Bone morphogenetic protein 6

Protein-coding gene in the species Homo sapiens

BMP6
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2QCW, 2R52, 2R53

Identifiers
AliasesBMP6, VGR, VGR1, bone morphogenetic protein 6
External IDsOMIM: 112266; MGI: 88182; HomoloGene: 1300; GeneCards: BMP6; OMA:BMP6 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for BMP6
Genomic location for BMP6
Band6p24.3Start7,726,099 bp[1]
End7,881,728 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • cartilage tissue

  • right lung

  • monocyte

  • periodontal fiber

  • subcutaneous adipose tissue

  • testicle

  • retinal pigment epithelium

  • tibia

  • right coronary artery
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • cytokine activity
  • BMP receptor binding
  • protein heterodimerization activity
  • transforming growth factor beta receptor binding
  • growth factor activity
Cellular component
  • cytoplasm
  • extracellular region
  • extracellular space
  • vesicle
Biological process
  • eye development
  • regulation of apoptotic process
  • skeletal system development
  • cell differentiation
  • cellular response to iron ion
  • male genitalia development
  • positive regulation of aldosterone secretion
  • positive regulation of endothelial cell differentiation
  • regulation of MAPK cascade
  • positive regulation of endothelial cell proliferation
  • SMAD protein signal transduction
  • positive regulation of aldosterone biosynthetic process
  • response to retinoic acid
  • ossification
  • kidney development
  • positive regulation of bone mineralization
  • positive regulation of epithelial cell proliferation
  • positive regulation of pathway-restricted SMAD protein phosphorylation
  • cellular response to BMP stimulus
  • response to magnesium ion
  • response to glucocorticoid
  • negative regulation of transcription by RNA polymerase II
  • endochondral ossification
  • response to activity
  • BMP signaling pathway
  • response to iron ion
  • positive regulation of lipopolysaccharide-mediated signaling pathway
  • multicellular organismal iron ion homeostasis
  • multicellular organism development
  • cellular response to mechanical stimulus
  • cartilage development
  • positive regulation of osteoblast differentiation
  • positive regulation of chondrocyte differentiation
  • osteoblast differentiation
  • immune response
  • positive regulation of neuron differentiation
  • positive regulation of protein secretion
  • inflammatory response
  • type B pancreatic cell development
  • positive regulation of transcription by RNA polymerase II
  • positive regulation of SMAD protein signal transduction
  • cellular iron ion homeostasis
  • regulation of signaling receptor activity
  • positive regulation of cell population proliferation
  • cell development
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

654

12161

Ensembl

ENSG00000153162

n/a

UniProt

P22004

P20722

RefSeq (mRNA)

NM_001718

NM_007556

RefSeq (protein)

NP_001709

NP_031582

Location (UCSC)Chr 6: 7.73 – 7.88 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Bone morphogenetic protein 6 is a protein that in humans is encoded by the BMP6 gene.[4][5][6]

The protein encoded by this gene is a member of the TGFβ superfamily. Bone morphogenetic proteins are known for their ability to induce the growth of bone and cartilage. BMP6 is able to induce all osteogenic markers in mesenchymal stem cells.

The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has led to speculation of possible bone inductive activity. As of April 2009, an additional function of BMP6 has been identified as described in Nature Genetics April; 41 [4]:386-8. BMP6 is the key regulator of hepcidin, the small peptide secreted by the liver which is the major regulator of iron metabolism in mammals.

[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000153162 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Hahn GV, Cohen RB, Wozney JM, Levitz CL, Shore EM, Zasloff MA, et al. (Dec 1992). "A bone morphogenetic protein subfamily: chromosomal localization of human genes for BMP5, BMP6, and BMP7". Genomics. 14 (3): 759–62. doi:10.1016/S0888-7543(05)80181-8. PMID 1427904.
  5. ^ Sauermann U, Meyermann R, Schluesener HJ (Jan 1993). "Cloning of a novel TGF-beta related cytokine, the vgr, from rat brain: cloning of and comparison to homologous human cytokines". J Neurosci Res. 33 (1): 142–7. doi:10.1002/jnr.490330118. PMID 1453478. S2CID 35064968.
  6. ^ a b "Entrez Gene: BMP6 bone morphogenetic protein 6".

Further reading

  • Celeste AJ, Iannazzi JA, Taylor RC, Hewick RM, Rosen V, Wang EA, et al. (1991). "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 (24): 9843–7. Bibcode:1990PNAS...87.9843C. doi:10.1073/pnas.87.24.9843. PMC 55270. PMID 2263636.
  • Schluesener HJ, Meyermann R (1995). "Immunolocalization of BMP-6, a novel TGF-beta-related cytokine, in normal and atherosclerotic smooth muscle cells". Atherosclerosis. 113 (2): 153–6. doi:10.1016/0021-9150(94)05438-O. PMID 7605353.
  • Gitelman SE, Kobrin MS, Ye JQ, Lopez AR, Lee A, Derynck R (1994). "Recombinant Vgr-1/BMP-6-expressing tumors induce fibrosis and endochondral bone formation in vivo". J. Cell Biol. 126 (6): 1595–609. doi:10.1083/jcb.126.6.1595. PMC 2290953. PMID 8089189.
  • Barnes J, Anthony CT, Wall N, Steiner MS (1997). "Bone morphogenetic protein-6 expression in normal and malignant prostate". World Journal of Urology. 13 (6): 337–43. doi:10.1007/BF00191214. PMID 9116752. S2CID 31317742.
  • Hamdy FC, Autzen P, Robinson MC, Horne CH, Neal DE, Robson CN (1997). "Immunolocalization and messenger RNA expression of bone morphogenetic protein-6 in human benign and malignant prostatic tissue". Cancer Res. 57 (19): 4427–31. PMID 9331107.
  • Olavesen MG, Bentley E, Mason RV, Stephens R, Ragoussis J (1998). "Fine mapping of 39 ESTs on human chromosome 6p23-p25". Genomics. 46 (2): 303–6. doi:10.1006/geno.1997.5032. PMID 9417921.
  • Rickard DJ, Hofbauer LC, Bonde SK, Gori F, Spelsberg TC, Riggs BL (1998). "Bone morphogenetic protein-6 production in human osteoblastic cell lines. Selective regulation by estrogen". J. Clin. Invest. 101 (2): 413–22. doi:10.1172/JCI119880. PMC 508581. PMID 9435314.
  • Tamada H, Kitazawa R, Gohji K, Kamidono S, Maeda S, Kitazawa S (1998). "Molecular cloning and analysis of the 5'-flanking region of the human bone morphogenetic protein-6 (BMP-6)". Biochim. Biophys. Acta. 1395 (3): 247–51. doi:10.1016/S0167-4781(97)00191-7. hdl:20.500.14094/D1002352. PMID 9512655.
  • Ebisawa T, Tada K, Kitajima I, Tojo K, Sampath TK, Kawabata M, et al. (2000). "Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation". J. Cell Sci. 112 (20): 3519–27. doi:10.1242/jcs.112.20.3519. PMID 10504300.
  • Heikinheimo KA, Laine MA, Ritvos OV, Voutilainen RJ, Hogan BL, Leivo IV (1999). "Bone morphogenetic protein-6 is a marker of serous acinar cell differentiation in normal and neoplastic human salivary gland". Cancer Res. 59 (22): 5815–21. PMID 10582704.
  • Ahmed N, Sammons J, Carson RJ, Khokher MA, Hassan HT (2001). "Effect of bone morphogenetic protein-6 on haemopoietic stem cells and cytokine production in normal human bone marrow stroma". Cell Biol. Int. 25 (5): 429–35. doi:10.1006/cbir.2000.0662. PMID 11401330. S2CID 85369468.
  • Shimizu M, Higuchi K, Kasai S, Tsuboyama T, Matsushita M, Matsumura T, et al. (2003). "A congenic mouse and candidate gene at the Chromosome 13 locus regulating bone density". Mamm. Genome. 13 (7): 335–40. doi:10.1007/s00335-001-2129-4. PMID 12140680. S2CID 23300962.
  • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Moser M, Binder O, Wu Y, Aitsebaomo J, Ren R, Bode C, et al. (2003). "BMPER, a novel endothelial cell precursor-derived protein, antagonizes bone morphogenetic protein signaling and endothelial cell differentiation". Mol. Cell. Biol. 23 (16): 5664–79. doi:10.1128/MCB.23.16.5664-5679.2003. PMC 166349. PMID 12897139.
  • Bobacz K, Gruber R, Soleiman A, Erlacher L, Smolen JS, Graninger WB (2003). "Expression of bone morphogenetic protein 6 in healthy and osteoarthritic human articular chondrocytes and stimulation of matrix synthesis in vitro". Arthritis Rheum. 48 (9): 2501–8. doi:10.1002/art.11248. PMID 13130469.
  • Lories RJ, Derese I, Ceuppens JL, Luyten FP (2003). "Bone morphogenetic proteins 2 and 6, expressed in arthritic synovium, are regulated by proinflammatory cytokines and differentially modulate fibroblast-like synoviocyte apoptosis". Arthritis Rheum. 48 (10): 2807–18. doi:10.1002/art.11389. PMID 14558086.
  • Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
  • Laurikkala J, Kassai Y, Pakkasjärvi L, Thesleff I, Itoh N (2004). "Identification of a secreted BMP antagonist, ectodin, integrating BMP, FGF, and SHH signals from the tooth enamel knot". Dev. Biol. 264 (1): 91–105. doi:10.1016/j.ydbio.2003.08.011. PMID 14623234.
  • v
  • t
  • e
TGF beta superfamily of ligands
Ligand of ACVR or TGFBR
Ligand of BMPR
TGF beta receptors
(Activin, BMP, family)
TGFBR1:
TGFBR2:
TGFBR3:
Transducers/SMADLigand inhibitors
CoreceptorsOther
  • v
  • t
  • e
TGFβ receptor superfamily modulators
Type I
ALK1 (ACVRL1)
  • Kinase inhibitors: K-02288
  • ML-347 (LDN-193719, VU0469381)
  • Other inhibitors: Disitertide
ALK2 (ACVR1A)
  • Kinase inhibitors: DMH-1
  • DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
  • ML-347 (LDN-193719, VU0469381)
ALK3 (BMPR1A)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK4 (ACVR1B)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
ALK5 (TGFβR1)
ALK6 (BMPR1B)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK7 (ACVR1C)
  • Antagonists: Lefty (1, 2)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
Type II
TGFβR2
  • Kinase inhibitors: DMH-2
  • LY-364947
BMPR2
ACVR2A (ACVR2)
ACVR2B
  • Decoy receptors: Ramatercept
AMHR2 (AMHR)
Type III
TGFβR3 (β-glycan)
Unsorted

This article incorporates text from the United States National Library of Medicine, which is in the public domain.