MTMRC_HUMAN - dbPTM
MTMRC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTMRC_HUMAN
UniProt AC Q9C0I1
Protein Name Myotubularin-related protein 12
Gene Name MTMR12
Organism Homo sapiens (Human).
Sequence Length 747
Subcellular Localization Cytoplasm . Localizes to punctate vesicles when associated with MTM1.
Protein Description Catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularin intracellular location..
Protein Sequence MLGKGVVGGGGGTKAPKPSFVSYVRPEEIHTNEKEVTEKEVTLHLLPGEQLLCEASTVLKYVQEDSCQHGVYGRLVCTDFKIAFLGDDESALDNDETQFKNKVIGENDITLHCVDQIYGVFDEKKKTLFGQLKKYPEKLIIHCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQAPKLLKRLFLFSYATAAQNNTVTDPKNHTVMFDTLKDWCWELERTKGNMKYKAVSVNEGYKVCERLPAYFVVPTPLPEENVQRFQGHGIPIWCWSCHNGSALLKMSALPKEQDDGILQIQKSFLDGIYKTIHRPPYEIVKTEDLSSNFLSLQEIQTAYSKFKQLFLIDNSTEFWDTDIKWFSLLESSSWLDIIRRCLKKAIEITECMEAQNMNVLLLEENASDLCCLISSLVQLMMDPHCRTRIGFQSLIQKEWVMGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQLVHQHPPAFEFTETYLTVLSDSLYIPIFSTFFFNSPHQKDTNMGREGQDTQSKPLNLLTVWDWSVQFEPKAQTLLKNPLYVEKPKLDKGQRKGMRFKHQRQLSLPLTQSKSSPKRGFFREETDHLIKNLLGKRISKLINSSDELQDNFREFYDSWHSKSTDYHGLLLPHIEGPEIKVWAQRYLRWIPEAQILGGGQVATLSKLLEMMEEVQSLQEKIDERHHSQQAPQAEAPCLLRNSARLSSLFPFALLQRHSSKPVLPTSGWKALGDEDDLAKREDEFVDLGDV
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
4Ubiquitination----MLGKGVVGGGG
----CCCCCCCCCCC		44.57-
13PhosphorylationVVGGGGGTKAPKPSF
CCCCCCCCCCCCCCC		27.5821406692
14UbiquitinationVGGGGGTKAPKPSFV
CCCCCCCCCCCCCCE		67.0027667366
19PhosphorylationGTKAPKPSFVSYVRP
CCCCCCCCCEEECCH		44.3921406692
22PhosphorylationAPKPSFVSYVRPEEI
CCCCCCEEECCHHHC		18.8528796482
22UbiquitinationAPKPSFVSYVRPEEI
CCCCCCEEECCHHHC		18.8527667366
23PhosphorylationPKPSFVSYVRPEEIH
CCCCCEEECCHHHCC		8.6528796482
31PhosphorylationVRPEEIHTNEKEVTE
CCHHHCCCCCCCCCC		51.2229978859
72PhosphorylationDSCQHGVYGRLVCTD
CCCCCCCCCEEEECC		10.91-
91UbiquitinationFLGDDESALDNDETQ
EECCCHHHCCCCCHH		19.5222817900
100 (in isoform 3)Ubiquitination-46.1421890473
100 (in isoform 2)Ubiquitination-46.1421890473
100UbiquitinationDNDETQFKNKVIGEN
CCCCHHHCHHCCCCC		46.1421906983
100 (in isoform 1)Ubiquitination-46.1421890473
102UbiquitinationDETQFKNKVIGENDI
CCHHHCHHCCCCCCC		35.5022817900
123UbiquitinationQIYGVFDEKKKTLFG
HHEECCCHHHHCHHH		56.1422817900
124UbiquitinationIYGVFDEKKKTLFGQ
HEECCCHHHHCHHHH		62.5132015554
130UbiquitinationEKKKTLFGQLKKYPE
HHHHCHHHHHHHCCC		34.7222817900
132UbiquitinationKKTLFGQLKKYPEKL
HHCHHHHHHHCCCCE		5.4522817900
133UbiquitinationKTLFGQLKKYPEKLI
HCHHHHHHHCCCCEE		42.2323000965
133MalonylationKTLFGQLKKYPEKLI
HCHHHHHHHCCCCEE		42.2332601280
134UbiquitinationTLFGQLKKYPEKLII
CHHHHHHHCCCCEEE		74.7123000965
135PhosphorylationLFGQLKKYPEKLIIH
HHHHHHHCCCCEEEE		18.29-
138 (in isoform 1)Ubiquitination-40.2521890473
138 (in isoform 2)Ubiquitination-40.2521890473
138UbiquitinationQLKKYPEKLIIHCKD
HHHHCCCCEEEEECH		40.2523000965
138 (in isoform 3)Ubiquitination-40.2521890473
138AcetylationQLKKYPEKLIIHCKD
HHHHCCCCEEEEECH		40.2525953088
144UbiquitinationEKLIIHCKDLRVFQF
CCEEEEECHHHHHHH		45.7123000965
162AcetylationYTKEEEVKRIVSGII
CCCHHHHHHHHHHHH		39.4218603167
162UbiquitinationYTKEEEVKRIVSGII
CCCHHHHHHHHHHHH		39.4222817900
164UbiquitinationKEEEVKRIVSGIIHH
CHHHHHHHHHHHHHH		2.1022817900
185PhosphorylationLKRLFLFSYATAAQN
HHHHHHHHHHHHHHC		18.9223663014
186PhosphorylationKRLFLFSYATAAQNN
HHHHHHHHHHHHHCC		10.7123663014
188PhosphorylationLFLFSYATAAQNNTV
HHHHHHHHHHHCCCC		17.8123663014
194PhosphorylationATAAQNNTVTDPKNH
HHHHHCCCCCCCCCC		32.1223663014
196PhosphorylationAAQNNTVTDPKNHTV
HHHCCCCCCCCCCEE		44.5423663014
225UbiquitinationTKGNMKYKAVSVNEG
CCCCCEEEEEEECCC		36.4727667366
233PhosphorylationAVSVNEGYKVCERLP
EEEECCCHHHHHCCC		8.2826546556
234UbiquitinationVSVNEGYKVCERLPA
EEECCCHHHHHCCCE		51.79-
294 (in isoform 1)Ubiquitination-44.8221890473
294 (in isoform 2)Ubiquitination-44.8221890473
294UbiquitinationDGILQIQKSFLDGIY
CCCHHHHHHHHHHHH		44.8221906983
294 (in isoform 3)Ubiquitination-44.8221890473
295PhosphorylationGILQIQKSFLDGIYK
CCHHHHHHHHHHHHH		18.05-
309PhosphorylationKTIHRPPYEIVKTED
HHCCCCCCEEEECCC		22.44-
326UbiquitinationSNFLSLQEIQTAYSK
CCCCCHHHHHHHHHH		42.2122817900
333UbiquitinationEIQTAYSKFKQLFLI
HHHHHHHHHHHEEEC		43.8622817900
333 (in isoform 1)Ubiquitination-43.8621890473
333 (in isoform 2)Ubiquitination-43.8621890473
333 (in isoform 3)Ubiquitination-43.8621890473
335UbiquitinationQTAYSKFKQLFLIDN
HHHHHHHHHEEECCC		50.2422817900
365UbiquitinationESSSWLDIIRRCLKK
HCCHHHHHHHHHHHH		2.1822817900
367UbiquitinationSSWLDIIRRCLKKAI
CHHHHHHHHHHHHHH		24.4822817900
377PhosphorylationLKKAIEITECMEAQN
HHHHHHHHHHHHHHC		15.44-
395PhosphorylationLLLEENASDLCCLIS
EEEECCHHHHHHHHH		42.57-
454 (in isoform 3)Phosphorylation-2.4529743597
454PhosphorylationEEVPVFLLFLDCVWQ
CCCCHHHHHHHHHHH		2.4532142685
487UbiquitinationLSDSLYIPIFSTFFF
HCCCCCEEEEEEECC		14.1729967540
502 (in isoform 2)Phosphorylation-33.8520068231
509UbiquitinationTNMGREGQDTQSKPL
CCCCCCCCCCCCCCC		45.9129967540
510 (in isoform 2)Phosphorylation-58.5320068231
510PhosphorylationNMGREGQDTQSKPLN
CCCCCCCCCCCCCCC		58.5332142685
513PhosphorylationREGQDTQSKPLNLLT
CCCCCCCCCCCCEEE		38.0324719451
514 (in isoform 2)Phosphorylation-43.6420068231
516 (in isoform 2)Phosphorylation-8.9620068231
518 (in isoform 2)Phosphorylation-5.8220068231
519 (in isoform 2)Phosphorylation-3.3620068231
537UbiquitinationPKAQTLLKNPLYVEK
CHHHHHHCCCEEECC		60.6829967540
543UbiquitinationLKNPLYVEKPKLDKG
HCCCEEECCCCCCCC		50.5129967540
544UbiquitinationKNPLYVEKPKLDKGQ
CCCEEECCCCCCCCC		37.0929967540
564PhosphorylationFKHQRQLSLPLTQSK
CCHHHHCCCCCCCCC		21.4322167270
565UbiquitinationKHQRQLSLPLTQSKS
CHHHHCCCCCCCCCC		5.6829967540
568PhosphorylationRQLSLPLTQSKSSPK
HHCCCCCCCCCCCCC		28.9330266825
570PhosphorylationLSLPLTQSKSSPKRG
CCCCCCCCCCCCCCC		29.3030266825
572PhosphorylationLPLTQSKSSPKRGFF
CCCCCCCCCCCCCCC		58.0617924679
573PhosphorylationPLTQSKSSPKRGFFR
CCCCCCCCCCCCCCH		37.8729214152
593AcetylationLIKNLLGKRISKLIN
HHHHHHHHHHHHHHC		46.6730590515
596PhosphorylationNLLGKRISKLINSSD
HHHHHHHHHHHCCCH		25.9929978859
597AcetylationLLGKRISKLINSSDE
HHHHHHHHHHCCCHH		51.5230590521
597UbiquitinationLLGKRISKLINSSDE
HHHHHHHHHHCCCHH		51.5229967540
601PhosphorylationRISKLINSSDELQDN
HHHHHHCCCHHHHHH		31.9725159151
602PhosphorylationISKLINSSDELQDNF
HHHHHCCCHHHHHHH		30.5325159151
606PhosphorylationINSSDELQDNFREFY
HCCCHHHHHHHHHHH		41.3732645325
619UbiquitinationFYDSWHSKSTDYHGL
HHHHHHCCCCCCCCC		44.4829967540
662PhosphorylationGGQVATLSKLLEMME
CHHHHHHHHHHHHHH		19.5332645325
684PhosphorylationKIDERHHSQQAPQAE
HHHHHHHHCCCCCCH		20.1928555341
699PhosphorylationAPCLLRNSARLSSLF
HCHHHCCHHHHHHHH		14.3428348404
703PhosphorylationLRNSARLSSLFPFAL
HCCHHHHHHHHHHHH		21.3124719451
704PhosphorylationRNSARLSSLFPFALL
CCHHHHHHHHHHHHH		38.3228857561
715PhosphorylationFALLQRHSSKPVLPT
HHHHHHCCCCCCCCC		42.1023403867
716PhosphorylationALLQRHSSKPVLPTS
HHHHHCCCCCCCCCC		34.5522617229
722PhosphorylationSSKPVLPTSGWKALG
CCCCCCCCCHHHHHC		35.3923403867
723PhosphorylationSKPVLPTSGWKALGD
CCCCCCCCHHHHHCC		40.4923403867
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 MTMRC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTMRC_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 MTMRC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPL4_HUMANNPLOC4physical
26344197
MTMRC_HUMANMTMR12physical
27432908
THEM6_HUMANTHEM6physical
27432908
ARK72_HUMANAKR7A2physical
27432908
VAPB_HUMANVAPBphysical
27432908
SCO2_HUMANSCO2physical
27432908
NDUAD_HUMANNDUFA13physical
27432908
ANFC_HUMANNPPCphysical
27432908
VAPA_HUMANVAPAphysical
27432908
TIM21_HUMANTIMM21physical
27432908
CY1_HUMANCYC1physical
27432908
GMPPB_HUMANGMPPBphysical
27432908
NDUS8_HUMANNDUFS8physical
27432908
SCO1_HUMANSCO1physical
27432908
1C07_HUMANHLA-Cphysical
27432908
SFXN4_HUMANSFXN4physical
27432908
DUS1_HUMANDUSP1physical
27432908
HAUS8_HUMANHAUS8physical
28514442
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 MTMRC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-572 AND SER-573, ANDMASS SPECTROMETRY.

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