MTMR1_HUMAN - dbPTM
MTMR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTMR1_HUMAN
UniProt AC Q13613
Protein Name Myotubularin-related protein 1
Gene Name MTMR1
Organism Homo sapiens (Human).
Sequence Length 665
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm .
Protein Description Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate. [PubMed: 11733541]
Protein Sequence MDRPAAAAAAGCEGGGGPNPGPAGGRRPPRAAGGATAGSRQPSVETLDSPTGSHVEWCKQLIAATISSQISGSVTSENVSRDYKALRDGNKLAQMEEAPLFPGESIKAIVKDVMYICPFMGAVSGTLTVTDFKLYFKNVERDPHFILDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAYKQEEQSKLGIFENLNKHAFPLSNGQALFAFSYKEKFPINGWKVYDPVSEYKRQGLPNESWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFETLVEKEWISFGHRFALRVGHGNDNHADADRSPIFLQFVDCVWQMTRQFPSAFEFNELFLITILDHLYSCLFGTFLCNCEQQRFKEDVYTKTISLWSYINSQLDEFSNPFFVNYENHVLYPVASLSHLELWVNYYVRWNPRMRPQMPIHQNLKELLAVRAELQKRVEGLQREVATRAVSSSSERGSSPSHSATSVHTSV
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
1Acetylation-------MDRPAAAA
-------CCCHHHHH
9.9522223895
36PhosphorylationPRAAGGATAGSRQPS
CCCCCCCCCCCCCCC
34.5223927012
39PhosphorylationAGGATAGSRQPSVET
CCCCCCCCCCCCCCC
25.8623927012
43PhosphorylationTAGSRQPSVETLDSP
CCCCCCCCCCCCCCC
25.0123401153
46PhosphorylationSRQPSVETLDSPTGS
CCCCCCCCCCCCCCH
33.4423927012
49PhosphorylationPSVETLDSPTGSHVE
CCCCCCCCCCCHHHH
27.7225159151
51PhosphorylationVETLDSPTGSHVEWC
CCCCCCCCCHHHHHH
56.0923927012
53PhosphorylationTLDSPTGSHVEWCKQ
CCCCCCCHHHHHHHH
27.1723403867
65PhosphorylationCKQLIAATISSQISG
HHHHHHHHHHHHCCC
16.6321406692
67PhosphorylationQLIAATISSQISGSV
HHHHHHHHHHCCCCC
16.3121406692
68PhosphorylationLIAATISSQISGSVT
HHHHHHHHHCCCCCC
27.9021406692
71PhosphorylationATISSQISGSVTSEN
HHHHHHCCCCCCCCC
19.8521406692
73PhosphorylationISSQISGSVTSENVS
HHHHCCCCCCCCCCC
18.5521406692
75PhosphorylationSQISGSVTSENVSRD
HHCCCCCCCCCCCHH
31.8321406692
76PhosphorylationQISGSVTSENVSRDY
HCCCCCCCCCCCHHH
25.6421406692
80PhosphorylationSVTSENVSRDYKALR
CCCCCCCCHHHHHHH
30.8921406692
91 (in isoform 2)Ubiquitination-51.2121890473
91UbiquitinationKALRDGNKLAQMEEA
HHHHCCCCCCCHHCC
51.2121906983
91 (in isoform 1)Ubiquitination-51.2121890473
107UbiquitinationLFPGESIKAIVKDVM
CCCHHHHHHHHHHHH
41.14-
115PhosphorylationAIVKDVMYICPFMGA
HHHHHHHHHHHCCCC
10.1421406692
124PhosphorylationCPFMGAVSGTLTVTD
HHCCCCCCCEEEEEE
26.0621406692
126PhosphorylationFMGAVSGTLTVTDFK
CCCCCCCEEEEEEEE
16.2621406692
128PhosphorylationGAVSGTLTVTDFKLY
CCCCCEEEEEEEEEE
22.6121406692
130PhosphorylationVSGTLTVTDFKLYFK
CCCEEEEEEEEEEEE
30.4021406692
155PhosphorylationDVPLGVISRVEKIGA
ECCHHHHHHHHHHCC
28.0624719451
159UbiquitinationGVISRVEKIGAQSHG
HHHHHHHHHCCCCCC
43.51-
159AcetylationGVISRVEKIGAQSHG
HHHHHHHHHCCCCCC
43.5125953088
177UbiquitinationCGIEIVCKDMRNLRL
CCEEEEEHHHHHCHH
43.60-
186PhosphorylationMRNLRLAYKQEEQSK
HHHCHHHHHHHHHHH
20.1430622161
187UbiquitinationRNLRLAYKQEEQSKL
HHCHHHHHHHHHHHH
45.70-
192PhosphorylationAYKQEEQSKLGIFEN
HHHHHHHHHHCHHCC
32.8830622161
193UbiquitinationYKQEEQSKLGIFENL
HHHHHHHHHCHHCCC
50.88-
237 (in isoform 2)Ubiquitination-33.9121890473
237AcetylationYDPVSEYKRQGLPNE
ECCHHHHHHCCCCCC
33.9130590509
237 (in isoform 1)Ubiquitination-33.9121890473
237UbiquitinationYDPVSEYKRQGLPNE
ECCHHHHHHCCCCCC
33.9121890473
247UbiquitinationGLPNESWKISKINSN
CCCCCCCEEEECCCC
46.51-
250UbiquitinationNESWKISKINSNYEF
CCCCEEEECCCCCCC
49.75-
253PhosphorylationWKISKINSNYEFCDT
CEEEECCCCCCCCCC
44.24-
278UbiquitinationVKDDDLSKVAAFRAK
CCCCCHHHHHHHHHC
43.10-
292O-linked_GlycosylationKGRVPVLSWIHPESQ
CCCCCEEEEECHHHC
24.9930379171
315UbiquitinationPLVGPNDKRCKEDEK
CCCCCCCCCCCCCHH
67.35-
458PhosphorylationLAMLMLDSYYRTIKG
HHHHHHHHHHHHHCC
21.8025072903
459PhosphorylationAMLMLDSYYRTIKGF
HHHHHHHHHHHHCCH
9.1625072903
460PhosphorylationMLMLDSYYRTIKGFE
HHHHHHHHHHHCCHH
12.7725072903
468PhosphorylationRTIKGFETLVEKEWI
HHHCCHHHHHHHHEC
33.57-
555PhosphorylationQRFKEDVYTKTISLW
HHCHHCCCHHHHHHH
18.1625839225
645PhosphorylationEVATRAVSSSSERGS
HHHHHHHCCCCCCCC
24.4224732914
646PhosphorylationVATRAVSSSSERGSS
HHHHHHCCCCCCCCC
31.1424732914
647PhosphorylationATRAVSSSSERGSSP
HHHHHCCCCCCCCCC
28.8124732914
648PhosphorylationTRAVSSSSERGSSPS
HHHHCCCCCCCCCCC
33.0124732914
650MethylationAVSSSSERGSSPSHS
HHCCCCCCCCCCCCC
52.84115484057
652PhosphorylationSSSSERGSSPSHSAT
CCCCCCCCCCCCCCC
45.3422167270
653PhosphorylationSSSERGSSPSHSATS
CCCCCCCCCCCCCCC
32.9922167270
655PhosphorylationSERGSSPSHSATSVH
CCCCCCCCCCCCCCC
31.8322167270
657PhosphorylationRGSSPSHSATSVHTS
CCCCCCCCCCCCCCC
37.2622167270
659PhosphorylationSSPSHSATSVHTSV-
CCCCCCCCCCCCCC-
34.0122167270
660PhosphorylationSPSHSATSVHTSV--
CCCCCCCCCCCCC--
16.1822167270
663PhosphorylationHSATSVHTSV-----
CCCCCCCCCC-----
29.0925159151
664O-linked_GlycosylationSATSVHTSV------
CCCCCCCCC------
15.7930379171
664PhosphorylationSATSVHTSV------
CCCCCCCCC------
15.7925159151

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 MTMR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTMR1_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 MTMR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NADAP_HUMANSLC4A1APphysical
27880917

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTMR1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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