneHs.387411.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QCQX-ray2.21A/B363-472[»]
ProteinModelPortalP12645.
SMRP12645. Positions 365-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107119. 2 interactions.
IntActP12645. 4 interactions.
MINTMINT-8044327.
STRING9606.ENSP00000282701.

PTM databases

PhosphoSiteP12645.

Polymorphism databases

DMDM215273985.

Proteomic databases

PaxDbP12645.
PRIDEP12645.

Protocols and materials databases

DNASU651.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282701; ENSP00000282701; ENSG00000152785.
GeneID651.
KEGGhsa:651.
UCSCuc003hmg.4. human.

Organism-specific databases

CTD651.
GeneCardsGC04P081952.
HGNCHGNC:1070. BMP3.
HPAHPA045344.
MIM112263. gene.
neXtProtNX_P12645.
PharmGKBPA25380.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300136.
HOGENOMHOG000232003.
HOVERGENHBG004857.
InParanoidP12645.
KOK05496.
OMALPFPEPY.
OrthoDBEOG70CR76.
PhylomeDBP12645.
TreeFamTF316134.

Gene expression databases

ArrayExpressP12645.
BgeeP12645.
CleanExHS_BMP3.
GenevestigatorP12645.

Family and domain databases

Gene3D2.10.90.10. 1 hit.
InterProIPR017197. BMP3/GDF10.
IPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFPIRSF037403. BMP3/GDF10. 1 hit.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMSSF57501. SSF57501. 1 hit.
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12645.
GeneWikiBone_morphogenetic_protein_3.
GenomeRNAi651.
NextBio2644.
PROP12645.
SOURCESearch...

Entry information

Entry nameBMP3_HUMAN
AccessionPrimary (citable) accession number: P12645
Secondary accession number(s): Q4VAS5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM