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UniProtKB/Swiss-Prot entry Q86UL8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MAGI2_HUMAN
Primary accession number Q86UL8
Secondary accession numbers O60434 O60510 Q86UI7 Q9NP44 Q9UDQ5 Q9UDU1
Integrated into Swiss-Prot on October 3, 2003
Sequence was last modified on February 7, 2006 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 61)
Name and origin of the protein
Protein name Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Synonyms Membrane-associated guanylate kinase inverted 2
MAGI-2
Atrophin-1-interacting protein 1
Atrophin-1-interacting protein A
Gene name
Name: MAGI2
Synonyms: ACVRINP1, AIP1, KIAA0705
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION WITH DRPLA.
TISSUE=Brain;
DOI=10.1006/mcne.1998.0677; PubMed=9647693 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins.";
Mol. Cell. Neurosci. 11:149-160(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1093/dnares/5.3.169; PubMed=9734811 [NCBI, ExPASy, EBI, Israel, Japan]
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"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.";
DNA Res. 5:169-176(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTEN.
DOI=10.1073/pnas.97.8.4233; PubMed=10760291 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2.";
Proc. Natl. Acad. Sci. U.S.A. 97:4233-4238(2000).
[5]
INTERACTION WITH PTEN.
DOI=10.1074/jbc.C100556200; PubMed=11707428 [NCBI, ExPASy, EBI, Israel, Japan]
Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N., Sellers W.R.;
"Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex.";
J. Biol. Chem. 276:48627-48630(2001).
[6]
STRUCTURE BY NMR OF 412-1230.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PDZ domains of human atrophin-1 interacting protein 1 (KIAA0705 protein).";
Submitted (FEB-2004) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF038563; AAC05370.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB014605; BAA31680.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004808; AAC23438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004945; AAC61488.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004990; AAC79151.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005246; AAC25530.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006043; AAD15413.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006324; AAF66080.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007237; AAP21886.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC073200; AAP22360.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_036433.2; -.
UniGene Hs.654788
3D structure databases
PDB
1UEP; NMR; -; A=774-865.[ExPASy / RCSB / EBI]
1UEQ; NMR; -; A=412-522.[ExPASy / RCSB / EBI]
1UEW; NMR; -; A=913-1015.[ExPASy / RCSB / EBI]
1UJV; NMR; -; A=600-682.[ExPASy / RCSB / EBI]
1WFV; NMR; -; A=1141-1230.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1UEP; -.
1UEQ; -.
1UEW; -.
1UJV; -.
1WFV; -.
ModBase Q86UL8.
Protein-protein interaction databases
IntAct Q86UL8; -.
PTM databases
PhosphoSite Q86UL8; -.
Organism-specific databases
H-InvDB HIX0006801; -.
HGNC HGNC:18957; MAGI2.
GeneLynx MAGI2; Homo sapiens.
GenAtlas MAGI2.
HPA HPA013650; -.
MIM 606382; gene. [NCBI / EBI]
PharmGKB PA142671484; -.
GeneCards Q86UL8.
HUGE KIAA0705.
Gene expression databases
ArrayExpress Q86UL8; -.
CleanEx HS_MAGI2; -.
GermOnline ENSG00000187391; Homo sapiens.
Ontologies
GO
GO:0019902; Molecular function: phosphatase binding (inferred from physical interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR008144; Guanylate_kin.
IPR008145; Guanylt/Ca.
IPR001478; PDZ.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF00625; Guanylate_kin; 1.
PF00595; PDZ; 6.
PF00397; WW; 2.
Pfam graphical view of domain structure.
SMART SM00072; GuKc; 1.
SM00228; PDZ; 6.
SM00456; WW; 2.
SMART graphical view of domain structure.
PROSITE PS00856; GUANYLATE_KINASE_1; 1.
PS50052; GUANYLATE_KINASE_2; 1.
PS50106; PDZ; 6.
PS01159; WW_DOMAIN_1; 2.
PS50020; WW_DOMAIN_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q86UL8.
Genome annotation databases
Ensembl ENSG00000187391; Homo sapiens. [Contig view]
GeneID 9863; -.
KEGG hsa:9863; -.
Phylogenomic databases
HOVERGEN Q86UL8; -.
Other
SOURCE MAGI2; Homo sapiens.
ProtoNet Q86UL8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell junction; Cell membrane; Membrane; Phosphoprotein; Repeat; Synapse; Synaptosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1455  1455     Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2. PRO_0000094586
DOMAIN   17    101  85     PDZ 1. 
DOMAIN   109    283  175     Guanylate kinase-like. 
DOMAIN   302    335  34     WW 1. 
DOMAIN   348    381  34     WW 2. 
DOMAIN   426    510  85     PDZ 2. 
DOMAIN   605    683  79     PDZ 3. 
DOMAIN   778    860  83     PDZ 4. 
DOMAIN   920   1010  91     PDZ 5. 
DOMAIN   1147   1229  83     PDZ 6. 
COMPBIAS   1015   1118  104     Pro-rich. 
COMPBIAS   1340   1430  91     Ala-rich. 
MOD_RES   362    362        Phosphotyrosine (By similarity). 
MOD_RES   366    366        Phosphotyrosine (By similarity). 
MOD_RES   827    827        Phosphotyrosine (By similarity). 
MOD_RES   1014   1014        Phosphoserine (By similarity). 
VAR_SEQ   757    771        QQVPPRTSFRMDSSG -> R (in isoform 2). VSP_008435
CONFLICT   1234   1234        E -> Q (in Ref. 1; AAC05370). 
CONFLICT   1250   1250        G -> C (in Ref. 1; AAC05370). 
CONFLICT   1291   1291        E -> K (in Ref. 1; AAC05370). 
CONFLICT   1383   1383        P -> L (in Ref. 1; AAC05370). 
CONFLICT   1389   1394        FAGPGG -> SADPAD (in Ref. 1; AAC05370). 
CONFLICT   1401   1401        E -> A (in Ref. 1; AAC05370). 
CONFLICT   1411   1411        G -> A (in Ref. 1; AAC05370). 
CONFLICT   1414   1415        PG -> SV (in Ref. 1; AAC05370). 
CONFLICT   1420   1420        G -> A (in Ref. 1; AAC05370). 
CONFLICT   1423   1423        P -> A (in Ref. 1; AAC05370). 
CONFLICT   1426   1426        K -> R (in Ref. 1; AAC05370). 
CONFLICT   1429   1429        V -> G (in Ref. 1; AAC05370). 
CONFLICT   1437   1437        P -> R (in Ref. 1; AAC05370). 
STRAND   415    417  3      
STRAND   422    430  9      
STRAND   437    441  5      
STRAND   444    447  4      
STRAND   451    455  5      
HELIX   460    463  4      
STRAND   472    476  5      
HELIX   486    494  9      
STRAND   501    509  9      
STRAND   604    609  6      
STRAND   612    622  11      
STRAND   625    632  8      
HELIX   634    636  3      
STRAND   645    649  5      
HELIX   659    668  10      
STRAND   673    680  8      
STRAND   774    777  4      
STRAND   780    787  8      
STRAND   790    792  3      
STRAND   803    807  5      
HELIX   814    816  3      
STRAND   824    828  5      
HELIX   838    851  14      
STRAND   853    861  9      
STRAND   919    924  6      
STRAND   933    936  4      
STRAND   953    957  5      
HELIX   964    966  3      
STRAND   974    978  5      
TURN   983    985  3      
HELIX   988    997  10      
TURN   998   1000  3      
STRAND   1001   1006  6      
STRAND   1156   1159  4      
STRAND   1162   1164  3      
TURN   1165   1168  4      
STRAND   1169   1172  4      
HELIX   1181   1185  5      
STRAND   1193   1197  5      
HELIX   1207   1217  11      
STRAND   1219   1221  3      
STRAND   1223   1226  4      
Sequence information
Length: 1455 AA [This is the length of the unprocessed precursor] Molecular weight: 158754 Da [This is the MW of the unprocessed precursor] CRC64: 93E170D070A70A9C [This is a checksum on the sequence]
        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       1430       1440 
EGPGAAPAFA GPGGGGSGAL EAEGRAGARA GPRPGPRPPG GAPARKAAVA PGPWKVPGSD 

      1450 
KLPSVLKPGA SAASR 

Q86UL8 in FASTA format

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