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Q86UL8

- MAGI2_HUMAN

UniProt

Q86UL8 - MAGI2_HUMAN

Protein

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2

Gene

MAGI2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (07 Feb 2006)
      Previous versions | rss
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    Functioni

    Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth.1 Publication

    GO - Molecular functioni

    1. beta-1 adrenergic receptor binding Source: UniProtKB
    2. phosphatase binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. receptor signaling complex scaffold activity Source: UniProtKB
    5. signal transducer activity Source: Ensembl
    6. SMAD binding Source: UniProtKB
    7. type II activin receptor binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to nerve growth factor stimulus Source: UniProtKB
    2. cytoplasmic transport Source: UniProtKB
    3. glomerular visceral epithelial cell development Source: UniProtKB
    4. mitotic cell cycle arrest Source: UniProtKB
    5. negative regulation of activin receptor signaling pathway Source: UniProtKB
    6. negative regulation of cell migration Source: UniProtKB
    7. negative regulation of cell proliferation Source: UniProtKB
    8. negative regulation of protein kinase B signaling Source: UniProtKB
    9. nerve growth factor signaling pathway Source: UniProtKB
    10. planar cell polarity pathway involved in axis elongation Source: UniProtKB
    11. positive regulation of neuron projection development Source: UniProtKB
    12. positive regulation of phosphoprotein phosphatase activity Source: UniProtKB
    13. positive regulation of receptor internalization Source: UniProtKB
    14. protein heterooligomerization Source: UniProtKB
    15. receptor clustering Source: UniProtKB
    16. SMAD protein signal transduction Source: UniProtKB

    Keywords - Biological processi

    Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_23832. Nephrin interactions.
    SignaLinkiQ86UL8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
    Alternative name(s):
    Atrophin-1-interacting protein 1
    Short name:
    AIP-1
    Atrophin-1-interacting protein A
    Membrane-associated guanylate kinase inverted 2
    Short name:
    MAGI-2
    Gene namesi
    Name:MAGI2
    Synonyms:ACVRINP1, AIP1, KIAA0705
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:18957. MAGI2.

    Subcellular locationi

    Cytoplasm By similarity. Late endosome By similarity. Cell junctionsynapsesynaptosome By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity
    Note: Localized diffusely in the cytoplasm before nerve growth factor (NGF) stimulation. Recruted to late endosomes after NGF stimulation. Membrane-associated in synaptosomes By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. dendrite Source: UniProtKB
    3. late endosome Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. perinuclear region of cytoplasm Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. postsynaptic density Source: UniProtKB
    8. protein complex Source: UniProtKB
    9. slit diaphragm Source: UniProtKB
    10. synapse Source: UniProtKB
    11. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Endosome, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671484.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14551455Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2PRO_0000094586Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei362 – 3621PhosphotyrosineBy similarity
    Modified residuei827 – 8271PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86UL8.
    PaxDbiQ86UL8.
    PRIDEiQ86UL8.

    PTM databases

    PhosphoSiteiQ86UL8.

    Expressioni

    Tissue specificityi

    Specifically expressed in brain.1 Publication

    Gene expression databases

    ArrayExpressiQ86UL8.
    BgeeiQ86UL8.
    GenevestigatoriQ86UL8.

    Organism-specific databases

    HPAiHPA013650.

    Interactioni

    Subunit structurei

    Interacts (via its WW domains) with DRPLA. Interacts (via its second PDZ domain) with PTEN (via unphosphorylated C-terminus); this interaction diminishes the degradation rate of PTEN By similarity. Interacts (via guanylate kinase domain) with DLGAP1 By similarity. Interacts (via the PDZ domains) with GRIN2A, GRID2 and NLGN1 By similarity. Interacts with CTNND2, CTNNB1, MAGUIN-1, ACVR2A, SMAD2 and SMAD3 By similarity. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 By similarity. May interact with HTR2A By similarity. Interacts with IGSF9, RAPGEF2 and HTR4 By similarity. Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 By similarity. Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a NGF-dependent manner By similarity. Interacts with RAPGEF2; the interaction occurs before or after nerve growth factor (NGF) stimulation By similarity. Interacts (via PDZ domain) with KIDINS220 (via C-terminal domain) By similarity. Interacts with DDN.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRB1P085882EBI-311035,EBI-991009

    Protein-protein interaction databases

    BioGridi115197. 8 interactions.
    IntActiQ86UL8. 5 interactions.
    MINTiMINT-109875.

    Structurei

    Secondary structure

    1
    1455
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi415 – 4173
    Beta strandi422 – 4309
    Beta strandi437 – 4415
    Beta strandi444 – 4474
    Beta strandi451 – 4555
    Helixi460 – 4634
    Beta strandi472 – 4765
    Helixi486 – 4949
    Beta strandi501 – 5099
    Beta strandi604 – 6096
    Beta strandi612 – 62211
    Beta strandi625 – 6328
    Helixi634 – 6363
    Beta strandi645 – 6495
    Helixi659 – 66810
    Beta strandi673 – 6808
    Beta strandi774 – 7774
    Beta strandi780 – 7878
    Beta strandi790 – 7923
    Beta strandi803 – 8075
    Helixi814 – 8163
    Beta strandi824 – 8285
    Helixi838 – 85114
    Beta strandi853 – 8619
    Beta strandi919 – 9246
    Beta strandi933 – 9364
    Beta strandi953 – 9575
    Helixi964 – 9663
    Beta strandi974 – 9785
    Turni983 – 9853
    Helixi988 – 99710
    Turni998 – 10003
    Beta strandi1001 – 10066
    Beta strandi1156 – 11594
    Beta strandi1162 – 11643
    Turni1165 – 11684
    Beta strandi1169 – 11724
    Helixi1181 – 11855
    Beta strandi1193 – 11975
    Helixi1207 – 121711
    Beta strandi1219 – 12213
    Beta strandi1223 – 12264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UEPNMR-A774-863[»]
    1UEQNMR-A412-522[»]
    1UEWNMR-A915-1015[»]
    1UJVNMR-A600-682[»]
    1WFVNMR-A1141-1230[»]
    ProteinModelPortaliQ86UL8.
    SMRiQ86UL8. Positions 25-96, 134-255, 303-379, 412-522, 594-682, 769-865, 898-1054, 1141-1233.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86UL8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 10185PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini109 – 283175Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini302 – 33534WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini348 – 38134WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini426 – 51085PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini605 – 68379PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini778 – 86083PDZ 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini920 – 101091PDZ 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1147 – 122983PDZ 6PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni302 – 38180Interaction with DDNAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1015 – 1118104Pro-richAdd
    BLAST
    Compositional biasi1340 – 143091Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MAGUK family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
    Contains 6 PDZ (DHR) domains.PROSITE-ProRule annotation
    Contains 2 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG320141.
    HOVERGENiHBG007091.
    InParanoidiQ86UL8.
    KOiK05629.
    OMAiHEDKSAG.
    OrthoDBiEOG7FV3PH.
    PhylomeDBiQ86UL8.
    TreeFamiTF316816.

    Family and domain databases

    Gene3Di2.30.42.10. 6 hits.
    InterProiIPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    IPR001478. PDZ.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    PF00595. PDZ. 6 hits.
    PF00397. WW. 2 hits.
    [Graphical view]
    SMARTiSM00072. GuKc. 1 hit.
    SM00228. PDZ. 6 hits.
    SM00456. WW. 2 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 6 hits.
    SSF51045. SSF51045. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    PS50106. PDZ. 6 hits.
    PS01159. WW_DOMAIN_1. 2 hits.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86UL8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG     50
    KVAYESGSKL VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ 100
    GGIVDKDLRH YLNLRFQKGS VDHELQQIIR DNLYLRTVPC TTRPHKEGEV 150
    PGVDYIFITV EDFMELEKSG ALLESGTYED NYYGTPKPPA EPAPLLLNVT 200
    DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP VVNGNGVVVT 250
    PESSEHEDKS AGASGEMPSQ PYPAPVYSQP EELKEQMDDT KPTKPEDNEE 300
    PDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PPEECKENEL 350
    PYGWEKIDDP IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK 400
    PLQAPGFREK PLFTRDASQL KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL 450
    QVKSVIPDGP AAQDGKMETG DVIVYINEVC VLGHTHADVV KLFQSVPIGQ 500
    SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG RHNYETYLEY 550
    ISRTSQSVPD ITDRPPHSLH SMPTDGQLDG TYPPPVHDDN VSMASSGATQ 600
    AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN 650
    QQNVQNLSHT EVVDILKDCP IGSETSLIIH RGGFFSPWKT PKPIMDRWEN 700
    QGSPQTSLSA PAIPQNLPFP PALHRSSFPD STEAFDPRKP DPYELYEKSR 750
    AIYESRQQVP PRTSFRMDSS GPDYKELDVH LRRMESGFGF RILGGDEPGQ 800
    PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY VIDLMHHAAR 850
    NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYTNSNHAA 900
    PSSNASPPEG FASHSLQTSD VVIHRKENEG FGFVIISSLN RPESGSTITV 950
    PHKIGRIIDG SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL 1000
    SVTLRIIPQE ELNSPTSAPS SEKQSPMAQQ SPLAQQSPLA QPSPATPNSP 1050
    IAQPAPPQPL QLQGHENSYR SEVKARQDVK PDIRQPPFTD YRQPPLDYRQ 1100
    PPGGDYQQPP PLDYRQPPLL DYRQHSPDTR QYPLSDYRQP QDFDYFTVDM 1150
    EKGAKGFGFS IRGGREYKMD LYVLRLAEDG PAIRNGRMRV GDQIIEINGE 1200
    STRDMTHARA IELIKSGGRR VRLLLKRGTG QVPEYDEPAP WSSPAAAAPG 1250
    LPEVGVSLDD GLAPFSPSHP APPSDPSHQI SPGPTWDIKR EHDVRKPKEL 1300
    SACGQKKQRL GEQRERSASP QRAARPRLEE APGGQGRPEA GRPASEARAP 1350
    GLAAADAADA ARAGGKEAPR AAAGSELCRR EGPGAAPAFA GPGGGGSGAL 1400
    EAEGRAGARA GPRPGPRPPG GAPARKAAVA PGPWKVPGSD KLPSVLKPGA 1450
    SAASR 1455
    Length:1,455
    Mass (Da):158,754
    Last modified:February 7, 2006 - v3
    Checksum:i93E170D070A70A9C
    GO
    Isoform 2 (identifier: Q86UL8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         757-771: QQVPPRTSFRMDSSG → R

    Show »
    Length:1,441
    Mass (Da):157,236
    Checksum:i505C382255497AFE
    GO

    Sequence cautioni

    The sequence BAA31680.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1234 – 12341E → Q in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1250 – 12501G → C in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1291 – 12911E → K in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1383 – 13831P → L in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1389 – 13946FAGPGG → SADPAD in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1401 – 14011E → A in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1411 – 14111G → A in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1414 – 14152PG → SV in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1420 – 14201G → A in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1423 – 14231P → A in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1426 – 14261K → R in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1429 – 14291V → G in AAC05370. (PubMed:9647693)Curated
    Sequence conflicti1437 – 14371P → R in AAC05370. (PubMed:9647693)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei757 – 77115QQVPP…MDSSG → R in isoform 2. 2 PublicationsVSP_008435Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038563 mRNA. Translation: AAC05370.1.
    AB014605 mRNA. Translation: BAA31680.2. Different initiation.
    AC004808 Genomic DNA. Translation: AAC23438.1.
    AC004945 Genomic DNA. Translation: AAC61488.1.
    AC004990 Genomic DNA. Translation: AAC79151.1.
    AC005246 Genomic DNA. Translation: AAC25530.1.
    AC006043 Genomic DNA. Translation: AAD15413.2.
    AC006324 Genomic DNA. Translation: AAF66080.1.
    AC007237 Genomic DNA. Translation: AAP21886.1.
    AC073200 Genomic DNA. Translation: AAP22360.1.
    CH236949 Genomic DNA. Translation: EAL24194.1.
    BC150277 mRNA. Translation: AAI50278.1.
    CCDSiCCDS5594.1. [Q86UL8-1]
    RefSeqiNP_036433.2. NM_012301.3. [Q86UL8-1]
    XP_005250782.1. XM_005250725.2. [Q86UL8-2]
    UniGeneiHs.603842.

    Genome annotation databases

    EnsembliENST00000354212; ENSP00000346151; ENSG00000187391. [Q86UL8-1]
    ENST00000419488; ENSP00000405766; ENSG00000187391. [Q86UL8-2]
    GeneIDi9863.
    KEGGihsa:9863.
    UCSCiuc003ugx.3. human. [Q86UL8-1]
    uc003ugy.3. human. [Q86UL8-2]

    Polymorphism databases

    DMDMi88909269.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038563 mRNA. Translation: AAC05370.1 .
    AB014605 mRNA. Translation: BAA31680.2 . Different initiation.
    AC004808 Genomic DNA. Translation: AAC23438.1 .
    AC004945 Genomic DNA. Translation: AAC61488.1 .
    AC004990 Genomic DNA. Translation: AAC79151.1 .
    AC005246 Genomic DNA. Translation: AAC25530.1 .
    AC006043 Genomic DNA. Translation: AAD15413.2 .
    AC006324 Genomic DNA. Translation: AAF66080.1 .
    AC007237 Genomic DNA. Translation: AAP21886.1 .
    AC073200 Genomic DNA. Translation: AAP22360.1 .
    CH236949 Genomic DNA. Translation: EAL24194.1 .
    BC150277 mRNA. Translation: AAI50278.1 .
    CCDSi CCDS5594.1. [Q86UL8-1 ]
    RefSeqi NP_036433.2. NM_012301.3. [Q86UL8-1 ]
    XP_005250782.1. XM_005250725.2. [Q86UL8-2 ]
    UniGenei Hs.603842.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UEP NMR - A 774-863 [» ]
    1UEQ NMR - A 412-522 [» ]
    1UEW NMR - A 915-1015 [» ]
    1UJV NMR - A 600-682 [» ]
    1WFV NMR - A 1141-1230 [» ]
    ProteinModelPortali Q86UL8.
    SMRi Q86UL8. Positions 25-96, 134-255, 303-379, 412-522, 594-682, 769-865, 898-1054, 1141-1233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115197. 8 interactions.
    IntActi Q86UL8. 5 interactions.
    MINTi MINT-109875.

    PTM databases

    PhosphoSitei Q86UL8.

    Polymorphism databases

    DMDMi 88909269.

    Proteomic databases

    MaxQBi Q86UL8.
    PaxDbi Q86UL8.
    PRIDEi Q86UL8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354212 ; ENSP00000346151 ; ENSG00000187391 . [Q86UL8-1 ]
    ENST00000419488 ; ENSP00000405766 ; ENSG00000187391 . [Q86UL8-2 ]
    GeneIDi 9863.
    KEGGi hsa:9863.
    UCSCi uc003ugx.3. human. [Q86UL8-1 ]
    uc003ugy.3. human. [Q86UL8-2 ]

    Organism-specific databases

    CTDi 9863.
    GeneCardsi GC07M077646.
    H-InvDB HIX0006801.
    HGNCi HGNC:18957. MAGI2.
    HPAi HPA013650.
    MIMi 606382. gene.
    neXtProti NX_Q86UL8.
    PharmGKBi PA142671484.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320141.
    HOVERGENi HBG007091.
    InParanoidi Q86UL8.
    KOi K05629.
    OMAi HEDKSAG.
    OrthoDBi EOG7FV3PH.
    PhylomeDBi Q86UL8.
    TreeFami TF316816.

    Enzyme and pathway databases

    Reactomei REACT_23832. Nephrin interactions.
    SignaLinki Q86UL8.

    Miscellaneous databases

    ChiTaRSi MAGI2. human.
    EvolutionaryTracei Q86UL8.
    GeneWikii MAGI2.
    GenomeRNAii 9863.
    NextBioi 37182.
    PROi Q86UL8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86UL8.
    Bgeei Q86UL8.
    Genevestigatori Q86UL8.

    Family and domain databases

    Gene3Di 2.30.42.10. 6 hits.
    InterProi IPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    IPR001478. PDZ.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    PF00595. PDZ. 6 hits.
    PF00397. WW. 2 hits.
    [Graphical view ]
    SMARTi SM00072. GuKc. 1 hit.
    SM00228. PDZ. 6 hits.
    SM00456. WW. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 6 hits.
    SSF51045. SSF51045. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    PS50106. PDZ. 6 hits.
    PS01159. WW_DOMAIN_1. 2 hits.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins."
      Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A.
      Mol. Cell. Neurosci. 11:149-160(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH DRPLA.
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "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].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
    6. "Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2."
      Wu X., Hepner K., Castelino-Prabhu S., Do D., Kaye M.B., Yuan X.-J., Wood J., Ross C., Sawyers C.L., Whang Y.E.
      Proc. Natl. Acad. Sci. U.S.A. 97:4233-4238(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTEN.
    7. "Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex."
      Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N., Sellers W.R.
      J. Biol. Chem. 276:48627-48630(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTEN.
    8. "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring."
      Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.
      J. Neurochem. 96:1659-1666(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDN.
    9. "Solution structure of the PDZ domains of human atrophin-1 interacting protein 1 (KIAA0705 protein)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 412-1230.

    Entry informationi

    Entry nameiMAGI2_HUMAN
    AccessioniPrimary (citable) accession number: Q86UL8
    Secondary accession number(s): A4D1C1
    , A7E2C3, O60434, O60510, Q86UI7, Q9NP44, Q9UDQ5, Q9UDU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 126 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3