CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001354
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 
Protein Synonyms/Alias
 Atrophin-1-interacting protein 1; AIP-1; Membrane-associated guanylate kinase inverted 2; MAGI-2; Synaptic-scaffolding molecule; S-SCAM 
Gene Name
 Magi2 
Gene Synonyms/Alias
 Acvrinp1; Aip1; Sscam 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
421TRDASQLKGTFLSTTubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 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). 
Sequence Annotation
 DOMAIN 17 101 PDZ.
 DOMAIN 109 283 Guanylate kinase-like.
 DOMAIN 302 335 WW 1.
 DOMAIN 348 381 WW 2.
 DOMAIN 426 510 PDZ 1.
 DOMAIN 605 683 PDZ 2.
 DOMAIN 778 860 PDZ 3.
 DOMAIN 920 1010 PDZ 4.
 DOMAIN 1141 1223 PDZ 5.
 REGION 302 381 Interaction with DDN (By similarity).
 MOD_RES 362 362 Phosphotyrosine (By similarity).
 MOD_RES 366 366 Phosphotyrosine (By similarity).
 MOD_RES 827 827 Phosphotyrosine (By similarity).  
Keyword
 Alternative splicing; Cell junction; Cell membrane; Complete proteome; Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1277 AA 
Protein Sequence
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL 60
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS 120
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED 180
NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VTNMEKASIE PPEEEEEERP 240
VVNGNGVVIT PESSEHEDKS AGASGETPSQ PYPAPVYSQP EELKDQMDDT KSTKPEENED 300
SDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PAEECKENEL PYGWEKIDDP 360
IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL 420
KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC 480
VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG 540
RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPADGQLDG TYPPPVHDDN VSVASSGATQ 600
AELMTLTIVK GAKGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT 660
EVVDILKDCP VGSETSLIIH RGGFFSPWKT PKPMVDRWEN QGSPQTSLSA PAVPQSLPFP 720
PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRQQVP PRTSFRMDSS GPDYKELDVH 780
LRRMESGFGF RILGGDEPGQ PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY 840
VIDLMHHAAR NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYANSNHAA 900
PSNNASPPEG FASHSLQTSD VIIHRKENEG FGFVIISSLN RPESGATITV PHKIGRIIDG 960
SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNNPTSAPS 1020
SEKQSPMAQQ HSPLAQQHSP LAQPSPATPN SPVAQPAPPQ PLQLQGHENS YRSEVKARQD 1080
VKPDIRQPPF TDYRQPPLDY RQPPGGDYSQ PSPLDYRQHS PDTRQYPLSD YRQPQDFDYF 1140
TVDMEKGAKG FGFSIRGGRE YKMDLYVLRL AEDGPAIRNG RMRVGDQIIE INGESTRDMT 1200
HARAIELIKS GGRRVRLLLK RGTGQVPEYG MVPSSLSMCM KSDKHGSPYF YLLGHPKDTT 1260
NPTPGALPLP PPQACRK 1277 
Gene Ontology
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0014069; C:postsynaptic density; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0036057; C:slit diaphragm; IDA:UniProtKB.
 GO:0005923; C:tight junction; ISS:UniProtKB.
 GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
 GO:0019902; F:phosphatase binding; ISS:UniProtKB.
 GO:0030159; F:receptor signaling complex scaffold activity; ISS:UniProtKB.
 GO:0004871; F:signal transducer activity; ISS:UniProtKB.
 GO:0046332; F:SMAD binding; ISS:UniProtKB.
 GO:0070699; F:type II activin receptor binding; ISS:UniProtKB.
 GO:0003094; P:glomerular filtration; IC:UniProtKB.
 GO:0072015; P:glomerular visceral epithelial cell development; IEP:UniProtKB.
 GO:0071850; P:mitotic cell cycle arrest; IDA:UniProtKB.
 GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:UniProtKB.
 GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; ISS:UniProtKB.
 GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
 GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
 GO:0051291; P:protein heterooligomerization; IDA:RGD.
 GO:0043113; P:receptor clustering; IDA:RGD.
 GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB. 
Interpro
 IPR008144; Guanylate_kin.
 IPR008145; Guanylate_kin/L-typ_Ca_channel.
 IPR020590; Guanylate_kinase_CS.
 IPR027417; P-loop_NTPase.
 IPR001478; PDZ.
 IPR001202; WW_dom. 
Pfam
 PF00625; Guanylate_kin
 PF00595; PDZ
 PF00397; WW 
SMART
 SM00072; GuKc
 SM00228; PDZ
 SM00456; WW 
PROSITE
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS50106; PDZ
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS