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)

Q13444

- ADA15_HUMAN

UniProt

Q13444 - ADA15_HUMAN

Protein

Disintegrin and metalloproteinase domain-containing protein 15

Gene

ADAM15

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 159 (01 Oct 2014)
      Sequence version 4 (13 Jul 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.7 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by hydroxamate-type metalloproteinase inhibitors such as marimastat. Inhibited by metalloproteinase inhibitor 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not significantly inhibited by TIMP-1 at concentrations of up to 100 nM. Not activated by PMA or ionomycin.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi179 – 1791Zinc; in inhibited formBy similarity
    Metal bindingi348 – 3481Zinc; catalyticBy similarity
    Active sitei349 – 3491PROSITE-ProRule annotation
    Metal bindingi352 – 3521Zinc; catalyticBy similarity
    Metal bindingi358 – 3581Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. metallopeptidase activity Source: BHF-UCL
    3. protein binding Source: IntAct
    4. SH3 domain binding Source: BHF-UCL
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cardiac epithelial to mesenchymal transition Source: Ensembl
    3. cell-matrix adhesion Source: ProtInc
    4. collagen catabolic process Source: UniProtKB-KW
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. tissue regeneration Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Angiogenesis, Cell adhesion, Collagen degradation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.215.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 15 (EC:3.4.24.-)
    Short name:
    ADAM 15
    Alternative name(s):
    Metalloprotease RGD disintegrin protein
    Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
    Short name:
    MDC-15
    Metargidin
    Gene namesi
    Name:ADAM15
    Synonyms:MDC15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:193. ADAM15.

    Subcellular locationi

    Endomembrane system 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junctionadherens junction 1 Publication. Cell projectionciliumflagellum By similarity. Cytoplasmic vesiclesecretory vesicleacrosome By similarity
    Note: The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed By similarity.By similarity

    GO - Cellular componenti

    1. acrosomal vesicle Source: UniProtKB-SubCell
    2. adherens junction Source: UniProtKB-SubCell
    3. cell projection Source: UniProtKB-KW
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi484 – 4852RG → SV: Reduces ADAM15-mediated T-cell aggregation. 1 Publication

    Organism-specific databases

    PharmGKBiPA24510.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 206189By similarityPRO_0000029082Add
    BLAST
    Chaini207 – 863657Disintegrin and metalloproteinase domain-containing protein 15PRO_0000029083Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi323 ↔ 409By similarity
    Disulfide bondi365 ↔ 393By similarity
    Disulfide bondi367 ↔ 376By similarity
    Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi480 ↔ 500By similarity
    Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi611 – 6111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi657 ↔ 667By similarity
    Disulfide bondi661 ↔ 673By similarity
    Disulfide bondi675 ↔ 684By similarity
    Modified residuei715 – 7151Phosphotyrosine; by HCK and LCK1 Publication
    Modified residuei735 – 7351Phosphotyrosine; by HCK and LCK1 Publication

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    Phosphorylation increases association with PTKs.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiQ13444.
    PaxDbiQ13444.
    PRIDEiQ13444.

    PTM databases

    PhosphoSiteiQ13444.

    Expressioni

    Tissue specificityi

    Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells.4 Publications

    Gene expression databases

    ArrayExpressiQ13444.
    BgeeiQ13444.
    CleanExiHS_ADAM15.
    GenevestigatoriQ13444.

    Organism-specific databases

    HPAiHPA011633.

    Interactioni

    Subunit structurei

    Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi. Interacts with ITAG9-ITGB1 By similarity. Interacts specifically with Src family protein-tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FYNP062412EBI-77818,EBI-515315
    GRB2P629933EBI-77818,EBI-401755
    HCKP086313EBI-77818,EBI-346340
    LCKP062393EBI-77818,EBI-1348
    NPHP1O152592EBI-77818,EBI-953828
    PACSIN3Q9UKS63EBI-77818,EBI-77926
    SH3GL2Q999622EBI-77818,EBI-77938
    SH3PXD2AQ5TCZ12EBI-77818,EBI-2483234
    SNX33Q8WV412EBI-77818,EBI-2481535
    SNX9Q9Y5X12EBI-77818,EBI-77848
    SRCP129313EBI-77818,EBI-621482

    Protein-protein interaction databases

    BioGridi114287. 27 interactions.
    IntActiQ13444. 27 interactions.
    MINTiMINT-108799.
    STRINGi9606.ENSP00000349436.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13444.
    SMRiQ13444. Positions 213-646.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini207 – 696490ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini718 – 863146CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei697 – 71721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini213 – 414202Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 50888DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini657 – 68529EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi177 – 1848Cysteine switchBy similarity
    Motifi484 – 4863Cell attachment sitePROSITE-ProRule annotation
    Motifi815 – 8217SH3-bindingSequence Analysis
    Motifi850 – 8567SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi509 – 656148Cys-richAdd
    BLAST

    Domaini

    The cytoplasmic domain is required for SH3GL2- and SNX9-binding.
    Disintegrin domain binds to integrin alphaV-beta3.
    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.

    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, SH3-binding, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG294463.
    HOGENOMiHOG000230884.
    HOVERGENiHBG006978.
    KOiK06836.
    OMAiHGVCDSN.
    OrthoDBiEOG7F7W89.
    PhylomeDBiQ13444.
    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.
    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.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (13)i

    Sequence statusi: Complete.

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

    This entry describes 13 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13444-1) [UniParc]FASTAAdd to Basket

    Also known as: 6b

    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

    MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ    50
    DDLPISLKKV LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY 100
    QPDGTRVVSE GHTLENCCYQ GRVRGYAGSW VSICTCSGLR GLVVLTPERS 150
    YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA LSWRESVHTQ KPPEHPLGQR 200
    HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL EVALLLDTFF 250
    RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 300
    AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL 350
    GHSLGLDHDL PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK 400
    ALLDGMGSCL FERLPSLPPM AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS 450
    LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC RPTRGDCDLP EFCPGDSSQC 500
    PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ PAAPLCLQTA 550
    NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 600
    ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD 650
    LLGAQECRSK CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL 700
    SLLVLLVLVM LGASYWYRAR LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ 750
    RALLARGTKQ ASALSFPAPP SRPLPPDPVS KRLQAELADR PNPPTRPLPA 800
    DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA GIPPLVVPSR 850
    PAPPPPTVSS LYL 863
    Length:863
    Mass (Da):92,959
    Last modified:July 13, 2010 - v4
    Checksum:i004936E9182629CA
    GO
    Isoform 2 (identifier: Q13444-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         760-808: Missing.

    Show »
    Length:814
    Mass (Da):87,744
    Checksum:iC6A297D51BED277E
    GO
    Isoform 3 (identifier: Q13444-3) [UniParc]FASTAAdd to Basket

    Also known as: 6a

    The sequence of this isoform differs from the canonical sequence as follows:
         760-760: Missing.

    Show »
    Length:862
    Mass (Da):92,831
    Checksum:iC39147754DD6B63C
    GO
    Isoform 4 (identifier: Q13444-4) [UniParc]FASTAAdd to Basket

    Also known as: 4a

    The sequence of this isoform differs from the canonical sequence as follows:
         785-808: Missing.

    Show »
    Length:839
    Mass (Da):90,383
    Checksum:i3B5F7590EFE0EBC1
    GO
    Isoform 5 (identifier: Q13444-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         760-784: Missing.

    Show »
    Length:838
    Mass (Da):90,320
    Checksum:i22637515284E16E8
    GO
    Isoform 6 (identifier: Q13444-6) [UniParc]FASTAAdd to Basket

    Also known as: 7b

    The sequence of this isoform differs from the canonical sequence as follows:
         809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT

    Show »
    Length:822
    Mass (Da):88,779
    Checksum:i2C01760368BEAF58
    GO
    Isoform 7 (identifier: Q13444-7) [UniParc]FASTAAdd to Basket

    Also known as: 7a

    The sequence of this isoform differs from the canonical sequence as follows:
         760-760: Missing.
         809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT

    Show »
    Length:821
    Mass (Da):88,651
    Checksum:i574AC60AD10ACFCE
    GO
    Isoform 8 (identifier: Q13444-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         760-784: Missing.
         809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT

    Show »
    Length:797
    Mass (Da):86,140
    Checksum:i402644A60C8BB7A3
    GO
    Isoform 9 (identifier: Q13444-9) [UniParc]FASTAAdd to Basket

    Also known as: 3a

    The sequence of this isoform differs from the canonical sequence as follows:
         737-796: AAQSGPSERP...LADRPNPPTR → LVLSASRPPL...CPAQGLESRP
         797-863: Missing.

    Show »
    Length:796
    Mass (Da):86,311
    Checksum:i7C808DCF0D1C296A
    GO
    Isoform 10 (identifier: Q13444-10) [UniParc]FASTAAdd to Basket

    Also known as: 1

    The sequence of this isoform differs from the canonical sequence as follows:
         736-772: RAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSR → SLRGQPSPHPQGSHCLPTPRAGAHRVTCPAQGLESRP
         773-863: Missing.

    Show »
    Length:772
    Mass (Da):83,664
    Checksum:i3EE4998C8EDCF958
    GO
    Isoform 11 (identifier: Q13444-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         94-387: Missing.
         760-808: Missing.

    Show »
    Length:520
    Mass (Da):55,446
    Checksum:i601F3874454899A0
    GO
    Isoform 12 (identifier: Q13444-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-26: I → IVLSWGVLGPA
         760-808: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:824
    Mass (Da):88,724
    Checksum:i84B3BF611CBF9E9D
    GO
    Isoform 13 (identifier: Q13444-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         27-87: GGTEEQQAES...DSHILELLQN → VSACNVEAPQ...ISQLASKRCF
         641-649: CIDHRCQRV → SSLGGQDQV
         650-863: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:633
    Mass (Da):68,256
    Checksum:i6C412A20B4E83369
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811I → V in BAG52157. (PubMed:16303743)Curated
    Sequence conflicti104 – 1041G → C in BAG59890. (PubMed:14702039)Curated
    Sequence conflicti191 – 1911K → T in BAG59890. (PubMed:14702039)Curated
    Sequence conflicti286 – 2861H → Y in BAG59477. (PubMed:14702039)Curated
    Sequence conflicti649 – 6491V → A in BAG52157. (PubMed:16303743)Curated
    Sequence conflicti714 – 7141S → G in AAC50404. (PubMed:9039960)Curated
    Sequence conflicti840 – 8401A → P in AAC51112. (PubMed:8617717)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti191 – 1911K → T.7 Publications
    Corresponds to variant rs6427128 [ dbSNP | Ensembl ].
    VAR_060315
    Natural varianti216 – 2161E → K.1 Publication
    Corresponds to variant rs115753757 [ dbSNP | Ensembl ].
    VAR_068970
    Natural varianti294 – 2941P → H.
    Corresponds to variant rs2306122 [ dbSNP | Ensembl ].
    VAR_060316
    Natural varianti502 – 5021P → Q.
    Corresponds to variant rs17093828 [ dbSNP | Ensembl ].
    VAR_054339

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei26 – 261I → IVLSWGVLGPA in isoform 12. 1 PublicationVSP_044695
    Alternative sequencei27 – 8761GGTEE…ELLQN → VSACNVEAPQVALRSSRQSQ RRPRGSPWSPRSFRTISQLA SKRCF in isoform 13. 1 PublicationVSP_055143Add
    BLAST
    Alternative sequencei94 – 387294Missing in isoform 11. 1 PublicationVSP_039524Add
    BLAST
    Alternative sequencei641 – 6499CIDHRCQRV → SSLGGQDQV in isoform 13. 1 PublicationVSP_055144
    Alternative sequencei650 – 863214Missing in isoform 13. 1 PublicationVSP_055145Add
    BLAST
    Alternative sequencei736 – 77237RAAQS…APPSR → SLRGQPSPHPQGSHCLPTPR AGAHRVTCPAQGLESRP in isoform 10. 3 PublicationsVSP_039525Add
    BLAST
    Alternative sequencei737 – 79660AAQSG…NPPTR → LVLSASRPPLPGRCRLTLCP RDSSLRGQPSPHPQGSHCLP TPRAGAHRVTCPAQGLESRP in isoform 9. 1 PublicationVSP_039526Add
    BLAST
    Alternative sequencei760 – 80849Missing in isoform 2, isoform 11 and isoform 12. 8 PublicationsVSP_039527Add
    BLAST
    Alternative sequencei760 – 78425Missing in isoform 5 and isoform 8. 1 PublicationVSP_039528Add
    BLAST
    Alternative sequencei760 – 7601Missing in isoform 3 and isoform 7. 1 PublicationVSP_039529
    Alternative sequencei773 – 86391Missing in isoform 10. 3 PublicationsVSP_039530Add
    BLAST
    Alternative sequencei785 – 80824Missing in isoform 4. 2 PublicationsVSP_039531Add
    BLAST
    Alternative sequencei797 – 86367Missing in isoform 9. 1 PublicationVSP_039532Add
    BLAST
    Alternative sequencei809 – 86355SQGPA…SSLYL → VTVGGEKGTASPPT in isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_039533Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41767 mRNA. Translation: AAC50404.1.
    U46005 mRNA. Translation: AAC51112.1.
    AY518542 mRNA. Translation: AAR99331.1.
    AF314227 Genomic DNA. Translation: AAM44189.1.
    AF314227 Genomic DNA. Translation: AAS48590.1.
    AF314227 Genomic DNA. Translation: AAS48591.1.
    AF314227 Genomic DNA. Translation: AAS48592.1.
    AF314227 Genomic DNA. Translation: AAS48593.1.
    AF314227 Genomic DNA. Translation: AAS48594.1.
    AF314227 Genomic DNA. Translation: AAS48595.1.
    AF314227 Genomic DNA. Translation: AAS48596.1.
    AF314227 Genomic DNA. Translation: AAS48597.1.
    AF314227 Genomic DNA. Translation: AAS72298.1.
    AY560593 mRNA. Translation: AAS72991.1.
    AY560594 mRNA. Translation: AAS72992.1.
    AY560595 mRNA. Translation: AAS72993.1.
    AY560596 mRNA. Translation: AAS72994.1.
    AY560597 mRNA. Translation: AAS72995.1.
    AY560598 mRNA. Translation: AAS72996.1.
    AY560599 mRNA. Translation: AAS72997.1.
    AY560600 mRNA. Translation: AAS72998.1.
    AY560601 mRNA. Translation: AAS72999.1.
    AY576417 mRNA. Translation: AAS73000.1.
    BT009764 mRNA. Translation: AAP88766.1.
    AK296925 mRNA. Translation: BAG59477.1.
    AK297468 mRNA. Translation: BAG59890.1.
    AK075498 mRNA. Translation: BAG52157.1.
    AL451085, AL691442 Genomic DNA. Translation: CAI13273.1.
    AL451085, AL691442 Genomic DNA. Translation: CAI13274.1.
    AL691442, AL451085 Genomic DNA. Translation: CAI15327.1.
    AL691442, AL451085 Genomic DNA. Translation: CAI15328.1.
    BC014566 mRNA. Translation: AAH14566.1.
    CCDSiCCDS1084.1. [Q13444-2]
    CCDS1085.1. [Q13444-4]
    CCDS1086.1. [Q13444-5]
    CCDS1087.1. [Q13444-1]
    CCDS1088.1. [Q13444-10]
    CCDS44236.1. [Q13444-3]
    CCDS58031.1. [Q13444-12]
    CCDS58032.1. [Q13444-9]
    CCDS60282.1. [Q13444-13]
    PIRiG02390.
    RefSeqiNP_001248393.1. NM_001261464.1. [Q13444-12]
    NP_001248394.1. NM_001261465.1. [Q13444-9]
    NP_001248395.1. NM_001261466.1.
    NP_003806.3. NM_003815.4. [Q13444-2]
    NP_997074.1. NM_207191.2. [Q13444-10]
    NP_997077.1. NM_207194.2. [Q13444-4]
    NP_997078.1. NM_207195.2. [Q13444-5]
    NP_997079.1. NM_207196.2. [Q13444-3]
    NP_997080.1. NM_207197.2. [Q13444-1]
    UniGeneiHs.312098.

    Genome annotation databases

    EnsembliENST00000271836; ENSP00000271836; ENSG00000143537. [Q13444-2]
    ENST00000355956; ENSP00000348227; ENSG00000143537. [Q13444-4]
    ENST00000356955; ENSP00000349436; ENSG00000143537. [Q13444-1]
    ENST00000359280; ENSP00000352226; ENSG00000143537. [Q13444-5]
    ENST00000360674; ENSP00000353892; ENSG00000143537. [Q13444-10]
    ENST00000368412; ENSP00000357397; ENSG00000143537. [Q13444-9]
    ENST00000368413; ENSP00000357398; ENSG00000143537. [Q13444-11]
    ENST00000447332; ENSP00000476000; ENSG00000143537. [Q13444-13]
    ENST00000449910; ENSP00000403843; ENSG00000143537. [Q13444-3]
    ENST00000526491; ENSP00000432347; ENSG00000143537. [Q13444-6]
    ENST00000529473; ENSP00000434227; ENSG00000143537. [Q13444-8]
    ENST00000531455; ENSP00000432927; ENSG00000143537. [Q13444-12]
    GeneIDi8751.
    KEGGihsa:8751.
    UCSCiuc001fgr.2. human. [Q13444-1]
    uc001fgs.2. human. [Q13444-9]
    uc001fgt.2. human. [Q13444-3]
    uc001fgu.2. human. [Q13444-5]
    uc001fgv.2. human. [Q13444-4]
    uc001fgw.2. human. [Q13444-2]
    uc001fgx.2. human. [Q13444-10]

    Polymorphism databases

    DMDMi300669614.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41767 mRNA. Translation: AAC50404.1 .
    U46005 mRNA. Translation: AAC51112.1 .
    AY518542 mRNA. Translation: AAR99331.1 .
    AF314227 Genomic DNA. Translation: AAM44189.1 .
    AF314227 Genomic DNA. Translation: AAS48590.1 .
    AF314227 Genomic DNA. Translation: AAS48591.1 .
    AF314227 Genomic DNA. Translation: AAS48592.1 .
    AF314227 Genomic DNA. Translation: AAS48593.1 .
    AF314227 Genomic DNA. Translation: AAS48594.1 .
    AF314227 Genomic DNA. Translation: AAS48595.1 .
    AF314227 Genomic DNA. Translation: AAS48596.1 .
    AF314227 Genomic DNA. Translation: AAS48597.1 .
    AF314227 Genomic DNA. Translation: AAS72298.1 .
    AY560593 mRNA. Translation: AAS72991.1 .
    AY560594 mRNA. Translation: AAS72992.1 .
    AY560595 mRNA. Translation: AAS72993.1 .
    AY560596 mRNA. Translation: AAS72994.1 .
    AY560597 mRNA. Translation: AAS72995.1 .
    AY560598 mRNA. Translation: AAS72996.1 .
    AY560599 mRNA. Translation: AAS72997.1 .
    AY560600 mRNA. Translation: AAS72998.1 .
    AY560601 mRNA. Translation: AAS72999.1 .
    AY576417 mRNA. Translation: AAS73000.1 .
    BT009764 mRNA. Translation: AAP88766.1 .
    AK296925 mRNA. Translation: BAG59477.1 .
    AK297468 mRNA. Translation: BAG59890.1 .
    AK075498 mRNA. Translation: BAG52157.1 .
    AL451085 , AL691442 Genomic DNA. Translation: CAI13273.1 .
    AL451085 , AL691442 Genomic DNA. Translation: CAI13274.1 .
    AL691442 , AL451085 Genomic DNA. Translation: CAI15327.1 .
    AL691442 , AL451085 Genomic DNA. Translation: CAI15328.1 .
    BC014566 mRNA. Translation: AAH14566.1 .
    CCDSi CCDS1084.1. [Q13444-2 ]
    CCDS1085.1. [Q13444-4 ]
    CCDS1086.1. [Q13444-5 ]
    CCDS1087.1. [Q13444-1 ]
    CCDS1088.1. [Q13444-10 ]
    CCDS44236.1. [Q13444-3 ]
    CCDS58031.1. [Q13444-12 ]
    CCDS58032.1. [Q13444-9 ]
    CCDS60282.1. [Q13444-13 ]
    PIRi G02390.
    RefSeqi NP_001248393.1. NM_001261464.1. [Q13444-12 ]
    NP_001248394.1. NM_001261465.1. [Q13444-9 ]
    NP_001248395.1. NM_001261466.1.
    NP_003806.3. NM_003815.4. [Q13444-2 ]
    NP_997074.1. NM_207191.2. [Q13444-10 ]
    NP_997077.1. NM_207194.2. [Q13444-4 ]
    NP_997078.1. NM_207195.2. [Q13444-5 ]
    NP_997079.1. NM_207196.2. [Q13444-3 ]
    NP_997080.1. NM_207197.2. [Q13444-1 ]
    UniGenei Hs.312098.

    3D structure databases

    ProteinModelPortali Q13444.
    SMRi Q13444. Positions 213-646.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114287. 27 interactions.
    IntActi Q13444. 27 interactions.
    MINTi MINT-108799.
    STRINGi 9606.ENSP00000349436.

    Chemistry

    ChEMBLi CHEMBL2331050.

    Protein family/group databases

    MEROPSi M12.215.

    PTM databases

    PhosphoSitei Q13444.

    Polymorphism databases

    DMDMi 300669614.

    Proteomic databases

    MaxQBi Q13444.
    PaxDbi Q13444.
    PRIDEi Q13444.

    Protocols and materials databases

    DNASUi 8751.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271836 ; ENSP00000271836 ; ENSG00000143537 . [Q13444-2 ]
    ENST00000355956 ; ENSP00000348227 ; ENSG00000143537 . [Q13444-4 ]
    ENST00000356955 ; ENSP00000349436 ; ENSG00000143537 . [Q13444-1 ]
    ENST00000359280 ; ENSP00000352226 ; ENSG00000143537 . [Q13444-5 ]
    ENST00000360674 ; ENSP00000353892 ; ENSG00000143537 . [Q13444-10 ]
    ENST00000368412 ; ENSP00000357397 ; ENSG00000143537 . [Q13444-9 ]
    ENST00000368413 ; ENSP00000357398 ; ENSG00000143537 . [Q13444-11 ]
    ENST00000447332 ; ENSP00000476000 ; ENSG00000143537 . [Q13444-13 ]
    ENST00000449910 ; ENSP00000403843 ; ENSG00000143537 . [Q13444-3 ]
    ENST00000526491 ; ENSP00000432347 ; ENSG00000143537 . [Q13444-6 ]
    ENST00000529473 ; ENSP00000434227 ; ENSG00000143537 . [Q13444-8 ]
    ENST00000531455 ; ENSP00000432927 ; ENSG00000143537 . [Q13444-12 ]
    GeneIDi 8751.
    KEGGi hsa:8751.
    UCSCi uc001fgr.2. human. [Q13444-1 ]
    uc001fgs.2. human. [Q13444-9 ]
    uc001fgt.2. human. [Q13444-3 ]
    uc001fgu.2. human. [Q13444-5 ]
    uc001fgv.2. human. [Q13444-4 ]
    uc001fgw.2. human. [Q13444-2 ]
    uc001fgx.2. human. [Q13444-10 ]

    Organism-specific databases

    CTDi 8751.
    GeneCardsi GC01P155023.
    HGNCi HGNC:193. ADAM15.
    HPAi HPA011633.
    MIMi 605548. gene.
    neXtProti NX_Q13444.
    PharmGKBi PA24510.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294463.
    HOGENOMi HOG000230884.
    HOVERGENi HBG006978.
    KOi K06836.
    OMAi HGVCDSN.
    OrthoDBi EOG7F7W89.
    PhylomeDBi Q13444.
    TreeFami TF314733.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.

    Miscellaneous databases

    GeneWikii ADAM15.
    GenomeRNAii 8751.
    NextBioi 32829.
    PROi Q13444.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13444.
    Bgeei Q13444.
    CleanExi HS_ADAM15.
    Genevestigatori Q13444.

    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.
    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.
    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. "Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence."
      Kraetzschmar J., Lum L., Blobel C.P.
      J. Biol. Chem. 271:4593-4596(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-191.
      Tissue: Mammary carcinoma.
    2. "Expression of a disintegrin-like protein in cultured human vascular cells and in vivo."
      Herren B., Raines E.W., Ross R.
      FASEB J. 11:173-180(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-191.
      Tissue: Umbilical vein.
    3. "ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers."
      Charrier L., Yan Y., Driss A., Laboisse C.L., Sitaraman S.V., Merlin D.
      Am. J. Physiol. 288:G346-G353(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORM 2).
    4. "ADAM15 gene structure and differential alternative exon use in human tissues."
      Kleino I., Ortiz R.M., Huovila A.P.
      BMC Mol. Biol. 8:90-90(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10), VARIANT THR-191.
    5. "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
      Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
      Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 10), ALTERNATIVE SPLICING, INTERACTION WITH GRB2; MAPK1; MAPK3; NCK1; PTK6; SH3PXD2A AND SRC.
    6. "Characterization of human ADAM15 gene and promoter, and evidence for alternative exon use."
      Karkkainen I., Ortiz R.M., Huovila A.-P.J.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9), VARIANT THR-191.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-191.
    8. "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] (ISOFORMS 12 AND 13), VARIANTS THR-191 AND LYS-216.
      Tissue: Tongue.
    9. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
      Tissue: Embryo.
    10. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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), VARIANT THR-191.
      Tissue: Kidney.
    12. "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.
    13. "Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3."
      Zhang X.P., Kamata T., Yokoyama K., Puzon-McLaughlin W., Takada Y.
      J. Biol. Chem. 273:7345-7350(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3.
    14. "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.
    15. "Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells."
      Nath D., Slocombe P.M., Stephens P.E., Warn A., Hutchinson G.R., Yamada K.M., Docherty A.J., Murphy G.
      J. Cell Sci. 112:579-587(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND INTEGRIN ALPHA5-BETA1.
    16. "ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin."
      Ham C., Levkau B., Raines E.W., Herren B.
      Exp. Cell Res. 279:239-247(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    17. "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases."
      Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R.
      J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-715 AND TYR-735, INTERACTION WITH GRB2; LCK AND HCK.
    18. "The role of ADAM 15 in glomerular mesangial cell migration."
      Martin J., Eynstone L.V., Davies M., Williams J.D., Steadman R.
      J. Biol. Chem. 277:33683-33689(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    19. "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
      Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
      J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH3PXD2A.
    20. "Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling."
      Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., Burkhardt H.
      Arthritis Rheum. 52:1100-1109(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Inhibition of airway smooth muscle adhesion and migration by the disintegrin domain of ADAM-15."
      Lu D., Xie S., Sukkar M.B., Lu X., Scully M.F., Chung K.F.
      Am. J. Respir. Cell Mol. Biol. 37:494-500(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    22. "ADAM-15/metargidin mediates homotypic aggregation of human T lymphocytes and heterotypic interactions of T lymphocytes with intestinal epithelial cells."
      Charrier L., Yan Y., Nguyen H.T., Dalmasso G., Laboisse C.L., Gewirtz A.T., Sitaraman S.V., Merlin D.
      J. Biol. Chem. 282:16948-16958(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 484-ARG-GLY-485.
    23. "ADAM15 suppresses cell motility by driving integrin alpha5beta1 cell surface expression via Erk inactivation."
      Chen Q., Meng L.H., Zhu C.H., Lin L.P., Lu H., Ding J.
      Int. J. Biochem. Cell Biol. 40:2164-2173(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation."
      Najy A.J., Day K.C., Day M.L.
      J. Biol. Chem. 283:18393-18401(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays."
      Maretzky T., Yang G., Ouerfelli O., Overall C.M., Worpenberg S., Hassiepen U., Eder J., Blobel C.P.
      Biochem. J. 420:105-113(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    26. "Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
      Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
      J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCK; ITSN1; ITSN2; LYN; NCF1; NEPHROCYSTIN; SH3PXD2A; SNX33; SNX9 AND SRC.

    Entry informationi

    Entry nameiADA15_HUMAN
    AccessioniPrimary (citable) accession number: Q13444
    Secondary accession number(s): B3KQU5
    , B4DLB5, B4DMH8, E9PN65, Q13493, Q53XQ0, Q5SR68, Q5SR69, Q6R267, Q71S61, Q71S62, Q71S63, Q71S64, Q71S65, Q71S66, Q71S67, Q71S68, Q71S69, Q96C78, U3KQL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 159 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 1
      Human chromosome 1: 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