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Q9BXN1 (ASPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Asporin
Alternative name(s):
Periodontal ligament-associated protein 1
Short name=PLAP-1
Gene names
Name:ASPN
Synonyms:PLAP1, SLRR1C
ORF Names:UNQ215/PRO241
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins By similarity. Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF-beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity. Ref.9 Ref.11

Subunit structure

Interacts with TGFB1, TGFB2 and TGFB3. DCN, BGN, and FMOD inhibit binding to TGFB1. Interacts with BMP2. Interacts in vitro with type II collagen By similarity. Interacts with type I collagen. DCN can inhibit collagen binding. Ref.11

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.9.

Tissue specificity

Higher levels in osteoarthritic articular cartilage, aorta, uterus. Moderate expression in small intestine, heart, liver, bladder, ovary, stomach, and in the adrenal, thyroid, and mammary glands. Low expression in trachea, bone marrow, and lung. Colocalizes with TGFB1 in chondrocytes within osteoarthritic (OA) lesions of articular cartilage. Ref.9

Induction

By TGFB1. Ref.9

Domain

The LRR 5 repeat can inhibit BMP2-induced cytodifferentiation and may be involved in the interaction with BMP2 By similarity. The repeats LRR 10, LRR 11 and LRR 12 are involved in binding type I collagen. The poly-Asp region is involved in binding calcium. Ref.11

Post-translational modification

There is no serine/glycine dipeptide sequence expected for the attachment of O-linked glycosaminoglycans and this is probably not a proteoglycan. The O-linked polysaccharide on 54-Ser is probably the mucin type linked to GalNAc.

The N-linked glycan at Asn-282 is composed of variable structures of GlcNAc, mannose, fucose, HexNAc and hexose.

Polymorphism

The poly-Asp region of ASPN is polymorphic and ranges at least from 11 to 17 Asp.

Involvement in disease

Osteoarthritis 3 (OS3) [MIM:607850]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to osteoarthritis is conferred by a triplet repeat expansion polymorphism. ASPN allele having 14 aspartic acid repeats in the N-terminal region of the protein (D14), is overrepresented relative to the common allele having 13 aspartic acid repeats (D13). The frequency of the D14 allele increases with disease severity. The D14 allele is also overrepresented in individuals with hip osteoarthritis. Ref.8

Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to intervertebral disk disease, particularly lumbar disk degeneration, is conferred by a triplet repeat expansion polymorphism. ASPN allele having 14 aspartic acid repeats in the N-terminal region of the protein (D14), is associated with the disorder in some populations (Ref.10). Ref.10

Sequence similarities

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

Contains 11 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Sequence caution

The sequence BAA90967.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Propeptide15 – 3218 Potential
PRO_0000032727
Chain33 – 380348Asporin
PRO_0000032728

Regions

Domain66 – 10237LRRNT
Repeat103 – 12422LRR 1
Repeat127 – 14822LRR 2
Repeat151 – 17323LRR 3
Repeat174 – 19320LRR 4
Repeat196 – 21924LRR 5
Repeat242 – 26322LRR 6
Repeat266 – 28722LRR 7
Repeat290 – 31223LRR 8
Repeat313 – 33422LRR 9
Repeat335 – 35723LRR 10
Repeat358 – 38023LRR 11
Region166 – 21247Interaction with TGFB1 By similarity
Compositional bias35 – 5319Poly-Asp
Compositional bias77 – 9014Cys-rich

Amino acid modifications

Glycosylation551O-linked (GalNAc...) Probable
Glycosylation2821N-linked (GlcNAc...) Ref.1 Ref.12
Disulfide bond75 ↔ 81 Ref.11
Disulfide bond79 ↔ 88 Ref.11
Disulfide bond333 ↔ 366 Ref.11

Experimental info

Sequence conflict238 – 2436GLPPTL → DNLPSF in BAB55060. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9BXN1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 2746A977FDCEBA5F

FASTA38043,417
        10         20         30         40         50         60 
MKEYVLLLFL ALCSAKPFFS PSHIALKNMM LKDMEDTDDD DDDDDDDDDD DEDNSLFPTR 

        70         80         90        100        110        120 
EPRSHFFPFD LFPMCPFGCQ CYSRVVHCSD LGLTSVPTNI PFDTRMLDLQ NNKIKEIKEN 

       130        140        150        160        170        180 
DFKGLTSLYG LILNNNKLTK IHPKAFLTTK KLRRLYLSHN QLSEIPLNLP KSLAELRIHE 

       190        200        210        220        230        240 
NKVKKIQKDT FKGMNALHVL EMSANPLDNN GIEPGAFEGV TVFHIRIAEA KLTSVPKGLP 

       250        260        270        280        290        300 
PTLLELHLDY NKISTVELED FKRYKELQRL GLGNNKITDI ENGSLANIPR VREIHLENNK 

       310        320        330        340        350        360 
LKKIPSGLPE LKYLQIIFLH SNSIARVGVN DFCPTVPKMK KSLYSAISLF NNPVKYWEMQ 

       370        380 
PATFRCVLSR MSVQLGNFGM 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of asporin. A novel member of the leucine-rich repeat protein family closely related to decorin and biglycan."
Lorenzo P., Aspberg A., Oennerfjord P., Bayliss M.T., Neame P.J., Heinegaard D.
J. Biol. Chem. 276:12201-12211(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-55 AND ASN-282, IDENTIFICATION BY MASS SPECTROMETRY, POLYMORPHISM OF POLY-ASP REGION.
Tissue: Cartilage.
[2]"Expression profile of active genes in human periodontal ligament and isolation of PLAP-1, a novel SLRP family gene."
Yamada S., Murakami S., Matoba R., Ozawa Y., Yokokoji T., Nakahira Y., Ikezawa K., Takayama S., Matsubara K., Okada H.
Gene 275:279-286(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Embryo.
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Expression pattern and gene characterization of asporin. A newly discovered member of the leucine-rich repeat protein family."
Henry S.P., Takanosu M., Boyd T.C., Mayne P.M., Eberspaecher H., Zhou W., de Crombrugghe B., Hoeoek M., Mayne R.
J. Biol. Chem. 276:12212-12221(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[8]"An aspartic acid repeat polymorphism in asporin inhibits chondrogenesis and increases susceptibility to osteoarthritis."
Kizawa H., Kou I., Iida A., Sudo A., Miyamoto Y., Fukuda A., Mabuchi A., Kotani A., Kawakami A., Yamamoto S., Uchida A., Nakamura K., Notoya K., Nakamura Y., Ikegawa S.
Nat. Genet. 37:138-144(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH OS3.
[9]"Mechanisms for asporin function and regulation in articular cartilage."
Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.
J. Biol. Chem. 282:32185-32192(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY TGFB1, TISSUE SPECIFICITY.
[10]"Association of the asporin D14 allele with lumbar-disc degeneration in Asians."
Song Y.Q., Cheung K.M., Ho D.W., Poon S.C., Chiba K., Kawaguchi Y., Hirose Y., Alini M., Grad S., Yee A.F., Leong J.C., Luk K.D., Yip S.P., Karppinen J., Cheah K.S., Sham P., Ikegawa S., Chan D.
Am. J. Hum. Genet. 82:744-747(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO IDD.
[11]"Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization."
Kalamajski S., Aspberg A., Lindblom K., Heinegaard D., Oldberg A.
Biochem. J. 423:53-59(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TYPE I COLLAGEN, DISULFIDE BOND, DOMAIN.
[12]"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-282.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF316824 mRNA. Translation: AAK35161.1.
AY029191 mRNA. Translation: AAK31800.1.
AK000136 mRNA. Translation: BAA90967.1. Different initiation.
AK027359 mRNA. Translation: BAB55060.1.
AY358329 mRNA. Translation: AAQ88695.1.
AL137848 Genomic DNA. Translation: CAI16697.1.
CH471089 Genomic DNA. Translation: EAW62822.1.
RefSeqNP_001180264.1. NM_001193335.1.
NP_060150.4. NM_017680.4.
UniGeneHs.435655.

3D structure databases

ProteinModelPortalQ9BXN1.
SMRQ9BXN1. Positions 74-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364694.

PTM databases

PhosphoSiteQ9BXN1.

Polymorphism databases

DMDM209572589.

Proteomic databases

PaxDbQ9BXN1.
PRIDEQ9BXN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375544; ENSP00000364694; ENSG00000106819.
GeneID54829.
KEGGhsa:54829.
UCSCuc004ase.2. human.

Organism-specific databases

CTD54829.
GeneCardsGC09M095218.
HGNCHGNC:14872. ASPN.
HPAHPA008435.
HPA024230.
MIM603932. phenotype.
607850. phenotype.
608135. gene.
neXtProtNX_Q9BXN1.
PharmGKBPA25057.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOVERGENHBG016052.
InParanoidQ9BXN1.
KOK08120.
OMAEDFIRYK.
OrthoDBEOG76739V.
PhylomeDBQ9BXN1.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9BXN1.
BgeeQ9BXN1.
CleanExHS_ASPN.
GenevestigatorQ9BXN1.

Family and domain databases

InterProIPR028548. Asporin.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERPTHR24369:SF10. PTHR24369:SF10. 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. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAsporin.
GenomeRNAi54829.
NextBio57604.
PROQ9BXN1.
SOURCESearch...

Entry information

Entry nameASPN_HUMAN
AccessionPrimary (citable) accession number: Q9BXN1
Secondary accession number(s): Q5TBF3 expand/collapse secondary AC list , Q96K79, Q96LD0, Q9NXP3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 14, 2008
Last modified: June 11, 2014
This is version 127 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 chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM