Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13443

- ADAM9_HUMAN

UniProt

Q13443 - ADAM9_HUMAN

Protein

Disintegrin and metalloproteinase domain-containing protein 9

Gene

ADAM9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Probable zinc protease. May mediate cell-cell or cell-matrix interactions. Isoform 2 displays alpha-secretase activity for APP.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi347 – 3471Zinc; catalyticBy similarity
    Active sitei348 – 3481PROSITE-ProRule annotation
    Metal bindingi351 – 3511Zinc; catalyticBy similarity
    Metal bindingi357 – 3571Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. collagen binding Source: BHF-UCL
    2. integrin binding Source: BHF-UCL
    3. laminin binding Source: BHF-UCL
    4. metalloendopeptidase activity Source: BHF-UCL
    5. metallopeptidase activity Source: BHF-UCL
    6. protein binding Source: IntAct
    7. protein kinase C binding Source: BHF-UCL
    8. SH3 domain binding Source: BHF-UCL
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of MAPKK activity Source: BHF-UCL
    2. cell adhesion Source: BHF-UCL
    3. cell adhesion mediated by integrin Source: BHF-UCL
    4. cell-cell adhesion mediated by integrin Source: BHF-UCL
    5. cell-matrix adhesion Source: BHF-UCL
    6. cellular response to lipopolysaccharide Source: BHF-UCL
    7. collagen catabolic process Source: Reactome
    8. extracellular matrix disassembly Source: Reactome
    9. extracellular matrix organization Source: Reactome
    10. integrin-mediated signaling pathway Source: BHF-UCL
    11. keratinocyte differentiation Source: BHF-UCL
    12. membrane protein ectodomain proteolysis Source: BHF-UCL
    13. monocyte activation Source: BHF-UCL
    14. PMA-inducible membrane protein ectodomain proteolysis Source: BHF-UCL
    15. positive regulation of cell adhesion mediated by integrin Source: BHF-UCL
    16. positive regulation of keratinocyte migration Source: BHF-UCL
    17. positive regulation of macrophage fusion Source: BHF-UCL
    18. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    19. positive regulation of protein secretion Source: BHF-UCL
    20. response to calcium ion Source: BHF-UCL
    21. response to glucocorticoid Source: BHF-UCL
    22. response to hydrogen peroxide Source: BHF-UCL
    23. response to laminar fluid shear stress Source: Ensembl
    24. response to manganese ion Source: BHF-UCL
    25. response to tumor necrosis factor Source: BHF-UCL
    26. transforming growth factor beta receptor signaling pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM12.209.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 9 (EC:3.4.24.-)
    Short name:
    ADAM 9
    Alternative name(s):
    Cellular disintegrin-related protein
    Meltrin-gamma
    Metalloprotease/disintegrin/cysteine-rich protein 9
    Myeloma cell metalloproteinase
    Gene namesi
    Name:ADAM9
    Synonyms:KIAA0021, MCMP, MDC9, MLTNG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:216. ADAM9.

    Subcellular locationi

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. cell surface Source: BHF-UCL
    3. cytoplasm Source: Ensembl
    4. extracellular space Source: BHF-UCL
    5. integral component of membrane Source: UniProtKB-KW
    6. intrinsic component of external side of plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Cone-rod dystrophy 9 (CORD9) [MIM:612775]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Cone-rod dystrophy

    Organism-specific databases

    MIMi612775. phenotype.
    Orphaneti1872. Cone rod dystrophy.
    PharmGKBiPA24534.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 819791Disintegrin and metalloproteinase domain-containing protein 9PRO_0000029062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi322 ↔ 401By similarity
    Disulfide bondi363 ↔ 385By similarity
    Disulfide bondi365 ↔ 370By similarity
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi473 ↔ 493By similarity
    Glycosylationi487 – 4871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi644 ↔ 656By similarity
    Disulfide bondi650 ↔ 662By similarity
    Disulfide bondi664 ↔ 673By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ13443.
    PaxDbiQ13443.
    PRIDEiQ13443.

    PTM databases

    PhosphoSiteiQ13443.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in chondrocytes. Isoform 2 is highly expressed in liver and heart.4 Publications

    Gene expression databases

    ArrayExpressiQ13443.
    BgeeiQ13443.
    CleanExiHS_ADAM9.
    GenevestigatoriQ13443.

    Organism-specific databases

    HPAiHPA004000.

    Interactioni

    Subunit structurei

    Interacts with SH3GL2 and SNX9 through its cytoplasmic tail.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAD2L2Q9UI953EBI-77903,EBI-77889
    PACSIN3Q9UKS62EBI-77903,EBI-77926
    SH3GL2Q999622EBI-77903,EBI-77938

    Protein-protein interaction databases

    BioGridi114290. 7 interactions.
    IntActiQ13443. 3 interactions.
    MINTiMINT-108373.
    STRINGi9606.ENSP00000305538.

    Structurei

    Secondary structure

    1
    819
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi212 – 2209
    Helixi222 – 2276
    Turni228 – 2303
    Helixi232 – 25019
    Helixi251 – 2533
    Beta strandi255 – 26410
    Helixi277 – 29014
    Turni291 – 2955
    Beta strandi299 – 3057
    Beta strandi311 – 3166
    Beta strandi327 – 3315
    Turni337 – 3393
    Helixi340 – 35213
    Beta strandi369 – 3746
    Helixi384 – 39714
    Helixi400 – 4023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M1Vmodel-A208-404[»]
    ProteinModelPortaliQ13443.
    SMRiQ13443. Positions 212-638, 647-675.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 697669ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini719 – 819101CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei698 – 71821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini212 – 406195Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini414 – 50188DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini644 – 69855EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi505 – 634130Cys-richAdd
    BLAST
    Compositional biasi790 – 7956Poly-Pro

    Sequence similaritiesi

    Contains 1 disintegrin domain.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG294463.
    HOGENOMiHOG000230883.
    HOVERGENiHBG006978.
    InParanoidiQ13443.
    KOiK06834.
    OMAiFCQPDVF.
    OrthoDBiEOG7F7W89.
    PhylomeDBiQ13443.
    TreeFamiTF314733.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProiIPR006586. ADAM_Cys-rich.
    IPR001762. Blood-coag_inhib_Disintegrin.
    IPR018358. Disintegrin_CS.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view]
    PfamiPF08516. ADAM_CR. 1 hit.
    PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    [Graphical view]
    SMARTiSM00608. ACR. 1 hit.
    SM00050. DISIN. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13443-1) [UniParc]FASTAAdd to Basket

    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

    MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR    50
    LTRERREAPR PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE 100
    GTLITDHPNI QNHCHYRGYV EGVHNSSIAL SDCFGLRGLL HLENASYGIE 150
    PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK DIEKETAKDE EEEPPSMTQL 200
    LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI LLANYLDSMY 250
    IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS 300
    AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG 350
    HNLGMNHDDG RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN 400
    CLLNIPKPDE AYSAPSCGNK LVDAGEECDC GTPKECELDP CCEGSTCKLK 450
    SFAECAYGDC CKDCRFLPGG TLCRGKTSEC DVPEYCNGSS QFCQPDVFIQ 500
    NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF IEVNSKGDRF 550
    GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC 600
    WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC 650
    HGHGVCNSNK NCHCENGWAP PNCETKGYGG SVDSGPTYNE MNTALRDGLL 700
    VFFFLIVPLI VCAIFIFIKR DQLWRSYFRK KRSQTYESDG KNQANPSRQP 750
    GSVPRHVSPV TPPREVPIYA NRFAVPTYAA KQPQQFPSRP PPPQPKVSSQ 800
    GNLIPARPAP APPLYSSLT 819
    Length:819
    Mass (Da):90,556
    Last modified:November 1, 1996 - v1
    Checksum:iBC186641833137FF
    GO
    Isoform 2 (identifier: Q13443-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         655-655: V → K
         656-819: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:655
    Mass (Da):72,359
    Checksum:i1E99DD3A056B90B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 118118Missing no nucleotide entry (PubMed:8809033)CuratedAdd
    BLAST
    Sequence conflicti117 – 1171R → Q in BAA03499. (PubMed:7584026)Curated
    Sequence conflicti119 – 13517YVEGV…SDCFG → MWREFIIHPLLLATVLD no nucleotide entry (PubMed:8809033)CuratedAdd
    BLAST
    Sequence conflicti154 – 1541N → M no nucleotide entry (PubMed:8809033)Curated
    Sequence conflicti566 – 5661G → GLSLKFHAPFLSTMLQEAVR QTGTYLGGSVCCMKSDCRIV TLVK no nucleotide entry (PubMed:8809033)Curated
    Sequence conflicti713 – 73523AIFIF…KRSQT → DYFYLHQEGSTVEKLLQKEE ITN no nucleotide entry (PubMed:8809033)CuratedAdd
    BLAST
    Sequence conflicti736 – 81984Missing no nucleotide entry (PubMed:8809033)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei655 – 6551V → K in isoform 2. 2 PublicationsVSP_011057
    Alternative sequencei656 – 819164Missing in isoform 2. 2 PublicationsVSP_011058Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41766 mRNA. Translation: AAC50403.1.
    AF495383 mRNA. Translation: AAM49575.1.
    D14665 mRNA. Translation: BAA03499.2.
    CH471080 Genomic DNA. Translation: EAW63284.1.
    BC143923 mRNA. Translation: AAI43924.1.
    CCDSiCCDS6112.1. [Q13443-1]
    PIRiJC7850.
    S71949.
    RefSeqiNP_003807.1. NM_003816.2. [Q13443-1]
    UniGeneiHs.591852.

    Genome annotation databases

    EnsembliENST00000379917; ENSP00000369249; ENSG00000168615. [Q13443-2]
    ENST00000487273; ENSP00000419446; ENSG00000168615. [Q13443-1]
    GeneIDi8754.
    KEGGihsa:8754.
    UCSCiuc003xmr.3. human. [Q13443-1]

    Polymorphism databases

    DMDMi24211441.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41766 mRNA. Translation: AAC50403.1 .
    AF495383 mRNA. Translation: AAM49575.1 .
    D14665 mRNA. Translation: BAA03499.2 .
    CH471080 Genomic DNA. Translation: EAW63284.1 .
    BC143923 mRNA. Translation: AAI43924.1 .
    CCDSi CCDS6112.1. [Q13443-1 ]
    PIRi JC7850.
    S71949.
    RefSeqi NP_003807.1. NM_003816.2. [Q13443-1 ]
    UniGenei Hs.591852.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M1V model - A 208-404 [» ]
    ProteinModelPortali Q13443.
    SMRi Q13443. Positions 212-638, 647-675.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114290. 7 interactions.
    IntActi Q13443. 3 interactions.
    MINTi MINT-108373.
    STRINGi 9606.ENSP00000305538.

    Chemistry

    BindingDBi Q13443.
    ChEMBLi CHEMBL5982.

    Protein family/group databases

    MEROPSi M12.209.

    PTM databases

    PhosphoSitei Q13443.

    Polymorphism databases

    DMDMi 24211441.

    Proteomic databases

    MaxQBi Q13443.
    PaxDbi Q13443.
    PRIDEi Q13443.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379917 ; ENSP00000369249 ; ENSG00000168615 . [Q13443-2 ]
    ENST00000487273 ; ENSP00000419446 ; ENSG00000168615 . [Q13443-1 ]
    GeneIDi 8754.
    KEGGi hsa:8754.
    UCSCi uc003xmr.3. human. [Q13443-1 ]

    Organism-specific databases

    CTDi 8754.
    GeneCardsi GC08P038871.
    HGNCi HGNC:216. ADAM9.
    HPAi HPA004000.
    MIMi 602713. gene.
    612775. phenotype.
    neXtProti NX_Q13443.
    Orphaneti 1872. Cone rod dystrophy.
    PharmGKBi PA24534.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294463.
    HOGENOMi HOG000230883.
    HOVERGENi HBG006978.
    InParanoidi Q13443.
    KOi K06834.
    OMAi FCQPDVF.
    OrthoDBi EOG7F7W89.
    PhylomeDBi Q13443.
    TreeFami TF314733.

    Enzyme and pathway databases

    Reactomei REACT_150401. Collagen degradation.

    Miscellaneous databases

    GeneWikii ADAM9.
    GenomeRNAii 8754.
    NextBioi 32845.
    PROi Q13443.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13443.
    Bgeei Q13443.
    CleanExi HS_ADAM9.
    Genevestigatori Q13443.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProi IPR006586. ADAM_Cys-rich.
    IPR001762. Blood-coag_inhib_Disintegrin.
    IPR018358. Disintegrin_CS.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view ]
    Pfami PF08516. ADAM_CR. 1 hit.
    PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    [Graphical view ]
    SMARTi SM00608. ACR. 1 hit.
    SM00050. DISIN. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains."
      Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P.
      J. Cell Biol. 132:717-726(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Mammary carcinoma.
    2. "Cloning of a novel membrane-linked metalloproteinase from human myeloma cells."
      McKie N., Dallas D.J., Edwards T., Apperley J.F., Russell R.G.G., Croucher P.I.
      Biochem. J. 318:459-462(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "A secreted form of human ADAM9 has an alpha-secretase activity for APP."
      Hotoda N., Koike H., Sasagawa N., Ishiura S.
      Biochem. Biophys. Res. Commun. 293:800-805(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    5. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Tissue: Lung.
    8. "Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes."
      McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R., Russell G., Croucher P.I.
      Biochem. Biophys. Res. Commun. 230:335-339(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
      Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
      J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH3GL2 AND SNX9.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: INVOLVEMENT IN CORD9.
    12. "Exploring the substrate affinities of MMP-3, ADAM-9 and ADAM-10 using molecular modelling and dynamics simulations."
      Manzetti S., McCulloch D.R., Herington A.C.
      Submitted (JUN-2002) to the PDB data bank
      Cited for: 3D-STRUCTURE MODELING OF 208-404.

    Entry informationi

    Entry nameiADAM9_HUMAN
    AccessioniPrimary (citable) accession number: Q13443
    Secondary accession number(s): B7ZLN7, Q10718, Q8NFM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3