MTM1_HUMAN - dbPTM
MTM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTM1_HUMAN
UniProt AC Q13496
Protein Name Myotubularin
Gene Name MTM1
Organism Homo sapiens (Human).
Sequence Length 603
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein . Cell projection, filopodium . Cell projection, ruffle . Late endosome . Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions suc
Protein 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..
Protein Sequence MASASTSKYNSHSLENESIKRTSRDGVNRDLTEAVPRLPGETLITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPLFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYLDVIRETNKQISKLTIYDARPSVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHTDADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLIIILDHLYSCRFGTFLFNCESARERQKVTERTVSLWSLINSNKEKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLEELQLANSAKLSDPPTSPSSPSQMMPHVQTHF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
8UbiquitinationMASASTSKYNSHSLE
CCCCCCCCCCCCCCC		48.84-
8UbiquitinationMASASTSKYNSHSLE
CCCCCCCCCCCCCCC		48.84-
9PhosphorylationASASTSKYNSHSLEN
CCCCCCCCCCCCCCC		22.9726657352
11PhosphorylationASTSKYNSHSLENES
CCCCCCCCCCCCCHH		16.0328102081
13PhosphorylationTSKYNSHSLENESIK
CCCCCCCCCCCHHHC		36.8825159151
18PhosphorylationSHSLENESIKRTSRD
CCCCCCHHHCCCCCC		45.0223401153
20UbiquitinationSLENESIKRTSRDGV
CCCCHHHCCCCCCCC		59.92-
20UbiquitinationSLENESIKRTSRDGV
CCCCHHHCCCCCCCC		59.92-
22PhosphorylationENESIKRTSRDGVNR
CCHHHCCCCCCCCCC		24.1023312004
23PhosphorylationNESIKRTSRDGVNRD
CHHHCCCCCCCCCCC		32.1928102081
64PhosphorylationGPIKGRVYITNYRLY
CCCCCEEEEEECEEE		10.7329759185
66PhosphorylationIKGRVYITNYRLYLR
CCCEEEEEECEEEEE		14.4429759185
68PhosphorylationGRVYITNYRLYLRSL
CEEEEEECEEEEEEC		8.0529759185
71PhosphorylationYITNYRLYLRSLETD
EEEECEEEEEECCCC		7.35-
74PhosphorylationNYRLYLRSLETDSSL
ECEEEEEECCCCCCE		28.1428857561
87UbiquitinationSLILDVPLGVISRIE
CEEEECCHHHHHHHH		9.57-
91PhosphorylationDVPLGVISRIEKMGG
ECCHHHHHHHHHCCC		25.4624719451
95UbiquitinationGVISRIEKMGGATSR
HHHHHHHHCCCCCCC		40.24-
106PhosphorylationATSRGENSYGLDITC
CCCCCCCCCCCCEEE		19.1016674116
107PhosphorylationTSRGENSYGLDITCK
CCCCCCCCCCCEEEC		33.03-
112PhosphorylationNSYGLDITCKDMRNL
CCCCCCEEECHHHHH		17.1116674116
114UbiquitinationYGLDITCKDMRNLRF
CCCCEEECHHHHHHH		46.00-
124UbiquitinationRNLRFALKQEGHSRR
HHHHHHHHHCCCCHH		42.76-
147PhosphorylationYAFPLAHSLPLFAFL
HHHHHHHHCCEEHHH		26.5224719451
199UbiquitinationYELCDTYPALLVVPY
HHHHHCCCEEEEEEE		20.65-
215UbiquitinationASDDDLRRVATFRSR
CCCCHHHHHHHHHHC		29.71-
222UbiquitinationRVATFRSRNRIPVLS
HHHHHHHCCCCCEEE		31.99-
236UbiquitinationSWIHPENKTVIVRCS
EEECCCCCEEEEEEC		42.37-
252UbiquitinationPLVGMSGKRNKDDEK
CCCCCCCCCCCCCHH		45.55-
259UbiquitinationKRNKDDEKYLDVIRE
CCCCCCHHHHHHHHH		59.10-
260PhosphorylationRNKDDEKYLDVIRET
CCCCCHHHHHHHHHH		13.1918083107
273UbiquitinationETNKQISKLTIYDAR
HHHHHHCEEEEEECC		51.80-
277PhosphorylationQISKLTIYDARPSVN
HHCEEEEEECCCCHH		9.79-
295PhosphorylationNKATGGGYESDDAYH
CCCCCCCCCCCHHHC		18.61-
297PhosphorylationATGGGYESDDAYHNA
CCCCCCCCCHHHCCC		32.10-
301PhosphorylationGYESDDAYHNAELFF
CCCCCHHHCCCEEEE		11.55-
386PhosphorylationWDRTAQLTSLAMLML
CHHHHHHHHHHHHHH		15.0423663014
413PhosphorylationLVQKEWISFGHKFAS
EEEHHHHHHCHHHHH		26.6720068231
420PhosphorylationSFGHKFASRIGHGDK
HHCHHHHHHCCCCCC		27.8020068231
495PhosphorylationRQKVTERTVSLWSLI
HHHHCHHHHHHHHHH		14.2816964243
509UbiquitinationINSNKEKFKNPFYTK
HHCCHHHHCCCCCHH		10.96-
546UbiquitinationIRWNPRIKQQQPNPV
HHCCCCHHCCCCCHH		43.25-
557PhosphorylationPNPVEQRYMELLALR
CCHHHHHHHHHHHHH		8.47-
579PhosphorylationEELQLANSAKLSDPP
HHHHCHHHCCCCCCC		22.6026074081
583PhosphorylationLANSAKLSDPPTSPS
CHHHCCCCCCCCCCC		47.5723927012
587PhosphorylationAKLSDPPTSPSSPSQ
CCCCCCCCCCCCHHH		59.6723927012
588PhosphorylationKLSDPPTSPSSPSQM
CCCCCCCCCCCHHHC		28.6723818870
590PhosphorylationSDPPTSPSSPSQMMP
CCCCCCCCCHHHCCC		55.4323401153
591PhosphorylationDPPTSPSSPSQMMPH
CCCCCCCCHHHCCCC		31.7723927012
593PhosphorylationPTSPSSPSQMMPHVQ
CCCCCCHHHCCCCCC		32.4323927012
601PhosphorylationQMMPHVQTHF-----
HCCCCCCCCC-----		24.9423927012
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MTM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTM1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MTM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIN1_HUMANBIN1physical
23917616
CUL4A_HUMANCUL4Aphysical
26344197
1C07_HUMANHLA-Cphysical
27880917
K1468_HUMANKIAA1468physical
27880917
K22E_HUMANKRT2physical
27880917
K2C5_HUMANKRT5physical
27880917
SNX17_HUMANSNX17physical
27880917
MTM1_HUMANMTM1physical
27432908
MTFR1_HUMANMTFR1physical
27432908
SAM50_HUMANSAMM50physical
27432908
CALU_HUMANCALUphysical
27432908
CIAO1_HUMANCIAO1physical
27432908
STIP1_HUMANSTIP1physical
27432908
RCN1_HUMANRCN1physical
27432908
SNX6_HUMANSNX6physical
27432908
PFD3_HUMANVBP1physical
27432908
SNX17_HUMANSNX17physical
27432908
TRBP2_HUMANTARBP2physical
27432908
ARK72_HUMANAKR7A2physical
27432908
NDUA9_HUMANNDUFA9physical
27432908
OXA1L_HUMANOXA1Lphysical
27432908
SOAT1_HUMANSOAT1physical
27432908
STML2_HUMANSTOML2physical
27432908
MIC60_HUMANIMMTphysical
27432908
ILK_HUMANILKphysical
27432908
SCO2_HUMANSCO2physical
27432908
TBA3C_HUMANTUBA3Cphysical
28514442
SNX17_HUMANSNX17physical
28514442
Drug and Disease Associations
Kegg Disease
H00700 Centronuclear myopathy
OMIM Disease
310400Myopathy, centronuclear, X-linked (CNMX)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTM1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-590, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-591, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-495, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory