CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012123
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myotubularin 
Protein Synonyms/Alias
  
Gene Name
 MTM1 
Gene Synonyms/Alias
 CG2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MASASTSKYNSHSLEubiquitination[1]
20SLENESIKRTSRDGVubiquitination[1]
95GVISRIEKMGGATSRubiquitination[1]
114YGLDITCKDMRNLRFubiquitination[1]
124RNLRFALKQEGHSRRubiquitination[1]
236SWIHPENKTVIVRCSubiquitination[1]
252PLVGMSGKRNKDDEKubiquitination[1]
259KRNKDDEKYLDVIREubiquitination[1]
546IRWNPRIKQQQPNPVubiquitination[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
 Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine- containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. 
Sequence Annotation
 DOMAIN 29 97 GRAM.
 DOMAIN 163 538 Myotubularin phosphatase.
 ACT_SITE 375 375 Phosphocysteine intermediate (By
 MOD_RES 495 495 Phosphothreonine.
 MOD_RES 588 588 Phosphoserine.  
Keyword
 Cell membrane; Cell projection; Complete proteome; Cytoplasm; Disease mutation; Endosome; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 603 AA 
Protein Sequence
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI YICPFNGPIK 60
GRVYITNYRL YLRSLETDSS LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDMRNLR 120
FALKQEGHSR RDMFEILTRY AFPLAHSLPL FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN 180
HHWRITFINK CYELCDTYPA LLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV 240
RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA 300
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV 360
ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS 420
RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE QFLIIILDHL YSCRFGTFLF 480
NCESARERQK VTERTVSLWS LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR 540
WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ 600
THF 603 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030175; C:filopodium; IDA:UniProtKB.
 GO:0031674; C:I band; IEA:Compara.
 GO:0005770; C:late endosome; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0019215; F:intermediate filament binding; IDA:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IDA:UniProtKB.
 GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB.
 GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
 GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
 GO:0048311; P:mitochondrion distribution; IMP:UniProtKB.
 GO:0070584; P:mitochondrion morphogenesis; IDA:UniProtKB.
 GO:0046716; P:muscle cell homeostasis; IEA:Compara.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
 GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0044088; P:regulation of vacuole organization; IDA:UniProtKB.
 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