Reviewed, UniProtKB/Swiss-Prot Q5TCQ9 (MAGI3_HUMAN)

Names and origin

Protein names

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 names

Name:	MAGI3
Synonyms:	KIAA1634

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1506 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Subcellular location	Cell membrane; Peripheral membrane protein. Cell junction › tight 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.
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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell junction Cell membrane Membrane Nucleus Tight junction
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1506	1506	Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3		PRO_0000341407
Regions
	Domain	18 – 106	89	PDZ 1
	Domain	114 – 288	175	Guanylate kinase-like
	Domain	293 – 326	34	WW 1
	Domain	339 – 372	34	WW 2
	Domain	435 – 517	83	PDZ 2
	Domain	603 – 679	77	PDZ 3
	Domain	751 – 833	83	PDZ 4
	Domain	876 – 963	88	PDZ 5
	Domain	1046 – 1128	83	PDZ 6
	Nucleotide binding	121 – 128	8	ATP By similarity
	Region	18 – 106	89	Interaction with ADRB1 and TGFA By similarity
	Region	435 – 517	83	Interaction with PTEN
	Region	751 – 833	83	Interaction with BAI1
	Region	876 – 963	88	Interaction with LPAR2 and GRIN2B
	Compositional bias	6 – 9	4	Poly-Lys
	Compositional bias	238 – 243	6	Poly-Glu
	Compositional bias	378 – 381	4	Poly-Pro
Amino acid modifications
	Modified residue	722	1	Phosphoserine By similarity
	Modified residue	724	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	360 – 384	25	Missing in isoform 3 and isoform 4.		VSP_034285
	Alternative sequence	1136 – 1150	15	DWDIN…NVIYD → LAPSGLCSYVKPEQH in isoform 2 and isoform 3.		VSP_034286
	Alternative sequence	1151 – 1506	356	Missing in isoform 2 and isoform 3.		VSP_034287
Experimental info
	Sequence conflict	9	1	K → R in AAG43837. Ref.2
	Sequence conflict	59	1	V → I in AAG24545. Ref.1
	Sequence conflict	66 – 68	3	SPG → NPS in AAG24545. Ref.1
	Sequence conflict	246	1	E → G in AAG24545. Ref.1
	Sequence conflict	257	1	R → G in AAG43837. Ref.2
	Sequence conflict	491	1	L → F in AAG24545. Ref.1
	Sequence conflict	573	1	L → S in AAG24545. Ref.1
	Sequence conflict	641	1	G → E in AAG24545. Ref.1
	Sequence conflict	685	1	P → T in AAG24545. Ref.1
	Sequence conflict	801	1	I → V in AAG43837. Ref.2
	Sequence conflict	823	1	R → P in AAG43837. Ref.2
	Sequence conflict	942	1	D → A in AAG24545. Ref.1
	Sequence conflict	1018	1	S → P in AAG43837. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 10, 2008. Version 2. Checksum: 0EA98F09F9AB109F	FASTA	1,506	165,608
	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
	Isoform 2. Checksum: 14DED25795278E3C	FASTA	1,150	125,998
	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 IPDHGLAPSG 1150 LCSYVKPEQH
	Isoform 3. Checksum: FA2340EA152503E9	FASTA	1,125	123,339
	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 PQYGTYYVDH 370 380 390 400 410 420 LNQKTQFENP VEEAKRKKQL GQVEIGSSKP DMEKSHFTRD PSQLKGVLVR ASLKKSTMGF 430 440 450 460 470 480 GFTIIGGDRP DEFLQVKNVL KDGPAAQDGK IAPGDVIVDI NGNCVLGHTH ADVVQMFQLV 490 500 510 520 530 540 PVNQYVNLTL CRGYPLPDDS EDPVVDIVAA TPVINGQSLT KGETCMNPQD FKPGAMVLEQ 550 560 570 580 590 600 NGKSGHTLTG DGLNGPSDAS EQRVSMASSG SSQPELVTIP LIKGPKGFGF AIADSPTGQK 610 620 630 640 650 660 VKMILDSQWC QGLQKGDIIK EIYHQNVQNL THLQVVEVLK QFPVGADVPL LILRGGPPSP 670 680 690 700 710 720 TKTAKMKTDK KENAGSLEAI NEPIPQPMPF PPSIIRSGSP KLDPSEVYLK SKTLYEDKPP 730 740 750 760 770 780 NTKDLDVFLR KQESGFGFRV LGGDGPDQSI YIGAIIPLGA AEKDGRLRAA DELMCIDGIP 790 800 810 820 830 840 VKGKSHKQVL DLMTTAARNG HVLLTVRRKI FYGEKQPEDD SSQAFISTQN GSPRLNRAEV 850 860 870 880 890 900 PARPAPQEPY DVVLQRKENE GFGFVILTSK NKPPPGVIPH KIGRVIEGSP ADRCGKLKVG 910 920 930 940 950 960 DHISAVNGQS IVELSHDNIV QLIKDAGVTV TLTVIAEEEH HGPPSGTNSA RQSPALQHRP 970 980 990 1000 1010 1020 MGQSQANHIP GDRSALEGEI GKDVSTSYRH SWSDHKHLAQ PDTAVISVVG SRHNQNLGCY 1030 1040 1050 1060 1070 1080 PVELERGPRG FGFSLRGGKE YNMGLFILRL AEDGPAIKDG RIHVGDQIVE INGEPTQGIT 1090 1100 1110 1120 HTRAIELIQA GGNKVLLLLR PGTGLIPDHG LAPSGLCSYV KPEQH
	Isoform 4. Checksum: 9C2B604D9B1B1B97	FASTA	1,481	162,949
	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 PQYGTYYVDH 370 380 390 400 410 420 LNQKTQFENP VEEAKRKKQL GQVEIGSSKP DMEKSHFTRD PSQLKGVLVR ASLKKSTMGF 430 440 450 460 470 480 GFTIIGGDRP DEFLQVKNVL KDGPAAQDGK IAPGDVIVDI NGNCVLGHTH ADVVQMFQLV 490 500 510 520 530 540 PVNQYVNLTL CRGYPLPDDS EDPVVDIVAA TPVINGQSLT KGETCMNPQD FKPGAMVLEQ 550 560 570 580 590 600 NGKSGHTLTG DGLNGPSDAS EQRVSMASSG SSQPELVTIP LIKGPKGFGF AIADSPTGQK 610 620 630 640 650 660 VKMILDSQWC QGLQKGDIIK EIYHQNVQNL THLQVVEVLK QFPVGADVPL LILRGGPPSP 670 680 690 700 710 720 TKTAKMKTDK KENAGSLEAI NEPIPQPMPF PPSIIRSGSP KLDPSEVYLK SKTLYEDKPP 730 740 750 760 770 780 NTKDLDVFLR KQESGFGFRV LGGDGPDQSI YIGAIIPLGA AEKDGRLRAA DELMCIDGIP 790 800 810 820 830 840 VKGKSHKQVL DLMTTAARNG HVLLTVRRKI FYGEKQPEDD SSQAFISTQN GSPRLNRAEV 850 860 870 880 890 900 PARPAPQEPY DVVLQRKENE GFGFVILTSK NKPPPGVIPH KIGRVIEGSP ADRCGKLKVG 910 920 930 940 950 960 DHISAVNGQS IVELSHDNIV QLIKDAGVTV TLTVIAEEEH HGPPSGTNSA RQSPALQHRP 970 980 990 1000 1010 1020 MGQSQANHIP GDRSALEGEI GKDVSTSYRH SWSDHKHLAQ PDTAVISVVG SRHNQNLGCY 1030 1040 1050 1060 1070 1080 PVELERGPRG FGFSLRGGKE YNMGLFILRL AEDGPAIKDG RIHVGDQIVE INGEPTQGIT 1090 1100 1110 1120 1130 1140 HTRAIELIQA GGNKVLLLLR PGTGLIPDHG DWDINNPSSS NVIYDEQSPL PPSSHFASIF 1150 1160 1170 1180 1190 1200 EESHVPVIEE SLRVQICEKA EELKDIVPEK KSTLNENQPE IKHQSLLQKN VSKRDPPSSH 1210 1220 1230 1240 1250 1260 GHSNKKNLLK VENGVTRRGR SVSPKKPASQ HSEEHLDKIP SPLKNNPKRR PRDQSLSPSK 1270 1280 1290 1300 1310 1320 GENKSCQVST RAGSGQDQCR KSRGRSASPK KQQKIEGSKA PSNAEAKLLE GKSRRIAGYT 1330 1340 1350 1360 1370 1380 GSNAEQIPDG KEKSDVIRKD AKQNQLEKSR TRSPEKKIKR MVEKSLPSKM TNKTTSKEVS 1390 1400 1410 1420 1430 1440 ENEKGKKVTT GETSSSNDKI GENVQLSEKR LKQEPEEKVV SNKTEDHKGK ELEAADKNKE 1450 1460 1470 1480 TGRFKPESSS PVKKTLITPG PWKVPSGNKV TGTIGMAEKR Q

References

	« Hide 'large scale' referencesShow '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: 10748157] [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: 15652357] [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: 16710414] [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. , 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: 15489334] [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: 10997877] [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: 14702039] [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: 11969287] [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: 12140759] [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: 15507623] [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: 15378012] [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: 15003862] [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: 17055267] [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: 16904289] [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: 17934525] [Abstract] Cited for: INTERACTION WITH HPV E6, PROBABLE UBIQUITINATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00170865. IPI00387038. IPI00514954. IPI00895871.
RefSeq	NP_001136254.1. NP_690864.2.
UniGene	Hs.486189
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSG00000081026. Homo sapiens. [Contig view]
GeneID	260425.
KEGG	hsa:260425.
UCSC	uc001edh.2. human. uc001edi.2. human.
Organism-specific databases
GeneCards	GC01P113646.
HGNC	HGNC:29647. MAGI3.
HPA	HPA007923.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
OMA	Q5TCQ9. EQNGKSG.
Gene expression databases
Bgee	Q5TCQ9.
CleanEx	HS_MAGI3.
Family and domain databases
InterPro	IPR008144. Guanylate_kin. IPR008145. Guanylt/Ca. IPR001478. PDZ/DHR/GLGF. IPR001202. WW_Rsp5_WWP. [Graphical view]
Pfam	PF00625. Guanylate_kin. 1 hit. PF00595. PDZ. 4 hits. PF00397. WW. 2 hits. [Graphical view]
SMART	SM00072. GuKc. 1 hit. SM00228. PDZ. 6 hits. SM00456. WW. 2 hits. [Graphical view]
PROSITE	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]
ProtoNet	Search...
Other Resources
NextBio	93203.

Entry information

Entry name

MAGI3_HUMAN

Accession

Primary (citable) accession number: Q5TCQ9
Secondary accession number(s): Q5TCQ8 , Q5TCR0, Q9H2V6, Q9H5Y8, Q9HBC4, Q9HCD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	July 7, 2009
This is version 17 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)