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Protein

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3

Gene

MAGI3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 1288ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29647. MAGI3.

Subcellular locationi

  1. Cell membrane; Peripheral membrane protein
  2. Cell junctiontight junction
  3. Nucleus By similarity

  4. Note: Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity).By similarity

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.

Polymorphism and mutation databases

BioMutaiMAGI3.
DMDMi190359882.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341PhosphoserineBy 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.

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.
ExpressionAtlasiQ5TCQ9. baseline and differential.
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.By similarity7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi129277. 16 interactions.
IntActiQ5TCQ9. 9 interactions.
MINTiMINT-6800638.
STRINGi9606.ENSP00000304604.

Structurei

Secondary structure

1
1506
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi601 – 6077Combined sources
Beta strandi612 – 6209Combined sources
Beta strandi623 – 6308Combined sources
Helixi632 – 6343Combined sources
Beta strandi643 – 6475Combined sources
Helixi657 – 66610Combined sources
Beta strandi672 – 68110Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 10689Interaction with ADRB1 and TGFABy similarityAdd
BLAST
Regioni435 – 51783Interaction with PTENAdd
BLAST
Regioni751 – 83383Interaction with BAI1Add
BLAST
Regioni876 – 96388Interaction with LPAR2 and GRIN2BAdd
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.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

eggNOGiCOG5021.
GeneTreeiENSGT00650000092997.
HOVERGENiHBG007091.
InParanoidiQ5TCQ9.
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.
IPR030035. MAGI3.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR10316:SF10. PTHR10316:SF10. 1 hit.
PfamiPF00625. Guanylate_kin. 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. AlignAdd to basket

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

        10         20         30         40         50
MSKTLKKKKH WLSKVQECAV SWAGPPGDFG AEIRGGAERG EFPYLGRLRE
60 70 80 90 100
EPGGGTCCVV SGKAPSPGDV LLEVNGTPVS GLTNRDTLAV IRHFREPIRL
110 120 130 140 150
KTVKPGKVIN KDLRHYLSLQ FQKGSIDHKL QQVIRDNLYL RTIPCTTRAP
160 170 180 190 200
RDGEVPGVDY NFISVEQFKA LEESGALLES GTYDGNFYGT PKPPAEPSPF
210 220 230 240 250
QPDPVDQVLF DNEFDAESQR KRTTSVSKME RMDSSLPEEE EDEDKEAING
260 270 280 290 300
SGNAENRERH SESSDWMKTV PSYNQTNSSM DFRNYMMRDE TLEPLPKNWE
310 320 330 340 350
MAYTDTGMIY FIDHNTKTTT WLDPRLCKKA KAPEDCEDGE LPYGWEKIED
360 370 380 390 400
PQYGTYYVDF TLVAQAGVQW HDLGSLQPPP PGFNHLNQKT QFENPVEEAK
410 420 430 440 450
RKKQLGQVEI GSSKPDMEKS HFTRDPSQLK GVLVRASLKK STMGFGFTII
460 470 480 490 500
GGDRPDEFLQ VKNVLKDGPA AQDGKIAPGD VIVDINGNCV LGHTHADVVQ
510 520 530 540 550
MFQLVPVNQY VNLTLCRGYP LPDDSEDPVV DIVAATPVIN GQSLTKGETC
560 570 580 590 600
MNPQDFKPGA MVLEQNGKSG HTLTGDGLNG PSDASEQRVS MASSGSSQPE
610 620 630 640 650
LVTIPLIKGP KGFGFAIADS PTGQKVKMIL DSQWCQGLQK GDIIKEIYHQ
660 670 680 690 700
NVQNLTHLQV VEVLKQFPVG ADVPLLILRG GPPSPTKTAK MKTDKKENAG
710 720 730 740 750
SLEAINEPIP QPMPFPPSII RSGSPKLDPS EVYLKSKTLY EDKPPNTKDL
760 770 780 790 800
DVFLRKQESG FGFRVLGGDG PDQSIYIGAI IPLGAAEKDG RLRAADELMC
810 820 830 840 850
IDGIPVKGKS HKQVLDLMTT AARNGHVLLT VRRKIFYGEK QPEDDSSQAF
860 870 880 890 900
ISTQNGSPRL NRAEVPARPA PQEPYDVVLQ RKENEGFGFV ILTSKNKPPP
910 920 930 940 950
GVIPHKIGRV IEGSPADRCG KLKVGDHISA VNGQSIVELS HDNIVQLIKD
960 970 980 990 1000
AGVTVTLTVI AEEEHHGPPS GTNSARQSPA LQHRPMGQSQ ANHIPGDRSA
1010 1020 1030 1040 1050
LEGEIGKDVS TSYRHSWSDH KHLAQPDTAV ISVVGSRHNQ NLGCYPVELE
1060 1070 1080 1090 1100
RGPRGFGFSL RGGKEYNMGL FILRLAEDGP AIKDGRIHVG DQIVEINGEP
1110 1120 1130 1140 1150
TQGITHTRAI ELIQAGGNKV LLLLRPGTGL IPDHGDWDIN NPSSSNVIYD
1160 1170 1180 1190 1200
EQSPLPPSSH FASIFEESHV PVIEESLRVQ ICEKAEELKD IVPEKKSTLN
1210 1220 1230 1240 1250
ENQPEIKHQS LLQKNVSKRD PPSSHGHSNK KNLLKVENGV TRRGRSVSPK
1260 1270 1280 1290 1300
KPASQHSEEH LDKIPSPLKN NPKRRPRDQS LSPSKGENKS CQVSTRAGSG
1310 1320 1330 1340 1350
QDQCRKSRGR SASPKKQQKI EGSKAPSNAE AKLLEGKSRR IAGYTGSNAE
1360 1370 1380 1390 1400
QIPDGKEKSD VIRKDAKQNQ LEKSRTRSPE KKIKRMVEKS LPSKMTNKTT
1410 1420 1430 1440 1450
SKEVSENEKG KKVTTGETSS SNDKIGENVQ LSEKRLKQEP EEKVVSNKTE
1460 1470 1480 1490 1500
DHKGKELEAA DKNKETGRFK PESSSPVKKT LITPGPWKVP SGNKVTGTIG

MAEKRQ
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. Curated
The sequence BAB15479.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91K → R in AAG43837 (PubMed:15652357).Curated
Sequence conflicti59 – 591V → I in AAG24545 (PubMed:10748157).Curated
Sequence conflicti66 – 683SPG → NPS in AAG24545 (PubMed:10748157).Curated
Sequence conflicti246 – 2461E → G in AAG24545 (PubMed:10748157).Curated
Sequence conflicti257 – 2571R → G in AAG43837 (PubMed:15652357).Curated
Sequence conflicti491 – 4911L → F in AAG24545 (PubMed:10748157).Curated
Sequence conflicti573 – 5731L → S in AAG24545 (PubMed:10748157).Curated
Sequence conflicti641 – 6411G → E in AAG24545 (PubMed:10748157).Curated
Sequence conflicti685 – 6851P → T in AAG24545 (PubMed:10748157).Curated
Sequence conflicti801 – 8011I → V in AAG43837 (PubMed:15652357).Curated
Sequence conflicti823 – 8231R → P in AAG43837 (PubMed:15652357).Curated
Sequence conflicti942 – 9421D → A in AAG24545 (PubMed:10748157).Curated
Sequence conflicti1018 – 10181S → P in AAG43837 (PubMed:15652357).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei360 – 38425Missing in isoform 3 and isoform 4. 1 PublicationVSP_034285Add
BLAST
Alternative sequencei1136 – 115015DWDIN…NVIYD → LAPSGLCSYVKPEQH in isoform 2 and isoform 3. 4 PublicationsVSP_034286Add
BLAST
Alternative sequencei1151 – 1506356Missing in isoform 2 and isoform 3. 4 PublicationsVSP_034287Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005270737.2. [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 and mutation databases

BioMutaiMAGI3.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005270737.2. [Q5TCQ9-3]
UniGeneiHs.486189.

3D structure databases

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

Protein-protein interaction databases

BioGridi129277. 16 interactions.
IntActiQ5TCQ9. 9 interactions.
MINTiMINT-6800638.
STRINGi9606.ENSP00000304604.

Chemistry

BindingDBiQ5TCQ9.
ChEMBLiCHEMBL5212.

PTM databases

PhosphoSiteiQ5TCQ9.

Polymorphism and mutation databases

BioMutaiMAGI3.
DMDMi190359882.

Proteomic databases

MaxQBiQ5TCQ9.
PaxDbiQ5TCQ9.
PRIDEiQ5TCQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi260425.
GeneCardsiGC01P113933.
H-InvDBHIX0000900.
HGNCiHGNC:29647. MAGI3.
HPAiHPA007923.
MIMi615943. gene.
neXtProtiNX_Q5TCQ9.
PharmGKBiPA142671485.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00650000092997.
HOVERGENiHBG007091.
InParanoidiQ5TCQ9.
KOiK06112.
OMAiPQEPYDV.
OrthoDBiEOG7FV3PH.
PhylomeDBiQ5TCQ9.
TreeFamiTF316816.

Enzyme and pathway databases

SignaLinkiQ5TCQ9.

Miscellaneous databases

ChiTaRSiMAGI3. human.
GeneWikiiMAGI3.
GenomeRNAii260425.
NextBioi93203.
PROiQ5TCQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5TCQ9.
CleanExiHS_MAGI3.
ExpressionAtlasiQ5TCQ9. baseline and differential.
GenevestigatoriQ5TCQ9.

Family and domain databases

Gene3Di2.30.42.10. 6 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR030035. MAGI3.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR10316:SF10. PTHR10316:SF10. 1 hit.
PfamiPF00625. Guanylate_kin. 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]
ProtoNetiSearch...

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: April 29, 2015
This is version 77 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. 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

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 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.