Q86UL8 (MAGI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2

Alternative name(s):
Atrophin-1-interacting protein 1
Short name=AIP-1
Atrophin-1-interacting protein A
Membrane-associated guanylate kinase inverted 2
Short name=MAGI-2

Gene names

Name:	MAGI2
Synonyms:	ACVRINP1, AIP1, KIAA0705

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1455 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation. Ref.6
Subunit structure	Interacts (via its WW domains) with DRPLA. Interacts (via its second PDZ domain) with PTEN (via unphosphorylated C-terminus); this interaction diminishes the degradation rate of PTEN By similarity. Interacts (via guanylate kinase domain) with DLGAP1 By similarity. Interacts (via the PDZ domains) with GRIN2A, GRID2 and NLGN1 By similarity. Interacts with CTNND2, CTNNB1, MAGUIN-1, ACVR2A, SMAD2 and SMAD3 By similarity. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 By similarity. May interact with HTR2A By similarity. Interacts with IGSF9, RAPGEF2 and HTR4 By similarity. Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 By similarity. Interacts with DDN. Ref.1 Ref.6 Ref.7 Ref.8
Subcellular location	Cell junction › synapse › synaptosome By similarity. Cell membrane; Peripheral membrane protein By similarity. Note: Membrane-associated in synaptosomes By similarity. Ref.6
Tissue specificity	Specifically expressed in brain. Ref.1
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 BAA31680.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphatase binding Inferred from physical interaction Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADRB1	P08588	2	EBI-311035,EBI-991009

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86UL8-1)

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: Q86UL8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     757-771: QQVPPRTSFRMDSSG → R

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1455

1455

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2

PRO_0000094586

Regions

Domain

17 – 101

85

PDZ 1

Domain

109 – 283

175

Guanylate kinase-like

Domain

302 – 335

34

WW 1

Domain

348 – 381

34

WW 2

Domain

426 – 510

85

PDZ 2

Domain

605 – 683

79

PDZ 3

Domain

778 – 860

83

PDZ 4

Domain

920 – 1010

91

PDZ 5

Domain

1147 – 1229

83

PDZ 6

Region

302 – 381

80

Interaction with DDN

Compositional bias

1015 – 1118

104

Pro-rich

Compositional bias

1340 – 1430

91

Ala-rich

Amino acid modifications

Modified residue

362

1

Phosphotyrosine By similarity

Modified residue

366

1

Phosphotyrosine By similarity

Modified residue

827

1

Phosphotyrosine By similarity

Modified residue

1014

1

Phosphoserine By similarity

Natural variations

Alternative sequence

757 – 771

15

QQVPP…MDSSG → R in isoform 2.

VSP_008435

Experimental info

Sequence conflict

1234

1

E → Q in AAC05370. Ref.1

Sequence conflict

1250

1

G → C in AAC05370. Ref.1

Sequence conflict

1291

1

E → K in AAC05370. Ref.1

Sequence conflict

1383

1

P → L in AAC05370. Ref.1

Sequence conflict

1389 – 1394

6

FAGPGG → SADPAD in AAC05370. Ref.1

Sequence conflict

1401

1

E → A in AAC05370. Ref.1

Sequence conflict

1411

1

G → A in AAC05370. Ref.1

Sequence conflict

1414 – 1415

2

PG → SV in AAC05370. Ref.1

Sequence conflict

1420

1

G → A in AAC05370. Ref.1

Sequence conflict

1423

1

P → A in AAC05370. Ref.1

Sequence conflict

1426

1

K → R in AAC05370. Ref.1

Sequence conflict

1429

1

V → G in AAC05370. Ref.1

Sequence conflict

1437

1

P → R in AAC05370. Ref.1

Secondary structure

1

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1455

Helix Strand Turn

Details...

Beta strand

415 – 417

3

Beta strand

422 – 430

9

Beta strand

437 – 441

5

Beta strand

444 – 447

4

Beta strand

451 – 455

5

Helix

460 – 463

4

Beta strand

472 – 476

5

Helix

486 – 494

9

Beta strand

501 – 509

9

Beta strand

604 – 609

6

Beta strand

612 – 622

11

Beta strand

625 – 632

8

Helix

634 – 636

3

Beta strand

645 – 649

5

Helix

659 – 668

10

Beta strand

673 – 680

8

Beta strand

774 – 777

4

Beta strand

780 – 787

8

Beta strand

790 – 792

3

Beta strand

803 – 807

5

Helix

814 – 816

3

Beta strand

824 – 828

5

Helix

838 – 851

14

Beta strand

853 – 861

9

Beta strand

919 – 924

6

Beta strand

933 – 936

4

Beta strand

953 – 957

5

Helix

964 – 966

3

Beta strand

974 – 978

5

Turn

983 – 985

3

Helix

988 – 997

10

Turn

998 – 1000

3

Beta strand

1001 – 1006

6

Beta strand

1156 – 1159

4

Beta strand

1162 – 1164

3

Turn

1165 – 1168

4

Beta strand

1169 – 1172

4

Helix

1181 – 1185

5

Beta strand

1193 – 1197

5

Helix

1207 – 1217

11

Beta strand

1219 – 1221

3

Beta strand

1223 – 1226

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 7, 2006. Version 3. Checksum: 93E170D070A70A9C	FASTA	1,455	158,754
	10 20 30 40 50 60 MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL 70 80 90 100 110 120 VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS 130 140 150 160 170 180 VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED 190 200 210 220 230 240 NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP 250 260 270 280 290 300 VVNGNGVVVT PESSEHEDKS AGASGEMPSQ PYPAPVYSQP EELKEQMDDT KPTKPEDNEE 310 320 330 340 350 360 PDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PPEECKENEL PYGWEKIDDP 370 380 390 400 410 420 IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL 430 440 450 460 470 480 KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC 490 500 510 520 530 540 VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG 550 560 570 580 590 600 RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPTDGQLDG TYPPPVHDDN VSMASSGATQ 610 620 630 640 650 660 AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT 670 680 690 700 710 720 EVVDILKDCP IGSETSLIIH RGGFFSPWKT PKPIMDRWEN QGSPQTSLSA PAIPQNLPFP 730 740 750 760 770 780 PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRQQVP PRTSFRMDSS GPDYKELDVH 790 800 810 820 830 840 LRRMESGFGF RILGGDEPGQ PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY 850 860 870 880 890 900 VIDLMHHAAR NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYTNSNHAA 910 920 930 940 950 960 PSSNASPPEG FASHSLQTSD VVIHRKENEG FGFVIISSLN RPESGSTITV PHKIGRIIDG 970 980 990 1000 1010 1020 SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNSPTSAPS 1030 1040 1050 1060 1070 1080 SEKQSPMAQQ SPLAQQSPLA QPSPATPNSP IAQPAPPQPL QLQGHENSYR SEVKARQDVK 1090 1100 1110 1120 1130 1140 PDIRQPPFTD YRQPPLDYRQ PPGGDYQQPP PLDYRQPPLL DYRQHSPDTR QYPLSDYRQP 1150 1160 1170 1180 1190 1200 QDFDYFTVDM EKGAKGFGFS IRGGREYKMD LYVLRLAEDG PAIRNGRMRV GDQIIEINGE 1210 1220 1230 1240 1250 1260 STRDMTHARA IELIKSGGRR VRLLLKRGTG QVPEYDEPAP WSSPAAAAPG LPEVGVSLDD 1270 1280 1290 1300 1310 1320 GLAPFSPSHP APPSDPSHQI SPGPTWDIKR EHDVRKPKEL SACGQKKQRL GEQRERSASP 1330 1340 1350 1360 1370 1380 QRAARPRLEE APGGQGRPEA GRPASEARAP GLAAADAADA ARAGGKEAPR AAAGSELCRR 1390 1400 1410 1420 1430 1440 EGPGAAPAFA GPGGGGSGAL EAEGRAGARA GPRPGPRPPG GAPARKAAVA PGPWKVPGSD 1450 KLPSVLKPGA SAASR
	Isoform 2 [UniParc]. Checksum: 505C382255497AFE	FASTA	1,441	157,236
	10 20 30 40 50 60 MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL 70 80 90 100 110 120 VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS 130 140 150 160 170 180 VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED 190 200 210 220 230 240 NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP 250 260 270 280 290 300 VVNGNGVVVT PESSEHEDKS AGASGEMPSQ PYPAPVYSQP EELKEQMDDT KPTKPEDNEE 310 320 330 340 350 360 PDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PPEECKENEL PYGWEKIDDP 370 380 390 400 410 420 IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL 430 440 450 460 470 480 KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC 490 500 510 520 530 540 VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG 550 560 570 580 590 600 RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPTDGQLDG TYPPPVHDDN VSMASSGATQ 610 620 630 640 650 660 AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT 670 680 690 700 710 720 EVVDILKDCP IGSETSLIIH RGGFFSPWKT PKPIMDRWEN QGSPQTSLSA PAIPQNLPFP 730 740 750 760 770 780 PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRRPDY KELDVHLRRM ESGFGFRILG 790 800 810 820 830 840 GDEPGQPILI GAVIAMGSAD RDGRLHPGDE LVYVDGIPVA GKTHRYVIDL MHHAARNGQV 850 860 870 880 890 900 NLTVRRKVLC GGEPCPENGR SPGSVSTHHS SPRSDYATYT NSNHAAPSSN ASPPEGFASH 910 920 930 940 950 960 SLQTSDVVIH RKENEGFGFV IISSLNRPES GSTITVPHKI GRIIDGSPAD RCAKLKVGDR 970 980 990 1000 1010 1020 ILAVNGQSII NMPHADIVKL IKDAGLSVTL RIIPQEELNS PTSAPSSEKQ SPMAQQSPLA 1030 1040 1050 1060 1070 1080 QQSPLAQPSP ATPNSPIAQP APPQPLQLQG HENSYRSEVK ARQDVKPDIR QPPFTDYRQP 1090 1100 1110 1120 1130 1140 PLDYRQPPGG DYQQPPPLDY RQPPLLDYRQ HSPDTRQYPL SDYRQPQDFD YFTVDMEKGA 1150 1160 1170 1180 1190 1200 KGFGFSIRGG REYKMDLYVL RLAEDGPAIR NGRMRVGDQI IEINGESTRD MTHARAIELI 1210 1220 1230 1240 1250 1260 KSGGRRVRLL LKRGTGQVPE YDEPAPWSSP AAAAPGLPEV GVSLDDGLAP FSPSHPAPPS 1270 1280 1290 1300 1310 1320 DPSHQISPGP TWDIKREHDV RKPKELSACG QKKQRLGEQR ERSASPQRAA RPRLEEAPGG 1330 1340 1350 1360 1370 1380 QGRPEAGRPA SEARAPGLAA ADAADAARAG GKEAPRAAAG SELCRREGPG AAPAFAGPGG 1390 1400 1410 1420 1430 1440 GGSGALEAEG RAGARAGPRP GPRPPGGAPA RKAAVAPGPW KVPGSDKLPS VLKPGASAAS R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins." Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A. Mol. Cell. Neurosci. 11:149-160(1998) [PubMed: 9647693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH DRPLA. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] 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]	"Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2." Wu X., Hepner K., Castelino-Prabhu S., Do D., Kaye M.B., Yuan X.-J., Wood J., Ross C., Sawyers C.L., Whang Y.E. Proc. Natl. Acad. Sci. U.S.A. 97:4233-4238(2000) [PubMed: 10760291] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTEN.
[7]	"Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex." Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N., Sellers W.R. J. Biol. Chem. 276:48627-48630(2001) [PubMed: 11707428] [Abstract] Cited for: INTERACTION WITH PTEN.
[8]	"Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring." Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A. J. Neurochem. 96:1659-1666(2006) [PubMed: 16464232] [Abstract] Cited for: INTERACTION WITH DDN.
[9]	"Solution structure of the PDZ domains of human atrophin-1 interacting protein 1 (KIAA0705 protein)." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 412-1230.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF038563 mRNA. Translation: AAC05370.1.
AB014605 mRNA. Translation: BAA31680.2. Different initiation.
AC004808 Genomic DNA. Translation: AAC23438.1.
AC004945 Genomic DNA. Translation: AAC61488.1.
AC004990 Genomic DNA. Translation: AAC79151.1.
AC005246 Genomic DNA. Translation: AAC25530.1.
AC006043 Genomic DNA. Translation: AAD15413.2.
AC006324 Genomic DNA. Translation: AAF66080.1.
AC007237 Genomic DNA. Translation: AAP21886.1.
AC073200 Genomic DNA. Translation: AAP22360.1.
CH236949 Genomic DNA. Translation: EAL24194.1.
BC150277 mRNA. Translation: AAI50278.1.

IPI

IPI00376306.
IPI00413880.

RefSeq

NP_036433.2. NM_012301.3.

UniGene

Hs.603842.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UEP	NMR	-	A	774-863	[»]
1UEQ	NMR	-	A	412-522	[»]
1UEW	NMR	-	A	915-1015	[»]
1UJV	NMR	-	A	600-682	[»]
1WFV	NMR	-	A	1141-1230	[»]

ProteinModelPortal

Q86UL8.

SMR

Q86UL8. Positions 14-100, 134-188, 298-380, 412-522, 594-682, 769-1021, 1141-1233.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q86UL8. 4 interactions.

MINT

MINT-109875.

STRING

Q86UL8.

PTM databases

PhosphoSite

Q86UL8.

Polymorphism databases

DMDM

88909269.

Proteomic databases

PRIDE

Q86UL8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354212; ENSP00000346151; ENSG00000187391.

GeneID

9863.

KEGG

hsa:9863.

UCSC

uc003ugx.1. human.
uc003ugy.1. human.

Organism-specific databases

CTD

9863.

GeneCards

GC07M077646.

H-InvDB

HIX0006801.

HGNC

HGNC:18957. MAGI2.

HPA

HPA013650.

MIM

606382. gene.

neXtProt

NX_Q86UL8.

PharmGKB

PA142671484.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16760.

GeneTree

ENSGT00530000063259.

HOVERGEN

HBG007091.

InParanoid

Q86UL8.

OMA

SDPSHQI.

PhylomeDB

Q86UL8.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

Q86UL8.

Bgee

Q86UL8.

Genevestigator

Q86UL8.

GermOnline

ENSG00000187391. Homo sapiens.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR001478. PDZ/DHR/GLGF.
IPR001202. WW_Rsp5_WWP.
[Graphical view]

Gene3D

G3DSA:2.20.70.10. G3DSA:2.20.70.10. 2 hits.

KO

K05629.

Pfam

PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 6 hits.
PF00397. WW. 2 hits.
[Graphical view]

SMART

SM00072. GuKc. 1 hit.
SM00228. PDZ. 6 hits.
SM00456. WW. 2 hits.
[Graphical view]

SUPFAM

SSF50156. PDZ. 6 hits.
SSF51045. WW_Rsp5_WWP. 1 hit.

PROSITE

PS00856. 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]

ProtoNet

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Other

NextBio

37182.

SOURCE

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Entry information

Entry name

MAGI2_HUMAN

Accession

Primary (citable) accession number: Q86UL8
Secondary accession number(s): A4D1C1 , A7E2C3, O60434, O60510, Q86UI7, Q9NP44, Q9UDQ5, Q9UDU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	February 7, 2006
Last modified:	January 25, 2012
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.