CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021844
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MAGUK p55 subfamily member 6 
Protein Synonyms/Alias
 Dlgh4 protein; P55T protein; Protein associated with Lin-7 2 
Gene Name
 Mpp6 
Gene Synonyms/Alias
 Dlgh4; Pals2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
416EADIKAGKYLEHGEYubiquitination[1, 2]
482ETLRAMHKAVVDAGIubiquitination[3]
528IVNDNLDKAFEKLQTubiquitination[3]
532NLDKAFEKLQTAIEKubiquitination[3]
539KLQTAIEKLRMEPQWubiquitination[3]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
  
Sequence Annotation
 DOMAIN 1 48 L27 1.
 DOMAIN 49 107 L27 2.
 DOMAIN 129 208 PDZ.
 DOMAIN 228 297 SH3.
 DOMAIN 351 538 Guanylate kinase-like.
 MOD_RES 513 513 Phosphotyrosine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Membrane; Phosphoprotein; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 553 AA 
Protein Sequence
MQQVLENLTE LPSSTGAEEI DLIFLKGIME NPIVKSLAKA HERLEDSKLE AVSDNNLELV 60
NEILEDITPL ISVDENVAEL VGILKEPHFQ SLLEAHDIVA SKCYDSPPSS PEMNIPSLNN 120
QLPVDAIRIL GIHKKAGEPL GVTFRVENND LVIARILHGG MIDRQGLLHV GDIIKEVNGH 180
EVGNNPKELQ ELLKNISGSV TLKILPSYRD TITPQQSYVN MERHPAHVRQ VFVKCHFDYN 240
PFNDNLIPCK EAGLKFSKGE ILQIVNREDP NWWQASHVKE GGSAGLIPSQ FLEEKRKAFV 300
RRDWDNSGPF CGTISNKKKK KMMYLTTRNA EFDRHEIQIY EEVAKMPPFQ RKTLVLIGAQ 360
GVGRRSLKNR FIVLNPARFG TTVPFTSRKP REDEKDGQAY KFVSRSEMEA DIKAGKYLEH 420
GEYEGNLYGT KIDSILEVVQ TGRTCILDVN PQALKVLRTS EFMPYVVFIA APELETLRAM 480
HKAVVDAGIT TKLLTDSDLK KTVDESARIQ RAYNHYFDLI IVNDNLDKAF EKLQTAIEKL 540
RMEPQWVPIS WVY 553 
Gene Ontology
 GO:0016021; C:integral to membrane; ISS:MGI.
 GO:0005886; C:plasma membrane; IDA:MGI.
 GO:0004385; F:guanylate kinase activity; ISS:MGI. 
Interpro
 IPR008144; Guanylate_kin.
 IPR008145; Guanylate_kin/L-typ_Ca_channel.
 IPR020590; Guanylate_kinase_CS.
 IPR004172; L27.
 IPR014775; L27_C.
 IPR027417; P-loop_NTPase.
 IPR001478; PDZ.
 IPR011511; SH3_2.
 IPR001452; SH3_domain. 
Pfam
 PF00625; Guanylate_kin
 PF02828; L27
 PF00595; PDZ
 PF07653; SH3_2 
SMART
 SM00072; GuKc
 SM00569; L27
 SM00228; PDZ
 SM00326; SH3 
PROSITE
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS51022; L27
 PS50106; PDZ
 PS50002; SH3 
PRINTS