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Q5TCQ9

- MAGI3_HUMAN

UniProt

Q5TCQ9 - MAGI3_HUMAN

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Protein
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
Gene
MAGI3, KIAA1634
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi121 – 1288ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanylate kinase activity Source: UniProtKB
  3. protein binding Source: IntAct

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. intracellular signal transduction Source: UniProtKB
  3. nucleotide phosphorylation Source: GOC
  4. positive regulation of JUN kinase activity Source: Ensembl
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ5TCQ9.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
Alternative name(s):
Membrane-associated guanylate kinase inverted 3
Short name:
MAGI-3
Gene namesi
Name:MAGI3
Synonyms:KIAA1634
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29647. MAGI3.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Cell junctiontight junction. Nucleus By similarity
Note: Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions By similarity.2 Publications

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleus Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
  4. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Nucleus, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671485.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15061506Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
PRO_0000341407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341Phosphoserine By similarity

Post-translational modificationi

Ubiquitinated following interaction with HPV E6 protein, leading to its degradation by the proteasome. Degradation is independent of E6AP ubiquitin ligase complex.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ5TCQ9.
PaxDbiQ5TCQ9.
PRIDEiQ5TCQ9.

PTM databases

PhosphoSiteiQ5TCQ9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ5TCQ9.
CleanExiHS_MAGI3.
GenevestigatoriQ5TCQ9.

Organism-specific databases

HPAiHPA007923.

Interactioni

Subunit structurei

Interacts with ADRB1, FZD4, FZD7, PTPRB, TGFA and VANGL2. Interacts with unidentified tyrosine phosphorylated proteins By similarity. Interacts with BAI1, LPAR2/EDG4, GRIN2B and PTEN. In case of infection, interacts with HTLV TAX1 protein, possibly affecting the transformation ability of TAX1. Does not interact with HTLV TAX2 or TAX3 proteins. In case of infection, interacts with HPV type 16 and HPV type 18 E6 protein.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRB1P085885EBI-310506,EBI-991009
ADRB2P075509EBI-310506,EBI-491169
MED28Q9H2042EBI-310506,EBI-514199

Protein-protein interaction databases

BioGridi129277. 11 interactions.
IntActiQ5TCQ9. 9 interactions.
MINTiMINT-6800638.
STRINGi9606.ENSP00000304604.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi601 – 6077
Beta strandi612 – 6209
Beta strandi623 – 6308
Helixi632 – 6343
Beta strandi643 – 6475
Helixi657 – 66610
Beta strandi672 – 68110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SOEX-ray1.60A601-691[»]
ProteinModelPortaliQ5TCQ9.
SMRiQ5TCQ9. Positions 57-109, 142-191, 292-326, 340-405, 422-528, 590-683, 748-975, 1045-1127.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 10689PDZ 1
Add
BLAST
Domaini114 – 288175Guanylate kinase-like
Add
BLAST
Domaini293 – 32634WW 1
Add
BLAST
Domaini339 – 37234WW 2
Add
BLAST
Domaini435 – 51783PDZ 2
Add
BLAST
Domaini603 – 67977PDZ 3
Add
BLAST
Domaini751 – 83383PDZ 4
Add
BLAST
Domaini876 – 96388PDZ 5
Add
BLAST
Domaini1046 – 112883PDZ 6
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 10689Interaction with ADRB1 and TGFA By similarity
Add
BLAST
Regioni435 – 51783Interaction with PTEN
Add
BLAST
Regioni751 – 83383Interaction with BAI1
Add
BLAST
Regioni876 – 96388Interaction with LPAR2 and GRIN2B
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 94Poly-Lys
Compositional biasi238 – 2436Poly-Glu
Compositional biasi378 – 3814Poly-Pro

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 6 PDZ (DHR) domains.
Contains 2 WW domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5021.
HOVERGENiHBG007091.
KOiK06112.
OMAiPQEPYDV.
OrthoDBiEOG7FV3PH.
PhylomeDBiQ5TCQ9.
TreeFamiTF316816.

Family and domain databases

Gene3Di2.30.42.10. 6 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR029484. GVQW.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF13900. GVQW. 1 hit.
PF00595. PDZ. 4 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. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 6 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5TCQ9-1) [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

MSKTLKKKKH WLSKVQECAV SWAGPPGDFG AEIRGGAERG EFPYLGRLRE     50
EPGGGTCCVV SGKAPSPGDV LLEVNGTPVS GLTNRDTLAV IRHFREPIRL 100
KTVKPGKVIN KDLRHYLSLQ FQKGSIDHKL QQVIRDNLYL RTIPCTTRAP 150
RDGEVPGVDY NFISVEQFKA LEESGALLES GTYDGNFYGT PKPPAEPSPF 200
QPDPVDQVLF DNEFDAESQR KRTTSVSKME RMDSSLPEEE EDEDKEAING 250
SGNAENRERH SESSDWMKTV PSYNQTNSSM DFRNYMMRDE TLEPLPKNWE 300
MAYTDTGMIY FIDHNTKTTT WLDPRLCKKA KAPEDCEDGE LPYGWEKIED 350
PQYGTYYVDF TLVAQAGVQW HDLGSLQPPP PGFNHLNQKT QFENPVEEAK 400
RKKQLGQVEI GSSKPDMEKS HFTRDPSQLK GVLVRASLKK STMGFGFTII 450
GGDRPDEFLQ VKNVLKDGPA AQDGKIAPGD VIVDINGNCV LGHTHADVVQ 500
MFQLVPVNQY VNLTLCRGYP LPDDSEDPVV DIVAATPVIN GQSLTKGETC 550
MNPQDFKPGA MVLEQNGKSG HTLTGDGLNG PSDASEQRVS MASSGSSQPE 600
LVTIPLIKGP KGFGFAIADS PTGQKVKMIL DSQWCQGLQK GDIIKEIYHQ 650
NVQNLTHLQV VEVLKQFPVG ADVPLLILRG GPPSPTKTAK MKTDKKENAG 700
SLEAINEPIP QPMPFPPSII RSGSPKLDPS EVYLKSKTLY EDKPPNTKDL 750
DVFLRKQESG FGFRVLGGDG PDQSIYIGAI IPLGAAEKDG RLRAADELMC 800
IDGIPVKGKS HKQVLDLMTT AARNGHVLLT VRRKIFYGEK QPEDDSSQAF 850
ISTQNGSPRL NRAEVPARPA PQEPYDVVLQ RKENEGFGFV ILTSKNKPPP 900
GVIPHKIGRV IEGSPADRCG KLKVGDHISA VNGQSIVELS HDNIVQLIKD 950
AGVTVTLTVI AEEEHHGPPS GTNSARQSPA LQHRPMGQSQ ANHIPGDRSA 1000
LEGEIGKDVS TSYRHSWSDH KHLAQPDTAV ISVVGSRHNQ NLGCYPVELE 1050
RGPRGFGFSL RGGKEYNMGL FILRLAEDGP AIKDGRIHVG DQIVEINGEP 1100
TQGITHTRAI ELIQAGGNKV LLLLRPGTGL IPDHGDWDIN NPSSSNVIYD 1150
EQSPLPPSSH FASIFEESHV PVIEESLRVQ ICEKAEELKD IVPEKKSTLN 1200
ENQPEIKHQS LLQKNVSKRD PPSSHGHSNK KNLLKVENGV TRRGRSVSPK 1250
KPASQHSEEH LDKIPSPLKN NPKRRPRDQS LSPSKGENKS CQVSTRAGSG 1300
QDQCRKSRGR SASPKKQQKI EGSKAPSNAE AKLLEGKSRR IAGYTGSNAE 1350
QIPDGKEKSD VIRKDAKQNQ LEKSRTRSPE KKIKRMVEKS LPSKMTNKTT 1400
SKEVSENEKG KKVTTGETSS SNDKIGENVQ LSEKRLKQEP EEKVVSNKTE 1450
DHKGKELEAA DKNKETGRFK PESSSPVKKT LITPGPWKVP SGNKVTGTIG 1500
MAEKRQ 1506
Length:1,506
Mass (Da):165,608
Last modified:June 10, 2008 - v2
Checksum:i0EA98F09F9AB109F
GO
Isoform 2 (identifier: Q5TCQ9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1136-1150: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH
     1151-1506: Missing.

Show »
Length:1,150
Mass (Da):125,998
Checksum:i14DED25795278E3C
GO
Isoform 3 (identifier: Q5TCQ9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     360-384: Missing.
     1136-1150: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH
     1151-1506: Missing.

Show »
Length:1,125
Mass (Da):123,339
Checksum:iFA2340EA152503E9
GO
Isoform 4 (identifier: Q5TCQ9-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     360-384: Missing.

Note: No experimental confirmation available.

Show »
Length:1,481
Mass (Da):162,949
Checksum:i9C2B604D9B1B1B97
GO

Sequence cautioni

The sequence BAB15479.1 differs from that shown. Reason: Frameshift at position 1373.
The sequence BAB15479.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei360 – 38425Missing in isoform 3 and isoform 4.
VSP_034285Add
BLAST
Alternative sequencei1136 – 115015DWDIN…NVIYD → LAPSGLCSYVKPEQH in isoform 2 and isoform 3.
VSP_034286Add
BLAST
Alternative sequencei1151 – 1506356Missing in isoform 2 and isoform 3.
VSP_034287Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91K → R in AAG43837. 1 Publication
Sequence conflicti59 – 591V → I in AAG24545. 1 Publication
Sequence conflicti66 – 683SPG → NPS in AAG24545. 1 Publication
Sequence conflicti246 – 2461E → G in AAG24545. 1 Publication
Sequence conflicti257 – 2571R → G in AAG43837. 1 Publication
Sequence conflicti491 – 4911L → F in AAG24545. 1 Publication
Sequence conflicti573 – 5731L → S in AAG24545. 1 Publication
Sequence conflicti641 – 6411G → E in AAG24545. 1 Publication
Sequence conflicti685 – 6851P → T in AAG24545. 1 Publication
Sequence conflicti801 – 8011I → V in AAG43837. 1 Publication
Sequence conflicti823 – 8231R → P in AAG43837. 1 Publication
Sequence conflicti942 – 9421D → A in AAG24545. 1 Publication
Sequence conflicti1018 – 10181S → P in AAG43837. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF257238 mRNA. Translation: AAG24545.1.
AF213259 mRNA. Translation: AAG43837.1.
AL365225
, AL133517, AL389921, AL390759 Genomic DNA. Translation: CAH70944.1.
AL365225
, AL133517, AL389921, AL390759 Genomic DNA. Translation: CAH70945.1.
AL365225
, AL133517, AL389921, AL390759 Genomic DNA. Translation: CAH70946.1.
AL389921
, AL133517, AL365225, AL390759 Genomic DNA. Translation: CAH71507.1.
AL389921
, AL133517, AL365225, AL390759 Genomic DNA. Translation: CAH71508.1.
AL389921
, AL133517, AL365225, AL390759 Genomic DNA. Translation: CAH71509.1.
AL390759
, AL133517, AL365225, AL389921 Genomic DNA. Translation: CAH74141.1.
AL390759
, AL133517, AL365225, AL389921 Genomic DNA. Translation: CAH74142.1.
AL390759
, AL133517, AL365225, AL389921 Genomic DNA. Translation: CAH74143.1.
AL133517
, AL365225, AL389921, AL390759 Genomic DNA. Translation: CAI22553.1.
AL133517
, AL365225, AL389921, AL390759 Genomic DNA. Translation: CAI22554.1.
AL133517
, AL365225, AL389921, AL390759 Genomic DNA. Translation: CAI22555.1.
CH471122 Genomic DNA. Translation: EAW56559.1.
CH471122 Genomic DNA. Translation: EAW56560.1.
CH471122 Genomic DNA. Translation: EAW56562.1.
BC130409 mRNA. Translation: AAI30410.1.
AB046854 mRNA. Translation: BAB13460.1.
AK026417 mRNA. Translation: BAB15479.1. Sequence problems.
CCDSiCCDS44196.1. [Q5TCQ9-4]
CCDS860.1. [Q5TCQ9-3]
RefSeqiNP_001136254.1. NM_001142782.1. [Q5TCQ9-4]
NP_690864.2. NM_152900.2. [Q5TCQ9-3]
XP_005270794.1. XM_005270737.1. [Q5TCQ9-3]
UniGeneiHs.486189.

Genome annotation databases

EnsembliENST00000307546; ENSP00000304604; ENSG00000081026. [Q5TCQ9-4]
ENST00000369611; ENSP00000358624; ENSG00000081026. [Q5TCQ9-3]
ENST00000369615; ENSP00000358628; ENSG00000081026. [Q5TCQ9-3]
ENST00000369617; ENSP00000358630; ENSG00000081026. [Q5TCQ9-2]
GeneIDi260425.
KEGGihsa:260425.
UCSCiuc001edh.3. human. [Q5TCQ9-2]
uc001edi.4. human. [Q5TCQ9-3]
uc001edk.3. human. [Q5TCQ9-4]

Polymorphism databases

DMDMi190359882.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF257238 mRNA. Translation: AAG24545.1 .
AF213259 mRNA. Translation: AAG43837.1 .
AL365225
, AL133517 , AL389921 , AL390759 Genomic DNA. Translation: CAH70944.1 .
AL365225
, AL133517 , AL389921 , AL390759 Genomic DNA. Translation: CAH70945.1 .
AL365225
, AL133517 , AL389921 , AL390759 Genomic DNA. Translation: CAH70946.1 .
AL389921
, AL133517 , AL365225 , AL390759 Genomic DNA. Translation: CAH71507.1 .
AL389921
, AL133517 , AL365225 , AL390759 Genomic DNA. Translation: CAH71508.1 .
AL389921
, AL133517 , AL365225 , AL390759 Genomic DNA. Translation: CAH71509.1 .
AL390759
, AL133517 , AL365225 , AL389921 Genomic DNA. Translation: CAH74141.1 .
AL390759
, AL133517 , AL365225 , AL389921 Genomic DNA. Translation: CAH74142.1 .
AL390759
, AL133517 , AL365225 , AL389921 Genomic DNA. Translation: CAH74143.1 .
AL133517
, AL365225 , AL389921 , AL390759 Genomic DNA. Translation: CAI22553.1 .
AL133517
, AL365225 , AL389921 , AL390759 Genomic DNA. Translation: CAI22554.1 .
AL133517
, AL365225 , AL389921 , AL390759 Genomic DNA. Translation: CAI22555.1 .
CH471122 Genomic DNA. Translation: EAW56559.1 .
CH471122 Genomic DNA. Translation: EAW56560.1 .
CH471122 Genomic DNA. Translation: EAW56562.1 .
BC130409 mRNA. Translation: AAI30410.1 .
AB046854 mRNA. Translation: BAB13460.1 .
AK026417 mRNA. Translation: BAB15479.1 . Sequence problems.
CCDSi CCDS44196.1. [Q5TCQ9-4 ]
CCDS860.1. [Q5TCQ9-3 ]
RefSeqi NP_001136254.1. NM_001142782.1. [Q5TCQ9-4 ]
NP_690864.2. NM_152900.2. [Q5TCQ9-3 ]
XP_005270794.1. XM_005270737.1. [Q5TCQ9-3 ]
UniGenei Hs.486189.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SOE X-ray 1.60 A 601-691 [» ]
ProteinModelPortali Q5TCQ9.
SMRi Q5TCQ9. Positions 57-109, 142-191, 292-326, 340-405, 422-528, 590-683, 748-975, 1045-1127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 129277. 11 interactions.
IntActi Q5TCQ9. 9 interactions.
MINTi MINT-6800638.
STRINGi 9606.ENSP00000304604.

Chemistry

BindingDBi Q5TCQ9.
ChEMBLi CHEMBL5212.

PTM databases

PhosphoSitei Q5TCQ9.

Polymorphism databases

DMDMi 190359882.

Proteomic databases

MaxQBi Q5TCQ9.
PaxDbi Q5TCQ9.
PRIDEi Q5TCQ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307546 ; ENSP00000304604 ; ENSG00000081026 . [Q5TCQ9-4 ]
ENST00000369611 ; ENSP00000358624 ; ENSG00000081026 . [Q5TCQ9-3 ]
ENST00000369615 ; ENSP00000358628 ; ENSG00000081026 . [Q5TCQ9-3 ]
ENST00000369617 ; ENSP00000358630 ; ENSG00000081026 . [Q5TCQ9-2 ]
GeneIDi 260425.
KEGGi hsa:260425.
UCSCi uc001edh.3. human. [Q5TCQ9-2 ]
uc001edi.4. human. [Q5TCQ9-3 ]
uc001edk.3. human. [Q5TCQ9-4 ]

Organism-specific databases

CTDi 260425.
GeneCardsi GC01P113933.
H-InvDB HIX0000900.
HGNCi HGNC:29647. MAGI3.
HPAi HPA007923.
neXtProti NX_Q5TCQ9.
PharmGKBi PA142671485.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
HOVERGENi HBG007091.
KOi K06112.
OMAi PQEPYDV.
OrthoDBi EOG7FV3PH.
PhylomeDBi Q5TCQ9.
TreeFami TF316816.

Enzyme and pathway databases

SignaLinki Q5TCQ9.

Miscellaneous databases

GeneWikii MAGI3.
GenomeRNAii 260425.
NextBioi 93203.
PROi Q5TCQ9.

Gene expression databases

Bgeei Q5TCQ9.
CleanExi HS_MAGI3.
Genevestigatori Q5TCQ9.

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.
IPR029484. GVQW.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF13900. GVQW. 1 hit.
PF00595. PDZ. 4 hits.
PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00072. GuKc. 1 hit.
SM00228. PDZ. 6 hits.
SM00456. WW. 2 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 6 hits.
SSF51045. SSF51045. 1 hit.
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. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase."
    Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.
    J. Biol. Chem. 275:21477-21485(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PTEN; BAI1 AND GRIN2B.
    Tissue: Mammary gland.
  2. "Identification of MAGI-3 as a transforming growth factor-alpha tail binding protein."
    Franklin J.L., Yoshiura K., Dempsey P.J., Bogatcheva G., Jeyakumar L., Meise K.S., Pearsall R.S., Threadgill D., Coffey R.J.
    Exp. Cell Res. 303:457-470(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-1506 (ISOFORM 2).
    Tissue: Brain.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 953-1506 (ISOFORM 1).
    Tissue: Ileal mucosa.
  8. "MAGI-1: a widely expressed, alternatively spliced tight junction protein."
    Laura R.P., Ross S., Koeppen H., Lasky L.A.
    Exp. Cell Res. 275:155-170(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation."
    Thomas M., Laura R., Hepner K., Guccione E., Sawyers C., Lasky L., Banks L.
    Oncogene 21:5088-5096(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HPV E6, PROBABLE UBIQUITINATION.
  10. "Role of the PDZ domain-binding motif of the oncoprotein E6 in the pathogenesis of human papillomavirus type 31."
    Lee C., Laimins L.A.
    J. Virol. 78:12366-12377(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HPV E6.
  11. "HPV E6 specifically targets different cellular pools of its PDZ domain-containing tumour suppressor substrates for proteasome-mediated degradation."
    Massimi P., Gammoh N., Thomas M., Banks L.
    Oncogene 23:8033-8039(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HPV E6.
  12. "Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts with a multi-PDZ domain protein, MAGI-3."
    Ohashi M., Sakurai M., Higuchi M., Mori N., Fukushi M., Oie M., Coffey R.J., Yoshiura K., Tanaka Y., Uchiyama M., Hatanaka M., Fujii M.
    Virology 320:52-62(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV TAX1.
  13. "Rational design of a nonpeptide general chemical scaffold for reversible inhibition of PDZ domain interactions."
    Fujii N., Haresco J.J., Novak K.A., Gage R.M., Pedemonte N., Stokoe D., Kuntz I.D., Guy R.K.
    Bioorg. Med. Chem. Lett. 17:549-552(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGANDS THAT BIND AND INHIBIT PDZ DOMAINS.
  14. "MAGI-3 regulates LPA-induced activation of Erk and RhoA."
    Zhang H., Wang D., Sun H., Hall R.A., Yun C.C.
    Cell. Signal. 19:261-268(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPAR2.
  15. "HPV E6 degradation of p53 and PDZ containing substrates in an E6AP null background."
    Massimi P., Shai A., Lambert P., Banks L.
    Oncogene 27:1800-1804(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HPV E6, PROBABLE UBIQUITINATION.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAGI3_HUMAN
AccessioniPrimary (citable) accession number: Q5TCQ9
Secondary accession number(s): Q5TCQ8
, Q5TCR0, Q9H2V6, Q9H5Y8, Q9HBC4, Q9HCD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: July 9, 2014
This is version 69 of the entry and version 2 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

Miscellaneous

MAGI3 PDZ domains are used to design peptide ligands that bind and inhibit PDZ domains.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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