MTMR2_HUMAN - dbPTM
MTMR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTMR2_HUMAN
UniProt AC Q13614
Protein Name Myotubularin-related protein 2
Gene Name MTMR2
Organism Homo sapiens (Human).
Sequence Length 643
Subcellular Localization Cytoplasm . Early endosome membrane
Peripheral membrane protein . Partly associated with membranes.
Protein Description Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate..
Protein Sequence MEKSSSCESLGSQPAAARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSADNFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKRTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERASSPAQCVTPVQTVV
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
4Phosphorylation----MEKSSSCESLG
----CCCCCCCCCCC		17.7423663014
5Phosphorylation---MEKSSSCESLGS
---CCCCCCCCCCCC		50.5023663014
6Phosphorylation--MEKSSSCESLGSQ
--CCCCCCCCCCCCC		29.0623663014
9PhosphorylationEKSSSCESLGSQPAA
CCCCCCCCCCCCCCC		42.2123663014
12PhosphorylationSSCESLGSQPAAARP
CCCCCCCCCCCCCCC		37.9823663014
21PhosphorylationPAAARPPSVDSLSSA
CCCCCCCCCCCCCCC		41.0423663014
24PhosphorylationARPPSVDSLSSASTS
CCCCCCCCCCCCCCC		28.1723663014
26PhosphorylationPPSVDSLSSASTSHS
CCCCCCCCCCCCCCC		28.0123927012
27PhosphorylationPSVDSLSSASTSHSE
CCCCCCCCCCCCCCC		31.3723927012
29PhosphorylationVDSLSSASTSHSENS
CCCCCCCCCCCCCCC		32.1823927012
30PhosphorylationDSLSSASTSHSENSV
CCCCCCCCCCCCCCC		30.1223927012
31PhosphorylationSLSSASTSHSENSVH
CCCCCCCCCCCCCCC		23.6323663014
33PhosphorylationSSASTSHSENSVHTK
CCCCCCCCCCCCCCC		37.9423927012
46PhosphorylationTKSASVVSSDSISTS
CCEEEEECCCCCCCC		26.6930266825
47PhosphorylationKSASVVSSDSISTSA
CEEEEECCCCCCCCC		24.6230266825
49PhosphorylationASVVSSDSISTSADN
EEEECCCCCCCCCCC		22.0130266825
51PhosphorylationVVSSDSISTSADNFS
EECCCCCCCCCCCCC		21.9130266825
52PhosphorylationVSSDSISTSADNFSP
ECCCCCCCCCCCCCC		26.6830266825
53PhosphorylationSSDSISTSADNFSPD
CCCCCCCCCCCCCCC		27.1730266825
58PhosphorylationSTSADNFSPDLRVLR
CCCCCCCCCCHHHHH		24.6122167270
69UbiquitinationRVLRESNKLAEMEEP
HHHHHHCCCCCCCCC		59.35-
73SulfoxidationESNKLAEMEEPPLLP
HHCCCCCCCCCCCCC		6.1721406390
106PhosphorylationGAVRGTLTVTNYRLY
CCCCCEEEEEEEEEE		25.7328152594
108PhosphorylationVRGTLTVTNYRLYFK
CCCEEEEEEEEEEEE		22.6928152594
110PhosphorylationGTLTVTNYRLYFKSM
CEEEEEEEEEEEEEC		7.8228152594
137UbiquitinationGVINRVEKIGGASSR
CHHHCCEECCCCCCC		43.74-
137AcetylationGVINRVEKIGGASSR
CHHHCCEECCCCCCC		43.7419823625
156UbiquitinationYGLETVCKDIRNLRF
CCHHHHHHHHHHCCC		52.43-
171PhosphorylationAHKPEGRTRRSIFEN
CCCCCCCCHHHHHHH		41.09-
260PhosphorylationEELKRVASFRSRGRI
HHHHHHHHHHHCCCC		20.5224719451
294AcetylationPMVGVSGKRSKEDEK
CCCCCCCCCCHHHHH		46.0911791337
301UbiquitinationKRSKEDEKYLQAIMD
CCCHHHHHHHHHHHC		64.68-
331UbiquitinationSVNAVANKAKGGGYE
HHHHHCHHCCCCCCC		41.56-
339PhosphorylationAKGGGYESEDAYQNA
CCCCCCCCCHHHHCC		32.09-
343PhosphorylationGYESEDAYQNAELVF
CCCCCHHHHCCEEEE		18.0227642862
424PhosphorylationCSDGWDRTAQLTSLA
CCCCCHHHHHHHHHH		19.1123663014
428PhosphorylationWDRTAQLTSLAMLML
CHHHHHHHHHHHHHH		15.0423663014
429PhosphorylationDRTAQLTSLAMLMLD
HHHHHHHHHHHHHHH		23.7923663014
438PhosphorylationAMLMLDGYYRTIRGF
HHHHHHCHHHHCCCE		6.8823663014
439PhosphorylationMLMLDGYYRTIRGFE
HHHHHCHHHHCCCEE		13.5523663014
558PhosphorylationFTNPLYGSYSNHVLY
CCCCCCCCCCCCCEE		16.3020068231
598UbiquitinationEPIHNRYKELLAKRA
CCCHHHHHHHHHHHH		38.35-
610UbiquitinationKRAELQKKVEELQRE
HHHHHHHHHHHHHHH		41.75-
619PhosphorylationEELQREISNRSTSSS
HHHHHHHHCCCCCCC		22.8026074081
622PhosphorylationQREISNRSTSSSERA
HHHHHCCCCCCCCCC		36.5726074081
623PhosphorylationREISNRSTSSSERAS
HHHHCCCCCCCCCCC		29.4126074081
624PhosphorylationEISNRSTSSSERASS
HHHCCCCCCCCCCCC		32.8726074081
625PhosphorylationISNRSTSSSERASSP
HHCCCCCCCCCCCCC		35.9926074081
626PhosphorylationSNRSTSSSERASSPA
HCCCCCCCCCCCCCC		30.7626074081
630PhosphorylationTSSSERASSPAQCVT
CCCCCCCCCCCCCCC		42.9730266825
631PhosphorylationSSSERASSPAQCVTP
CCCCCCCCCCCCCCC		24.2230266825
637PhosphorylationSSPAQCVTPVQTVV-
CCCCCCCCCCEECC-		25.9325159151
641PhosphorylationQCVTPVQTVV-----
CCCCCCEECC-----		24.3829632367
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
58SPhosphorylationKinaseMAPK1P28482
GPS
58SPhosphorylationKinaseMAPK3P27361
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
58SPhosphorylation

18669648
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 MTMR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTMR5_HUMANSBF1physical
12668758
MTMR2_HUMANMTMR2physical
12668758
RFC5_HUMANRFC5physical
22939629
HSF1_HUMANHSF1physical
22863883
XPP1_HUMANXPNPEP1physical
22863883
CCD22_HUMANCCDC22physical
27880917
MTMR1_HUMANMTMR1physical
27880917
MTMRA_HUMANMTMR10physical
27880917
MTMRC_HUMANMTMR12physical
27880917
NFKB1_HUMANNFKB1physical
27880917
MTMR5_HUMANSBF1physical
27880917
MTMRD_HUMANSBF2physical
27880917
TBA1B_HUMANTUBA1Bphysical
27880917
MTMR2_HUMANMTMR2physical
27432908
SPCS_HUMANSEPSECSphysical
27432908
MTMR1_HUMANMTMR1physical
27432908
NUD16_HUMANNUDT16physical
27432908
G45IP_HUMANGADD45GIP1physical
27432908
AROS_HUMANRPS19BP1physical
27432908
MTMRA_HUMANMTMR10physical
27432908
MRT4_HUMANMRTO4physical
27432908
EBP2_HUMANEBNA1BP2physical
27432908
RL3L_HUMANRPL3Lphysical
27432908
Drug and Disease Associations
Kegg Disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
601382Charcot-Marie-Tooth disease 4B1 (CMT4B1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTMR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Endosomal targeting of the phosphoinositide 3-phosphatase MTMR2 isregulated by an N-terminal phosphorylation site.";
Franklin N.E., Taylor G.S., Vacratsis P.O.;
J. Biol. Chem. 286:15841-15853(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-58.
"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-58, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.
"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-58, AND MASSSPECTROMETRY.

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