MTMRE_HUMAN - dbPTM
MTMRE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTMRE_HUMAN
UniProt AC Q8NCE2
Protein Name Myotubularin-related protein 14
Gene Name MTMR14
Organism Homo sapiens (Human).
Sequence Length 650
Subcellular Localization Cytoplasm . Found in reticular structures and plasma membrane ruffles. Concentrated near the nucleus.
Protein Description Lipid phosphatase which efficiently dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3..
Protein Sequence MAGARAAAAAASAGSSASSGNQPPQELGLGELLEEFSRTQYRAKDGSGTGGSKVERIEKRCLELFGRDYCFSVIPNTNGDICGHYPRHIVFLEYESSEKEKDTFESTVQVSKLQDLIHRSKMARCRGRFVCPVILFKGKHICRSATLAGWGELYGRSGYNYFFSGGADDAWADVEDVTEEDCALRSGDTHLFDKVRGYDIKLLRYLSVKYICDLMVENKKVKFGMNVTSSEKVDKAQRYADFTLLSIPYPGCEFFKEYKDRDYMAEGLIFNWKQDYVDAPLSIPDFLTHSLNIDWSQYQCWDLVQQTQNYLKLLLSLVNSDDDSGLLVHCISGWDRTPLFISLLRLSLWADGLIHTSLKPTEILYLTVAYDWFLFGHMLVDRLSKGEEIFFFCFNFLKHITSEEFSALKTQRRKSLPARDGGFTLEDICMLRRKDRGSTTSLGSDFSLVMESSPGATGSFTYEAVELVPAGAPTQAAWRKSHSSSPQSVLWNRPQPSEDRLPSQQGLAEARSSSSSSSNHSDNFFRMGSSPLEVPKPRSVDHPLPGSSLSTDYGSWQMVTGCGSIQERAVLHTDSSLPFSFPDELPNSCLLAALSDRETRLQEVRSAFLAAYSSTVGLRAVAPSPSGAIGGLLEQFARGVGLRSISSNAL
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
47PhosphorylationQYRAKDGSGTGGSKV
CCCCCCCCCCCCHHH		43.23-
49PhosphorylationRAKDGSGTGGSKVER
CCCCCCCCCCHHHHH		39.81-
52PhosphorylationDGSGTGGSKVERIEK
CCCCCCCHHHHHHHH		34.57-
101UbiquitinationYESSEKEKDTFESTV
ECCCHHHCCCHHHHH		73.47-
106PhosphorylationKEKDTFESTVQVSKL
HHCCCHHHHHHHHHH		29.6823403867
107PhosphorylationEKDTFESTVQVSKLQ
HCCCHHHHHHHHHHH		14.0423403867
112UbiquitinationESTVQVSKLQDLIHR
HHHHHHHHHHHHHHH		51.84-
120PhosphorylationLQDLIHRSKMARCRG
HHHHHHHHHHHHCCC		16.7826074081
154PhosphorylationLAGWGELYGRSGYNY
CCCHHHHHCCCCCCE		13.2429978859
194MalonylationGDTHLFDKVRGYDIK
CCCCHHHHCCCCCHH		26.8826320211
194UbiquitinationGDTHLFDKVRGYDIK
CCCCHHHHCCCCCHH		26.8821890473
194AcetylationGDTHLFDKVRGYDIK
CCCCHHHHCCCCCHH		26.8819608861
201UbiquitinationKVRGYDIKLLRYLSV
HCCCCCHHHHHHHCH		38.27-
210PhosphorylationLRYLSVKYICDLMVE
HHHHCHHHHHHHHCC		12.48-
226N-linked_GlycosylationKKVKFGMNVTSSEKV
CCEEEECCCCCHHHC		34.00UniProtKB CARBOHYD
228PhosphorylationVKFGMNVTSSEKVDK
EEEECCCCCHHHCCH		22.8724505115
409 (in isoform 2)Ubiquitination-42.1821890473
409 (in isoform 1)Ubiquitination-42.1821890473
409 (in isoform 3)Ubiquitination-42.1821890473
409UbiquitinationSEEFSALKTQRRKSL
HHHHHHHHHHHHHCC		42.1821890473
415PhosphorylationLKTQRRKSLPARDGG
HHHHHHHCCCCCCCC		37.4622617229
424PhosphorylationPARDGGFTLEDICML
CCCCCCCCHHHHHEE		32.2928450419
452PhosphorylationDFSLVMESSPGATGS
CEEEEEECCCCCCCC		24.6024275569
462PhosphorylationGATGSFTYEAVELVP
CCCCCEEEEEEEEEC		10.40-
462 (in isoform 3)Phosphorylation-10.4022210691
474 (in isoform 3)Phosphorylation-30.2422210691
481PhosphorylationTQAAWRKSHSSSPQS
CHHHHHHHCCCCCCC		21.7425159151
483PhosphorylationAAWRKSHSSSPQSVL
HHHHHHCCCCCCCCC		39.3327732954
484PhosphorylationAWRKSHSSSPQSVLW
HHHHHCCCCCCCCCC		40.3825849741
485PhosphorylationWRKSHSSSPQSVLWN
HHHHCCCCCCCCCCC		29.9425159151
488PhosphorylationSHSSSPQSVLWNRPQ
HCCCCCCCCCCCCCC		23.6727732954
497PhosphorylationLWNRPQPSEDRLPSQ
CCCCCCCCCCCCCCH		47.0527732954
503PhosphorylationPSEDRLPSQQGLAEA
CCCCCCCCHHHHHHH		39.4617924679
512PhosphorylationQGLAEARSSSSSSSN
HHHHHHHCCCCCCCC		41.4428450419
513PhosphorylationGLAEARSSSSSSSNH
HHHHHHCCCCCCCCC		28.7828450419
514PhosphorylationLAEARSSSSSSSNHS
HHHHHCCCCCCCCCC		35.1725849741
515PhosphorylationAEARSSSSSSSNHSD
HHHHCCCCCCCCCCC		35.8723186163
516PhosphorylationEARSSSSSSSNHSDN
HHHCCCCCCCCCCCC		39.4723186163
517PhosphorylationARSSSSSSSNHSDNF
HHCCCCCCCCCCCCC		36.7928450419
518PhosphorylationRSSSSSSSNHSDNFF
HCCCCCCCCCCCCCC		40.2723312004
519N-linked_GlycosylationSSSSSSSNHSDNFFR
CCCCCCCCCCCCCCC		40.40UniProtKB CARBOHYD
521PhosphorylationSSSSSNHSDNFFRMG
CCCCCCCCCCCCCCC		38.2023186163
529PhosphorylationDNFFRMGSSPLEVPK
CCCCCCCCCCCCCCC		21.3129255136
530 (in isoform 2)Phosphorylation-27.9825849741
530PhosphorylationNFFRMGSSPLEVPKP
CCCCCCCCCCCCCCC		27.9829255136
539PhosphorylationLEVPKPRSVDHPLPG
CCCCCCCCCCCCCCC		40.19-
547PhosphorylationVDHPLPGSSLSTDYG
CCCCCCCCCCCCCCC		26.6027080861
548PhosphorylationDHPLPGSSLSTDYGS
CCCCCCCCCCCCCCC		32.0527080861
550PhosphorylationPLPGSSLSTDYGSWQ
CCCCCCCCCCCCCEE		22.6027080861
551PhosphorylationLPGSSLSTDYGSWQM
CCCCCCCCCCCCEEE		38.2327080861
553PhosphorylationGSSLSTDYGSWQMVT
CCCCCCCCCCEEEEC		17.1027080861
555PhosphorylationSLSTDYGSWQMVTGC
CCCCCCCCEEEECCC		14.1227080861
573PhosphorylationQERAVLHTDSSLPFS
CCEEEEECCCCCCCC		33.1528450419
575PhosphorylationRAVLHTDSSLPFSFP
EEEEECCCCCCCCCC		34.6228450419
576PhosphorylationAVLHTDSSLPFSFPD
EEEECCCCCCCCCCC		42.7626657352
580PhosphorylationTDSSLPFSFPDELPN
CCCCCCCCCCCCCCC		33.6528450419
606PhosphorylationTRLQEVRSAFLAAYS
HHHHHHHHHHHHHHH		28.6617924679
613PhosphorylationSAFLAAYSSTVGLRA
HHHHHHHHCCCCCEE		18.1417924679
615PhosphorylationFLAAYSSTVGLRAVA
HHHHHHCCCCCEEEC		16.8017924679
624PhosphorylationGLRAVAPSPSGAIGG
CCEEECCCCCCHHHH		23.2021712546
626PhosphorylationRAVAPSPSGAIGGLL
EEECCCCCCHHHHHH		45.2328102081
638MethylationGLLEQFARGVGLRSI
HHHHHHHHHCCCHHH		41.4324129315
644PhosphorylationARGVGLRSISSNAL-
HHHCCCHHHCCCCC-		31.6828102081
646PhosphorylationGVGLRSISSNAL---
HCCCHHHCCCCC---		20.8428102081
647PhosphorylationVGLRSISSNAL----
CCCHHHCCCCC----		25.1824719451
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 MTMRE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTMRE_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 MTMRE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ACSL3_HUMANACSL3physical
27880917
ACSL4_HUMANACSL4physical
27880917
ATX10_HUMANATXN10physical
27880917
GBRAP_HUMANGABARAPphysical
27880917
DHB12_HUMANHSD17B12physical
27880917
IDE_HUMANIDEphysical
27880917
PLK1_HUMANPLK1physical
27880917
POSTN_HUMANPOSTNphysical
27880917
RAB10_HUMANRAB10physical
27880917
SCPDL_HUMANSCCPDHphysical
27880917
LAP2A_HUMANTMPOphysical
27880917
LAP2B_HUMANTMPOphysical
27880917
MTMRE_HUMANMTMR14physical
27432908
DBLOH_HUMANDIABLOphysical
27432908
AFAM_HUMANAFMphysical
27432908
BPIB1_HUMANBPIFB1physical
27432908
SOAT1_HUMANSOAT1physical
27432908
GNB1L_HUMANGNB1Lphysical
27432908
SEH1_HUMANSEH1Lphysical
27432908
TRAF2_HUMANTRAF2physical
27432908
GMPPA_HUMANGMPPAphysical
27432908
MISSL_HUMANMAPK1IP1Lphysical
27432908
ANFC_HUMANNPPCphysical
27432908
CDK4_HUMANCDK4physical
27432908
ADPPT_HUMANAASDHPPTphysical
27432908
ACOT8_HUMANACOT8physical
27432908
PDIA6_HUMANPDIA6physical
27432908
PLK1_HUMANPLK1physical
27432908
ARK72_HUMANAKR7A2physical
27432908
CARM1_HUMANCARM1physical
27432908
SCO2_HUMANSCO2physical
27432908
SFXN4_HUMANSFXN4physical
27432908
ACAD8_HUMANACAD8physical
27432908
P5CR3_HUMANPYCRLphysical
27432908
DUS7_HUMANDUSP7physical
27432908
IDE_HUMANIDEphysical
27432908
WDR54_HUMANWDR54physical
28514442
PLSI_HUMANPLS1physical
28514442
PDP1_HUMANPDP1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
160150Myopathy, centronuclear, 1 (CNM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTMRE_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND SER-624, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606; SER-613 ANDTHR-615, AND MASS SPECTROMETRY.

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