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P78325

- ADAM8_HUMAN

UniProt

P78325 - ADAM8_HUMAN

Protein

Disintegrin and metalloproteinase domain-containing protein 8

Gene

ADAM8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Possible involvement in extravasation of leukocytes.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi334 – 3341Zinc; catalytic
    Active sitei335 – 3351PROSITE-ProRule annotation
    Metal bindingi338 – 3381Zinc; catalytic
    Metal bindingi344 – 3441Zinc; catalytic

    GO - Molecular functioni

    1. calcium ion binding Source: BHF-UCL
    2. cell adhesion molecule binding Source: BHF-UCL
    3. metalloendopeptidase activity Source: InterPro
    4. metallopeptidase activity Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. protein self-association Source: BHF-UCL
    7. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. activation of MAPK activity involved in innate immune response Source: BHF-UCL
    2. angiogenesis Source: BHF-UCL
    3. cell morphogenesis Source: BHF-UCL
    4. cellular response to hypoxia Source: BHF-UCL
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. inflammatory response Source: BHF-UCL
    8. leukocyte migration involved in inflammatory response Source: BHF-UCL
    9. lymphocyte chemotaxis Source: BHF-UCL
    10. negative regulation of neuron apoptotic process Source: BHF-UCL
    11. positive regulation of acute inflammatory response Source: BHF-UCL
    12. positive regulation of bone resorption Source: BHF-UCL
    13. positive regulation of cell adhesion Source: BHF-UCL
    14. positive regulation of eosinophil migration Source: BHF-UCL
    15. positive regulation of fibronectin-dependent thymocyte migration Source: BHF-UCL
    16. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    17. positive regulation of neutrophil extravasation Source: BHF-UCL
    18. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    19. positive regulation of protein kinase B signaling Source: BHF-UCL
    20. positive regulation of protein processing Source: BHF-UCL
    21. positive regulation of protein secretion Source: BHF-UCL
    22. positive regulation of T cell differentiation in thymus Source: BHF-UCL
    23. positive regulation of thymocyte apoptotic process Source: BHF-UCL
    24. positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: BHF-UCL
    25. regulation of cell-cell adhesion Source: BHF-UCL
    26. single organismal cell-cell adhesion Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.208.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 8 (EC:3.4.24.-)
    Short name:
    ADAM 8
    Alternative name(s):
    Cell surface antigen MS2
    CD_antigen: CD156a
    Gene namesi
    Name:ADAM8
    Synonyms:MS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:215. ADAM8.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha9-beta1 integrin-ADAM8 complex Source: BHF-UCL
    2. cell surface Source: BHF-UCL
    3. cytoplasm Source: BHF-UCL
    4. dense core granule membrane Source: BHF-UCL
    5. integral component of plasma membrane Source: BHF-UCL
    6. phagolysosome Source: BHF-UCL
    7. plasma membrane Source: BHF-UCL
    8. podosome Source: BHF-UCL
    9. specific granule Source: BHF-UCL
    10. tertiary granule Source: BHF-UCL

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 824808Disintegrin and metalloproteinase domain-containing protein 8PRO_0000029060Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi310 ↔ 395By similarity
    Disulfide bondi351 ↔ 379By similarity
    Disulfide bondi353 ↔ 362By similarity
    Glycosylationi436 – 4361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi466 ↔ 486By similarity
    Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi613 ↔ 623By similarity
    Disulfide bondi617 ↔ 629By similarity
    Disulfide bondi631 ↔ 640By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP78325.
    PaxDbiP78325.
    PRIDEiP78325.

    PTM databases

    PhosphoSiteiP78325.

    Expressioni

    Tissue specificityi

    Expressed on neutrophils and monocytes.

    Gene expression databases

    ArrayExpressiP78325.
    CleanExiHS_ADAM8.
    GenevestigatoriP78325.

    Interactioni

    Subunit structurei

    Interacts with FST3.2 Publications

    Protein-protein interaction databases

    IntActiP78325. 2 interactions.
    STRINGi9606.ENSP00000390728.

    Structurei

    Secondary structure

    1
    824
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi200 – 2089
    Helixi210 – 2167
    Helixi219 – 23719
    Helixi238 – 2403
    Beta strandi242 – 25110
    Helixi264 – 27613
    Beta strandi286 – 2927
    Beta strandi302 – 3043
    Beta strandi315 – 3195
    Helixi325 – 33915
    Helixi345 – 3473
    Helixi378 – 38710
    Helixi391 – 3966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DD8X-ray2.10A/B/C/D196-403[»]
    ProteinModelPortaliP78325.
    SMRiP78325. Positions 197-605, 617-643.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 655639ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini677 – 824148CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei656 – 67621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini200 – 400201Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini408 – 49487DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini609 – 64133EGF-likePROSITE-ProRule annotationAdd
    BLAST

    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

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG310718.
    HOVERGENiHBG006978.
    InParanoidiP78325.
    KOiK06540.
    OMAiCYNGACP.
    OrthoDBiEOG74N5G6.
    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]
    PRINTSiPR00289. DISINTEGRIN.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78325-1) [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

    MRGLGLWLLG AMMLPAIAPS RPWALMEQYE VVLPWRLPGP RVRRALPSHL    50
    GLHPERVSYV LGATGHNFTL HLRKNRDLLG SGYTETYTAA NGSEVTEQPR 100
    GQDHCFYQGH VEGYPDSAAS LSTCAGLRGF FQVGSDLHLI EPLDEGGEGG 150
    RHAVYQAEHL LQTAGTCGVS DDSLGSLLGP RTAAVFRPRP GDSLPSRETR 200
    YVELYVVVDN AEFQMLGSEA AVRHRVLEVV NHVDKLYQKL NFRVVLVGLE 250
    IWNSQDRFHV SPDPSVTLEN LLTWQARQRT RRHLHDNVQL ITGVDFTGTT 300
    VGFARVSAMC SHSSGAVNQD HSKNPVGVAC TMAHEMGHNL GMDHDENVQG 350
    CRCQERFEAG RCIMAGSIGS SFPRMFSDCS QAYLESFLER PQSVCLANAP 400
    DLSHLVGGPV CGNLFVERGE QCDCGPPEDC RNRCCNSTTC QLAEGAQCAH 450
    GTCCQECKVK PAGELCRPKK DMCDLEEFCD GRHPECPEDA FQENGTPCSG 500
    GYCYNGACPT LAQQCQAFWG PGGQAAEESC FSYDILPGCK ASRYRADMCG 550
    VLQCKGGQQP LGRAICIVDV CHALTTEDGT AYEPVPEGTR CGPEKVCWKG 600
    RCQDLHVYRS SNCSAQCHNH GVCNHKQECH CHAGWAPPHC AKLLTEVHAA 650
    SGSLPVFVVV VLVLLAVVLV TLAGIIVYRK ARSRILSRNV APKTTMGRSN 700
    PLFHQAASRV PAKGGAPAPS RGPQELVPTT HPGQPARHPA SSVALKRPPP 750
    APPVTVSSPP FPVPVYTRQA PKQVIKPTFA PPVPPVKPGA GAANPGPAEG 800
    AVGPKVALKP PIQRKQGAGA PTAP 824
    Length:824
    Mass (Da):88,771
    Last modified:October 3, 2012 - v2
    Checksum:iCE3D31330E153DB8
    GO
    Isoform 2 (identifier: P78325-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-92: AIAPSRPWAL...YTETYTAANG → GPAPREGELR...SRQPQHLCRP
         93-131: Missing.
         596-621: Missing.
         774-799: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:733
    Mass (Da):78,850
    Checksum:i56F70752E92C2FE4
    GO
    Isoform 3 (identifier: P78325-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         650-742: ASGSLPVFVV...GQPARHPASS → GCQPRAGQGR...RGWCGQPWSS
         743-824: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:742
    Mass (Da):80,262
    Checksum:iF02B705D4AA89ED3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061F → L in BAA05626. (PubMed:9126482)Curated
    Sequence conflicti372 – 3721F → L in BAG62738. (PubMed:14702039)Curated
    Sequence conflicti648 – 6481H → D in BAG62738. (PubMed:14702039)Curated
    Isoform 2 (identifier: P78325-2)
    Sequence conflicti46 – 461L → F in BAG62738. (PubMed:14702039)Curated
    Isoform 3 (identifier: P78325-3)
    Sequence conflicti693 – 6931A → S in BC064500. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351W → R.2 Publications
    Corresponds to variant rs2275725 [ dbSNP | Ensembl ].
    VAR_069144
    Natural varianti101 – 1011G → R.
    Corresponds to variant rs11101675 [ dbSNP | Ensembl ].
    VAR_059760
    Natural varianti189 – 1891R → W.
    Corresponds to variant rs45451297 [ dbSNP | Ensembl ].
    VAR_061735
    Natural varianti433 – 4331R → C.
    Corresponds to variant rs12257830 [ dbSNP | Ensembl ].
    VAR_061736
    Natural varianti657 – 6571F → L.1 Publication
    Corresponds to variant rs2275720 [ dbSNP | Ensembl ].
    VAR_069145
    Natural varianti775 – 7751I → T.
    Corresponds to variant rs3008319 [ dbSNP | Ensembl ].
    VAR_061737

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei16 – 9277AIAPS…TAANG → GPAPREGELRPWGHRAQLHP PPAEEQGPAGLRLHRDLYGC QWLRGDGAASRAGPLLLPGP RRGVPGLSRQPQHLCRP in isoform 2. 1 PublicationVSP_046154Add
    BLAST
    Alternative sequencei93 – 13139Missing in isoform 2. 1 PublicationVSP_046155Add
    BLAST
    Alternative sequencei596 – 62126Missing in isoform 2. 1 PublicationVSP_046156Add
    BLAST
    Alternative sequencei650 – 74293ASGSL…HPASS → GCQPRAGQGRGSSPIQGPPR AGPHHPPGPARPTPGLLGGS EEAAPCSSGHCVQPTLPSSC LHPAGTKAGHQANVRTPSAP SQTRGWCGQPWSS in isoform 3. 1 PublicationVSP_046157Add
    BLAST
    Alternative sequencei743 – 82482Missing in isoform 3. 1 PublicationVSP_046158Add
    BLAST
    Alternative sequencei774 – 79926Missing in isoform 2. 1 PublicationVSP_046159Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26579 mRNA. Translation: BAA05626.1.
    AK301147 mRNA. Translation: BAG62738.1.
    AL592071 Genomic DNA. No translation available.
    BC064500 mRNA. No translation available.
    CCDSiCCDS31319.2. [P78325-1]
    CCDS58102.1. [P78325-2]
    CCDS58103.1. [P78325-3]
    RefSeqiNP_001100.3. NM_001109.4. [P78325-1]
    NP_001157961.1. NM_001164489.1. [P78325-3]
    NP_001157962.1. NM_001164490.1. [P78325-2]
    UniGeneiHs.501574.

    Genome annotation databases

    EnsembliENST00000415217; ENSP00000453855; ENSG00000151651. [P78325-3]
    ENST00000445355; ENSP00000453302; ENSG00000151651. [P78325-1]
    ENST00000485491; ENSP00000453043; ENSG00000151651. [P78325-2]
    GeneIDi101.
    KEGGihsa:101.
    UCSCiuc021qbe.1. human. [P78325-1]

    Polymorphism databases

    DMDMi408359955.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26579 mRNA. Translation: BAA05626.1 .
    AK301147 mRNA. Translation: BAG62738.1 .
    AL592071 Genomic DNA. No translation available.
    BC064500 mRNA. No translation available.
    CCDSi CCDS31319.2. [P78325-1 ]
    CCDS58102.1. [P78325-2 ]
    CCDS58103.1. [P78325-3 ]
    RefSeqi NP_001100.3. NM_001109.4. [P78325-1 ]
    NP_001157961.1. NM_001164489.1. [P78325-3 ]
    NP_001157962.1. NM_001164490.1. [P78325-2 ]
    UniGenei Hs.501574.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DD8 X-ray 2.10 A/B/C/D 196-403 [» ]
    ProteinModelPortali P78325.
    SMRi P78325. Positions 197-605, 617-643.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P78325. 2 interactions.
    STRINGi 9606.ENSP00000390728.

    Chemistry

    BindingDBi P78325.
    ChEMBLi CHEMBL5665.

    Protein family/group databases

    MEROPSi M12.208.

    PTM databases

    PhosphoSitei P78325.

    Polymorphism databases

    DMDMi 408359955.

    Proteomic databases

    MaxQBi P78325.
    PaxDbi P78325.
    PRIDEi P78325.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000415217 ; ENSP00000453855 ; ENSG00000151651 . [P78325-3 ]
    ENST00000445355 ; ENSP00000453302 ; ENSG00000151651 . [P78325-1 ]
    ENST00000485491 ; ENSP00000453043 ; ENSG00000151651 . [P78325-2 ]
    GeneIDi 101.
    KEGGi hsa:101.
    UCSCi uc021qbe.1. human. [P78325-1 ]

    Organism-specific databases

    CTDi 101.
    GeneCardsi GC10M135075.
    H-InvDB HIX0035404.
    HGNCi HGNC:215. ADAM8.
    MIMi 602267. gene.
    neXtProti NX_P78325.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310718.
    HOVERGENi HBG006978.
    InParanoidi P78325.
    KOi K06540.
    OMAi CYNGACP.
    OrthoDBi EOG74N5G6.
    TreeFami TF314733.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.

    Miscellaneous databases

    GeneWikii ADAM8.
    GenomeRNAii 101.
    NextBioi 381.
    PROi P78325.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78325.
    CleanExi HS_ADAM8.
    Genevestigatori P78325.

    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 ]
    PRINTSi PR00289. DISINTEGRIN.
    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. "CD156 (human ADAM8): expression, primary amino acid sequence, and gene location."
      Yoshiyama K., Higuchi Y., Kataoka M., Matsuura K., Yamamoto S.
      Genomics 41:56-62(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-35.
      Tissue: Blood.
    2. "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] (ISOFORM 2), VARIANT LEU-657.
      Tissue: Spleen.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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] (ISOFORM 3), VARIANT ARG-35.
      Tissue: Pancreatic cancer.
    5. "FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation."
      Bartholin L., Destaing O., Forissier S., Martel S., Maguer-Satta V., Jurdic P., Rimokh R.
      Biol. Cell 97:577-588(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FST3.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 196-403 IN COMPLEX WITH INHIBITOR AND ZINC IONS.

    Entry informationi

    Entry nameiADAM8_HUMAN
    AccessioniPrimary (citable) accession number: P78325
    Secondary accession number(s): B4DVM6
    , H0YL36, H0YLR0, H0YN39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 144 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Peptidase families
      Classification of peptidase families and list of entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3