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Q5TCQ9 (MAGI3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MAGI3
Synonyms:KIAA1634
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1506 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

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. Ref.1 Ref.8

Tissue specificity

Widely expressed. Ref.1

Post-translational modification

Ubiquitinated following interaction with HPV E6 protein, leading to its degradation by the proteasome. Degradation is independent of E6AP ubiquitin ligase complex. Ref.9 Ref.15

Miscellaneous

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

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 6 PDZ (DHR) domains.

Contains 2 WW domains.

Sequence caution

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

The sequence BAB15479.1 differs from that shown. Reason: Frameshift at position 1373.

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5TCQ9-1)

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.
Isoform 2 (identifier: Q5TCQ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1136-1150: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH
     1151-1506: Missing.
Isoform 3 (identifier: Q5TCQ9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     360-384: Missing.
     1136-1150: DWDINNPSSSNVIYD → LAPSGLCSYVKPEQH
     1151-1506: Missing.
Isoform 4 (identifier: Q5TCQ9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     360-384: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15061506Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
PRO_0000341407

Regions

Domain18 – 10689PDZ 1
Domain114 – 288175Guanylate kinase-like
Domain293 – 32634WW 1
Domain339 – 37234WW 2
Domain435 – 51783PDZ 2
Domain603 – 67977PDZ 3
Domain751 – 83383PDZ 4
Domain876 – 96388PDZ 5
Domain1046 – 112883PDZ 6
Nucleotide binding121 – 1288ATP By similarity
Region18 – 10689Interaction with ADRB1 and TGFA By similarity
Region435 – 51783Interaction with PTEN
Region751 – 83383Interaction with BAI1
Region876 – 96388Interaction with LPAR2 and GRIN2B
Compositional bias6 – 94Poly-Lys
Compositional bias238 – 2436Poly-Glu
Compositional bias378 – 3814Poly-Pro

Amino acid modifications

Modified residue2341Phosphoserine By similarity

Natural variations

Alternative sequence360 – 38425Missing in isoform 3 and isoform 4.
VSP_034285
Alternative sequence1136 – 115015DWDIN…NVIYD → LAPSGLCSYVKPEQH in isoform 2 and isoform 3.
VSP_034286
Alternative sequence1151 – 1506356Missing in isoform 2 and isoform 3.
VSP_034287

Experimental info

Sequence conflict91K → R in AAG43837. Ref.2
Sequence conflict591V → I in AAG24545. Ref.1
Sequence conflict66 – 683SPG → NPS in AAG24545. Ref.1
Sequence conflict2461E → G in AAG24545. Ref.1
Sequence conflict2571R → G in AAG43837. Ref.2
Sequence conflict4911L → F in AAG24545. Ref.1
Sequence conflict5731L → S in AAG24545. Ref.1
Sequence conflict6411G → E in AAG24545. Ref.1
Sequence conflict6851P → T in AAG24545. Ref.1
Sequence conflict8011I → V in AAG43837. Ref.2
Sequence conflict8231R → P in AAG43837. Ref.2
Sequence conflict9421D → A in AAG24545. Ref.1
Sequence conflict10181S → P in AAG43837. Ref.2

Secondary structure

............... 1506
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 0EA98F09F9AB109F

FASTA1,506165,608
        10         20         30         40         50         60 
MSKTLKKKKH WLSKVQECAV SWAGPPGDFG AEIRGGAERG EFPYLGRLRE EPGGGTCCVV 

        70         80         90        100        110        120 
SGKAPSPGDV LLEVNGTPVS GLTNRDTLAV IRHFREPIRL KTVKPGKVIN KDLRHYLSLQ 

       130        140        150        160        170        180 
FQKGSIDHKL QQVIRDNLYL RTIPCTTRAP RDGEVPGVDY NFISVEQFKA LEESGALLES 

       190        200        210        220        230        240 
GTYDGNFYGT PKPPAEPSPF QPDPVDQVLF DNEFDAESQR KRTTSVSKME RMDSSLPEEE 

       250        260        270        280        290        300 
EDEDKEAING SGNAENRERH SESSDWMKTV PSYNQTNSSM DFRNYMMRDE TLEPLPKNWE 

       310        320        330        340        350        360 
MAYTDTGMIY FIDHNTKTTT WLDPRLCKKA KAPEDCEDGE LPYGWEKIED PQYGTYYVDF 

       370        380        390        400        410        420 
TLVAQAGVQW HDLGSLQPPP PGFNHLNQKT QFENPVEEAK RKKQLGQVEI GSSKPDMEKS 

       430        440        450        460        470        480 
HFTRDPSQLK GVLVRASLKK STMGFGFTII GGDRPDEFLQ VKNVLKDGPA AQDGKIAPGD 

       490        500        510        520        530        540 
VIVDINGNCV LGHTHADVVQ MFQLVPVNQY VNLTLCRGYP LPDDSEDPVV DIVAATPVIN 

       550        560        570        580        590        600 
GQSLTKGETC MNPQDFKPGA MVLEQNGKSG HTLTGDGLNG PSDASEQRVS MASSGSSQPE 

       610        620        630        640        650        660 
LVTIPLIKGP KGFGFAIADS PTGQKVKMIL DSQWCQGLQK GDIIKEIYHQ NVQNLTHLQV 

       670        680        690        700        710        720 
VEVLKQFPVG ADVPLLILRG GPPSPTKTAK MKTDKKENAG SLEAINEPIP QPMPFPPSII 

       730        740        750        760        770        780 
RSGSPKLDPS EVYLKSKTLY EDKPPNTKDL DVFLRKQESG FGFRVLGGDG PDQSIYIGAI 

       790        800        810        820        830        840 
IPLGAAEKDG RLRAADELMC IDGIPVKGKS HKQVLDLMTT AARNGHVLLT VRRKIFYGEK 

       850        860        870        880        890        900 
QPEDDSSQAF ISTQNGSPRL NRAEVPARPA PQEPYDVVLQ RKENEGFGFV ILTSKNKPPP 

       910        920        930        940        950        960 
GVIPHKIGRV IEGSPADRCG KLKVGDHISA VNGQSIVELS HDNIVQLIKD AGVTVTLTVI 

       970        980        990       1000       1010       1020 
AEEEHHGPPS GTNSARQSPA LQHRPMGQSQ ANHIPGDRSA LEGEIGKDVS TSYRHSWSDH 

      1030       1040       1050       1060       1070       1080 
KHLAQPDTAV ISVVGSRHNQ NLGCYPVELE RGPRGFGFSL RGGKEYNMGL FILRLAEDGP 

      1090       1100       1110       1120       1130       1140 
AIKDGRIHVG DQIVEINGEP TQGITHTRAI ELIQAGGNKV LLLLRPGTGL IPDHGDWDIN 

      1150       1160       1170       1180       1190       1200 
NPSSSNVIYD EQSPLPPSSH FASIFEESHV PVIEESLRVQ ICEKAEELKD IVPEKKSTLN 

      1210       1220       1230       1240       1250       1260 
ENQPEIKHQS LLQKNVSKRD PPSSHGHSNK KNLLKVENGV TRRGRSVSPK KPASQHSEEH 

      1270       1280       1290       1300       1310       1320 
LDKIPSPLKN NPKRRPRDQS LSPSKGENKS CQVSTRAGSG QDQCRKSRGR SASPKKQQKI 

      1330       1340       1350       1360       1370       1380 
EGSKAPSNAE AKLLEGKSRR IAGYTGSNAE QIPDGKEKSD VIRKDAKQNQ LEKSRTRSPE 

      1390       1400       1410       1420       1430       1440 
KKIKRMVEKS LPSKMTNKTT SKEVSENEKG KKVTTGETSS SNDKIGENVQ LSEKRLKQEP 

      1450       1460       1470       1480       1490       1500 
EEKVVSNKTE DHKGKELEAA DKNKETGRFK PESSSPVKKT LITPGPWKVP SGNKVTGTIG 


MAEKRQ 

« Hide

Isoform 2 [UniParc].

Checksum: 14DED25795278E3C
Show »

FASTA1,150125,998
Isoform 3 [UniParc].

Checksum: FA2340EA152503E9
Show »

FASTA1,125123,339
Isoform 4 [UniParc].

Checksum: 9C2B604D9B1B1B97
Show »

FASTA1,481162,949

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF257238 mRNA. Translation: AAG24545.1.
AF213259 mRNA. Translation: AAG43837.1.
AL365225 expand/collapse EMBL AC list , AL133517, AL389921, AL390759 Genomic DNA. Translation: CAH70944.1.
AL365225 expand/collapse EMBL AC list , AL133517, AL389921, AL390759 Genomic DNA. Translation: CAH70945.1.
AL365225 expand/collapse EMBL AC list , AL133517, AL389921, AL390759 Genomic DNA. Translation: CAH70946.1.
AL389921 expand/collapse EMBL AC list , AL133517, AL365225, AL390759 Genomic DNA. Translation: CAH71507.1.
AL389921 expand/collapse EMBL AC list , AL133517, AL365225, AL390759 Genomic DNA. Translation: CAH71508.1.
AL389921 expand/collapse EMBL AC list , AL133517, AL365225, AL390759 Genomic DNA. Translation: CAH71509.1.
AL390759 expand/collapse EMBL AC list , AL133517, AL365225, AL389921 Genomic DNA. Translation: CAH74141.1.
AL390759 expand/collapse EMBL AC list , AL133517, AL365225, AL389921 Genomic DNA. Translation: CAH74142.1.
AL390759 expand/collapse EMBL AC list , AL133517, AL365225, AL389921 Genomic DNA. Translation: CAH74143.1.
AL133517 expand/collapse EMBL AC list , AL365225, AL389921, AL390759 Genomic DNA. Translation: CAI22553.1.
AL133517 expand/collapse EMBL AC list , AL365225, AL389921, AL390759 Genomic DNA. Translation: CAI22554.1.
AL133517 expand/collapse EMBL AC list , 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.
CCDSCCDS44196.1. [Q5TCQ9-4]
CCDS860.1. [Q5TCQ9-3]
RefSeqNP_001136254.1. NM_001142782.1. [Q5TCQ9-4]
NP_690864.2. NM_152900.2. [Q5TCQ9-3]
XP_005270794.1. XM_005270737.1. [Q5TCQ9-3]
UniGeneHs.486189.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SOEX-ray1.60A601-691[»]
ProteinModelPortalQ5TCQ9.
SMRQ5TCQ9. Positions 57-109, 142-191, 292-326, 340-405, 422-528, 590-683, 748-975, 1045-1127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129277. 11 interactions.
IntActQ5TCQ9. 9 interactions.
MINTMINT-6800638.
STRING9606.ENSP00000304604.

Chemistry

BindingDBQ5TCQ9.
ChEMBLCHEMBL5212.

PTM databases

PhosphoSiteQ5TCQ9.

Polymorphism databases

DMDM190359882.

Proteomic databases

MaxQBQ5TCQ9.
PaxDbQ5TCQ9.
PRIDEQ5TCQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307546; ENSP00000304604; ENSG00000081026. [Q5TCQ9-4]
ENST00000369611; ENSP00000358624; ENSG00000081026. [Q5TCQ9-3]
ENST00000369615; ENSP00000358628; ENSG00000081026. [Q5TCQ9-3]
ENST00000369617; ENSP00000358630; ENSG00000081026. [Q5TCQ9-2]
GeneID260425.
KEGGhsa:260425.
UCSCuc001edh.3. human. [Q5TCQ9-2]
uc001edi.4. human. [Q5TCQ9-3]
uc001edk.3. human. [Q5TCQ9-4]

Organism-specific databases

CTD260425.
GeneCardsGC01P113933.
H-InvDBHIX0000900.
HGNCHGNC:29647. MAGI3.
HPAHPA007923.
neXtProtNX_Q5TCQ9.
PharmGKBPA142671485.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOVERGENHBG007091.
KOK06112.
OMAPQEPYDV.
OrthoDBEOG7FV3PH.
PhylomeDBQ5TCQ9.
TreeFamTF316816.

Enzyme and pathway databases

SignaLinkQ5TCQ9.

Gene expression databases

BgeeQ5TCQ9.
CleanExHS_MAGI3.
GenevestigatorQ5TCQ9.

Family and domain databases

Gene3D2.30.42.10. 6 hits.
InterProIPR008145. 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]
PfamPF00625. Guanylate_kin. 1 hit.
PF13900. GVQW. 1 hit.
PF00595. PDZ. 4 hits.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 6 hits.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 6 hits.
SSF51045. SSF51045. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. 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]
ProtoNetSearch...

Other

GeneWikiMAGI3.
GenomeRNAi260425.
NextBio93203.
PROQ5TCQ9.

Entry information

Entry nameMAGI3_HUMAN
AccessionPrimary (citable) accession number: Q5TCQ9
Secondary accession number(s): Q5TCQ8 expand/collapse secondary AC list , Q5TCR0, Q9H2V6, Q9H5Y8, Q9HBC4, Q9HCD8
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM