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Q9P0K1

- ADA22_HUMAN

UniProt

Q9P0K1 - ADA22_HUMAN

Protein

Disintegrin and metalloproteinase domain-containing protein 22

Gene

ADAM22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1.3 Publications

    GO - Molecular functioni

    1. integrin binding Source: UniProtKB
    2. metalloendopeptidase activity Source: InterPro
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. cell adhesion Source: UniProtKB-KW
    3. central nervous system development Source: ProtInc
    4. myelination in peripheral nervous system Source: Ensembl
    5. negative regulation of cell adhesion Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Cell adhesion

    Protein family/group databases

    MEROPSiM12.978.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 22
    Short name:
    ADAM 22
    Alternative name(s):
    Metalloproteinase-disintegrin ADAM22-3
    Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2
    Gene namesi
    Name:ADAM22
    Synonyms:MDC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:201. ADAM22.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi834 – 8341S → A: Abolishes interactions with YWHAB and YWHAZ; when associated with A-857. 2 Publications
    Mutagenesisi857 – 8571S → A: Abolishes interactions with YWHAB and YWHAZ; when associated with A-834. 2 Publications

    Organism-specific databases

    PharmGKBiPA24518.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Propeptidei26 – 222197By similarityPRO_0000029112Add
    BLAST
    Chaini223 – 906684Disintegrin and metalloproteinase domain-containing protein 22PRO_0000029113Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi349 ↔ 4331 Publication
    Disulfide bondi392 ↔ 4171 Publication
    Disulfide bondi394 ↔ 4011 Publication
    Disulfide bondi447 ↔ 4771 Publication
    Disulfide bondi458 ↔ 4741 Publication
    Disulfide bondi460 ↔ 4661 Publication
    Disulfide bondi473 ↔ 4941 Publication
    Disulfide bondi485 ↔ 4911 Publication
    Disulfide bondi490 ↔ 5161 Publication
    Disulfide bondi503 ↔ 5231 Publication
    Disulfide bondi510 ↔ 5421 Publication
    Glycosylationi519 – 5191N-linked (GlcNAc...)1 Publication
    Disulfide bondi535 ↔ 5471 Publication
    Disulfide bondi554 ↔ 6051 Publication
    Disulfide bondi569 ↔ 6351 Publication
    Disulfide bondi583 ↔ 5931 Publication
    Disulfide bondi600 ↔ 6631 Publication
    Glycosylationi634 – 6341N-linked (GlcNAc...)1 Publication
    Disulfide bondi657 ↔ 6681 Publication
    Glycosylationi675 – 6751N-linked (GlcNAc...)1 Publication
    Disulfide bondi679 ↔ 6941 Publication
    Disulfide bondi688 ↔ 7001 Publication
    Disulfide bondi702 ↔ 7111 Publication
    Modified residuei834 – 8341Phosphoserine1 Publication

    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

    Proteomic databases

    MaxQBiQ9P0K1.
    PaxDbiQ9P0K1.
    PRIDEiQ9P0K1.

    PTM databases

    PhosphoSiteiQ9P0K1.

    Expressioni

    Tissue specificityi

    Highly expressed in the brain and in some high-grade but not low-grade gliomas. Detected slightly or not at all in other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9P0K1.
    BgeeiQ9P0K1.
    CleanExiHS_ADAM22.
    GenevestigatoriQ9P0K1.

    Organism-specific databases

    HPAiHPA045282.

    Interactioni

    Subunit structurei

    Interacts with LGI1 and can bind to LGI4 By similarity. Interacts through its C-terminal region with YWHAB/14-3-3 beta and YWHAZ/14-3-3 zeta but not with YWHAE/14-3-3 epsilon or YWHAH/14-3-3 eta.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YWHABP319462EBI-1567267,EBI-359815
    YWHAQP273482EBI-1567267,EBI-359854
    YWHAZP631043EBI-1567267,EBI-347088

    Protein-protein interaction databases

    BioGridi119789. 6 interactions.
    IntActiQ9P0K1. 11 interactions.
    MINTiMINT-252818.
    STRINGi9606.ENSP00000265727.

    Structurei

    Secondary structure

    1
    906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi235 – 2373
    Beta strandi239 – 2479
    Helixi249 – 2535
    Turni254 – 2574
    Helixi259 – 28022
    Beta strandi281 – 29212
    Helixi305 – 31814
    Beta strandi325 – 3339
    Beta strandi336 – 3383
    Beta strandi341 – 3433
    Turni351 – 3533
    Beta strandi354 – 3596
    Helixi363 – 37816
    Helixi384 – 3896
    Helixi416 – 42712
    Helixi432 – 4354
    Helixi463 – 4664
    Turni467 – 4737
    Beta strandi486 – 4883
    Beta strandi491 – 4966
    Beta strandi502 – 5043
    Turni536 – 5394
    Beta strandi540 – 5434
    Beta strandi546 – 5483
    Helixi550 – 5589
    Helixi567 – 5737
    Turni574 – 5763
    Beta strandi585 – 5906
    Helixi595 – 5973
    Beta strandi600 – 6023
    Beta strandi605 – 6073
    Beta strandi613 – 6175
    Beta strandi622 – 6287
    Beta strandi631 – 6377
    Beta strandi640 – 6456
    Beta strandi656 – 6583
    Beta strandi661 – 6666
    Beta strandi668 – 6703
    Helixi671 – 6744
    Helixi688 – 6903
    Beta strandi692 – 6954
    Beta strandi700 – 7023
    Beta strandi706 – 7083

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3G5CX-ray2.36A/B233-736[»]
    ProteinModelPortaliQ9P0K1.
    SMRiQ9P0K1. Positions 233-718.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P0K1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini223 – 736514ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini758 – 906149CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei737 – 75721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini239 – 438200Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini444 – 53188DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini675 – 71238EGF-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi532 – 678147Cys-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG256419.
    HOGENOMiHOG000231962.
    HOVERGENiHBG050456.
    InParanoidiQ9P0K1.
    KOiK16068.
    OMAiFSGSQFE.
    OrthoDBiEOG7B31M6.
    PhylomeDBiQ9P0K1.
    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.
    PS00022. EGF_1. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P0K1-1) [UniParc]FASTAAdd to Basket

    Also known as: Epsilon

    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

    MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI    50
    VPLRLIYRSG GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF 100
    ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA 150
    LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL 200
    PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL 250
    MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA 300
    ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS 350
    LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG 400
    CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG 450
    FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG 500
    TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR 550
    DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC 600
    GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY 650
    VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC 700
    VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA 750
    LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS 800
    KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR 850
    FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR 900
    LWETSI 906
    Length:906
    Mass (Da):100,433
    Last modified:October 1, 2000 - v1
    Checksum:i265ECCD0FA6C088B
    GO
    Isoform 2 (identifier: Q9P0K1-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta

    The sequence of this isoform differs from the canonical sequence as follows:
         768-803: Missing.
         859-859: E → EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR

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

    Show »
    Length:899
    Mass (Da):100,269
    Checksum:i5AB89C258ECE0736
    GO
    Isoform 3 (identifier: Q9P0K1-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         860-906: Missing.

    Show »
    Length:859
    Mass (Da):95,288
    Checksum:i6105B681A1331D55
    GO
    Isoform 4 (identifier: Q9P0K1-4) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         768-803: Missing.
         860-906: Missing.

    Show »
    Length:823
    Mass (Da):91,492
    Checksum:iE9FD1A9BA99DE0DB
    GO
    Isoform 5 (identifier: Q9P0K1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         768-803: Missing.

    Show »
    Length:870
    Mass (Da):96,637
    Checksum:iC236086AD0BCCA2F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q9P0K1-2)
    Sequence conflicti848 – 8481G → E in AAF73288. (PubMed:11050470)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811P → R.2 Publications
    Corresponds to variant rs2279542 [ dbSNP | Ensembl ].
    VAR_020057
    Natural varianti119 – 1191H → Y.
    Corresponds to variant rs4728730 [ dbSNP | Ensembl ].
    VAR_051589
    Natural varianti207 – 2071V → I.
    Corresponds to variant rs17255978 [ dbSNP | Ensembl ].
    VAR_051590

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei768 – 80336Missing in isoform 2, isoform 4 and isoform 5. 3 PublicationsVSP_005482Add
    BLAST
    Alternative sequencei859 – 8591E → EYLNPWFKRDYNVAKWVEDV NKNTEGPYFR in isoform 2. 1 PublicationVSP_005484
    Alternative sequencei860 – 90647Missing in isoform 3 and isoform 4. 1 PublicationVSP_005483Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009671 mRNA. Translation: BAA32349.1.
    AB009671 mRNA. Translation: BAA32350.1.
    AF155381 mRNA. Translation: AAF73288.1.
    AF155382 mRNA. Translation: AAF73289.1.
    AF073291 mRNA. Translation: AAF22476.2.
    AC005075 Genomic DNA. No translation available.
    AF158637 mRNA. Translation: AAD55251.1.
    CCDSiCCDS43608.1. [Q9P0K1-2]
    CCDS43609.1. [Q9P0K1-5]
    CCDS43610.1. [Q9P0K1-3]
    CCDS47637.1. [Q9P0K1-1]
    RefSeqiNP_004185.1. NM_004194.3. [Q9P0K1-3]
    NP_068367.1. NM_021721.3. [Q9P0K1-4]
    NP_068368.2. NM_021722.4. [Q9P0K1-2]
    NP_068369.1. NM_021723.3. [Q9P0K1-1]
    UniGeneiHs.256398.

    Genome annotation databases

    EnsembliENST00000265727; ENSP00000265727; ENSG00000008277. [Q9P0K1-1]
    ENST00000398201; ENSP00000381260; ENSG00000008277. [Q9P0K1-3]
    ENST00000398204; ENSP00000381262; ENSG00000008277. [Q9P0K1-5]
    ENST00000398209; ENSP00000381267; ENSG00000008277. [Q9P0K1-2]
    GeneIDi53616.
    KEGGihsa:53616.
    UCSCiuc003ujk.2. human. [Q9P0K1-1]
    uc003ujl.2. human. [Q9P0K1-4]
    uc003ujm.3. human. [Q9P0K1-2]
    uc003ujo.3. human. [Q9P0K1-5]

    Polymorphism databases

    DMDMi14423634.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009671 mRNA. Translation: BAA32349.1 .
    AB009671 mRNA. Translation: BAA32350.1 .
    AF155381 mRNA. Translation: AAF73288.1 .
    AF155382 mRNA. Translation: AAF73289.1 .
    AF073291 mRNA. Translation: AAF22476.2 .
    AC005075 Genomic DNA. No translation available.
    AF158637 mRNA. Translation: AAD55251.1 .
    CCDSi CCDS43608.1. [Q9P0K1-2 ]
    CCDS43609.1. [Q9P0K1-5 ]
    CCDS43610.1. [Q9P0K1-3 ]
    CCDS47637.1. [Q9P0K1-1 ]
    RefSeqi NP_004185.1. NM_004194.3. [Q9P0K1-3 ]
    NP_068367.1. NM_021721.3. [Q9P0K1-4 ]
    NP_068368.2. NM_021722.4. [Q9P0K1-2 ]
    NP_068369.1. NM_021723.3. [Q9P0K1-1 ]
    UniGenei Hs.256398.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3G5C X-ray 2.36 A/B 233-736 [» ]
    ProteinModelPortali Q9P0K1.
    SMRi Q9P0K1. Positions 233-718.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119789. 6 interactions.
    IntActi Q9P0K1. 11 interactions.
    MINTi MINT-252818.
    STRINGi 9606.ENSP00000265727.

    Protein family/group databases

    MEROPSi M12.978.

    PTM databases

    PhosphoSitei Q9P0K1.

    Polymorphism databases

    DMDMi 14423634.

    Proteomic databases

    MaxQBi Q9P0K1.
    PaxDbi Q9P0K1.
    PRIDEi Q9P0K1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265727 ; ENSP00000265727 ; ENSG00000008277 . [Q9P0K1-1 ]
    ENST00000398201 ; ENSP00000381260 ; ENSG00000008277 . [Q9P0K1-3 ]
    ENST00000398204 ; ENSP00000381262 ; ENSG00000008277 . [Q9P0K1-5 ]
    ENST00000398209 ; ENSP00000381267 ; ENSG00000008277 . [Q9P0K1-2 ]
    GeneIDi 53616.
    KEGGi hsa:53616.
    UCSCi uc003ujk.2. human. [Q9P0K1-1 ]
    uc003ujl.2. human. [Q9P0K1-4 ]
    uc003ujm.3. human. [Q9P0K1-2 ]
    uc003ujo.3. human. [Q9P0K1-5 ]

    Organism-specific databases

    CTDi 53616.
    GeneCardsi GC07P087563.
    HGNCi HGNC:201. ADAM22.
    HPAi HPA045282.
    MIMi 603709. gene.
    neXtProti NX_Q9P0K1.
    PharmGKBi PA24518.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256419.
    HOGENOMi HOG000231962.
    HOVERGENi HBG050456.
    InParanoidi Q9P0K1.
    KOi K16068.
    OMAi FSGSQFE.
    OrthoDBi EOG7B31M6.
    PhylomeDBi Q9P0K1.
    TreeFami TF314733.

    Miscellaneous databases

    ChiTaRSi ADAM22. human.
    EvolutionaryTracei Q9P0K1.
    GeneWikii ADAM22.
    GenomeRNAii 53616.
    NextBioi 56096.
    PROi Q9P0K1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0K1.
    Bgeei Q9P0K1.
    CleanExi HS_ADAM22.
    Genevestigatori Q9P0K1.

    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.
    PS00022. EGF_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain."
      Sagane K., Ohya Y., Hasegawa Y., Tanaka I.
      Biochem. J. 334:93-98(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
      Tissue: Brain.
    2. "The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in brain tissues and gliomas."
      Harada T., Nishie A., Torigoe K., Ikezaki K., Shono T., Maehara Y., Kuwano M., Wada M.
      Jpn. J. Cancer Res. 91:1001-1006(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    3. "Isolation and tissue specific expression of novel ADAM family from 7q21.1 region."
      Wada M., Torigoe K., Harada T., Kuwano M.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT ARG-81.
      Tissue: Brain.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries."
      Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.
      Gene 237:61-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-906 (ISOFORM 1), VARIANT ARG-81.
      Tissue: Cerebellum.
    6. "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading."
      Zhu P., Sun Y., Xu R., Sang Y., Zhao J., Liu G., Cai L., Li C., Zhao S.
      Biochem. Biophys. Res. Commun. 301:991-999(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YWHAZ, MUTAGENESIS OF SER-834 AND SER-857.
    7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. "ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3."
      Zhu P., Sang Y., Xu H., Zhao J., Xu R., Sun Y., Xu T., Wang X., Chen L., Feng H., Li C., Zhao S.
      Biochem. Biophys. Res. Commun. 331:938-946(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YWHAB, MUTAGENESIS OF SER-834 AND SER-857.
    9. "ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain."
      D'Abaco G.M., Ng K., Paradiso L., Godde N.J., Kaye A., Novak U.
      Neurosurgery 58:179-186(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function."
      Liu H., Shim A.H., He X.
      J. Biol. Chem. 284:29077-29086(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 233-736, GLYCOSYLATION AT ASN-519; ASN-634 AND ASN-675, DISULFIDE BONDS.

    Entry informationi

    Entry nameiADA22_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0K1
    Secondary accession number(s): O75075
    , O75076, Q9P0K2, Q9UIA1, Q9UKK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3