MTMRA_HUMAN - dbPTM
MTMRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTMRA_HUMAN
UniProt AC Q9NXD2
Protein Name Myotubularin-related protein 10
Gene Name MTMR10
Organism Homo sapiens (Human).
Sequence Length 777
Subcellular Localization
Protein Description Probable pseudophosphatase. Contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential)..
Protein Sequence MFSLKPPKPTFRSYLLPPPQTDDKINSEPKIKKLEPVLLPGEIVVNEVNFVRKCIATDTSQYDLWGKLICSNFKISFITDDPMPLQKFHYRNLLLGEHDVPLTCIEQIVTVNDHKRKQKVLGPNQKLKFNPTELIIYCKDFRIVRFRFDESGPESAKKVCLAIAHYSQPTDLQLLFAFEYVGKKYHNSANKINGIPSGDGGGGGGGGNGAGGGSSQKTPLFETYSDWDREIKRTGASGWRVCSINEGYMISTCLPEYIVVPSSLADQDLKIFSHSFVGRRMPLWCWSHSNGSALVRMALIKDVLQQRKIDQRICNAITKSHPQRSDVYKSDLDKTLPNIQEVQAAFVKLKQLCVNEPFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKESPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYDSTRISLFGTFLFNSPHQRVKQSTEFAISKNIQLGDEKGLKFPSVWDWSLQFTAKDRTLFHNPFYIGKSTPCIQNGSVKSFKRTKKSYSSTLRGMPSALKNGIISDQELLPRRNSLILKPKPDPAQQTDSQNSDTEQYFREWFSKPANLHGVILPRVSGTHIKLWKLCYFRWVPEAQISLGGSITAFHKLSLLADEVDVLSRMLRQQRSGPLEACYGELGQSRMYFNASGPHHTDTSGTPEFLSSSFPFSPVGNLCRRSILGTPLSKFLSGAKIWLSTETLANED
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
8UbiquitinationMFSLKPPKPTFRSYL
CCCCCCCCCCCHHHC		66.28-
87UbiquitinationDDPMPLQKFHYRNLL
CCCCCHHHHHHCCCC		41.62-
137PhosphorylationNPTELIIYCKDFRIV
CCCEEEEEECCCEEE		6.10-
224PhosphorylationKTPLFETYSDWDREI
CCCCEECCCCHHHHH		9.4625999147
225PhosphorylationTPLFETYSDWDREIK
CCCEECCCCHHHHHH		39.3825999147
251PhosphorylationINEGYMISTCLPEYI
ECCCEEEEECCCCEE		9.1323663014
252PhosphorylationNEGYMISTCLPEYIV
CCCEEEEECCCCEEE		13.7223663014
257PhosphorylationISTCLPEYIVVPSSL
EEECCCCEEECCHHH		9.3323663014
262PhosphorylationPEYIVVPSSLADQDL
CCEEECCHHHCCCCC		26.7823663014
263PhosphorylationEYIVVPSSLADQDLK
CEEECCHHHCCCCCH		22.8523663014
275PhosphorylationDLKIFSHSFVGRRMP
CCHHHCCCCCCCCCC		22.0428857561
292PhosphorylationCWSHSNGSALVRMAL
EEECCCCHHHHHHHH		23.7622210691
319UbiquitinationRICNAITKSHPQRSD
HHHHHHHHCCCCHHH		40.42-
350UbiquitinationQAAFVKLKQLCVNEP
HHHHHHHHHHHHCCC		35.19-
367O-linked_GlycosylationETEEKWLSSLENTRW
HHHHHHHHHHHHHHH		31.5930379171
368O-linked_GlycosylationTEEKWLSSLENTRWL
HHHHHHHHHHHHHHH		37.2230379171
427PhosphorylationMLDPYFRTITGFQSL
HHCHHHHHHHCHHHH		17.00-
522UbiquitinationSTEFAISKNIQLGDE
HHHEHHHCCCCCCCC		52.54-
530UbiquitinationNIQLGDEKGLKFPSV
CCCCCCCCCCCCCCH		74.43-
561PhosphorylationNPFYIGKSTPCIQNG
CCEECCCCCCCCCCC		32.1623403867
562PhosphorylationPFYIGKSTPCIQNGS
CEECCCCCCCCCCCC		26.1823403867
569PhosphorylationTPCIQNGSVKSFKRT
CCCCCCCCCCCCCCC		33.6425159151
572PhosphorylationIQNGSVKSFKRTKKS
CCCCCCCCCCCCCHH		33.5721712546
579PhosphorylationSFKRTKKSYSSTLRG
CCCCCCHHHHHHHCC		31.6323312004
580PhosphorylationFKRTKKSYSSTLRGM
CCCCCHHHHHHHCCC		18.6027642862
581PhosphorylationKRTKKSYSSTLRGMP
CCCCHHHHHHHCCCC		24.7628857561
582PhosphorylationRTKKSYSSTLRGMPS
CCCHHHHHHHCCCCH		24.1925159151
583PhosphorylationTKKSYSSTLRGMPSA
CCHHHHHHHCCCCHH		17.9725159151
607PhosphorylationELLPRRNSLILKPKP
HHCCCCCCEEECCCC		18.2528731282
611UbiquitinationRRNSLILKPKPDPAQ
CCCCEEECCCCCHHH		43.96-
613UbiquitinationNSLILKPKPDPAQQT
CCEEECCCCCHHHCC		61.54-
620PhosphorylationKPDPAQQTDSQNSDT
CCCHHHCCCCCCCHH		26.0723403867
622PhosphorylationDPAQQTDSQNSDTEQ
CHHHCCCCCCCHHHH		34.3523663014
625PhosphorylationQQTDSQNSDTEQYFR
HCCCCCCCHHHHHHH		37.9723663014
627PhosphorylationTDSQNSDTEQYFREW
CCCCCCHHHHHHHHH		25.4723663014
630PhosphorylationQNSDTEQYFREWFSK
CCCHHHHHHHHHHCC		9.8127732954
701PhosphorylationRMLRQQRSGPLEACY
HHHHHHCCCCHHHHH		40.1921945579
708PhosphorylationSGPLEACYGELGQSR
CCCHHHHHHHCCCCE		22.2321945579
714PhosphorylationCYGELGQSRMYFNAS
HHHHCCCCEEEEECC		19.7421945579
751PhosphorylationVGNLCRRSILGTPLS
CCHHHHHHHCCCCHH		11.6525159151
755PhosphorylationCRRSILGTPLSKFLS
HHHHHCCCCHHHHHH		20.0130266825
758PhosphorylationSILGTPLSKFLSGAK
HHCCCCHHHHHHCCE		23.6730266825
769PhosphorylationSGAKIWLSTETLANE
HCCEEEEEHHHHCCC		14.8126846344
770PhosphorylationGAKIWLSTETLANED
CCEEEEEHHHHCCCC		30.7126846344
772PhosphorylationKIWLSTETLANED--
EEEEEHHHHCCCC--		31.1228176443
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 MTMRA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTMRA_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 MTMRA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEOX2_HUMANMEOX2physical
24722188
MTMRA_HUMANMTMR10physical
27432908
MTM1_HUMANMTM1physical
27432908
MTMR2_HUMANMTMR2physical
27432908
LONP2_HUMANLONP2physical
27432908
PRPK_HUMANTP53RKphysical
27432908
NMNA1_HUMANNMNAT1physical
27432908
OSGEP_HUMANOSGEPphysical
27432908
NUD16_HUMANNUDT16physical
27432908
G45IP_HUMANGADD45GIP1physical
27432908
IDE_HUMANIDEphysical
27432908
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 MTMRA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-770, AND MASSSPECTROMETRY.

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