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Q86UL8

- MAGI2_HUMAN

UniProt

Q86UL8 - MAGI2_HUMAN

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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

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. receptor signaling complex scaffold activity Source: UniProtKB
  4. signal transducer activity Source: Ensembl
  5. SMAD binding Source: UniProtKB
  6. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ86UL8.
ExpressionAtlasiQ86UL8. baseline and differential.
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 17-102, 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.
GeneTreeiENSGT00650000092997.
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

        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 EDFMELEKSG ALLESGTYED NYYGTPKPPA EPAPLLLNVT
210 220 230 240 250
DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP VVNGNGVVVT
260 270 280 290 300
PESSEHEDKS AGASGEMPSQ PYPAPVYSQP EELKEQMDDT KPTKPEDNEE
310 320 330 340 350
PDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PPEECKENEL
360 370 380 390 400
PYGWEKIDDP IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK
410 420 430 440 450
PLQAPGFREK PLFTRDASQL KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL
460 470 480 490 500
QVKSVIPDGP AAQDGKMETG DVIVYINEVC VLGHTHADVV KLFQSVPIGQ
510 520 530 540 550
SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG RHNYETYLEY
560 570 580 590 600
ISRTSQSVPD ITDRPPHSLH SMPTDGQLDG TYPPPVHDDN VSMASSGATQ
610 620 630 640 650
AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN
660 670 680 690 700
QQNVQNLSHT EVVDILKDCP IGSETSLIIH RGGFFSPWKT PKPIMDRWEN
710 720 730 740 750
QGSPQTSLSA PAIPQNLPFP PALHRSSFPD STEAFDPRKP DPYELYEKSR
760 770 780 790 800
AIYESRQQVP PRTSFRMDSS GPDYKELDVH LRRMESGFGF RILGGDEPGQ
810 820 830 840 850
PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY VIDLMHHAAR
860 870 880 890 900
NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYTNSNHAA
910 920 930 940 950
PSSNASPPEG FASHSLQTSD VVIHRKENEG FGFVIISSLN RPESGSTITV
960 970 980 990 1000
PHKIGRIIDG SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL
1010 1020 1030 1040 1050
SVTLRIIPQE ELNSPTSAPS SEKQSPMAQQ SPLAQQSPLA QPSPATPNSP
1060 1070 1080 1090 1100
IAQPAPPQPL QLQGHENSYR SEVKARQDVK PDIRQPPFTD YRQPPLDYRQ
1110 1120 1130 1140 1150
PPGGDYQQPP PLDYRQPPLL DYRQHSPDTR QYPLSDYRQP QDFDYFTVDM
1160 1170 1180 1190 1200
EKGAKGFGFS IRGGREYKMD LYVLRLAEDG PAIRNGRMRV GDQIIEINGE
1210 1220 1230 1240 1250
STRDMTHARA IELIKSGGRR VRLLLKRGTG QVPEYDEPAP WSSPAAAAPG
1260 1270 1280 1290 1300
LPEVGVSLDD GLAPFSPSHP APPSDPSHQI SPGPTWDIKR EHDVRKPKEL
1310 1320 1330 1340 1350
SACGQKKQRL GEQRERSASP QRAARPRLEE APGGQGRPEA GRPASEARAP
1360 1370 1380 1390 1400
GLAAADAADA ARAGGKEAPR AAAGSELCRR EGPGAAPAFA GPGGGGSGAL
1410 1420 1430 1440 1450
EAEGRAGARA GPRPGPRPPG GAPARKAAVA PGPWKVPGSD KLPSVLKPGA

SAASR
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]
CCDS75623.1. [Q86UL8-2]
RefSeqiNP_036433.2. NM_012301.3. [Q86UL8-1]
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 ]
CCDS75623.1. [Q86UL8-2 ]
RefSeqi NP_036433.2. NM_012301.3. [Q86UL8-1 ]
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 17-102, 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.
GeneTreei ENSGT00650000092997.
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

Bgeei Q86UL8.
ExpressionAtlasi Q86UL8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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