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Q6RHR9 (MAGI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·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 1
Alternative name(s):
BAI1-associated protein 1
Short name=BAP-1
Membrane-associated guanylate kinase inverted 1
Short name=MAGI-1
Gene names
Name:Magi1
Synonyms:Baiap1, Bap1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ACCN3 currents by modulating its expression at the cell surface. Ref.6

Subunit structure

Interacts through its WW 2 domain with SYNPO and through its PDZ 5 domain with ACTN4. Interacts with cytoplasmic domain of BAI1. Interacts with AMOT and via its WW domains with DRPLA By similarity. Interacts with ESAM, LRP2 and CXADR. Isoform 2 interacts with CTNNB1. Interacts through its PDZ 1 domain with NET1. Interacts with ACCN3. Interacts with FCHSD2 By similarity. Interacts with IGSF5/JAM4 and through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex By similarity. Interacts with DDN By similarity. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Isoform 2: Cytoplasm Probable. Cell membrane; Peripheral membrane protein Probable. Cell junction › tight junction By similarity. Note: Localizes to epithelial cells tight junctions By similarity. Ref.2 Ref.3

Isoform 3: Cytoplasm Probable. Cell membrane; Peripheral membrane protein Probable Ref.2 Ref.3.

Isoform 1: Nucleus Probable Ref.2 Ref.3.

Tissue specificity

Widely expressed, including kidney glomeruli. Ref.2 Ref.5

Sequence similarities

Contains 1 guanylate kinase-like domain.

Contains 6 PDZ (DHR) domains.

Contains 2 WW domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
Nucleus
Tight junction
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

tight junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: MGI

Complete GO annotation...

Alternative products

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

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q6RHR9-1)

Also known as: MAGI1c alpha beta2 gamma; MAGI-1c;

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: Q6RHR9-2)

Also known as: MAGI-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     348-359: Missing.
     798-826: PMSPSPASGLSKGERDREINSTNFGECQI → L
     1019-1074: Missing.
     1221-1268: DPSSDRNGPS...ELHKSSQHAE → AMIPPKIAAC...PPPVHKVFRK
     1269-1471: Missing.
Isoform 3 (identifier: Q6RHR9-3)

Also known as: MAGI-1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1221-1236: DPSSDRNGPSTGAQGV → GGSNYENIPSFPGMTP
     1238-1268: Missing.
     1269-1471: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14711471Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
PRO_0000094590

Regions

Domain17 – 10589PDZ 1
Domain96 – 287192Guanylate kinase-like
Domain300 – 33334WW 1
Domain359 – 39234WW 2
Domain464 – 54683PDZ 2
Domain635 – 71379PDZ 3
Domain833 – 91583PDZ 4
Domain990 – 107485PDZ 5
Domain1132 – 121483PDZ 6
Nucleotide binding103 – 1108ATP By similarity
Region990 – 107485Interaction with FCHSD2 By similarity
Compositional bias237 – 2426Poly-Glu
Compositional bias402 – 4109Poly-Gln
Compositional bias970 – 98011Poly-Gly
Compositional bias1378 – 13814Poly-Arg

Amino acid modifications

Modified residue3761Phosphotyrosine By similarity
Modified residue8581Phosphotyrosine Ref.8
Modified residue14701Phosphoserine By similarity

Natural variations

Alternative sequence348 – 35912Missing in isoform 2.
VSP_011673
Alternative sequence798 – 82629PMSPS…GECQI → L in isoform 2.
VSP_011674
Alternative sequence1019 – 107456Missing in isoform 2.
VSP_011675
Alternative sequence1221 – 126848DPSSD…SQHAE → AMIPPKIAACMRNEKLGEAC FYLMGHNQTTTPAATGTAPP PVHKVFRK in isoform 2.
VSP_011676
Alternative sequence1221 – 123616DPSSD…GAQGV → GGSNYENIPSFPGMTP in isoform 3.
VSP_011678
Alternative sequence1238 – 126831Missing in isoform 3.
VSP_011679
Alternative sequence1269 – 1471203Missing in isoform 2 and isoform 3.
VSP_011677

Experimental info

Sequence conflict7261Missing in AAB91995. Ref.2
Sequence conflict13421A → D in AAB91997. Ref.2

Secondary structure

1 ............... 1471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MAGI1c alpha beta2 gamma) (MAGI-1c) [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6C780C71CAC37CB1

FASTA1,471161,974
        10         20         30         40         50         60 
MSKVIQKKNH WTGRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAA EAAGLPGGGE 

        70         80         90        100        110        120 
GPKLAEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF 

       130        140        150        160        170        180 
QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYS FLTVKEFLDL EQSGTLLEVG 

       190        200        210        220        230        240 
TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHPENEE 

       250        260        270        280        290        300 
EEDVPEMNSS FTADSGDQDE HTLQEATLPP VNSSILAAPI TDPSQKFPQY LPLSAEDNLG 

       310        320        330        340        350        360 
PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE 

       370        380        390        400        410        420 
LPAGWEKIED PVYGVYYVDH INRKTQYENP VLEAKRKKQL EQQQQQQQPQ PPQPEEWTED 

       430        440        450        460        470        480 
HASVVPPVAP SHPPSNPEPA RETPLQGKPF FTRNPSELKG KFIHTKLRKS SRGFGFTVVG 

       490        500        510        520        530        540 
GDEPDEFLQI KSLVLDGPAA LDGKMETGDV IVSVNDTCVL GHTHAQVVKI FQSIPIGASV 

       550        560        570        580        590        600 
DLELCRGYPL PFDPDDPNTS LVTSVAILDK EPIIVNGQET YDSPASHSSK TGKVSSMKDA 

       610        620        630        640        650        660 
RPSSPADVAS NSSHGYPNDT VSLASSIATQ PELITVHIVK GPMGFGFTIA DSPGGGGQRV 

       670        680        690        700        710        720 
KQIVDSPRCR GLKEGDLIVE VNKKNVQALT HNQVVDMLIE CPKGSEVTLL VQRGGLPVPK 

       730        740        750        760        770        780 
KSPKSQPLER KDSQNSSQHS VSSHRSLHTA SPSHGIQVLP EYLPADAPAP DQTDSSGQKK 

       790        800        810        820        830        840 
PDPFKIWAQS RSMYENRPMS PSPASGLSKG ERDREINSTN FGECQIPDYQ EQDIFLWRKE 

       850        860        870        880        890        900 
TGFGFRILGG NEPGEPIYIG HIVPLGAADT DGRLRSGDEL ICVDGTPVIG KSHQLVVQLM 

       910        920        930        940        950        960 
QQAAKQGHVN LTVRRKVVFA VPKAENEVPS PASSHHSSNQ PASLTEEKRT PQGSQNSLNT 

       970        980        990       1000       1010       1020 
VSSGSGSTSG IGSGGGGGSG VVSAVLQPYD VEIRRGENEG FGFVIVSSVS RPEAGTTFGR 

      1030       1040       1050       1060       1070       1080 
IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI IPGDESSNAT 

      1090       1100       1110       1120       1130       1140 
LLTNAEKIAT ITTTHAPSQQ GTQETRTTTK PKQDSQFEFK GPQAAQEQDF YTVELERGAK 

      1150       1160       1170       1180       1190       1200 
GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL EINGETTKNM KHSRAIELIK 

      1210       1220       1230       1240       1250       1260 
NGGRRVRLFL RRGDGSVPEY DPSSDRNGPS TGAQGVPEVR PGPPDHRPHP ALESSYPPEL 

      1270       1280       1290       1300       1310       1320 
HKSSQHAEKR AHAKDPKGNR EHSKQPNEHH TWNGTSRKQD SGACRPKDRP PDAWREAQPE 

      1330       1340       1350       1360       1370       1380 
RTATNGSKRR SPEKRREGTR SADNTLERRE KHEKRREISP ERKRERSPTR RKDSSPSRRR 

      1390       1400       1410       1420       1430       1440 
RSLERLLDQR RSPERRRGGS PERRAKSTDR RRARSPERRR ERSLDKRNRD DKVGHREREE 

      1450       1460       1470 
AGLKLEAGRS PRNPPEQRRR PYKECSTDLS I

« Hide

Isoform 2 (MAGI-1b) [UniParc].

Checksum: 1255479BA421DAA0
Show »

FASTA1,172127,651
Isoform 3 (MAGI-1a) [UniParc].

Checksum: 4B2D712E64126A55
Show »

FASTA1,237134,404

References

« Hide 'large scale' references
[1]"Endothelial adhesion molecule ESAM binds directly to the multidomain adaptor MAGI-1 and recruits it to cell contacts."
Wegmann F., Ebnet K., Du Pasquier L., Vestweber D., Butz S.
Exp. Cell Res. 300:121-133(2004) [PubMed: 15383320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ESAM.
Strain: 129/SvHe.
Tissue: Brain endothelium.
[2]"MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains."
Dobrosotskaya I.Y., Guy R.K., James G.L.
J. Biol. Chem. 272:31589-31597(1997) [PubMed: 9395497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: C57BL/6 X CBA.
[3]"MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures."
Dobrosotskaya I.Y., James G.L.
Biochem. Biophys. Res. Commun. 270:903-909(2000) [PubMed: 10772923] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
[4]"Identification of mNET1 as a candidate ligand for the first PDZ domain of MAGI-1."
Dobrosotskaya I.Y.
Biochem. Biophys. Res. Commun. 283:969-975(2001) [PubMed: 11350080] [Abstract]
Cited for: INTERACTION WITH NET1.
[5]"The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes."
Patrie K.M., Drescher A.J., Goyal M., Wiggins R.C., Margolis B.
J. Am. Soc. Nephrol. 12:667-677(2001) [PubMed: 11274227] [Abstract]
Cited for: INTERACTION WITH LRP2, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[6]"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."
Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.
J. Biol. Chem. 279:46962-46968(2004) [PubMed: 15317815] [Abstract]
Cited for: INTERACTION WITH ACCN3, FUNCTION.
[7]"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth."
Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J.
J. Cell Sci. 117:4401-4409(2004) [PubMed: 15304526] [Abstract]
Cited for: INTERACTION WITH CXADR.
[8]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-858, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY497557 mRNA. Translation: AAS77818.1.
AF027503 mRNA. Translation: AAB91995.1.
AF027504 mRNA. Translation: AAB91996.1.
AF027505 mRNA. Translation: AAB91997.1.
IPIIPI00454120.
IPI00471107.
IPI00471108.
PIRT42372.
RefSeqNP_001025021.1. NM_001029850.3.
NP_034497.1. NM_010367.2.
UniGeneMm.217216.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I04X-ray2.15A/B463-546[»]
ProteinModelPortalQ6RHR9.
SMRQ6RHR9. Positions 14-106, 137-192, 295-401, 447-572, 632-713, 831-915, 986-1217.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-150460.
STRINGQ6RHR9.

PTM databases

PhosphoSiteQ6RHR9.

Proteomic databases

PRIDEQ6RHR9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055224; ENSMUSP00000062085; ENSMUSG00000045095.
ENSMUST00000089317; ENSMUSP00000086730; ENSMUSG00000045095.
GeneID14924.
KEGGmmu:14924.
UCSCuc009czi.1. mouse.
uc009czk.1. mouse.

Organism-specific databases

CTD9223.
MGIMGI:1203522. Magi1.

Phylogenomic databases

GeneTreeENSGT00530000063259.
HOGENOMHBG315069.
HOVERGENHBG007091.
InParanoidQ6RHR9.
OMAETRNTTK.
OrthoDBEOG4CZBF2.
PhylomeDBQ6RHR9.

Gene expression databases

ArrayExpressQ6RHR9.
BgeeQ6RHR9.
CleanExMM_BAP1.
GenevestigatorQ6RHR9.
GermOnlineENSMUSG00000045095. Mus musculus.

Family and domain databases

InterProIPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR001478. PDZ/DHR/GLGF.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
Gene3DG3DSA:2.20.70.10. G3DSA:2.20.70.10. 2 hits.
KOK05631.
PfamPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 5 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 6 hits.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF50156. PDZ. 6 hits.
SSF51045. WW_Rsp5_WWP. 2 hits.
PROSITEPS00856. 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]
ProtoNetSearch...

Other

NextBio287235.
SOURCESearch...

Entry information

Entry nameMAGI1_MOUSE
AccessionPrimary (citable) accession number: Q6RHR9
Secondary accession number(s): O54893, O54894, O54895
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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