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O43184

- ADA12_HUMAN

UniProt

O43184 - ADA12_HUMAN

Protein

Disintegrin and metalloproteinase domain-containing protein 12

Gene

ADAM12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (05 May 2009)
      Previous versions | rss
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    Functioni

    Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors By similarity.By similarity

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi179 – 1791Zinc; in inhibited formBy similarity
    Metal bindingi350 – 3501Zinc; catalytic
    Active sitei351 – 3511
    Metal bindingi354 – 3541Zinc; catalytic
    Metal bindingi360 – 3601Zinc; catalytic

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. epidermal growth factor receptor signaling pathway Source: Reactome
    3. myoblast fusion Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_9417. Signaling by EGFR.

    Protein family/group databases

    MEROPSiM12.212.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 12 (EC:3.4.24.-)
    Short name:
    ADAM 12
    Alternative name(s):
    Meltrin-alpha
    Gene namesi
    Name:ADAM12
    Synonyms:MLTN
    ORF Names:UNQ346/PRO545
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:190. ADAM12.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24507.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – 207179By similarityPRO_0000029078Add
    BLAST
    Chaini208 – 909702Disintegrin and metalloproteinase domain-containing protein 12PRO_0000029079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi325 ↔ 411By similarity
    Disulfide bondi367 ↔ 395By similarity
    Disulfide bondi369 ↔ 378By similarity
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi482 ↔ 502By similarity
    Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi660 ↔ 670By similarity
    Disulfide bondi664 ↔ 676By similarity
    Disulfide bondi678 ↔ 687By similarity
    Modified residuei907 – 9071Phosphotyrosine; by SRCBy similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiO43184.
    PaxDbiO43184.
    PRIDEiO43184.

    PTM databases

    PhosphoSiteiO43184.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in placenta and skeletal, cardiac, and smooth muscle. Isoform 2 seems to be expressed only in placenta or in embryo and fetus. Both forms were expressed in some tumor cells lines. Not detected in brain, lung, liver, kidney or pancreas.

    Gene expression databases

    ArrayExpressiO43184.
    BgeeiO43184.
    CleanExiHS_ADAM12.
    GenevestigatoriO43184.

    Organism-specific databases

    HPAiHPA030866.
    HPA030867.
    HPA030868.

    Interactioni

    Subunit structurei

    Interacts with alpha-actinin-2 and with syndecans By similarity. Interacts with SH3PXD2A. Interacts with FST3. Interacts with GNB2L1/RACK1; the interaction is required for PKC-dependent translocation of ADAM12 to the cell membrane.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FSTL3O956334EBI-2625865,EBI-2625790

    Protein-protein interaction databases

    BioGridi113731. 4 interactions.
    IntActiO43184. 2 interactions.
    MINTiMINT-246189.
    STRINGi9606.ENSP00000357668.

    Structurei

    3D structure databases

    ProteinModelPortaliO43184.
    SMRiO43184. Positions 213-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini208 – 708501ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini730 – 909180CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei709 – 72921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini214 – 416203Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini424 – 51087DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini656 – 68833EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi177 – 1848Cysteine switchBy similarity
    Motifi828 – 8347SH3-binding; class IIBy similarity
    Motifi834 – 8418SH3-binding; class IBy similarity
    Motifi885 – 8917SH3-binding; class IBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi514 – 649136Cys-richAdd
    BLAST

    Domaini

    The cysteine-rich domain supports cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. In carcinomas cells the binding of this domain to syndecans does not allow the integrin-mediated cell spreading.
    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.
    HOGENOMiHOG000230883.
    HOVERGENiHBG006978.
    InParanoidiO43184.
    KOiK06835.
    OMAiPPFCDKF.
    OrthoDBiEOG7F7W89.
    PhylomeDBiO43184.
    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.
    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.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43184-1) [UniParc]FASTAAdd to Basket

    Also known as: 12L

    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

    MAARPLPVSP ARALLLALAG ALLAPCEARG VSLWNQGRAD EVVSASVGSG    50
    DLWIPVKSFD SKNHPEVLNI RLQRESKELI INLERNEGLI ASSFTETHYL 100
    QDGTDVSLAR NYTVILGHCY YHGHVRGYSD SAVSLSTCSG LRGLIVFENE 150
    SYVLEPMKSA TNRYKLFPAK KLKSVRGSCG SHHNTPNLAA KNVFPPPSQT 200
    WARRHKRETL KATKYVELVI VADNREFQRQ GKDLEKVKQR LIEIANHVDK 250
    FYRPLNIRIV LVGVEVWNDM DKCSVSQDPF TSLHEFLDWR KMKLLPRKSH 300
    DNAQLVSGVY FQGTTIGMAP IMSMCTADQS GGIVMDHSDN PLGAAVTLAH 350
    ELGHNFGMNH DTLDRGCSCQ MAVEKGGCIM NASTGYPFPM VFSSCSRKDL 400
    ETSLEKGMGV CLFNLPEVRE SFGGQKCGNR FVEEGEECDC GEPEECMNRC 450
    CNATTCTLKP DAVCAHGLCC EDCQLKPAGT ACRDSSNSCD LPEFCTGASP 500
    HCPANVYLHD GHSCQDVDGY CYNGICQTHE QQCVTLWGPG AKPAPGICFE 550
    RVNSAGDPYG NCGKVSKSSF AKCEMRDAKC GKIQCQGGAS RPVIGTNAVS 600
    IETNIPLQQG GRILCRGTHV YLGDDMPDPG LVLAGTKCAD GKICLNRQCQ 650
    NISVFGVHEC AMQCHGRGVC NNRKNCHCEA HWAPPFCDKF GFGGSTDSGP 700
    IRQADNQGLT IGILVTILCL LAAGFVVYLK RKTLIRLLFT NKKTTIEKLR 750
    CVRPSRPPRG FQPCQAHLGH LGKGLMRKPP DSYPPKDNPR RLLQCQNVDI 800
    SRPLNGLNVP QPQSTQRVLP PLHRAPRAPS VPARPLPAKP ALRQAQGTCK 850
    PNPPQKPLPA DPLARTTRLT HALARTPGQW ETGLRLAPLR PAPQYPHQVP 900
    RSTHTAYIK 909
    Length:909
    Mass (Da):99,542
    Last modified:May 5, 2009 - v3
    Checksum:iE28131C64C4304AB
    GO
    Isoform 2 (identifier: O43184-2) [UniParc]FASTAAdd to Basket

    Also known as: 12S

    The sequence of this isoform differs from the canonical sequence as follows:
         705-738: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLL → EARQEAAESNRERGQGQEPVGSQEHASTASLTLI
         739-909: Missing.

    Show »
    Length:738
    Mass (Da):80,403
    Checksum:i19699D2852ED28F6
    GO
    Isoform 3 (identifier: O43184-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         114-116: Missing.
         705-738: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLL → EARQEAAESNRERGQGQEPVGSQEHASTASLTLI
         739-909: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:735
    Mass (Da):80,078
    Checksum:i664D4EDA47F8B533
    GO
    Isoform 4 (identifier: O43184-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         114-116: Missing.
         705-740: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFT → GKEARQEAAESNRERGQGQEPVGSQEHASTASLTLI
         741-909: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:737
    Mass (Da):80,263
    Checksum:iD86FE821BCBC62C6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481G → R.4 Publications
    Corresponds to variant rs3740199 [ dbSNP | Ensembl ].
    VAR_038542
    Natural varianti301 – 3011D → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036143
    Natural varianti479 – 4791G → E in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036144
    Natural varianti712 – 7121G → E in a cutaneous metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_066310
    Natural varianti792 – 7921L → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036145
    Natural varianti893 – 8931P → S in a cutaneous metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_066311

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei114 – 1163Missing in isoform 3 and isoform 4. 2 PublicationsVSP_031001
    Alternative sequencei705 – 74036DNQGL…RLLFT → GKEARQEAAESNRERGQGQE PVGSQEHASTASLTLI in isoform 4. 1 PublicationVSP_031002Add
    BLAST
    Alternative sequencei705 – 73834DNQGL…LIRLL → EARQEAAESNRERGQGQEPV GSQEHASTASLTLI in isoform 2 and isoform 3. 2 PublicationsVSP_005476Add
    BLAST
    Alternative sequencei739 – 909171Missing in isoform 2 and isoform 3. 2 PublicationsVSP_005477Add
    BLAST
    Alternative sequencei741 – 909169Missing in isoform 4. 1 PublicationVSP_031003Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023476 mRNA. Translation: AAC08702.2.
    AF023477 mRNA. Translation: AAC08703.2.
    AY358878 mRNA. Translation: AAQ89237.1.
    AL589787
    , AC022015, AC026226, AC063963 Genomic DNA. Translation: CAI40682.1.
    AL589787
    , AC022015, AC026226, AC063963 Genomic DNA. Translation: CAI40683.1.
    CH471066 Genomic DNA. Translation: EAW49206.1.
    CH471066 Genomic DNA. Translation: EAW49209.1.
    BC060804 mRNA. Translation: AAH60804.1.
    CCDSiCCDS7653.1. [O43184-1]
    CCDS7654.1. [O43184-2]
    RefSeqiNP_001275903.1. NM_001288974.1. [O43184-4]
    NP_001275904.1. NM_001288975.1. [O43184-3]
    NP_003465.3. NM_003474.5. [O43184-1]
    NP_067673.2. NM_021641.4. [O43184-2]
    UniGeneiHs.594351.
    Hs.741333.

    Genome annotation databases

    EnsembliENST00000368676; ENSP00000357665; ENSG00000148848. [O43184-2]
    ENST00000368679; ENSP00000357668; ENSG00000148848. [O43184-1]
    GeneIDi8038.
    KEGGihsa:8038.
    UCSCiuc001ljk.2. human. [O43184-1]
    uc001ljl.4. human. [O43184-4]
    uc001ljm.3. human. [O43184-2]
    uc001ljn.3. human. [O43184-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023476 mRNA. Translation: AAC08702.2 .
    AF023477 mRNA. Translation: AAC08703.2 .
    AY358878 mRNA. Translation: AAQ89237.1 .
    AL589787
    , AC022015 , AC026226 , AC063963 Genomic DNA. Translation: CAI40682.1 .
    AL589787
    , AC022015 , AC026226 , AC063963 Genomic DNA. Translation: CAI40683.1 .
    CH471066 Genomic DNA. Translation: EAW49206.1 .
    CH471066 Genomic DNA. Translation: EAW49209.1 .
    BC060804 mRNA. Translation: AAH60804.1 .
    CCDSi CCDS7653.1. [O43184-1 ]
    CCDS7654.1. [O43184-2 ]
    RefSeqi NP_001275903.1. NM_001288974.1. [O43184-4 ]
    NP_001275904.1. NM_001288975.1. [O43184-3 ]
    NP_003465.3. NM_003474.5. [O43184-1 ]
    NP_067673.2. NM_021641.4. [O43184-2 ]
    UniGenei Hs.594351.
    Hs.741333.

    3D structure databases

    ProteinModelPortali O43184.
    SMRi O43184. Positions 213-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113731. 4 interactions.
    IntActi O43184. 2 interactions.
    MINTi MINT-246189.
    STRINGi 9606.ENSP00000357668.

    Chemistry

    BindingDBi O43184.
    ChEMBLi CHEMBL5030.

    Protein family/group databases

    MEROPSi M12.212.

    PTM databases

    PhosphoSitei O43184.

    Proteomic databases

    MaxQBi O43184.
    PaxDbi O43184.
    PRIDEi O43184.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368676 ; ENSP00000357665 ; ENSG00000148848 . [O43184-2 ]
    ENST00000368679 ; ENSP00000357668 ; ENSG00000148848 . [O43184-1 ]
    GeneIDi 8038.
    KEGGi hsa:8038.
    UCSCi uc001ljk.2. human. [O43184-1 ]
    uc001ljl.4. human. [O43184-4 ]
    uc001ljm.3. human. [O43184-2 ]
    uc001ljn.3. human. [O43184-3 ]

    Organism-specific databases

    CTDi 8038.
    GeneCardsi GC10M127693.
    H-InvDB HIX0009299.
    HGNCi HGNC:190. ADAM12.
    HPAi HPA030866.
    HPA030867.
    HPA030868.
    MIMi 602714. gene.
    neXtProti NX_O43184.
    PharmGKBi PA24507.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294463.
    HOGENOMi HOG000230883.
    HOVERGENi HBG006978.
    InParanoidi O43184.
    KOi K06835.
    OMAi PPFCDKF.
    OrthoDBi EOG7F7W89.
    PhylomeDBi O43184.
    TreeFami TF314733.

    Enzyme and pathway databases

    Reactomei REACT_9417. Signaling by EGFR.

    Miscellaneous databases

    ChiTaRSi ADAM12. human.
    GeneWikii ADAM12.
    GenomeRNAii 8038.
    NextBioi 30628.
    PROi O43184.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43184.
    Bgeei O43184.
    CleanExi HS_ADAM12.
    Genevestigatori O43184.

    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.
    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.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo."
      Gilpin B.J., Loechel F., Mattei M.-G., Engvall E., Albrechtsen R., Wewer U.M.
      J. Biol. Chem. 273:157-166(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-48.
      Tissue: Placenta.
    2. Gilpin B.J., Loechel F., Mattei M.-G., Engvall E., Albrechtsen R., Wewer U.M.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 36.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ARG-48.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-48.
    6. "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 4), VARIANT ARG-48.
      Tissue: Placenta.
    7. "Human ADAM 12 (meltrin alpha) is an active metalloprotease."
      Loechel F., Gilpin B.J., Engvall E., Albrechtsen R., Wewer U.M.
      J. Biol. Chem. 273:16993-16997(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading."
      Iba K., Albrechtsen R., Gilpin B.J., Froehlich C., Loechel F., Zolkiewska A., Ishiguro K., Kojima T., Liu W., Langford J.K., Sanderson R.D., Brakebusch C., Faessler R., Wewer U.M.
      J. Cell Biol. 149:1143-1156(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNDECANS.
    9. "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.
    10. "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.
    11. "RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis."
      Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., Theret N.
      J. Biol. Chem. 283:26000-26009(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GNB2L1.
    12. Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-301; GLU-479 AND PHE-792.
    13. "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma."
      Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.
      Hum. Mutat. 32:E2148-E2175(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLU-712 AND SER-893.

    Entry informationi

    Entry nameiADA12_HUMAN
    AccessioniPrimary (citable) accession number: O43184
    Secondary accession number(s): O60470
    , Q5JRP0, Q5JRP1, Q6P9E3, Q6UWB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 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 10
      Human chromosome 10: 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