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Q9BXN1

- ASPN_HUMAN

UniProt

Q9BXN1 - ASPN_HUMAN

Protein

Asporin

Gene

ASPN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    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.By similarity2 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB

    GO - Biological processi

    1. bone mineralization Source: UniProtKB
    2. negative regulation of tooth mineralization Source: UniProtKB
    3. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Biomineralization

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_163906. ECM proteoglycans.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asporin
    Alternative name(s):
    Periodontal ligament-associated protein 1
    Short name:
    PLAP-1
    Gene namesi
    Name:ASPN
    Synonyms:PLAP1, SLRR1C
    ORF Names:UNQ215/PRO241
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:14872. ASPN.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix 1 Publication

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.
    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.1 Publication
    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 (PubMed:18304494).1 Publication

    Organism-specific databases

    MIMi603932. phenotype.
    607850. phenotype.
    PharmGKBiPA25057.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Sequence AnalysisAdd
    BLAST
    Propeptidei15 – 3218Sequence AnalysisPRO_0000032727Add
    BLAST
    Chaini33 – 380348AsporinPRO_0000032728Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi55 – 551O-linked (GalNAc...)1 Publication
    Disulfide bondi75 ↔ 811 Publication
    Disulfide bondi79 ↔ 881 Publication
    Glycosylationi282 – 2821N-linked (GlcNAc...)2 Publications
    Disulfide bondi333 ↔ 3661 Publication

    Post-translational modificationi

    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.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9BXN1.
    PRIDEiQ9BXN1.

    PTM databases

    PhosphoSiteiQ9BXN1.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Inductioni

    By TGFB1.1 Publication

    Gene expression databases

    ArrayExpressiQ9BXN1.
    BgeeiQ9BXN1.
    CleanExiHS_ASPN.
    GenevestigatoriQ9BXN1.

    Organism-specific databases

    HPAiHPA008435.
    HPA024230.

    Interactioni

    Subunit structurei

    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.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000364694.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXN1.
    SMRiQ9BXN1. Positions 74-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 10237LRRNTAdd
    BLAST
    Repeati103 – 12422LRR 1Add
    BLAST
    Repeati127 – 14822LRR 2Add
    BLAST
    Repeati151 – 17323LRR 3Add
    BLAST
    Repeati174 – 19320LRR 4Add
    BLAST
    Repeati196 – 21924LRR 5Add
    BLAST
    Repeati242 – 26322LRR 6Add
    BLAST
    Repeati266 – 28722LRR 7Add
    BLAST
    Repeati290 – 31223LRR 8Add
    BLAST
    Repeati313 – 33422LRR 9Add
    BLAST
    Repeati335 – 35723LRR 10Add
    BLAST
    Repeati358 – 38023LRR 11Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 21247Interaction with TGFB1By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi35 – 5319Poly-AspAdd
    BLAST
    Compositional biasi77 – 9014Cys-richAdd
    BLAST

    Domaini

    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.By similarity1 Publication

    Sequence similaritiesi

    Contains 11 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    HOVERGENiHBG016052.
    InParanoidiQ9BXN1.
    KOiK08120.
    OMAiEDFIRYK.
    OrthoDBiEOG76739V.
    PhylomeDBiQ9BXN1.
    TreeFamiTF334562.

    Family and domain databases

    InterProiIPR028548. Asporin.
    IPR001611. Leu-rich_rpt.
    IPR000372. LRR-contain_N.
    IPR016352. SLRP_I_decor/aspor/byglycan.
    [Graphical view]
    PANTHERiPTHR24369:SF10. PTHR24369:SF10. 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. 7 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9BXN1-1 [UniParc]FASTAAdd to Basket

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    MKEYVLLLFL ALCSAKPFFS PSHIALKNMM LKDMEDTDDD DDDDDDDDDD    50
    DEDNSLFPTR EPRSHFFPFD LFPMCPFGCQ CYSRVVHCSD LGLTSVPTNI 100
    PFDTRMLDLQ NNKIKEIKEN DFKGLTSLYG LILNNNKLTK IHPKAFLTTK 150
    KLRRLYLSHN QLSEIPLNLP KSLAELRIHE NKVKKIQKDT FKGMNALHVL 200
    EMSANPLDNN GIEPGAFEGV TVFHIRIAEA KLTSVPKGLP PTLLELHLDY 250
    NKISTVELED FKRYKELQRL GLGNNKITDI ENGSLANIPR VREIHLENNK 300
    LKKIPSGLPE LKYLQIIFLH SNSIARVGVN DFCPTVPKMK KSLYSAISLF 350
    NNPVKYWEMQ PATFRCVLSR MSVQLGNFGM 380
    Length:380
    Mass (Da):43,417
    Last modified:October 14, 2008 - v2
    Checksum:i2746A977FDCEBA5F
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2436GLPPTL → DNLPSF in BAB55060. (PubMed:14702039)Curated

    Polymorphismi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_001180264.1. NM_001193335.1.
    NP_060150.4. NM_017680.4.
    UniGeneiHs.435655.

    Genome annotation databases

    EnsembliENST00000375544; ENSP00000364694; ENSG00000106819.
    GeneIDi54829.
    KEGGihsa:54829.
    UCSCiuc004ase.2. human.

    Polymorphism databases

    DMDMi209572589.

    Keywords - Coding sequence diversityi

    Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_001180264.1. NM_001193335.1.
    NP_060150.4. NM_017680.4.
    UniGenei Hs.435655.

    3D structure databases

    ProteinModelPortali Q9BXN1.
    SMRi Q9BXN1. Positions 74-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000364694.

    PTM databases

    PhosphoSitei Q9BXN1.

    Polymorphism databases

    DMDMi 209572589.

    Proteomic databases

    PaxDbi Q9BXN1.
    PRIDEi Q9BXN1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375544 ; ENSP00000364694 ; ENSG00000106819 .
    GeneIDi 54829.
    KEGGi hsa:54829.
    UCSCi uc004ase.2. human.

    Organism-specific databases

    CTDi 54829.
    GeneCardsi GC09M095218.
    HGNCi HGNC:14872. ASPN.
    HPAi HPA008435.
    HPA024230.
    MIMi 603932. phenotype.
    607850. phenotype.
    608135. gene.
    neXtProti NX_Q9BXN1.
    PharmGKBi PA25057.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOVERGENi HBG016052.
    InParanoidi Q9BXN1.
    KOi K08120.
    OMAi EDFIRYK.
    OrthoDBi EOG76739V.
    PhylomeDBi Q9BXN1.
    TreeFami TF334562.

    Enzyme and pathway databases

    Reactomei REACT_163906. ECM proteoglycans.

    Miscellaneous databases

    GeneWikii Asporin.
    GenomeRNAii 54829.
    NextBioi 57604.
    PROi Q9BXN1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BXN1.
    Bgeei Q9BXN1.
    CleanExi HS_ASPN.
    Genevestigatori Q9BXN1.

    Family and domain databases

    InterProi IPR028548. Asporin.
    IPR001611. Leu-rich_rpt.
    IPR000372. LRR-contain_N.
    IPR016352. SLRP_I_decor/aspor/byglycan.
    [Graphical view ]
    PANTHERi PTHR24369:SF10. PTHR24369:SF10. 1 hit.
    Pfami PF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002490. SLRP_I. 1 hit.
    SMARTi SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiASPN_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXN1
    Secondary accession number(s): Q5TBF3
    , Q96K79, Q96LD0, Q9NXP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 129 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3