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P02818 (OSTCN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Osteocalcin
Alternative name(s):
Bone Gla protein
Short name=BGP
Gamma-carboxyglutamic acid-containing protein
Gene names
Name:BGLAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.

Subcellular location

Secreted.

Post-translational modification

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.

Sequence similarities

Belongs to the osteocalcin/matrix Gla protein family.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Ontologies

Keywords
   Biological processBiomineralization
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   PTMCleavage on pair of basic residues
Disulfide bond
Gamma-carboxyglutamic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from electronic annotation. Source: Ensembl

bone mineralization

Non-traceable author statement PubMed 10486212. Source: UniProtKB

cell adhesion

Non-traceable author statement PubMed 12202187. Source: UniProtKB

cell aging

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to vitamin D

Inferred from electronic annotation. Source: Ensembl

odontogenesis

Non-traceable author statement PubMed 11856645. Source: UniProtKB

osteoblast development

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from expression pattern PubMed 17023519. Source: BHF-UCL

regulation of bone mineralization

Inferred from electronic annotation. Source: InterPro

regulation of bone resorption

Non-traceable author statement PubMed 10486212. Source: UniProtKB

regulation of osteoclast differentiation

Non-traceable author statement PubMed 10486212. Source: UniProtKB

response to activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to gravity

Inferred from electronic annotation. Source: Ensembl

response to hydroxyisoflavone

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from expression pattern PubMed 17023519. Source: BHF-UCL

response to vitamin K

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Traceable author statement PubMed 10865224. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular region

Non-traceable author statement PubMed 11856645. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

membrane-bounded vesicle

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

hydroxyapatite binding

Non-traceable author statement PubMed 10486212. Source: UniProtKB

structural constituent of bone

Non-traceable author statement PubMed 12467198. Source: UniProtKB

structural molecule activity

Non-traceable author statement PubMed 10486212. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Probable
Propeptide24 – 5128 Probable
PRO_0000011086
Chain52 – 10049Osteocalcin
PRO_0000011087

Regions

Domain52 – 9847Gla

Sites

Metal binding681Calcium 3 By similarity
Metal binding721Calcium 2 By similarity
Metal binding751Calcium 1 By similarity
Metal binding751Calcium 2 By similarity
Metal binding811Calcium 1 By similarity
Site601Not hydroxylated

Amino acid modifications

Modified residue6814-carboxyglutamate; partial Ref.7
Modified residue7214-carboxyglutamate Ref.7
Modified residue7514-carboxyglutamate Ref.7
Disulfide bond74 ↔ 80

Natural variations

Natural variant941R → Q. Ref.3
Corresponds to variant rs34702397 [ dbSNP | Ensembl ].
VAR_038743

Experimental info

Sequence conflict33 – 342Missing in CAA27763. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02818 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 4DF2A0A80849CB71

FASTA10010,963
        10         20         30         40         50         60 
MRALTLLALL ALAALCIAGQ AGAKPSGAES SKGAAFVSKQ EGSEVVKRPR RYLYQWLGAP 

        70         80         90        100 
VPYPDPLEPR REVCELNPDC DELADHIGFQ EAYRRFYGPV 

« Hide

References

« Hide 'large scale' references
[1]"The cDNA and derived amino acid sequences of human and bovine bone Gla protein."
Kiefer M.C., Saphire A.C.S., Bauer D.M., Barr P.J.
Nucleic Acids Res. 18:1909-1909(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation of the human gene for bone gla protein utilizing mouse and rat cDNA clones."
Celeste A.J., Buecker J.L., Kriz R., Wang E.A., Wozney J.M.
EMBO J. 5:1885-1890(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]SeattleSNPs variation discovery resource
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-94.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
[7]"Isolation and sequence of the vitamin K-dependent protein from human bone. Undercarboxylation of the first glutamic acid residue."
Poser J.W., Esch F.S., Ling N.C., Price P.A.
J. Biol. Chem. 255:8685-8691(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 52-100, GAMMA-CARBOXYGLUTAMATION AT GLU-68; GLU-72 AND GLU-75, ABSENCE OF HYDROXYLATION AT PRO-60.
+Additional computationally mapped references.

Web resources

Wikipedia

Osteocalcin entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53698 mRNA. Translation: CAA37736.1.
X51699 mRNA. Translation: CAA35996.1.
X04143 Genomic DNA. Translation: CAA27763.1.
DQ007079 Genomic DNA. Translation: AAY16981.1.
AL135927 Genomic DNA. Translation: CAI15541.1.
CH471121 Genomic DNA. Translation: EAW52986.1.
BC113432 mRNA. Translation: AAI13433.1.
BC113434 mRNA. Translation: AAI13435.1.
CCDSCCDS1134.1.
PIRGEHU. S12652.
RefSeqNP_954642.1. NM_199173.4.
UniGeneHs.654541.

3D structure databases

ProteinModelPortalP02818.
SMRP02818. Positions 68-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107101. 1 interaction.
STRING9606.ENSP00000357255.

Chemistry

DrugBankDB01022. Phytonadione.

Polymorphism databases

DMDM129253.

Proteomic databases

PaxDbP02818.
PeptideAtlasP02818.
PRIDEP02818.

Protocols and materials databases

DNASU632.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368272; ENSP00000357255; ENSG00000242252.
GeneID632.
KEGGhsa:632.
UCSCuc001fnt.3. human.

Organism-specific databases

CTD632.
GeneCardsGC01P156211.
HGNCHGNC:1043. BGLAP.
MIM112260. gene.
neXtProtNX_P02818.
PharmGKBPA25345.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72046.
HOGENOMHOG000115820.
OMAPKREVCE.
OrthoDBEOG7VDXRQ.
PhylomeDBP02818.
TreeFamTF330920.

Gene expression databases

BgeeP02818.
CleanExHS_BGLAP.
GenevestigatorP02818.

Family and domain databases

InterProIPR000294. GLA_domain.
IPR002384. Osteocalcin/MGP.
[Graphical view]
PfamPF00594. Gla. 1 hit.
[Graphical view]
PRINTSPR00002. GLABONE.
SMARTSM00069. GLA. 1 hit.
[Graphical view]
SUPFAMSSF57630. SSF57630. 1 hit.
PROSITEPS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiOsteocalcin.
GenomeRNAi632.
NextBio2554.
PMAP-CutDBP02818.
PROP02818.
SOURCESearch...

Entry information

Entry nameOSTCN_HUMAN
AccessionPrimary (citable) accession number: P02818
Secondary accession number(s): Q5TCK6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 137 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM