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Protein

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

Gene

Magi2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • beta-1 adrenergic receptor binding Source: UniProtKB
  • PDZ domain binding Source: UniProtKB
  • phosphatase binding Source: UniProtKB
  • receptor signaling complex scaffold activity Source: UniProtKB
  • signal transducer activity Source: MGI
  • SMAD binding Source: UniProtKB
  • type II activin receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Alternative name(s):
Activin receptor-interacting protein 1
Short name:
Acvrip1
Atrophin-1-interacting protein 1
Short name:
AIP-1
Membrane-associated guanylate kinase inverted 2
Short name:
MAGI-2
Gene namesi
Name:Magi2
Synonyms:Acvrinp1, Aip1, Arip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1354953. Magi2.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • dendrite Source: UniProtKB
  • late endosome Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: UniProtKB
  • protein complex Source: UniProtKB
  • slit diaphragm Source: UniProtKB
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12751275Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2PRO_0000094587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611PhosphotyrosineCombined sources
Modified residuei685 – 6851PhosphoserineBy similarity
Modified residuei826 – 8261PhosphotyrosineCombined sources
Modified residuei883 – 8831PhosphoserineBy similarity
Modified residuei884 – 8841PhosphoserineBy similarity
Modified residuei1013 – 10131PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9WVQ1.
MaxQBiQ9WVQ1.
PaxDbiQ9WVQ1.
PRIDEiQ9WVQ1.

PTM databases

iPTMnetiQ9WVQ1.
PhosphoSiteiQ9WVQ1.

Expressioni

Tissue specificityi

Specifically expressed in brain.

Gene expression databases

BgeeiQ9WVQ1.
ExpressionAtlasiQ9WVQ1. baseline and differential.
GenevisibleiQ9WVQ1. MM.

Interactioni

Subunit structurei

Interacts (via its WW domains) with DRPLA (By similarity). 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 and MAGUIN-1 (By similarity). Interacts with ACVR2A, SMAD2 and SMAD3 (PubMed:10681527). Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (PubMed:10681527). May interact with HTR2A (PubMed:14988405). Interacts with RAPGEF2 (By similarity). Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 (By similarity). Interacts with DDN (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 IGSF9 and HTR4 (PubMed:15466885, PubMed:15340156). Interacts with DLL1 (PubMed:15509766). Found in a complex with IGSF9B and NLGN2; the interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains, while the interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2 domains (PubMed:23751499).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dll1Q614832EBI-297151,EBI-297125

GO - Molecular functioni

  • beta-1 adrenergic receptor binding Source: UniProtKB
  • PDZ domain binding Source: UniProtKB
  • phosphatase binding Source: UniProtKB
  • receptor signaling complex scaffold activity Source: UniProtKB
  • SMAD binding Source: UniProtKB
  • type II activin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi206123. 2 interactions.
IntActiQ9WVQ1. 1 interaction.
MINTiMINT-122116.
STRINGi10090.ENSMUSP00000085872.

Structurei

3D structure databases

ProteinModelPortaliQ9WVQ1.
SMRiQ9WVQ1. Positions 302-339, 346-378, 411-521, 593-681, 768-864, 915-1020, 1133-1228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 10185PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 283175Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST
Domaini301 – 33434WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 38034WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini425 – 50985PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini604 – 68279PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini777 – 85983PDZ 4PROSITE-ProRule annotationAdd
BLAST
Domaini919 – 100991PDZ 5PROSITE-ProRule annotationAdd
BLAST
Domaini1139 – 122183PDZ 6PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni301 – 38080Interaction with DDNBy similarityAdd
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

eggNOGiENOG410ISXI. Eukaryota.
ENOG410XNXK. LUCA.
GeneTreeiENSGT00650000092997.
HOGENOMiHOG000113463.
HOVERGENiHBG007091.
InParanoidiQ9WVQ1.
KOiK05629.
OrthoDBiEOG7FV3PH.
PhylomeDBiQ9WVQ1.
TreeFamiTF316816.

Family and domain databases

Gene3Di2.30.42.10. 6 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR030036. MAGI2.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR10316:SF27. PTHR10316:SF27. 3 hits.
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 5 hits.
PF00397. WW. 1 hit.
[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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WVQ1-1) [UniParc]FASTAAdd to basket

Also known as: long

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

        10         20         30         40         50
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG
60 70 80 90 100
KVAYESGSKL VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ
110 120 130 140 150
GGIVDKDLRH YLNLRFQKGS VDHELQQIIR DNLYLRTVPC TTRPHKEGEV
160 170 180 190 200
PGVDYIFITV EEFMELEKSG ALLESGTYED NYYGTPKPPA EPAPLLNVTD
210 220 230 240 250
QILPGATPSA EGKRKRNKSV TNMEKASIEP PEEEEEERPV VNGNGVVITP
260 270 280 290 300
ESSEHEDKSA GASGETPSQP YPAPVYSQPE ELKDQMDDTK PTKPEENEDS
310 320 330 340 350
DPLPDNWEMA YTEKGEVYFI DHNTKTTSWL DPRLAKKAKP PEECKENELP
360 370 380 390 400
YGWEKIDDPI YGTYYVDHIN RRTQFENPVL EAKRKLQQHN MPHTELGAKP
410 420 430 440 450
LQAPGFREKP LFTRDASQLK GTFLSTTLKK SNMGFGFTII GGDEPDEFLQ
460 470 480 490 500
VKSVIPDGPA AQDGKMETGD VIVYINEVCV LGHTHADVVK LFQSVPIGQS
510 520 530 540 550
VNLVLCRGYP LPFDPEDPAN SMVPPLAIME RPPPVMVNGR HNYETYLEYI
560 570 580 590 600
SRTSQSVPDI TDRPPHSLHS MPADGQLDGT YPPPVHDDNV SMASSGATQA
610 620 630 640 650
ELMTLTIVKG AQGFGFTIAD SPTGQRVKQI LDIQGCPGLC EGDLIVEINQ
660 670 680 690 700
QNVQNLSHTE VVDILKDCPV GSETSLIIHR GGFFSPWKTP KPMMDRWENQ
710 720 730 740 750
GSPQTSLSAP AVPQNLPFPP ALHRSSFPDS TEAFDPRKPD PYELYEKSRA
760 770 780 790 800
IYESRQQVPP RTSFRMDSSG PDYKELDVHL RRMESGFGFR ILGGDEPGQP
810 820 830 840 850
ILIGAVIAMG SADRDGRLHP GDELVYVDGI PVAGKTHRYV IDLMHHAARN
860 870 880 890 900
GQVNLTVRRK VLCGGEPCPE NGRSPGSVST HHSSPRSDYA TYSNSNHAAP
910 920 930 940 950
SSNASPPEGF ASHSLQTSDV VIHRKENEGF GFVIISSLNR PESGATITVP
960 970 980 990 1000
HKIGRIIDGS PADRCAKLKV GDRILAVNGQ SIINMPHADI VKLIKDAGLS
1010 1020 1030 1040 1050
VTLRIIPQEE LNSPTSAPSS EKQSPMAQQH SPLAQQSPLA QPSPATPNSP
1060 1070 1080 1090 1100
VAQPAPPQPL QLQGHENSYR SEVKARQDVK PDIRQPPFTD YRQPPLDYRQ
1110 1120 1130 1140 1150
PPGGDYSQPP PLDYRQHSPD TRQYPLSDYR QPQDFDYFTV DMEKGAKGFG
1160 1170 1180 1190 1200
FSIRGGREYK MDLYVLRLAE DGPAIRNGRM RVGDQIIEIN GESTRDMTHA
1210 1220 1230 1240 1250
RAIELIKSGG RRVRLLLKRG TGQVPEYGMV PSSLSMCMKS DKHGSPYFYL
1260 1270
LGHPKDTTNP TPGVLPLPPP QACRK
Length:1,275
Mass (Da):140,919
Last modified:October 3, 2003 - v2
Checksum:iF17DC52517806354
GO
Isoform 2 (identifier: Q9WVQ1-2) [UniParc]FASTAAdd to basket

Also known as: short

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.

Note: Major.
Show »
Length:1,112
Mass (Da):122,599
Checksum:i7B782082930C8490
GO
Isoform 3 (identifier: Q9WVQ1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-390: Missing.
     1229-1275: MVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPPPQACRK → AFHSFLHLCSAFSVF

Note: May be due to an intron retention. No experimental confirmation available.
Show »
Length:853
Mass (Da):93,543
Checksum:iAE241248B7C055A1
GO
Isoform 4 (identifier: Q9WVQ1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.
     756-770: QQVPPRTSFRMDSSG → R

Note: No experimental confirmation available.
Show »
Length:1,098
Mass (Da):121,080
Checksum:i57B20658576A87B6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 390390Missing in isoform 3. 1 PublicationVSP_018580Add
BLAST
Alternative sequencei1 – 163163Missing in isoform 2 and isoform 4. 3 PublicationsVSP_008436Add
BLAST
Alternative sequencei756 – 77015QQVPP…MDSSG → R in isoform 4. 1 PublicationVSP_018581Add
BLAST
Alternative sequencei1229 – 127547MVPSS…QACRK → AFHSFLHLCSAFSVF in isoform 3. 1 PublicationVSP_008437Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029485 mRNA. Translation: BAA82294.1.
AK039336 mRNA. Translation: BAC30321.1.
AK147530 mRNA. Translation: BAE27976.1.
BC059005 mRNA. Translation: AAH59005.1.
CCDSiCCDS39019.1. [Q9WVQ1-2]
CCDS51424.1. [Q9WVQ1-1]
CCDS51425.1. [Q9WVQ1-4]
RefSeqiNP_001164216.1. NM_001170745.1. [Q9WVQ1-4]
NP_001164217.1. NM_001170746.1. [Q9WVQ1-1]
NP_056638.1. NM_015823.3. [Q9WVQ1-2]
UniGeneiMm.332231.
Mm.441283.

Genome annotation databases

EnsembliENSMUST00000088516; ENSMUSP00000085872; ENSMUSG00000040003. [Q9WVQ1-1]
ENSMUST00000101558; ENSMUSP00000099094; ENSMUSG00000040003. [Q9WVQ1-4]
ENSMUST00000115267; ENSMUSP00000110922; ENSMUSG00000040003. [Q9WVQ1-2]
ENSMUST00000197553; ENSMUSP00000146769; ENSMUSG00000040003. [Q9WVQ1-3]
GeneIDi50791.
KEGGimmu:50791.
UCSCiuc008wnv.2. mouse. [Q9WVQ1-1]
uc008wnw.2. mouse. [Q9WVQ1-4]
uc008wnx.1. mouse. [Q9WVQ1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029485 mRNA. Translation: BAA82294.1.
AK039336 mRNA. Translation: BAC30321.1.
AK147530 mRNA. Translation: BAE27976.1.
BC059005 mRNA. Translation: AAH59005.1.
CCDSiCCDS39019.1. [Q9WVQ1-2]
CCDS51424.1. [Q9WVQ1-1]
CCDS51425.1. [Q9WVQ1-4]
RefSeqiNP_001164216.1. NM_001170745.1. [Q9WVQ1-4]
NP_001164217.1. NM_001170746.1. [Q9WVQ1-1]
NP_056638.1. NM_015823.3. [Q9WVQ1-2]
UniGeneiMm.332231.
Mm.441283.

3D structure databases

ProteinModelPortaliQ9WVQ1.
SMRiQ9WVQ1. Positions 302-339, 346-378, 411-521, 593-681, 768-864, 915-1020, 1133-1228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206123. 2 interactions.
IntActiQ9WVQ1. 1 interaction.
MINTiMINT-122116.
STRINGi10090.ENSMUSP00000085872.

PTM databases

iPTMnetiQ9WVQ1.
PhosphoSiteiQ9WVQ1.

Proteomic databases

EPDiQ9WVQ1.
MaxQBiQ9WVQ1.
PaxDbiQ9WVQ1.
PRIDEiQ9WVQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088516; ENSMUSP00000085872; ENSMUSG00000040003. [Q9WVQ1-1]
ENSMUST00000101558; ENSMUSP00000099094; ENSMUSG00000040003. [Q9WVQ1-4]
ENSMUST00000115267; ENSMUSP00000110922; ENSMUSG00000040003. [Q9WVQ1-2]
ENSMUST00000197553; ENSMUSP00000146769; ENSMUSG00000040003. [Q9WVQ1-3]
GeneIDi50791.
KEGGimmu:50791.
UCSCiuc008wnv.2. mouse. [Q9WVQ1-1]
uc008wnw.2. mouse. [Q9WVQ1-4]
uc008wnx.1. mouse. [Q9WVQ1-3]

Organism-specific databases

CTDi9863.
MGIiMGI:1354953. Magi2.

Phylogenomic databases

eggNOGiENOG410ISXI. Eukaryota.
ENOG410XNXK. LUCA.
GeneTreeiENSGT00650000092997.
HOGENOMiHOG000113463.
HOVERGENiHBG007091.
InParanoidiQ9WVQ1.
KOiK05629.
OrthoDBiEOG7FV3PH.
PhylomeDBiQ9WVQ1.
TreeFamiTF316816.

Miscellaneous databases

ChiTaRSiMagi2. mouse.
NextBioi307779.
PROiQ9WVQ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVQ1.
ExpressionAtlasiQ9WVQ1. baseline and differential.
GenevisibleiQ9WVQ1. MM.

Family and domain databases

Gene3Di2.30.42.10. 6 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR030036. MAGI2.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR10316:SF27. PTHR10316:SF27. 3 hits.
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 5 hits.
PF00397. WW. 1 hit.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a PDZ protein that interacts with activin types II receptors."
    Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z., Nakamura T., Sugino H.
    J. Biol. Chem. 275:5485-5492(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH SMAD2; SMAD3 AND ACVR2A, IDENTIFICATION IN A COMPLEX WITH ACVR2A; ACVR1B AND SMAD3.
    Strain: ICR.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Brain and Spinal cord.
  3. "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).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Delta proteins and MAGI proteins: an interaction of Notch ligands with intracellular scaffolding molecules and its significance for zebrafish development."
    Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.
    Development 131:5659-5669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLL1.
  5. "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins."
    Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P.
    J. Biol. Chem. 279:20257-20266(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTR2A.
  6. "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting."
    Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., Marin P., Dumuis A., Bockaert J.
    J. Cell Sci. 117:5367-5379(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTR4.
  7. "The immunoglobulin family member dendrite arborization and synapse maturation 1 (Dasm1) controls excitatory synapse maturation."
    Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.
    Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGSF9.
  8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361 AND TYR-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361 AND SER-1013, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to promote inhibitory synapse development."
    Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J., Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S., Craig A.M., Kim E.
    J. Cell Biol. 201:929-944(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH IGSF9B AND NLGN2.

Entry informationi

Entry nameiMAGI2_MOUSE
AccessioniPrimary (citable) accession number: Q9WVQ1
Secondary accession number(s): Q3UH81
, Q6GT88, Q8BYT1, Q8CA85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: May 11, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.