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

Preferred order of sections

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
Membrane-associated guanylate kinase inverted 2
Short name=MAGI-2
Synaptic-scaffolding molecule
Short name=S-SCAM

Gene names

Name:	Magi2
Synonyms:	Acvrinp1, Aip1, Sscam

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1277 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 By similarity. Ref.1
Subunit structure	Interacts (via its WW domains) with DRPLA By similarity. Interacts with CTNNB1, ACVR2A, SMAD2 and SMAD3 By similarity. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 By similarity. May interact with HTR2A and IGSF9 By similarity. Interacts with HTR4 By similarity. Interacts (via guanylate kinase domain) with DLGAP1. Interacts (via PDZ domains) with GRIN2A, GRID2 and NLGN1. Interacts with CTNND2 and MAGUIN-1. Interacts (via its second PDZ domain) with PTEN (via unphosphorylated C-terminus); this interaction diminishes the degradation rate of PTEN. Interacts with RAPGEF2. Interacts with DDN. Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Cell junction › synapse › synaptosome. Cell membrane; Peripheral membrane protein. Note: Membrane-associated in synaptosomes. Ref.1
Tissue specificity	Expressed in the foot process layer of podocytes of the kidney glomeruli but not in tubules (at protein level). Expressed in the brain. Ref.1 Ref.8
Developmental stage	Expressed during the late capillary loop stage of glomerulogenesis. First detected in junctional complexes in podocytes after their migration to the base of cells. Up-regulated upon foot process differentiation. Ref.8
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 5 PDZ (DHR) domains. Contains 2 WW domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SMAD protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB glomerular filtration Inferred by curator Ref.8. Source: UniProtKB glomerular visceral epithelial cell development Inferred from expression pattern Ref.8. Source: UniProtKB mitotic cell cycle arrest Inferred from direct assay PubMed 17880912. Source: UniProtKB negative regulation of activin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell migration Inferred from direct assay PubMed 17880912. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay PubMed 17880912. Source: UniProtKB negative regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphoprotein phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of receptor internalization Inferred from sequence or structural similarity. Source: UniProtKB protein heterooligomerization Inferred from direct assay Ref.2. Source: RGD receptor clustering Inferred from direct assay Ref.2. Source: RGD
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic density Inferred from direct assay Ref.6. Source: UniProtKB protein complex Inferred from direct assay PubMed 15331416. Source: RGD slit diaphragm Inferred from direct assay Ref.8. Source: UniProtKB tight junction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	SMAD binding Inferred from sequence or structural similarity. Source: UniProtKB beta-1 adrenergic receptor binding Inferred from sequence or structural similarity. Source: UniProtKB phosphatase binding Inferred from sequence or structural similarity. Source: UniProtKB receptor signaling complex scaffold activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from sequence or structural similarity. Source: UniProtKB type II activin receptor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDN	O94850	3	EBI-696179,EBI-5240523	From a different organism.
PTEN	P60484	3	EBI-696179,EBI-696162	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88382-1) Also known as: alpha; 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: O88382-2) Also known as: beta; The sequence of this isoform differs from the canonical sequence as follows: 1-163: Missing.

Isoform 3 (identifier: O88382-3) Also known as: gamma; The sequence of this isoform differs from the canonical sequence as follows: 1-223: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1277

1277

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

PRO_0000094588

Regions

Domain

17 – 101

85

PDZ

Domain

109 – 283

175

Guanylate kinase-like

Domain

302 – 335

34

WW 1

Domain

348 – 381

34

WW 2

Domain

426 – 510

85

PDZ 1

Domain

605 – 683

79

PDZ 2

Domain

778 – 860

83

PDZ 3

Domain

920 – 1010

91

PDZ 4

Domain

1141 – 1223

83

PDZ 5

Region

302 – 381

80

Interaction with DDN By similarity

Amino acid modifications

Modified residue

362

1

Phosphotyrosine By similarity

Modified residue

366

1

Phosphotyrosine By similarity

Modified residue

827

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 223

223

Missing in isoform 3.

VSP_008439

Alternative sequence

1 – 163

163

Missing in isoform 2.

VSP_008438

Experimental info

Sequence conflict

645

1

L → F in AAD31015. Ref.2

Sequences

Sequence		Length	Mass (Da)
Isoform 1 (alpha) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: E1A435FF35549DF9 Show »	FASTA	1,277	141,072
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 VTNMEKASIE PPEEEEEERP 250 260 270 280 290 300 VVNGNGVVIT PESSEHEDKS AGASGETPSQ PYPAPVYSQP EELKDQMDDT KSTKPEENED 310 320 330 340 350 360 SDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PAEECKENEL 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 SMPADGQLDG TYPPPVHDDN VSVASSGATQ 610 620 630 640 650 660 AELMTLTIVK GAKGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT 670 680 690 700 710 720 EVVDILKDCP VGSETSLIIH RGGFFSPWKT PKPMVDRWEN QGSPQTSLSA PAVPQSLPFP 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 ATYANSNHAA 910 920 930 940 950 960 PSNNASPPEG FASHSLQTSD VIIHRKENEG FGFVIISSLN RPESGATITV PHKIGRIIDG 970 980 990 1000 1010 1020 SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNNPTSAPS 1030 1040 1050 1060 1070 1080 SEKQSPMAQQ HSPLAQQHSP LAQPSPATPN SPVAQPAPPQ PLQLQGHENS YRSEVKARQD 1090 1100 1110 1120 1130 1140 VKPDIRQPPF TDYRQPPLDY RQPPGGDYSQ PSPLDYRQHS PDTRQYPLSD YRQPQDFDYF 1150 1160 1170 1180 1190 1200 TVDMEKGAKG FGFSIRGGRE YKMDLYVLRL AEDGPAIRNG RMRVGDQIIE INGESTRDMT 1210 1220 1230 1240 1250 1260 HARAIELIKS GGRRVRLLLK RGTGQVPEYG MVPSSLSMCM KSDKHGSPYF YLLGHPKDTT 1270 NPTPGALPLP PPQACRK « Hide
Isoform 2 (beta) [UniParc]. Checksum: 7B1BA3E0049DBD30 Show »	FASTA	1,114	122,766
10 20 30 40 50 60 MELEKSGALL ESGTYEDNYY GTPKPPAEPA PLLLNVTDQI LPGATPSAEG KRKRNKSVTN 70 80 90 100 110 120 MEKASIEPPE EEEEERPVVN GNGVVITPES SEHEDKSAGA SGETPSQPYP APVYSQPEEL 130 140 150 160 170 180 KDQMDDTKST KPEENEDSDP LPDNWEMAYT EKGEVYFIDH NTKTTSWLDP RLAKKAKPAE 190 200 210 220 230 240 ECKENELPYG WEKIDDPIYG TYYVDHINRR TQFENPVLEA KRKLQQHNMP HTELGTKPLQ 250 260 270 280 290 300 APGFREKPLF TRDASQLKGT FLSTTLKKSN MGFGFTIIGG DEPDEFLQVK SVIPDGPAAQ 310 320 330 340 350 360 DGKMETGDVI VYINEVCVLG HTHADVVKLF QSVPIGQSVN LVLCRGYPLP FDPEDPANSM 370 380 390 400 410 420 VPPLAIMERP PPVMVNGRHN YETYLEYISR TSQSVPDITD RPPHSLHSMP ADGQLDGTYP 430 440 450 460 470 480 PPVHDDNVSV ASSGATQAEL MTLTIVKGAK GFGFTIADSP TGQRVKQILD IQGCPGLCEG 490 500 510 520 530 540 DLIVEINQQN VQNLSHTEVV DILKDCPVGS ETSLIIHRGG FFSPWKTPKP MVDRWENQGS 550 560 570 580 590 600 PQTSLSAPAV PQSLPFPPAL HRSSFPDSTE AFDPRKPDPY ELYEKSRAIY ESRQQVPPRT 610 620 630 640 650 660 SFRMDSSGPD YKELDVHLRR MESGFGFRIL GGDEPGQPIL IGAVIAMGSA DRDGRLHPGD 670 680 690 700 710 720 ELVYVDGIPV AGKTHRYVID LMHHAARNGQ VNLTVRRKVL CGGEPCPENG RSPGSVSTHH 730 740 750 760 770 780 SSPRSDYATY ANSNHAAPSN NASPPEGFAS HSLQTSDVII HRKENEGFGF VIISSLNRPE 790 800 810 820 830 840 SGATITVPHK IGRIIDGSPA DRCAKLKVGD RILAVNGQSI INMPHADIVK LIKDAGLSVT 850 860 870 880 890 900 LRIIPQEELN NPTSAPSSEK QSPMAQQHSP LAQQHSPLAQ PSPATPNSPV AQPAPPQPLQ 910 920 930 940 950 960 LQGHENSYRS EVKARQDVKP DIRQPPFTDY RQPPLDYRQP PGGDYSQPSP LDYRQHSPDT 970 980 990 1000 1010 1020 RQYPLSDYRQ PQDFDYFTVD MEKGAKGFGF SIRGGREYKM DLYVLRLAED GPAIRNGRMR 1030 1040 1050 1060 1070 1080 VGDQIIEING ESTRDMTHAR AIELIKSGGR RVRLLLKRGT GQVPEYGMVP SSLSMCMKSD 1090 1100 1110 KHGSPYFYLL GHPKDTTNPT PGALPLPPPQ ACRK « Hide
Isoform 3 (gamma) [UniParc]. Checksum: 718C43F950E5365E Show »	FASTA	1,054	116,325
10 20 30 40 50 60 MEKASIEPPE EEEEERPVVN GNGVVITPES SEHEDKSAGA SGETPSQPYP APVYSQPEEL 70 80 90 100 110 120 KDQMDDTKST KPEENEDSDP LPDNWEMAYT EKGEVYFIDH NTKTTSWLDP RLAKKAKPAE 130 140 150 160 170 180 ECKENELPYG WEKIDDPIYG TYYVDHINRR TQFENPVLEA KRKLQQHNMP HTELGTKPLQ 190 200 210 220 230 240 APGFREKPLF TRDASQLKGT FLSTTLKKSN MGFGFTIIGG DEPDEFLQVK SVIPDGPAAQ 250 260 270 280 290 300 DGKMETGDVI VYINEVCVLG HTHADVVKLF QSVPIGQSVN LVLCRGYPLP FDPEDPANSM 310 320 330 340 350 360 VPPLAIMERP PPVMVNGRHN YETYLEYISR TSQSVPDITD RPPHSLHSMP ADGQLDGTYP 370 380 390 400 410 420 PPVHDDNVSV ASSGATQAEL MTLTIVKGAK GFGFTIADSP TGQRVKQILD IQGCPGLCEG 430 440 450 460 470 480 DLIVEINQQN VQNLSHTEVV DILKDCPVGS ETSLIIHRGG FFSPWKTPKP MVDRWENQGS 490 500 510 520 530 540 PQTSLSAPAV PQSLPFPPAL HRSSFPDSTE AFDPRKPDPY ELYEKSRAIY ESRQQVPPRT 550 560 570 580 590 600 SFRMDSSGPD YKELDVHLRR MESGFGFRIL GGDEPGQPIL IGAVIAMGSA DRDGRLHPGD 610 620 630 640 650 660 ELVYVDGIPV AGKTHRYVID LMHHAARNGQ VNLTVRRKVL CGGEPCPENG RSPGSVSTHH 670 680 690 700 710 720 SSPRSDYATY ANSNHAAPSN NASPPEGFAS HSLQTSDVII HRKENEGFGF VIISSLNRPE 730 740 750 760 770 780 SGATITVPHK IGRIIDGSPA DRCAKLKVGD RILAVNGQSI INMPHADIVK LIKDAGLSVT 790 800 810 820 830 840 LRIIPQEELN NPTSAPSSEK QSPMAQQHSP LAQQHSPLAQ PSPATPNSPV AQPAPPQPLQ 850 860 870 880 890 900 LQGHENSYRS EVKARQDVKP DIRQPPFTDY RQPPLDYRQP PGGDYSQPSP LDYRQHSPDT 910 920 930 940 950 960 RQYPLSDYRQ PQDFDYFTVD MEKGAKGFGF SIRGGREYKM DLYVLRLAED GPAIRNGRMR 970 980 990 1000 1010 1020 VGDQIIEING ESTRDMTHAR AIELIKSGGR RVRLLLKRGT GQVPEYGMVP SSLSMCMKSD 1030 1040 1050 KHGSPYFYLL GHPKDTTNPT PGALPLPPPQ ACRK « Hide

References

[1]	"A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins." Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., Toyoda A., Suedhof T.C., Takai Y. J. Biol. Chem. 273:21105-21110(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH DLGAP1; NLGN1 AND GRIN2A.
[2]	"Three isoforms of synaptic scaffolding molecule and their characterization: multimerization between the isoforms and their interaction with N-methyl-D-aspartate receptors and SAP90/PSD-95-associated protein." Hirao K., Hata Y., Yao I., Deguchi M., Kawabe H., Mizoguchi A., Takai Y. J. Biol. Chem. 275:2966-2972(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 3).
[3]	"Interaction of S-SCAM with neural plakophilin-related Armadillo-repeat protein/delta-catenin." Ide N., Hata Y., Deguchi M., Hirao K., Yao I., Takai Y. Biochem. Biophys. Res. Commun. 256:456-461(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTNND2.
[4]	"nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM)." Ohtsuka T., Hata Y., Ide N., Yasuda T., Inoue E., Inoue T., Mizoguchi A., Takai Y. Biochem. Biophys. Res. Commun. 265:38-44(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAPGEF2.
[5]	"MAGUIN, a novel neuronal membrane-associated guanylate kinase-interacting protein." Yao I., Hata Y., Ide N., Hirao K., Deguchi M., Nishioka H., Mizoguchi A., Takai Y. J. Biol. Chem. 274:11889-11896(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAGUIN-1.
[6]	"PKC regulates the delta2 glutamate receptor interaction with S-SCAM/MAGI-2 protein." Yap C.C., Muto Y., Kishida H., Hashikawa T., Yano R. Biochem. Biophys. Res. Commun. 301:1122-1128(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRID2.
[7]	"Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases." Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., Antonarakis S.E., Pulido R. J. Biol. Chem. 280:28936-28943(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTEN.
[8]	"Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and alpha-actinin are components of the nephrin multiprotein complex." Lehtonen S., Ryan J.J., Kudlicka K., Iino N., Zhou H., Farquhar M.G. Proc. Natl. Acad. Sci. U.S.A. 102:9814-9819(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH ACTN4; CASK; IQGAP1; NPHS1; SPTAN1 AND SPTBN1, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Sprague-Dawley. Tissue: Renal glomerulus.
[9]	"CIN85 is localized at synapses and forms a complex with S-SCAM via dendrin." Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K., Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y. J. Biochem. 139:931-939(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDN.
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF034863 mRNA. Translation: AAC31124.1. AF130819 mRNA. Translation: AAD31015.1.
IPI	IPI00208755. IPI00382118. IPI00950201.
PIR	T14152.
RefSeq	NP_446073.1. NM_053621.1.
UniGene	Rn.205058.
3D structure databases
ProteinModelPortal	O88382.
SMR	O88382. Positions 303-340, 347-395, 412-522, 594-682, 769-865, 916-1021, 1135-1230.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88382. 6 interactions.
MINT	MINT-87246.
STRING	10116.ENSRNOP00000036634.
PTM databases
PhosphoSite	O88382.
Proteomic databases
PaxDb	O88382.
PRIDE	O88382.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	113970.
KEGG	rno:113970.
Organism-specific databases
CTD	9863.
RGD	621855. Magi2.
Phylogenomic databases
eggNOG	COG5021.
HOGENOM	HOG000113463.
HOVERGEN	HBG007091.
InParanoid	O88382.
KO	K05629.
Gene expression databases
ArrayExpress	O88382.
Genevestigator	O88382.
Family and domain databases
InterPro	IPR008144. Guanylate_kin. IPR008145. Guanylate_kin/L-typ_Ca_channel. IPR020590. Guanylate_kinase_CS. IPR001478. PDZ. IPR001202. WW_dom. [Graphical view]
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	Search...
Other
NextBio	618109.

Entry information

Entry name

MAGI2_RAT

Accession

Primary (citable) accession number: O88382
Secondary accession number(s): Q9R271

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents