CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012166
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myotubularin-related protein 2 
Protein Synonyms/Alias
  
Gene Name
 MTMR2 
Gene Synonyms/Alias
 KIAA1073 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
156YGLETVCKDIRNLRFubiquitination[1]
598EPIHNRYKELLAKRAubiquitination[1]
Reference
 [1] 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
Functional Description
 Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. 
Sequence Annotation
 DOMAIN 68 139 GRAM.
 DOMAIN 205 580 Myotubularin phosphatase.
 REGION 330 333 Substrate binding.
 REGION 355 356 Substrate binding.
 REGION 417 423 Substrate binding.
 ACT_SITE 417 417 Phosphocysteine intermediate.
 BINDING 463 463 Substrate.
 MOD_RES 58 58 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Charcot-Marie-Tooth disease; Coiled coil; Complete proteome; Cytoplasm; Disease mutation; Endosome; Hydrolase; Membrane; Neuropathy; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 643 AA 
Protein Sequence
MEKSSSCESL GSQPAAARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI STSADNFSPD 60
LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA VRGTLTVTNY RLYFKSMERD 120
PPFVLDASLG VINRVEKIGG ASSRGENSYG LETVCKDIRN LRFAHKPEGR TRRSIFENLM 180
KYAFPVSNNL PLFAFEYKEV FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY 240
PALLVVPANI PDEELKRVAS FRSRGRIPVL SWIHPESQAT ITRCSQPMVG VSGKRSKEDE 300
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF LDIHNIHVMR 360
ESLRKLKEIV YPNIEETHWL SNLESTHWLE HIKLILAGAL RIADKVESGK TSVVVHCSDG 420
WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE KEWLSFGHRF QLRVGHGDKN HADADRSPVF 480
LQFIDCVWQM TRQFPTAFEF NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKRTVSL 540
WSYINSQLED FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHNRYKEL 600
LAKRAELQKK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV 643 
Gene Ontology
 GO:0030424; C:axon; ISS:BHF-UCL.
 GO:0005829; C:cytosol; ISS:BHF-UCL.
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
 GO:0097060; C:synaptic membrane; ISS:BHF-UCL.
 GO:0008021; C:synaptic vesicle; ISS:BHF-UCL.
 GO:0005774; C:vacuolar membrane; IEA:Compara.
 GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IEA:Compara.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; NAS:UniProtKB.
 GO:0097062; P:dendritic spine maintenance; ISS:BHF-UCL.
 GO:0046855; P:inositol phosphate dephosphorylation; IEA:Compara.
 GO:0032288; P:myelin assembly; IEA:Compara.
 GO:0090394; P:negative regulation of excitatory postsynaptic membrane potential; ISS:BHF-UCL.
 GO:0031642; P:negative regulation of myelination; IEA:Compara.
 GO:2000645; P:negative regulation of receptor catabolic process; ISS:BHF-UCL.
 GO:0002091; P:negative regulation of receptor internalization; ISS:BHF-UCL.
 GO:0048666; P:neuron development; IEA:Compara.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
 GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Compara.
 GO:2000643; P:positive regulation of early endosome to late endosome transport; ISS:BHF-UCL.
 GO:0051262; P:protein tetramerization; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR004182; GRAM.
 IPR010569; Myotub-related.
 IPR017906; Myotubularin_phosphatase_dom.
 IPR011993; PH_like_dom.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS. 
Pfam
 PF02893; GRAM
 PF06602; Myotub-related 
SMART
 SM00568; GRAM 
PROSITE
 PS51339; PPASE_MYOTUBULARIN
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2 
PRINTS