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Reviewed, UniProtKB/Swiss-Prot Q86UL8 (MAGI2_HUMAN)

Last modified November 25, 2008. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Alternative name(s):
    Membrane-associated guanylate kinase inverted 2
      Short name=MAGI-2
    Atrophin-1-interacting protein 1
    Atrophin-1-interacting protein A
Gene names
Name: MAGI2
Synonyms: ACVRINP1, AIP1, KIAA0705
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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.

Subunit structure

Interacts via its WW domains with DRPLA. Interacts via its second PDZ domain with PTEN unphosphorylated C-terminus. Interacts through its guanylate kinase domain with DLGAP1 By similarity. Interacts through 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.

Subcellular location

Cell junction › synapse › synaptosomeBy similarity. Cell membrane; Peripheral membrane proteinBy similarity. Note= Membrane-associated in synaptosomes By similarity.

Tissue specificity

Specifically expressed in brain.

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 6 PDZ (DHR) domains.

Contains 2 WW domains.

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Ontologies

Keywords

   Cellular componentCell junction
Cell membrane
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Cellular componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

synaptosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphatase binding Ref.4

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86UL8-1)

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.
Isoform 2 (identifier: Q86UL8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     757-771: QQVPPRTSFRMDSSG → R
Notes: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14551455Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
PRO_0000094586

Regions

Domain17 – 10185PDZ 1
Domain109 – 283175Guanylate kinase-like
Domain302 – 33534WW 1
Domain348 – 38134WW 2
Domain426 – 51085PDZ 2
Domain605 – 68379PDZ 3
Domain778 – 86083PDZ 4
Domain920 – 101091PDZ 5
Domain1147 – 122983PDZ 6
Compositional bias1015 – 1118104Pro-rich
Compositional bias1340 – 143091Ala-rich

Amino acid modifications

Modified residue3621Phosphotyrosine By similarity
Modified residue3661Phosphotyrosine By similarity
Modified residue8271Phosphotyrosine By similarity
Modified residue10141Phosphoserine By similarity

Natural variations

Alternative sequence757 – 77115QQVPP…MDSSG → R in isoform 2.
VSP_008435

Experimental info

Sequence conflict12341E → Q in AAC05370. Ref.1
Sequence conflict12501G → C in AAC05370. Ref.1
Sequence conflict12911E → K in AAC05370. Ref.1
Sequence conflict13831P → L in AAC05370. Ref.1
Sequence conflict1389 – 13946FAGPGG → SADPAD in AAC05370. Ref.1
Sequence conflict14011E → A in AAC05370. Ref.1
Sequence conflict14111G → A in AAC05370. Ref.1
Sequence conflict1414 – 14152PG → SV in AAC05370. Ref.1
Sequence conflict14201G → A in AAC05370. Ref.1
Sequence conflict14231P → A in AAC05370. Ref.1
Sequence conflict14261K → R in AAC05370. Ref.1
Sequence conflict14291V → G in AAC05370. Ref.1
Sequence conflict14371P → R in AAC05370. Ref.1

Secondary structure

1 ................................................................................. 1455
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 7, 2006. Version 3.
Checksum: 93E170D070A70A9C

FASTA1,455158,754
        10         20         30         40         50         60 
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL 

        70         80         90        100        110        120 
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS 

       130        140        150        160        170        180 
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED 

       190        200        210        220        230        240 
NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP 

       250        260        270        280        290        300 
VVNGNGVVVT PESSEHEDKS AGASGEMPSQ PYPAPVYSQP EELKEQMDDT KPTKPEDNEE 

       310        320        330        340        350        360 
PDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PPEECKENEL PYGWEKIDDP 

       370        380        390        400        410        420 
IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL 

       430        440        450        460        470        480 
KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC 

       490        500        510        520        530        540 
VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG 

       550        560        570        580        590        600 
RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPTDGQLDG TYPPPVHDDN VSMASSGATQ 

       610        620        630        640        650        660 
AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT 

       670        680        690        700        710        720 
EVVDILKDCP IGSETSLIIH RGGFFSPWKT PKPIMDRWEN QGSPQTSLSA PAIPQNLPFP 

       730        740        750        760        770        780 
PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRQQVP PRTSFRMDSS GPDYKELDVH 

       790        800        810        820        830        840 
LRRMESGFGF RILGGDEPGQ PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY 

       850        860        870        880        890        900 
VIDLMHHAAR NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYTNSNHAA 

       910        920        930        940        950        960 
PSSNASPPEG FASHSLQTSD VVIHRKENEG FGFVIISSLN RPESGSTITV PHKIGRIIDG 

       970        980        990       1000       1010       1020 
SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNSPTSAPS 

      1030       1040       1050       1060       1070       1080 
SEKQSPMAQQ SPLAQQSPLA QPSPATPNSP IAQPAPPQPL QLQGHENSYR SEVKARQDVK 

      1090       1100       1110       1120       1130       1140 
PDIRQPPFTD YRQPPLDYRQ PPGGDYQQPP PLDYRQPPLL DYRQHSPDTR QYPLSDYRQP 

      1150       1160       1170       1180       1190       1200 
QDFDYFTVDM EKGAKGFGFS IRGGREYKMD LYVLRLAEDG PAIRNGRMRV GDQIIEINGE 

      1210       1220       1230       1240       1250       1260 
STRDMTHARA IELIKSGGRR VRLLLKRGTG QVPEYDEPAP WSSPAAAAPG LPEVGVSLDD 

      1270       1280       1290       1300       1310       1320 
GLAPFSPSHP APPSDPSHQI SPGPTWDIKR EHDVRKPKEL SACGQKKQRL GEQRERSASP 

      1330       1340       1350       1360       1370       1380 
QRAARPRLEE APGGQGRPEA GRPASEARAP GLAAADAADA ARAGGKEAPR AAAGSELCRR 

      1390       1400       1410       1420