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Protein

Biglycan

Gene

BGN

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

Functioni

May be involved in collagen fiber assembly.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_120800. Dermatan sulfate biosynthesis.
REACT_120888. CS/DS degradation.
REACT_120989. Chondroitin sulfate biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_163906. ECM proteoglycans.
REACT_267648. Defective CHST3 causes SEDCJD.
REACT_267917. Defective CHST14 causes EDS, musculocontractural type.
REACT_268113. Defective CHSY1 causes TPBS.
REACT_268678. Defective B3GAT3 causes JDSSDHD.
REACT_268749. Defective B4GALT7 causes EDS, progeroid type.

Names & Taxonomyi

Protein namesi
Recommended name:
Biglycan
Alternative name(s):
Bone/cartilage proteoglycan I
PG-S1
Gene namesi
Name:BGN
Synonyms:SLRR1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:1044. BGN.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • Golgi lumen Source: Reactome
  • lysosomal lumen Source: Reactome
  • proteinaceous extracellular matrix Source: UniProtKB
  • sarcolemma Source: Ensembl
  • transport vesicle Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25346.

Polymorphism and mutation databases

BioMutaiBGN.
DMDMi266762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 37182 PublicationsPRO_0000032691Add
BLAST
Chaini38 – 368331BiglycanPRO_0000032692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421O-linked (Xyl...) (glycosaminoglycan)1 Publication
Glycosylationi47 – 471O-linked (Xyl...) (glycosaminoglycan)1 Publication
Disulfide bondi63 ↔ 69By similarity
Disulfide bondi67 ↔ 76By similarity
Glycosylationi180 – 1801O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi198 – 1981O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi270 – 2701N-linked (GlcNAc...)1 Publication
Glycosylationi311 – 3111N-linked (GlcNAc...)1 Publication
Disulfide bondi321 ↔ 354By similarity

Post-translational modificationi

The two attached glycosaminoglycan chains can be either chondroitin sulfate or dermatan sulfate.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

MaxQBiP21810.
PaxDbiP21810.
PRIDEiP21810.

PTM databases

PhosphoSiteiP21810.

Miscellaneous databases

PMAP-CutDBP21810.

Expressioni

Tissue specificityi

Found in several connective tissues, especially in articular cartilages.

Gene expression databases

BgeeiP21810.
CleanExiHS_BGN.
ExpressionAtlasiP21810. baseline and differential.
GenevestigatoriP21810.

Organism-specific databases

HPAiCAB003678.
HPA003157.

Interactioni

Subunit structurei

Homodimer. Forms a ternary complex with MFAP2 and ELN (By similarity).By similarity

Protein-protein interaction databases

BioGridi107102. 9 interactions.
IntActiP21810. 13 interactions.
MINTiMINT-4529946.
STRINGi9606.ENSP00000327336.

Structurei

3D structure databases

ProteinModelPortaliP21810.
SMRiP21810. Positions 61-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati82 – 10221LRR 1Add
BLAST
Repeati103 – 12624LRR 2Add
BLAST
Repeati127 – 15024LRR 3Add
BLAST
Repeati151 – 17121LRR 4Add
BLAST
Repeati172 – 19524LRR 5Add
BLAST
Repeati196 – 22025LRR 6Add
BLAST
Repeati221 – 24121LRR 7Add
BLAST
Repeati242 – 26524LRR 8Add
BLAST
Repeati266 – 28924LRR 9Add
BLAST
Repeati290 – 31223LRR 10Add
BLAST
Repeati313 – 34230LRR 11Add
BLAST
Repeati343 – 36826LRR 12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 7614Cys-richAdd
BLAST

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiP21810.
KOiK08118.
OMAiQRGFWDF.
PhylomeDBiP21810.
TreeFamiTF334562.

Family and domain databases

InterProiIPR028547. Biglycan.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF6. PTHR24369:SF6. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21810-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWPLWRLVSL LALSQALPFE QRGFWDFTLD DGPFMMNDEE ASGADTSGVL
60 70 80 90 100
DPDSVTPTYS AMCPFGCHCH LRVVQCSDLG LKSVPKEISP DTTLLDLQNN
110 120 130 140 150
DISELRKDDF KGLQHLYALV LVNNKISKIH EKAFSPLRKL QKLYISKNHL
160 170 180 190 200
VEIPPNLPSS LVELRIHDNR IRKVPKGVFS GLRNMNCIEM GGNPLENSGF
210 220 230 240 250
EPGAFDGLKL NYLRISEAKL TGIPKDLPET LNELHLDHNK IQAIELEDLL
260 270 280 290 300
RYSKLYRLGL GHNQIRMIEN GSLSFLPTLR ELHLDNNKLA RVPSGLPDLK
310 320 330 340 350
LLQVVYLHSN NITKVGVNDF CPMGFGVKRA YYNGISLFNN PVPYWEVQPA
360
TFRCVTDRLA IQFGNYKK
Length:368
Mass (Da):41,654
Last modified:April 1, 1993 - v2
Checksum:iBF16F304C5CD3B3E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1402KL → NV in AAA52287 (PubMed:2647739).Curated
Sequence conflicti163 – 1642EL → DV (PubMed:2647739).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti266 – 2661R → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_036605
Natural varianti288 – 2881K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036606

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04599 mRNA. Translation: AAA36009.1.
M65153, M65152 Genomic DNA. Translation: AAA52287.1. Sequence problems.
U82695 Genomic DNA. No translation available.
BT007323 mRNA. Translation: AAP35987.1.
CH471172 Genomic DNA. Translation: EAW72863.1.
CH471172 Genomic DNA. Translation: EAW72864.1.
BC002416 mRNA. Translation: AAH02416.1.
BC004244 mRNA. Translation: AAH04244.1.
U11686 mRNA. Translation: AAC50117.1.
CCDSiCCDS14721.1.
PIRiA40757. BGHUN.
RefSeqiNP_001702.1. NM_001711.4.
UniGeneiHs.821.

Genome annotation databases

EnsembliENST00000331595; ENSP00000327336; ENSG00000182492.
GeneIDi633.
KEGGihsa:633.
UCSCiuc004fhr.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04599 mRNA. Translation: AAA36009.1.
M65153, M65152 Genomic DNA. Translation: AAA52287.1. Sequence problems.
U82695 Genomic DNA. No translation available.
BT007323 mRNA. Translation: AAP35987.1.
CH471172 Genomic DNA. Translation: EAW72863.1.
CH471172 Genomic DNA. Translation: EAW72864.1.
BC002416 mRNA. Translation: AAH02416.1.
BC004244 mRNA. Translation: AAH04244.1.
U11686 mRNA. Translation: AAC50117.1.
CCDSiCCDS14721.1.
PIRiA40757. BGHUN.
RefSeqiNP_001702.1. NM_001711.4.
UniGeneiHs.821.

3D structure databases

ProteinModelPortaliP21810.
SMRiP21810. Positions 61-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107102. 9 interactions.
IntActiP21810. 13 interactions.
MINTiMINT-4529946.
STRINGi9606.ENSP00000327336.

PTM databases

PhosphoSiteiP21810.

Polymorphism and mutation databases

BioMutaiBGN.
DMDMi266762.

Proteomic databases

MaxQBiP21810.
PaxDbiP21810.
PRIDEiP21810.

Protocols and materials databases

DNASUi633.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331595; ENSP00000327336; ENSG00000182492.
GeneIDi633.
KEGGihsa:633.
UCSCiuc004fhr.2. human.

Organism-specific databases

CTDi633.
GeneCardsiGC0XP152762.
HGNCiHGNC:1044. BGN.
HPAiCAB003678.
HPA003157.
MIMi301870. gene.
neXtProtiNX_P21810.
PharmGKBiPA25346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiP21810.
KOiK08118.
OMAiQRGFWDF.
PhylomeDBiP21810.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiREACT_120800. Dermatan sulfate biosynthesis.
REACT_120888. CS/DS degradation.
REACT_120989. Chondroitin sulfate biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_163906. ECM proteoglycans.
REACT_267648. Defective CHST3 causes SEDCJD.
REACT_267917. Defective CHST14 causes EDS, musculocontractural type.
REACT_268113. Defective CHSY1 causes TPBS.
REACT_268678. Defective B3GAT3 causes JDSSDHD.
REACT_268749. Defective B4GALT7 causes EDS, progeroid type.

Miscellaneous databases

ChiTaRSiBGN. human.
GeneWikiiBiglycan.
GenomeRNAii633.
NextBioi2558.
PMAP-CutDBP21810.
PROiP21810.
SOURCEiSearch...

Gene expression databases

BgeeiP21810.
CleanExiHS_BGN.
ExpressionAtlasiP21810. baseline and differential.
GenevestigatoriP21810.

Family and domain databases

InterProiIPR028547. Biglycan.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF6. PTHR24369:SF6. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species."
    Fisher L.W., Termine J.D., Young M.F.
    J. Biol. Chem. 264:4571-4576(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone.
  2. "Human biglycan gene. Putative promoter, intron-exon junctions, and chromosomal localization."
    Fisher L.W., Heegaard A.M., Vetter U., Vogel W., Just W., Termine J.D., Young M.F.
    J. Biol. Chem. 266:14371-14377(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "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].
    Tissue: Brain.
  8. "Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II."
    Roughley P.J., White R.J.
    Biochem. J. 262:823-827(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-57.
  9. "Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone."
    Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.
    J. Biol. Chem. 262:9702-9708(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-66.
  10. "Dinucleotide repeat polymorphism at the human biglycan (BGN) locus."
    Just W., Rau W., Muller R., Geerkens C., Vogel W.
    Hum. Mol. Genet. 3:2268-2268(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-368.
    Tissue: Skin.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-311.
    Tissue: Liver.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-266 AND ASN-288.

Entry informationi

Entry nameiPGS1_HUMAN
AccessioniPrimary (citable) accession number: P21810
Secondary accession number(s): D3DWU3, P13247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: April 1, 1993
Last modified: May 27, 2015
This is version 157 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. 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.