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P21810 (PGS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biglycan
Alternative name(s):
Bone/cartilage proteoglycan I
PG-S1
Gene names
Name:BGN
Synonyms:SLRR1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in collagen fiber assembly By similarity.

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Found in several connective tissues, especially in articular cartilages.

Post-translational modification

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

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily.

Contains 12 LRR (leucine-rich) repeats.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainLeucine-rich repeat
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate biosynthetic process

Traceable author statement. Source: Reactome

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

dermatan sulfate biosynthetic process

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

cell surface

Inferred from direct assay PubMed 2212616. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

lysosomal lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Non-traceable author statement Ref.2. Source: UniProtKB

sarcolemma

Inferred from electronic annotation. Source: Ensembl

transport vesicle

Inferred from direct assay. Source: LIFEdb

   Molecular_functionextracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

extracellular matrix structural constituent

Non-traceable author statement Ref.2. Source: UniProtKB

glycosaminoglycan binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 3718
PRO_0000032691
Chain38 – 368331Biglycan
PRO_0000032692

Regions

Repeat82 – 10221LRR 1
Repeat103 – 12624LRR 2
Repeat127 – 15024LRR 3
Repeat151 – 17121LRR 4
Repeat172 – 19524LRR 5
Repeat196 – 22025LRR 6
Repeat221 – 24121LRR 7
Repeat242 – 26524LRR 8
Repeat266 – 28924LRR 9
Repeat290 – 31223LRR 10
Repeat313 – 34230LRR 11
Repeat343 – 36826LRR 12
Compositional bias63 – 7614Cys-rich

Amino acid modifications

Glycosylation421O-linked (Xyl...) (glycosaminoglycan) Ref.8
Glycosylation471O-linked (Xyl...) (glycosaminoglycan) Ref.8
Glycosylation1801O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1981O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation2701N-linked (GlcNAc...) Ref.11
Glycosylation3111N-linked (GlcNAc...) Ref.11
Disulfide bond63 ↔ 69 By similarity
Disulfide bond67 ↔ 76 By similarity
Disulfide bond321 ↔ 354 By similarity

Natural variations

Natural variant2661R → T in a breast cancer sample; somatic mutation. Ref.12
VAR_036605
Natural variant2881K → N in a breast cancer sample; somatic mutation. Ref.12
VAR_036606

Experimental info

Sequence conflict139 – 1402KL → NV in AAA52287. Ref.1
Sequence conflict163 – 1642EL → DV Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21810 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: BF16F304C5CD3B3E

FASTA36841,654
        10         20         30         40         50         60 
MWPLWRLVSL LALSQALPFE QRGFWDFTLD DGPFMMNDEE ASGADTSGVL DPDSVTPTYS 

        70         80         90        100        110        120 
AMCPFGCHCH LRVVQCSDLG LKSVPKEISP DTTLLDLQNN DISELRKDDF KGLQHLYALV 

       130        140        150        160        170        180 
LVNNKISKIH EKAFSPLRKL QKLYISKNHL VEIPPNLPSS LVELRIHDNR IRKVPKGVFS 

       190        200        210        220        230        240 
GLRNMNCIEM GGNPLENSGF EPGAFDGLKL NYLRISEAKL TGIPKDLPET LNELHLDHNK 

       250        260        270        280        290        300 
IQAIELEDLL RYSKLYRLGL GHNQIRMIEN GSLSFLPTLR ELHLDNNKLA RVPSGLPDLK 

       310        320        330        340        350        360 
LLQVVYLHSN NITKVGVNDF CPMGFGVKRA YYNGISLFNN PVPYWEVQPA TFRCVTDRLA 


IQFGNYKK 

« Hide

References

« Hide 'large scale' references
[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]"Comparative genome sequence analysis of the Bpa/Str region in mouse and man."
Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., Greystrong J.S., Clarke D. expand/collapse author list , Kimberley C., Goerdes M., Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A., Brown S.D.M.
Genome Res. 10:758-775(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]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]"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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-266 AND ASN-288.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14721.1.
PIRBGHUN. A40757.
RefSeqNP_001702.1. NM_001711.4.
UniGeneHs.821.

3D structure databases

ProteinModelPortalP21810.
SMRP21810. Positions 61-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107102. 9 interactions.
IntActP21810. 8 interactions.
MINTMINT-4529946.
STRING9606.ENSP00000327336.

PTM databases

PhosphoSiteP21810.

Polymorphism databases

DMDM266762.

Proteomic databases

MaxQBP21810.
PaxDbP21810.
PRIDEP21810.

Protocols and materials databases

DNASU633.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331595; ENSP00000327336; ENSG00000182492.
ENST00000594173; ENSP00000471199; ENSG00000269168.
GeneID633.
KEGGhsa:633.
UCSCuc004fhr.2. human.

Organism-specific databases

CTD633.
GeneCardsGC0XP152762.
HGNCHGNC:1044. BGN.
HPACAB003678.
HPA003157.
MIM301870. gene.
neXtProtNX_P21810.
PharmGKBPA25346.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000261690.
HOVERGENHBG016052.
InParanoidP21810.
KOK08118.
OMAIQFGNYK.
PhylomeDBP21810.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP21810.
BgeeP21810.
CleanExHS_BGN.
GenevestigatorP21810.

Family and domain databases

InterProIPR028547. Biglycan.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERPTHR24369:SF6. PTHR24369:SF6. 1 hit.
PfamPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFPIRSF002490. SLRP_I. 1 hit.
SMARTSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBGN. human.
GeneWikiBiglycan.
GenomeRNAi633.
NextBio2558.
PMAP-CutDBP21810.
PROP21810.
SOURCESearch...

Entry information

Entry namePGS1_HUMAN
AccessionPrimary (citable) accession number: P21810
Secondary accession number(s): D3DWU3, P13247
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 148 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 X

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