Q9BXN1 · ASPN_HUMAN

Function

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

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell projection
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Biological Processbone mineralization
Biological Processnegative regulation of tooth mineralization
Biological Processnegative regulation of transforming growth factor beta receptor signaling pathway
Biological Processresponse to fluoride

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Asporin
  • Alternative names
    • Periodontal ligament-associated protein 1 (PLAP-1)

Gene names

    • Name
      ASPN
    • Synonyms
      PLAP1, SLRR1C
    • ORF names
      UNQ215/PRO241

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9BXN1
  • Secondary accessions
    • Q5TBF3
    • Q96K79
    • Q96LD0
    • Q9NXP3

Proteomes

Organism-specific databases

Disease & Variants

Involvement in disease

Osteoarthritis 3 (OS3)

  • Note
    • Disease susceptibility is associated with variants 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
  • Description
    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.
  • See also
    MIM:607850

Intervertebral disc disease (IDD)

  • Note
    • Disease susceptibility is associated with variants 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 (PubMed:18304494)
  • Description
    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.
  • See also
    MIM:603932

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 374 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for signal, propeptide, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-14
PropeptidePRO_000003272715-32
ChainPRO_000003272833-380Asporin
Glycosylation55O-linked (GalNAc...) serine
Disulfide bond75↔81
Disulfide bond79↔88
Glycosylation282N-linked (GlcNAc...) asparagine
Disulfide bond333↔366

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.

Keywords

Proteomic databases

PTM databases

Expression

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.

Induction

By TGFB1.

Gene expression databases

Organism-specific databases

Interaction

Subunit

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

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, repeat.

TypeIDPosition(s)Description
Compositional bias35-55Acidic residues
Region35-59Disordered
Domain66-102LRRNT
Repeat103-124LRR 1
Repeat127-148LRR 2
Repeat151-173LRR 3
Region166-212Interaction with TGFB1
Repeat174-193LRR 4
Repeat196-219LRR 5
Repeat242-263LRR 6
Repeat266-287LRR 7
Repeat290-312LRR 8
Repeat313-334LRR 9
Repeat335-357LRR 10
Repeat358-380LRR 11

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

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    380
  • Mass (Da)
    43,417
  • Last updated
    2008-10-14 v2
  • Checksum
    2746A977FDCEBA5F
MKEYVLLLFLALCSAKPFFSPSHIALKNMMLKDMEDTDDDDDDDDDDDDDDEDNSLFPTREPRSHFFPFDLFPMCPFGCQCYSRVVHCSDLGLTSVPTNIPFDTRMLDLQNNKIKEIKENDFKGLTSLYGLILNNNKLTKIHPKAFLTTKKLRRLYLSHNQLSEIPLNLPKSLAELRIHENKVKKIQKDTFKGMNALHVLEMSANPLDNNGIEPGAFEGVTVFHIRIAEAKLTSVPKGLPPTLLELHLDYNKISTVELEDFKRYKELQRLGLGNNKITDIENGSLANIPRVREIHLENNKLKKIPSGLPELKYLQIIFLHSNSIARVGVNDFCPTVPKMKKSLYSAISLFNNPVKYWEMQPATFRCVLSRMSVQLGNFGM

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q5TBF2Q5TBF2_HUMANASPN243
A0AAG2UW46A0AAG2UW46_HUMANASPN379
A0A494C1J0A0A494C1J0_HUMANASPN152
A0A494C084A0A494C084_HUMANASPN124

Sequence caution

The sequence BAA90967.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias35-55Acidic residues
Sequence conflict238-243in Ref. 3; BAB55060

Polymorphism

The poly-Asp region of ASPN is polymorphic and ranges at least from 11 to 17 Asp (PubMed:11152692).

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF316824
EMBL· GenBank· DDBJ
AAK35161.1
EMBL· GenBank· DDBJ
mRNA
AY029191
EMBL· GenBank· DDBJ
AAK31800.1
EMBL· GenBank· DDBJ
mRNA
AK000136
EMBL· GenBank· DDBJ
BAA90967.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK027359
EMBL· GenBank· DDBJ
BAB55060.1
EMBL· GenBank· DDBJ
mRNA
AY358329
EMBL· GenBank· DDBJ
AAQ88695.1
EMBL· GenBank· DDBJ
mRNA
AL137848
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471089
EMBL· GenBank· DDBJ
EAW62822.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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