CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023582
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myotubularin-related protein 6 
Protein Synonyms/Alias
  
Gene Name
 MTMR6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13TTKVEQVKLLDRFSTubiquitination[1, 2]
100NSLLQLSKQAKYEDLubiquitination[2]
103LQLSKQAKYEDLYAFubiquitination[2]
115YAFSYNPKQNDSERLubiquitination[1, 2, 3]
135IDLAEEYKRMGVPNSubiquitination[1, 2, 3]
154SDANRDYKICETYPRubiquitination[2]
171YVPRIASKPIIVGSSubiquitination[2, 4]
179PIIVGSSKFRSKGRFubiquitination[2, 5, 6]
242YVMDTRPKLNAMANRubiquitination[2]
253MANRAAGKGYENEDNubiquitination[1, 2, 4, 7]
283VMRSSLQKLLEVNGTubiquitination[2]
291LLEVNGTKGLSVNDFubiquitination[1]
453EELKLKEKTYSLWPFubiquitination[2]
466PFLLEDQKKYLNPLYubiquitination[1, 3]
467FLLEDQKKYLNPLYSubiquitination[2]
536DIKDLESKIKQRKNKubiquitination[2]
565HPESPNLKTSLCFKEubiquitination[2]
571LKTSLCFKEQTLLPVubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Phosphatase that acts on lipids with a phosphoinositol headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3 phosphatase. Negatively regulates proliferation of reactivated CD4+ T-cells. 
Sequence Annotation
 DOMAIN 124 499 Myotubularin phosphatase.
 REGION 248 251 Substrate binding (By similarity).
 REGION 273 274 Substrate binding (By similarity).
 REGION 336 342 Substrate binding (By similarity).
 ACT_SITE 336 336 Phosphocysteine intermediate (By
 BINDING 382 382 Substrate (By similarity).
 MOD_RES 108 108 Phosphotyrosine (By similarity).
 MOD_RES 561 561 Phosphoserine.
 MOD_RES 589 589 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 621 AA 
Protein Sequence
MEHIRTTKVE QVKLLDRFST SNKSLTGTLY LTATHLLFID SHQKETWILH HHIASVEKLA 60
LTTSGCPLVI QCKNFRTVHF IVPRERDCHD IYNSLLQLSK QAKYEDLYAF SYNPKQNDSE 120
RLQGWQLIDL AEEYKRMGVP NSHWQLSDAN RDYKICETYP RELYVPRIAS KPIIVGSSKF 180
RSKGRFPVLS YYHQDKEAAI CRCSQPLSGF SARCLEDEHL LQAISKANPV NRYMYVMDTR 240
PKLNAMANRA AGKGYENEDN YSNIRFQFVG IENIHVMRSS LQKLLEVNGT KGLSVNDFYS 300
GLESSGWLRH IKAVMDAAIF LAKAITVENA SVLVHCSDGW DRTSQVCSLG SLLLDSYYRT 360
IKGFMVLIEK DWISFGHKFS ERCGQLDGDP KEVSPVFTQF LECVWHLTEQ FPQAFEFSEA 420
FLLQIHEHIH SCQFGNFLGN CQKEREELKL KEKTYSLWPF LLEDQKKYLN PLYSSESHRF 480
TVLEPNTVSF NFKFWRNMYH QFDRTLHPRQ SVFNIIMNMN EQNKQLEKDI KDLESKIKQR 540
KNKQTDGILT KELLHSVHPE SPNLKTSLCF KEQTLLPVND ALRTIEGSSP ADNRYSEYAE 600
EFSKSEPAVV SLEYGVARMT C 621 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
 GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB.
 GO:0004722; F:protein serine/threonine phosphatase activity; NAS:UniProtKB.
 GO:0004725; F:protein tyrosine phosphatase activity; NAS:UniProtKB.
 GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR010569; Myotub-related.
 IPR017906; Myotubularin_phosphatase_dom.
 IPR011993; PH_like_dom.
 IPR016130; Tyr_Pase_AS. 
Pfam
 PF06602; Myotub-related 
SMART
  
PROSITE
 PS51339; PPASE_MYOTUBULARIN
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2 
PRINTS