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Protein

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

Gene

Magi3

Organism
Mus musculus (Mouse)
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 VANGL2.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi123 – 1308ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • frizzled binding Source: MGI

GO - Biological processi

  • positive regulation of JUN kinase activity Source: MGI
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1923484. Magi3.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Cell junctiontight junction 1 Publication
  • 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).By similarity

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB-SubCell
  • cell-cell junction Source: MGI
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14761476Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3PRO_0000341408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei236 – 2361PhosphoserineCombined sources
Modified residuei598 – 5981PhosphoserineBy similarity
Modified residuei702 – 7021PhosphoserineBy similarity
Modified residuei833 – 8331PhosphoserineBy similarity
Modified residuei916 – 9161PhosphoserineCombined sources
Modified residuei1321 – 13211PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EQJ9.
PaxDbiQ9EQJ9.
PeptideAtlasiQ9EQJ9.
PRIDEiQ9EQJ9.

PTM databases

iPTMnetiQ9EQJ9.

Expressioni

Tissue specificityi

Widely expressed. Colocalizes with TGFA in neurons in the cortex and dentate gyrus, as well as in ependymal cells and some astrocytes (at protein level). Present in lens epithelium.2 Publications

Gene expression databases

BgeeiQ9EQJ9.
ExpressionAtlasiQ9EQJ9. baseline and differential.
GenevisibleiQ9EQJ9. MM.

Interactioni

Subunit structurei

Interacts with ADRB1, BAI1, LPAR2/EDG4, GRIN2B, PTEN, and PTPRB. Interacts with unidentified tyrosine phosphorylated proteins (By similarity). Interacts with FZD4, FZD7, TGFA and VANGL2. Interacts with DLL1 (PubMed:15509766).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TGFAP011354EBI-7455245,EBI-1034374From a different organism.

GO - Molecular functioni

  • frizzled binding Source: MGI

Protein-protein interaction databases

IntActiQ9EQJ9. 4 interactions.
MINTiMINT-1894696.
STRINGi10090.ENSMUSP00000112934.

Structurei

3D structure databases

ProteinModelPortaliQ9EQJ9.
SMRiQ9EQJ9. Positions 295-329, 343-383, 400-506, 579-660, 726-816, 1021-1103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 10891PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini116 – 290175Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST
Domaini296 – 32934WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 37534WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini413 – 49583PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini581 – 65777PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini729 – 81183PDZ 4PROSITE-ProRule annotationAdd
BLAST
Domaini852 – 93988PDZ 5PROSITE-ProRule annotationAdd
BLAST
Domaini1022 – 110483PDZ 6PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 10891Interaction with ADRB1 and TGFAAdd
BLAST
Regioni413 – 49583Interaction with PTENBy similarityAdd
BLAST
Regioni729 – 81183Interaction with BAI1By similarityAdd
BLAST
Regioni852 – 93988Interaction with LPAR2 and GRIN2BBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 94Poly-Lys
Compositional biasi240 – 2456Poly-Glu

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

eggNOGiKOG0707. Eukaryota.
KOG3209. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00650000092997.
HOGENOMiHOG000113463.
HOVERGENiHBG007091.
InParanoidiQ9EQJ9.
KOiK06112.
OrthoDBiEOG7FV3PH.
PhylomeDBiQ9EQJ9.

Family and domain databases

Gene3Di2.30.42.10. 6 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
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. 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. AlignAdd to basket

Isoform 1 (identifier: Q9EQJ9-1) [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 SWAGPPGDLG AEIRGGAERG EFPYLGRLRD
60 70 80 90 100
EAGGGGGTCC VVSGKAPSPG DVLLEVNGTP VSGLTNRDTL AVIRHFREPI
110 120 130 140 150
RLKTVKPGKV INKDLRHYLS LQFQKGSIDH KLQQVIRDNL YLRTIPCTTR
160 170 180 190 200
APRDGEVPGV DYNFISVEQF KALEESGALL ESGTYDGNFY GTPKPPAEPS
210 220 230 240 250
PFQPDPVDQV LFDNEFDTES QRKRTTSVSK MERMDSSLPE EEEDEDKEAV
260 270 280 290 300
NGSGSMETRE MHSETSDCWM KTVPSYNQTN SSMDFRNYMM RDENLEPLPK
310 320 330 340 350
NWEMAYTDTG MIYFIDHNTK TTTWLDPRLC KKAKAPEDCE DGELPYGWEK
360 370 380 390 400
IEDPQYGTYY VDHLNQKTQF ENPVEEAKRK KQLGQAEIHS AKTDVERAHF
410 420 430 440 450
TRDPSQLKGV LVRASLKKST MGFGFTIIGG DRPDEFLQVK NVLKDGPAAQ
460 470 480 490 500
DGKIAPGDVI VDINGNCVLG HTHADVVQMF QLVPVNQYVN LTLCRGYPLP
510 520 530 540 550
DDSEDPVVDI VAATPVINGQ SLTKGETCMN TQDFKLGAMV LDQNGKSGQI
560 570 580 590 600
LASDRLNGPS ESSEQRASLA SSGSSQPELV TIPLIKGPKG FGFAIADSPT
610 620 630 640 650
GQKVKMILDS QWCQGLQKGD IIKEIYHQNV QNLTHLQVVE VLKQFPVGAD
660 670 680 690 700
VPLLILRGGP CSPTKTAKTK TDTKENSGSL ETINEPIPQP MPFPPSIIRS
710 720 730 740 750
GSPKLDPSEV YLKSKTLYED KPPNTKDLDV FLRKQESGFG FRVLGGDGPD
760 770 780 790 800
QSIYIGAIIP LGAAEKDGRL RAADELMCID GIPVKGKSHK QVLDLMTTAA
810 820 830 840 850
RNGHVLLTVR RKIFYGEKQP EDESHQAFSQ NGSPRLNRAE LPTRSAPQEA
860 870 880 890 900
YDVTLQRKEN EGFGFVILTS KSKPPPGVIP HKIGRVIDGS PADRCGGLKV
910 920 930 940 950
GDHISAVNGQ SIVDLSHDNI VQLIKDAGVT VTLTVVAEEE HHGPPSGTNS
960 970 980 990 1000
ARQSPALQHR PMGQAQANHI PGDRIALEGE IGRDVCSSYR HSWSDHKHLA
1010 1020 1030 1040 1050
QPDTAVISVV GSRHNQSLGC YPVELERGPR GFGFSLRGGK EYNMGLFILR
1060 1070 1080 1090 1100
LAEDGPAIKD GRIHVGDQIV EINGEPTQGI THTRAIELIQ AGGNKVLLLL
1110 1120 1130 1140 1150
RPGTGLIPDH GDWDTNSPSS SNVIYDEQPP PLPSSHSAST FEESHVPATE
1160 1170 1180 1190 1200
DSLTRVQICE KAEELKDTVQ EKKSTLNGSQ PEMKYQSVHK TMSKKDPPRG
1210 1220 1230 1240 1250
SGHGEKSRLK GENGVTRRGR SASPKKSVNR HSEEHLEKIP RPLKSDPKEK
1260 1270 1280 1290 1300
SRDRSLSPRK GESKGRLTIK AGSGQDPYRK DRGRSSSPKK QQKIGGNSLS
1310 1320 1330 1340 1350
NTEGKLSEAG SRRAAGHPRD STEQLPDGRE KSGVSRKDLK QSQPGKTRTK
1360 1370 1380 1390 1400
SPEKKSSKVD ETSLPSKKTS STAGRVVSEK EKGKKPTAGE TSRETVEHTQ
1410 1420 1430 1440 1450
ISAKQLKQEA QEKTALGNAD DHKGRESEVT DRCRERAGCT PQSSSLVKKA
1460 1470
PITPGPWRVP RANKVTGTTG MADKQL
Length:1,476
Mass (Da):161,672
Last modified:June 10, 2008 - v2
Checksum:iA9F041B5EA4B6F3F
GO
Isoform 2 (identifier: Q9EQJ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1112-1126: DWDTNSPSSSNVIYD → LAPSGLCSYVKPEQH
     1127-1476: Missing.

Show »
Length:1,126
Mass (Da):123,360
Checksum:iF015C302BC5D1BA8
GO

Sequence cautioni

The sequence BAD32503.1 differs from that shown.The sequence differs from that shown because it seems to be derived from a pre-mRNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti625 – 6251I → N in BAC26773 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1112 – 112615DWDTN…NVIYD → LAPSGLCSYVKPEQH in isoform 2. 2 PublicationsVSP_034288Add
BLAST
Alternative sequencei1127 – 1476350Missing in isoform 2. 2 PublicationsVSP_034289Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF213258 mRNA. Translation: AAG43836.1.
AC162922 Genomic DNA. No translation available.
CU210868 Genomic DNA. Translation: CAQ12905.1.
CU210868 Genomic DNA. Translation: CAQ12906.1.
AK030083 mRNA. Translation: BAC26773.1.
AK173225 Transcribed RNA. Translation: BAD32503.1. Sequence problems.
CCDSiCCDS17699.1. [Q9EQJ9-2]
CCDS51031.1. [Q9EQJ9-1]
RefSeqiNP_598614.1. NM_133853.3. [Q9EQJ9-2]
UniGeneiMm.264849.

Genome annotation databases

EnsembliENSMUST00000064371; ENSMUSP00000067932; ENSMUSG00000052539. [Q9EQJ9-2]
ENSMUST00000122303; ENSMUSP00000113713; ENSMUSG00000052539. [Q9EQJ9-2]
GeneIDi99470.
KEGGimmu:99470.
UCSCiuc008qua.2. mouse. [Q9EQJ9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF213258 mRNA. Translation: AAG43836.1.
AC162922 Genomic DNA. No translation available.
CU210868 Genomic DNA. Translation: CAQ12905.1.
CU210868 Genomic DNA. Translation: CAQ12906.1.
AK030083 mRNA. Translation: BAC26773.1.
AK173225 Transcribed RNA. Translation: BAD32503.1. Sequence problems.
CCDSiCCDS17699.1. [Q9EQJ9-2]
CCDS51031.1. [Q9EQJ9-1]
RefSeqiNP_598614.1. NM_133853.3. [Q9EQJ9-2]
UniGeneiMm.264849.

3D structure databases

ProteinModelPortaliQ9EQJ9.
SMRiQ9EQJ9. Positions 295-329, 343-383, 400-506, 579-660, 726-816, 1021-1103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EQJ9. 4 interactions.
MINTiMINT-1894696.
STRINGi10090.ENSMUSP00000112934.

PTM databases

iPTMnetiQ9EQJ9.

Proteomic databases

MaxQBiQ9EQJ9.
PaxDbiQ9EQJ9.
PeptideAtlasiQ9EQJ9.
PRIDEiQ9EQJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064371; ENSMUSP00000067932; ENSMUSG00000052539. [Q9EQJ9-2]
ENSMUST00000122303; ENSMUSP00000113713; ENSMUSG00000052539. [Q9EQJ9-2]
GeneIDi99470.
KEGGimmu:99470.
UCSCiuc008qua.2. mouse. [Q9EQJ9-2]

Organism-specific databases

CTDi260425.
MGIiMGI:1923484. Magi3.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0707. Eukaryota.
KOG3209. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00650000092997.
HOGENOMiHOG000113463.
HOVERGENiHBG007091.
InParanoidiQ9EQJ9.
KOiK06112.
OrthoDBiEOG7FV3PH.
PhylomeDBiQ9EQJ9.

Miscellaneous databases

ChiTaRSiMagi3. mouse.
PROiQ9EQJ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQJ9.
ExpressionAtlasiQ9EQJ9. baseline and differential.
GenevisibleiQ9EQJ9. 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.
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. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TGFA.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 53-1355 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1476 (ISOFORM 1).
  5. "Requirement of PDZ-containing proteins for cell cycle regulation and differentiation in the mouse lens epithelium."
    Nguyen M.M., Nguyen M.L., Caruana G., Bernstein A., Lambert P.F., Griep A.E.
    Mol. Cell. Biol. 23:8970-8981(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "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.
  7. "MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap."
    Yao R., Natsume Y., Noda T.
    Oncogene 23:6023-6030(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZD4; FZD7 AND VANGL2.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiMAGI3_MOUSE
AccessioniPrimary (citable) accession number: Q9EQJ9
Secondary accession number(s): B0V3N7
, B0V3N8, Q69ZE1, Q8C0P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: July 6, 2016
This is version 105 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.