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Q9P2N4

- ATS9_HUMAN

UniProt

Q9P2N4 - ATS9_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 9

Gene

ADAMTS9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 4 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Cleaves the large aggregating proteoglycans, aggrecan and versican. Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos.2 Publications

    Catalytic activityi

    Cleaves aggrecan at the 1838-Glu-|-Ala-1839 site and versican at the 1428-Glu-|-Ala-1429 site.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi223 – 2231Zinc; in inhibited formBy similarity
    Metal bindingi434 – 4341Zinc; catalyticBy similarity
    Active sitei435 – 4351PROSITE-ProRule annotation
    Metal bindingi438 – 4381Zinc; catalyticBy similarity
    Metal bindingi444 – 4441Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. metallopeptidase activity Source: MGI
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. glycoprotein catabolic process Source: ProtInc
    2. multicellular organismal development Source: ProtInc
    3. positive regulation of melanocyte differentiation Source: Ensembl
    4. protein transport Source: UniProtKB-KW
    5. proteolysis Source: MGI
    6. vesicle-mediated transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 9 (EC:3.4.24.-)
    Short name:
    ADAM-TS 9
    Short name:
    ADAM-TS9
    Short name:
    ADAMTS-9
    Gene namesi
    Name:ADAMTS9
    Synonyms:KIAA1312
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:13202. ADAMTS9.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix By similarity. Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. extracellular space Source: Ensembl
    3. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24553.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 287269PRO_0000029182Add
    BLAST
    Chaini288 – 19351648A disintegrin and metalloproteinase with thrombospondin motifs 9PRO_0000029183Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi368 ↔ 418By similarity
    Disulfide bondi394 ↔ 400By similarity
    Disulfide bondi412 ↔ 494By similarity
    Disulfide bondi450 ↔ 478By similarity
    Disulfide bondi521 ↔ 543By similarity
    Disulfide bondi532 ↔ 553By similarity
    Disulfide bondi538 ↔ 572By similarity
    Disulfide bondi566 ↔ 577By similarity
    Disulfide bondi600 ↔ 637By similarity
    Disulfide bondi604 ↔ 642By similarity
    Disulfide bondi615 ↔ 627By similarity
    Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi840 – 8401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi890 ↔ 931By similarity
    Disulfide bondi894 ↔ 935By similarity
    Disulfide bondi904 ↔ 918By similarity
    Glycosylationi1213 – 12131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1250 ↔ 1290By similarity
    Disulfide bondi1254 ↔ 1295By similarity
    Disulfide bondi1265 ↔ 1278By similarity
    Glycosylationi1267 – 12671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1624 ↔ 1670By similarity
    Disulfide bondi1628 ↔ 1675By similarity
    Disulfide bondi1639 ↔ 1659By similarity
    Glycosylationi1788 – 17881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1806 – 18061N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9P2N4.
    PRIDEiQ9P2N4.

    PTM databases

    PhosphoSiteiQ9P2N4.

    Miscellaneous databases

    PMAP-CutDBQ9P2N4.

    Expressioni

    Tissue specificityi

    Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ9P2N4.
    BgeeiQ9P2N4.
    CleanExiHS_ADAMTS9.
    GenevestigatoriQ9P2N4.

    Organism-specific databases

    HPAiHPA028567.
    HPA028577.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9P2N4. 1 interaction.
    STRINGi9606.ENSP00000418735.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P2N4.
    SMRiQ9P2N4. Positions 293-759.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini293 – 499207Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini509 – 58779DisintegrinAdd
    BLAST
    Domaini588 – 64356TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini878 – 93659TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini939 – 99759TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini998 – 104952TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1052 – 110958TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1110 – 116657TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1182 – 124059TSP type-1 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1241 – 129656TSP type-1 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1328 – 137952TSP type-1 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1382 – 144059TSP type-1 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1441 – 149454TSP type-1 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1497 – 155559TSP type-1 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1556 – 161156TSP type-1 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1612 – 167665TSP type-1 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1677 – 173458TSP type-1 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1735 – 1935201GONPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni753 – 877125SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi221 – 2288Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi88 – 969Poly-Ser
    Compositional biasi644 – 752109Cys-richAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.By similarity
    The ancillary domains, including the TSRs domain, are required for specific extracellular localization and for its versicanase and aggrecanase activities.
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
    The GON domain mediates protease-independent function in ER to Golgi transport.

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 GON domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 15 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG237764.
    HOGENOMiHOG000004798.
    HOVERGENiHBG037334.
    InParanoidiQ9P2N4.
    KOiK08624.
    OMAiCQGERKR.
    PhylomeDBiQ9P2N4.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 2 hits.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR012314. Pept_M12B_GON-ADAMTSs.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF08685. GON. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 13 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 15 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 14 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS51046. GON. 1 hit.
    PS50092. TSP1. 14 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P2N4-3) [UniParc]FASTAAdd to Basket

    Also known as: ADAMTS-9B

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI     50
    VSPIRVNALG EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY 100
    RLSAFGQQFL FNLTANAGFI APLFTVTLLG TPGVNQTKFY SEEEAELKHC 150
    FYKGYVNTNS EHTAVISLCS GMLGTFRSHD GDYFIEPLQS MDEQEDEEEQ 200
    NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR ARKWGERINL 250
    AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV 300
    ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE 350
    QDGPSISFNA QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC 400
    DTLGLAELGT ICDPYRSCSI SEDSGLSTAF TIAHELGHVF NMPHDDNNKC 450
    KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR KYITEFLDTG YGECLLNEPE 500
    SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR LWCNNVNGVH 550
    KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC 600
    SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR 650
    DEQCAHFDGK HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ 700
    LRDRVIDGTP CGQDTNDICV QGLCRQAGCD HVLNSKARRD KCGVCGGDNS 750
    SCKTVAGTFN TVHYGYNTVV RIPAGATNID VRQHSFSGET DDDNYLALSS 800
    SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN STDRIEQELL 850
    LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR 900
    KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ 950
    CGLGYRTLDI YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG 1000
    WRYSAWTECS KSCDGGTQRR RAICVNTRND VLDDSKCTHQ EKVTIQRCSE 1050
    FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ FGEDRLNDRM CDPETKPTSM 1100
    QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM SVVDDNDCNA 1150
    ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK 1200
    GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC 1250
    SVTCGQGRAT RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP 1300
    DSGLAQHPFQ NEDYRPRSAS PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR 1350
    RVVVCQDENG YTANDCVERI KPDEQRACES GPCPQWAYGN WGECTKLCGG 1400
    GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP HDAAWSTGPW 1450
    SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK 1500
    WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ 1550
    GPRCPLYTWR AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR 1600
    PVDRESCSLQ PCEYVWITGE WSECSVTCGK GYKQRLVSCS EIYTGKENYE 1650
    YSYQTTINCP GTQPPSVHPC YLRDCPVSAT WRVGNWGSCS VSCGVGVMQR 1700
    SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK EVKRLKGASE 1750
    DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP 1800
    TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS 1850
    EGHPVPFATA GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS 1900
    DIKKSPDGTR VVGKCGGYCG KCTPSSGTGL EVRVL 1935
    Length:1,935
    Mass (Da):216,491
    Last modified:November 4, 2008 - v4
    Checksum:i150B78D4C5CC2CCC
    GO
    Isoform 2 (identifier: Q9P2N4-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1624-1629: CSVTCG → VPSWEL
         1630-1935: Missing.

    Note: May result from the retention of an intron in the cDNA leading to a prematurate stop codon.

    Show »
    Length:1,629
    Mass (Da):182,680
    Checksum:iE72B933CEED67809
    GO
    Isoform 3 (identifier: Q9P2N4-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1064-1072: CLVTCGKGH → VRWEGCYFP
         1073-1935: Missing.

    Show »
    Length:1,072
    Mass (Da):120,717
    Checksum:i85251C8E59449E0C
    GO
    Isoform 4 (identifier: Q9P2N4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         324-351: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,907
    Mass (Da):213,420
    Checksum:i24BD2199B1142022
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461S → G in AAF89106. (PubMed:10936055)Curated
    Sequence conflicti182 – 1821D → G in AAO15765. (PubMed:12514189)Curated
    Sequence conflicti367 – 3671F → L in AAF89106. (PubMed:10936055)Curated
    Sequence conflicti1117 – 11171G → V in AAO15765. (PubMed:12514189)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961S → P.1 Publication
    Corresponds to variant rs36115950 [ dbSNP | Ensembl ].
    VAR_047081
    Natural varianti96 – 961S → T.
    Corresponds to variant rs36115950 [ dbSNP | Ensembl ].
    VAR_051592
    Natural varianti1579 – 15791K → E.
    Corresponds to variant rs17071010 [ dbSNP | Ensembl ].
    VAR_047082
    Natural varianti1674 – 16741D → E.1 Publication
    Corresponds to variant rs6787633 [ dbSNP | Ensembl ].
    VAR_047083
    Natural varianti1740 – 17401K → R.
    Corresponds to variant rs17070967 [ dbSNP | Ensembl ].
    VAR_047084
    Natural varianti1791 – 17911E → Q.
    Corresponds to variant rs3796381 [ dbSNP | Ensembl ].
    VAR_047085
    Natural varianti1921 – 19211K → E.
    Corresponds to variant rs17070909 [ dbSNP | Ensembl ].
    VAR_051593
    Natural varianti1933 – 19331R → Q.
    Corresponds to variant rs17070905 [ dbSNP | Ensembl ].
    VAR_047086

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei324 – 35128Missing in isoform 4. 1 PublicationVSP_053399Add
    BLAST
    Alternative sequencei1064 – 10729CLVTCGKGH → VRWEGCYFP in isoform 3. 1 PublicationVSP_005499
    Alternative sequencei1073 – 1935863Missing in isoform 3. 1 PublicationVSP_005500Add
    BLAST
    Alternative sequencei1624 – 16296CSVTCG → VPSWEL in isoform 2. 1 PublicationVSP_007548
    Alternative sequencei1630 – 1935306Missing in isoform 2. 1 PublicationVSP_007549Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261918 mRNA. Translation: AAF89106.1.
    AF488803 mRNA. Translation: AAO15765.1.
    AC096888 Genomic DNA. No translation available.
    AC122178 Genomic DNA. No translation available.
    BC130578 mRNA. Translation: AAI30579.1.
    BC171764 mRNA. Translation: AAI71764.1.
    AB037733 mRNA. Translation: BAA92550.1.
    CCDSiCCDS2903.1. [Q9P2N4-3]
    RefSeqiNP_891550.1. NM_182920.1. [Q9P2N4-3]
    XP_005265386.1. XM_005265329.1. [Q9P2N4-4]
    UniGeneiHs.656071.

    Genome annotation databases

    EnsembliENST00000295903; ENSP00000295903; ENSG00000163638. [Q9P2N4-4]
    ENST00000498707; ENSP00000418735; ENSG00000163638. [Q9P2N4-3]
    GeneIDi56999.
    KEGGihsa:56999.
    UCSCiuc003dmg.3. human. [Q9P2N4-3]
    uc003dmh.1. human. [Q9P2N4-1]
    uc003dmk.1. human. [Q9P2N4-2]
    uc011bfo.2. human.

    Polymorphism databases

    DMDMi212276516.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261918 mRNA. Translation: AAF89106.1 .
    AF488803 mRNA. Translation: AAO15765.1 .
    AC096888 Genomic DNA. No translation available.
    AC122178 Genomic DNA. No translation available.
    BC130578 mRNA. Translation: AAI30579.1 .
    BC171764 mRNA. Translation: AAI71764.1 .
    AB037733 mRNA. Translation: BAA92550.1 .
    CCDSi CCDS2903.1. [Q9P2N4-3 ]
    RefSeqi NP_891550.1. NM_182920.1. [Q9P2N4-3 ]
    XP_005265386.1. XM_005265329.1. [Q9P2N4-4 ]
    UniGenei Hs.656071.

    3D structure databases

    ProteinModelPortali Q9P2N4.
    SMRi Q9P2N4. Positions 293-759.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9P2N4. 1 interaction.
    STRINGi 9606.ENSP00000418735.

    Protein family/group databases

    MEROPSi M12.021.

    PTM databases

    PhosphoSitei Q9P2N4.

    Polymorphism databases

    DMDMi 212276516.

    Proteomic databases

    PaxDbi Q9P2N4.
    PRIDEi Q9P2N4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295903 ; ENSP00000295903 ; ENSG00000163638 . [Q9P2N4-4 ]
    ENST00000498707 ; ENSP00000418735 ; ENSG00000163638 . [Q9P2N4-3 ]
    GeneIDi 56999.
    KEGGi hsa:56999.
    UCSCi uc003dmg.3. human. [Q9P2N4-3 ]
    uc003dmh.1. human. [Q9P2N4-1 ]
    uc003dmk.1. human. [Q9P2N4-2 ]
    uc011bfo.2. human.

    Organism-specific databases

    CTDi 56999.
    GeneCardsi GC03M064501.
    HGNCi HGNC:13202. ADAMTS9.
    HPAi HPA028567.
    HPA028577.
    MIMi 605421. gene.
    neXtProti NX_Q9P2N4.
    PharmGKBi PA24553.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237764.
    HOGENOMi HOG000004798.
    HOVERGENi HBG037334.
    InParanoidi Q9P2N4.
    KOi K08624.
    OMAi CQGERKR.
    PhylomeDBi Q9P2N4.
    TreeFami TF331949.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Miscellaneous databases

    GeneWikii ADAMTS9.
    GenomeRNAii 56999.
    NextBioi 35481460.
    PMAP-CutDB Q9P2N4.
    PROi Q9P2N4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P2N4.
    Bgeei Q9P2N4.
    CleanExi HS_ADAMTS9.
    Genevestigatori Q9P2N4.

    Family and domain databases

    Gene3Di 3.40.390.10. 2 hits.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR012314. Pept_M12B_GON-ADAMTSs.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF08685. GON. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 13 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 15 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 14 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS51046. GON. 1 hit.
    PS50092. TSP1. 14 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family."
      Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A., Maki R.A.
      Genomics 67:343-350(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Fetus.
    2. "Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
      Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
      J. Biol. Chem. 278:9503-9513(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS PRO-96 AND GLU-1674.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 4).
    5. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2).
      Tissue: Brain.
    6. "Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi."
      Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H., Iino Y., Mitani S.
      Mol. Biol. Cell 23:1728-1741(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSPORT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiATS9_HUMAN
    AccessioniPrimary (citable) accession number: Q9P2N4
    Secondary accession number(s): A1L4L0
    , B7ZVX9, B9ZVN0, Q9NR29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3