CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015361
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 
Protein Synonyms/Alias
 BAI1-associated protein 1; BAP-1; Membrane-associated guanylate kinase inverted 1; MAGI-1 
Gene Name
 Magi1 
Gene Synonyms/Alias
 Baiap1; Bap1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MSKVIQKKNHacetylation[1]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379
Functional Description
 May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface. 
Sequence Annotation
 DOMAIN 17 105 PDZ 1.
 DOMAIN 96 287 Guanylate kinase-like.
 DOMAIN 300 333 WW 1.
 DOMAIN 359 392 WW 2.
 DOMAIN 464 546 PDZ 2.
 DOMAIN 635 713 PDZ 3.
 DOMAIN 833 915 PDZ 4.
 DOMAIN 990 1074 PDZ 5.
 DOMAIN 1132 1214 PDZ 6.
 NP_BIND 103 110 ATP (By similarity).
 REGION 990 1074 Interaction with FCHSD2 (By similarity).
 MOD_RES 722 722 Phosphoserine (By similarity).
 MOD_RES 733 733 Phosphoserine (By similarity).
 MOD_RES 858 858 Phosphotyrosine.
 MOD_RES 1341 1341 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1471 AA 
Protein Sequence
MSKVIQKKNH WTGRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAA EAAGLPGGGE 60
GPKLAEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF 120
QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYS FLTVKEFLDL EQSGTLLEVG 180
TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHPENEE 240
EEDVPEMNSS FTADSGDQDE HTLQEATLPP VNSSILAAPI TDPSQKFPQY LPLSAEDNLG 300
PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE 360
LPAGWEKIED PVYGVYYVDH INRKTQYENP VLEAKRKKQL EQQQQQQQPQ PPQPEEWTED 420
HASVVPPVAP SHPPSNPEPA RETPLQGKPF FTRNPSELKG KFIHTKLRKS SRGFGFTVVG 480
GDEPDEFLQI KSLVLDGPAA LDGKMETGDV IVSVNDTCVL GHTHAQVVKI FQSIPIGASV 540
DLELCRGYPL PFDPDDPNTS LVTSVAILDK EPIIVNGQET YDSPASHSSK TGKVSSMKDA 600
RPSSPADVAS NSSHGYPNDT VSLASSIATQ PELITVHIVK GPMGFGFTIA DSPGGGGQRV 660
KQIVDSPRCR GLKEGDLIVE VNKKNVQALT HNQVVDMLIE CPKGSEVTLL VQRGGLPVPK 720
KSPKSQPLER KDSQNSSQHS VSSHRSLHTA SPSHGIQVLP EYLPADAPAP DQTDSSGQKK 780
PDPFKIWAQS RSMYENRPMS PSPASGLSKG ERDREINSTN FGECQIPDYQ EQDIFLWRKE 840
TGFGFRILGG NEPGEPIYIG HIVPLGAADT DGRLRSGDEL ICVDGTPVIG KSHQLVVQLM 900
QQAAKQGHVN LTVRRKVVFA VPKAENEVPS PASSHHSSNQ PASLTEEKRT PQGSQNSLNT 960
VSSGSGSTSG IGSGGGGGSG VVSAVLQPYD VEIRRGENEG FGFVIVSSVS RPEAGTTFGR 1020
IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI IPGDESSNAT 1080
LLTNAEKIAT ITTTHAPSQQ GTQETRTTTK PKQDSQFEFK GPQAAQEQDF YTVELERGAK 1140
GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL EINGETTKNM KHSRAIELIK 1200
NGGRRVRLFL RRGDGSVPEY DPSSDRNGPS TGAQGVPEVR PGPPDHRPHP ALESSYPPEL 1260
HKSSQHAEKR AHAKDPKGNR EHSKQPNEHH TWNGTSRKQD SGACRPKDRP PDAWREAQPE 1320
RTATNGSKRR SPEKRREGTR SADNTLERRE KHEKRREISP ERKRERSPTR RKDSSPSRRR 1380
RSLERLLDQR RSPERRRGGS PERRAKSTDR RRARSPERRR ERSLDKRNRD DKVGHREREE 1440
AGLKLEAGRS PRNPPEQRRR PYKECSTDLS I 1471 
Gene Ontology
 GO:0042995; C:cell projection; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 
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