CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024141
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myotubularin 
Protein Synonyms/Alias
  
Gene Name
 Mtm1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
252PLVGMSGKRNKDDEKubiquitination[1]
255GMSGKRNKDDEKYLDubiquitination[1]
259KRNKDDEKYLDVIREubiquitination[1]
Reference
 [1] 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
 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 (By similarity). 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 (By similarity).
 MOD_RES 588 588 Phosphoserine (By similarity).  
Keyword
 Cell membrane; Cell projection; Complete proteome; Cytoplasm; Endosome; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 603 AA 
Protein Sequence
MASASASKYN SHSLENESIK KVSQDGVSQD VSETVPRLPG ELLITEKEVI YICPFNGPIK 60
GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDLRNLR 120
FALKQEGHSR RDMFEILVKH AFPLAHNLPL FAFVNEEKFN VDGWTVYNPV EEYRRQGLPN 180
HHWRISFINK CYELCETYPA LLVVPYRTSD DDLRRIATFR SRNRLPVLSW IHPENKMVIM 240
RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ TSKLMIYDAR PSVNAVANKA TGGGYESDDA 300
YQNSELSFLD IHNIHVMRES LKKVKDIVYP NIEESHWLSS LESTHWLEHI KLVLTGAIQV 360
ADQVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRTI EGFEILVQKE WISFGHKFAS 420
RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE GFLITVLDHL YSCRFGTFLF 480
NCDSARERQK LTERTVSLWS LINSNKDKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR 540
WNPRVKQQQP NPVEQRYMEL LALRDDYIKR LEELQLANSA KLADAPASTS SSSQMVPHVQ 600
THF 603 
Gene Ontology
 GO:0030175; C:filopodium; ISS:UniProtKB.
 GO:0031674; C:I band; IDA:MGI.
 GO:0005770; C:late endosome; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0019215; F:intermediate filament binding; ISS:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
 GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
 GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
 GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
 GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
 GO:0048311; P:mitochondrion distribution; IMP:UniProtKB.
 GO:0070584; P:mitochondrion morphogenesis; IMP:UniProtKB.
 GO:0046716; P:muscle cell homeostasis; IMP:MGI.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0044088; P:regulation of vacuole organization; ISS:UniProtKB. 
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