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Q86UL8 (MAGI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MAGI2
Synonyms:ACVRINP1, AIP1, KIAA0705
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1455 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. Ref.6

Subunit structure

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. Ref.1 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm By similarity. Late endosome By similarity. Cell junctionsynapsesynaptosome By similarity. Cell membrane; 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. Ref.6

Tissue specificity

Specifically expressed in brain. Ref.1

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 6 PDZ (DHR) domains.

Contains 2 WW domains.

Sequence caution

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

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Endosome
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to nerve growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic transport

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular visceral epithelial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of activin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from direct assay Ref.6. Source: UniProtKB

nerve growth factor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

planar cell polarity pathway involved in axis elongation

Non-traceable author statement PubMed 20534871. Source: UniProtKB

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphoprotein phosphatase activity

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of receptor internalization

Inferred from direct assay PubMed 11526121. Source: UniProtKB

protein heterooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

receptor clustering

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11526121. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

late endosome

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.6PubMed 11526121. Source: UniProtKB

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

slit diaphragm

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

tight junction

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionSMAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

beta-1 adrenergic receptor binding

Inferred from physical interaction PubMed 11526121. Source: UniProtKB

phosphatase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10548487Ref.1. Source: UniProtKB

receptor signaling complex scaffold activity

Inferred from direct assay PubMed 11526121. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

type II activin receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADRB1P085882EBI-311035,EBI-991009

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

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
Region302 – 38180Interaction with DDN
Compositional bias1015 – 1118104Pro-rich
Compositional bias1340 – 143091Ala-rich

Amino acid modifications

Modified residue3621Phosphotyrosine By similarity
Modified residue8271Phosphotyrosine 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

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

Details...

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       1430       1440 
EGPGAAPAFA GPGGGGSGAL EAEGRAGARA GPRPGPRPPG GAPARKAAVA PGPWKVPGSD 

      1450 
KLPSVLKPGA SAASR 

« Hide

Isoform 2 [UniParc].

Checksum: 505C382255497AFE
Show »

FASTA1,441157,236

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5594.1. [Q86UL8-1]
RefSeqNP_036433.2. NM_012301.3. [Q86UL8-1]
XP_005250782.1. XM_005250725.2. [Q86UL8-2]
UniGeneHs.603842.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UEPNMR-A774-863[»]
1UEQNMR-A412-522[»]
1UEWNMR-A915-1015[»]
1UJVNMR-A600-682[»]
1WFVNMR-A1141-1230[»]
ProteinModelPortalQ86UL8.
SMRQ86UL8. Positions 25-96, 134-255, 303-379, 412-522, 594-682, 769-865, 898-1054, 1141-1233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115197. 8 interactions.
IntActQ86UL8. 5 interactions.
MINTMINT-109875.

PTM databases

PhosphoSiteQ86UL8.

Polymorphism databases

DMDM88909269.

Proteomic databases

MaxQBQ86UL8.
PaxDbQ86UL8.
PRIDEQ86UL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354212; ENSP00000346151; ENSG00000187391. [Q86UL8-1]
ENST00000419488; ENSP00000405766; ENSG00000187391. [Q86UL8-2]
GeneID9863.
KEGGhsa:9863.
UCSCuc003ugx.3. human. [Q86UL8-1]
uc003ugy.3. human. [Q86UL8-2]

Organism-specific databases

CTD9863.
GeneCardsGC07M077646.
H-InvDBHIX0006801.
HGNCHGNC:18957. MAGI2.
HPAHPA013650.
MIM606382. gene.
neXtProtNX_Q86UL8.
PharmGKBPA142671484.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320141.
HOVERGENHBG007091.
InParanoidQ86UL8.
KOK05629.
OMAHEDKSAG.
OrthoDBEOG7FV3PH.
PhylomeDBQ86UL8.
TreeFamTF316816.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkQ86UL8.

Gene expression databases

ArrayExpressQ86UL8.
BgeeQ86UL8.
GenevestigatorQ86UL8.

Family and domain databases

Gene3D2.30.42.10. 6 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 6 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 6 hits.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 6 hits.
SSF51045. SSF51045. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. 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]
ProtoNetSearch...

Other

ChiTaRSMAGI2. human.
EvolutionaryTraceQ86UL8.
GeneWikiMAGI2.
GenomeRNAi9863.
NextBio37182.
PROQ86UL8.
SOURCESearch...

Entry information

Entry nameMAGI2_HUMAN
AccessionPrimary (citable) accession number: Q86UL8
Secondary accession number(s): A4D1C1 expand/collapse secondary AC list , A7E2C3, O60434, O60510, Q86UI7, Q9NP44, Q9UDQ5, Q9UDU1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM