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Protein

Bone morphogenetic protein 6

Gene

BMP6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Induces cartilage and bone formation.

GO - Molecular functioni

  1. BMP receptor binding Source: MGI
  2. cytokine activity Source: GO_Central
  3. protein heterodimerization activity Source: MGI
  4. transforming growth factor beta receptor binding Source: GO_Central

GO - Biological processi

  1. BMP signaling pathway Source: BHF-UCL
  2. cartilage development Source: UniProtKB-KW
  3. cellular iron ion homeostasis Source: Ensembl
  4. cellular response to mechanical stimulus Source: Ensembl
  5. endochondral ossification Source: Ensembl
  6. eye development Source: Ensembl
  7. growth Source: InterPro
  8. immune response Source: BHF-UCL
  9. inflammatory response Source: Ensembl
  10. kidney development Source: Ensembl
  11. male genitalia development Source: Ensembl
  12. osteoblast differentiation Source: Ensembl
  13. positive regulation of aldosterone biosynthetic process Source: UniProtKB
  14. positive regulation of aldosterone secretion Source: Ensembl
  15. positive regulation of bone mineralization Source: BHF-UCL
  16. positive regulation of chondrocyte differentiation Source: Ensembl
  17. positive regulation of DNA-dependent DNA replication Source: BHF-UCL
  18. positive regulation of endothelial cell differentiation Source: Ensembl
  19. positive regulation of endothelial cell proliferation Source: Ensembl
  20. positive regulation of epithelial cell proliferation Source: BHF-UCL
  21. positive regulation of neuron differentiation Source: Ensembl
  22. positive regulation of osteoblast differentiation Source: BHF-UCL
  23. positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  24. positive regulation of protein secretion Source: BHF-UCL
  25. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  26. regulation of apoptotic process Source: GO_Central
  27. regulation of MAPK cascade Source: GO_Central
  28. response to activity Source: Ensembl
  29. response to glucocorticoid Source: Ensembl
  30. response to iron ion Source: Ensembl
  31. response to magnesium ion Source: Ensembl
  32. response to retinoic acid Source: Ensembl
  33. skeletal system development Source: ProtInc
  34. SMAD protein signal transduction Source: UniProtKB
  35. type B pancreatic cell development Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Developmental protein, Growth factor

Keywords - Biological processi

Chondrogenesis, Differentiation, Osteogenesis

Enzyme and pathway databases

SignaLinkiP22004.

Names & Taxonomyi

Protein namesi
Recommended name:
Bone morphogenetic protein 6
Short name:
BMP-6
Alternative name(s):
VG-1-related protein
Short name:
VG-1-R
Short name:
VGR-1
Gene namesi
Name:BMP6
Synonyms:VGR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1073. BMP6.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular space Source: GO_Central
  3. membrane-bounded vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25383.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 374354Sequence AnalysisPRO_0000033870Add
BLAST
Chaini375 – 513139Bone morphogenetic protein 6PRO_0000033871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi412 ↔ 478By similarity
Disulfide bondi441 ↔ 510By similarity
Disulfide bondi445 ↔ 512By similarity
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi477 – 477InterchainBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP22004.
PaxDbiP22004.
PRIDEiP22004.

PTM databases

PhosphoSiteiP22004.

Expressioni

Gene expression databases

BgeeiP22004.
CleanExiHS_BMP6.
ExpressionAtlasiP22004. baseline and differential.
GenevestigatoriP22004.

Organism-specific databases

HPAiCAB002773.

Interactioni

Subunit structurei

Interacts with SOSTDC1.By similarity

Protein-protein interaction databases

BioGridi107122. 5 interactions.
DIPiDIP-5797N.
STRINGi9606.ENSP00000283147.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi411 – 4155Combined sources
Beta strandi418 – 4203Combined sources
Turni421 – 4255Combined sources
Turni427 – 4293Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi434 – 4374Combined sources
Beta strandi440 – 4423Combined sources
Turni451 – 4544Combined sources
Helixi457 – 46812Combined sources
Turni470 – 4723Combined sources
Beta strandi477 – 49115Combined sources
Beta strandi497 – 51317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QCWX-ray2.49A/B382-513[»]
2R52X-ray2.50A/B375-513[»]
2R53X-ray2.10A/B411-513[»]
ProteinModelPortaliP22004.
SMRiP22004. Positions 411-513.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22004.

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG272883.
GeneTreeiENSGT00760000118883.
HOGENOMiHOG000249476.
HOVERGENiHBG004860.
InParanoidiP22004.
KOiK16620.
OMAiWWGLLCS.
OrthoDBiEOG7J9VPQ.
PhylomeDBiP22004.
TreeFamiTF316134.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGLGRRAQW LCWWWGLLCS CCGPPPLRPP LPAAAAAAAG GQLLGDGGSP
60 70 80 90 100
GRTEQPPPSP QSSSGFLYRR LKTQEKREMQ KEILSVLGLP HRPRPLHGLQ
110 120 130 140 150
QPQPPALRQQ EEQQQQQQLP RGEPPPGRLK SAPLFMLDLY NALSADNDED
160 170 180 190 200
GASEGERQQS WPHEAASSSQ RRQPPPGAAH PLNRKSLLAP GSGSGGASPL
210 220 230 240 250
TSAQDSAFLN DADMVMSFVN LVEYDKEFSP RQRHHKEFKF NLSQIPEGEV
260 270 280 290 300
VTAAEFRIYK DCVMGSFKNQ TFLISIYQVL QEHQHRDSDL FLLDTRVVWA
310 320 330 340 350
SEEGWLEFDI TATSNLWVVT PQHNMGLQLS VVTRDGVHVH PRAAGLVGRD
360 370 380 390 400
GPYDKQPFMV AFFKVSEVHV RTTRSASSRR RQQSRNRSTQ SQDVARVSSA
410 420 430 440 450
SDYNSSELKT ACRKHELYVS FQDLGWQDWI IAPKGYAANY CDGECSFPLN
460 470 480 490 500
AHMNATNHAI VQTLVHLMNP EYVPKPCCAP TKLNAISVLY FDDNSNVILK
510
KYRNMVVRAC GCH
Length:513
Mass (Da):57,226
Last modified:July 31, 1991 - v1
Checksum:i3F19155B36049278
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti257 – 2571R → C.
Corresponds to variant rs10458105 [ dbSNP | Ensembl ].
VAR_047055
Natural varianti343 – 3431A → D in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036200
Natural varianti476 – 4761P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036201

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60315 mRNA. Translation: AAA36737.1.
AL135778, AL133541 Genomic DNA. Translation: CAI19426.1.
AL133541, AL135778 Genomic DNA. Translation: CAI19472.1.
CCDSiCCDS4503.1.
PIRiB39263. BMHU6.
RefSeqiNP_001709.1. NM_001718.4.
UniGeneiHs.285671.

Genome annotation databases

EnsembliENST00000283147; ENSP00000283147; ENSG00000153162.
GeneIDi654.
KEGGihsa:654.
UCSCiuc003mxu.4. human.

Polymorphism databases

DMDMi115076.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Bone morphogenetic protein 6 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60315 mRNA. Translation: AAA36737.1.
AL135778, AL133541 Genomic DNA. Translation: CAI19426.1.
AL133541, AL135778 Genomic DNA. Translation: CAI19472.1.
CCDSiCCDS4503.1.
PIRiB39263. BMHU6.
RefSeqiNP_001709.1. NM_001718.4.
UniGeneiHs.285671.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QCWX-ray2.49A/B382-513[»]
2R52X-ray2.50A/B375-513[»]
2R53X-ray2.10A/B411-513[»]
ProteinModelPortaliP22004.
SMRiP22004. Positions 411-513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107122. 5 interactions.
DIPiDIP-5797N.
STRINGi9606.ENSP00000283147.

Chemistry

ChEMBLiCHEMBL3286078.

PTM databases

PhosphoSiteiP22004.

Polymorphism databases

DMDMi115076.

Proteomic databases

MaxQBiP22004.
PaxDbiP22004.
PRIDEiP22004.

Protocols and materials databases

DNASUi654.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000283147; ENSP00000283147; ENSG00000153162.
GeneIDi654.
KEGGihsa:654.
UCSCiuc003mxu.4. human.

Organism-specific databases

CTDi654.
GeneCardsiGC06P007672.
HGNCiHGNC:1073. BMP6.
HPAiCAB002773.
MIMi112266. gene.
neXtProtiNX_P22004.
PharmGKBiPA25383.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG272883.
GeneTreeiENSGT00760000118883.
HOGENOMiHOG000249476.
HOVERGENiHBG004860.
InParanoidiP22004.
KOiK16620.
OMAiWWGLLCS.
OrthoDBiEOG7J9VPQ.
PhylomeDBiP22004.
TreeFamiTF316134.

Enzyme and pathway databases

SignaLinkiP22004.

Miscellaneous databases

ChiTaRSiBMP6. human.
EvolutionaryTraceiP22004.
GeneWikiiBone_morphogenetic_protein_6.
GenomeRNAii654.
NextBioi2660.
PROiP22004.
SOURCEiSearch...

Gene expression databases

BgeeiP22004.
CleanExiHS_BMP6.
ExpressionAtlasiP22004. baseline and differential.
GenevestigatoriP22004.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-343 AND LEU-476.
  4. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 382-513.

Entry informationi

Entry nameiBMP6_HUMAN
AccessioniPrimary (citable) accession number: P22004
Secondary accession number(s): Q5TCP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: July 31, 1991
Last modified: March 31, 2015
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.