MIO_HUMAN - dbPTM
MIO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIO_HUMAN
UniProt AC Q9NXC5
Protein Name GATOR complex protein MIOS {ECO:0000305}
Gene Name MIOS {ECO:0000312|HGNC:HGNC:21905}
Organism Homo sapiens (Human).
Sequence Length 875
Subcellular Localization Lysosome membrane .
Protein Description As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. [PubMed: 23723238 It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1]
Protein Sequence MSGTKPDILWAPHHVDRFVVCDSELSLYHVESTVNSELKAGSLRLSEDSAATLLSINSDTPYMKCVAWYLNYDPECLLAVGQANGRVVLTSLGQDHNSKFKDLIGKEFVPKHARQCNTLAWNPLDSNWLAAGLDKHRADFSVLIWDICSKYTPDIVPMEKVKLSAGETETTLLVTKPLYELGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVNTKAVQGVTVDPYFHDRVASFYEGQVAIWDLRKFEKPVLTLTEQPKPLTKVAWCPTRTGLLATLTRDSNIIRLYDMQHTPTPIGDETEPTIIERSVQPCDNYIASFAWHPTSQNRMIVVTPNRTMSDFTVFERISLAWSPITSLMWACGRHLYECTEEENDNSLEKDIATKMRLRALSRYGLDTEQVWRNHILAGNEDPQLKSLWYTLHFMKQYTEDMDQKSPGNKGSLVYAGIKSIVKSSLGMVESSRHNWSGLDKQSDIQNLNEERILALQLCGWIKKGTDVDVGPFLNSLVQEGEWERAAAVALFNLDIRRAIQILNEGASSEKGDLNLNVVAMALSGYTDEKNSLWREMCSTLRLQLNNPYLCVMFAFLTSETGSYDGVLYENKVAVRDRVAFACKFLSDTQLNRYIEKLTNEMKEAGNLEGILLTGLTKDGVDLMESYVDRTGDVQTASYCMLQGSPLDVLKDERVQYWIENYRNLLDAWRFWHKRAEFDIHRSKLDPSSKPLAQVFVSCNFCGKSISYSCSAVPHQGRGFSQYGVSGSPTKSKVTSCPGCRKPLPRCALCLINMGTPVSSCPGGTKSDEKVDLSKDKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKCMQLDTTGNLVPAETVQP
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
2Phosphorylation------MSGTKPDIL
------CCCCCCCCC		55.99-
5Acetylation---MSGTKPDILWAP
---CCCCCCCCCCCC		44.1922424773
90PhosphorylationANGRVVLTSLGQDHN
ECCEEEEEECCCCCC		15.4222985185
99UbiquitinationLGQDHNSKFKDLIGK
CCCCCCHHHHHHHCC		62.8521890473
99 (in isoform 2)Ubiquitination-62.8521890473
99 (in isoform 1)Ubiquitination-62.8521890473
99AcetylationLGQDHNSKFKDLIGK
CCCCCCHHHHHHHCC		62.8523236377
99UbiquitinationLGQDHNSKFKDLIGK
CCCCCCHHHHHHHCC		62.8521890473
106UbiquitinationKFKDLIGKEFVPKHA
HHHHHHCCCCCCHHH		40.77-
231PhosphorylationTKAVQGVTVDPYFHD
CCCCCCEEECCHHHH		26.47-
235PhosphorylationQGVTVDPYFHDRVAS
CCEEECCHHHHHHHH		14.75-
280PhosphorylationVAWCPTRTGLLATLT
EEECCCCCCHHHHCC		34.36-
285PhosphorylationTRTGLLATLTRDSNI
CCCCHHHHCCCCCCE		28.73-
393UbiquitinationLEKDIATKMRLRALS
HHHHHHHHHHHHHHH		17.01-
429PhosphorylationQLKSLWYTLHFMKQY
HHHHHHHHHHHHHHH		11.3729507054
436PhosphorylationTLHFMKQYTEDMDQK
HHHHHHHHHHCCCCC		13.43-
444PhosphorylationTEDMDQKSPGNKGSL
HHCCCCCCCCCCCCH		32.1929214152
448UbiquitinationDQKSPGNKGSLVYAG
CCCCCCCCCCHHHHH		56.65-
450PhosphorylationKSPGNKGSLVYAGIK
CCCCCCCCHHHHHHH		19.10-
453PhosphorylationGNKGSLVYAGIKSIV
CCCCCHHHHHHHHHH		12.38-
479UbiquitinationHNWSGLDKQSDIQNL
CCCCCCCCHHHHCCC		57.6621890473
479 (in isoform 1)Ubiquitination-57.6621890473
479UbiquitinationHNWSGLDKQSDIQNL
CCCCCCCCHHHHCCC		57.6621890473
479 (in isoform 2)Ubiquitination-57.6621890473
481PhosphorylationWSGLDKQSDIQNLNE
CCCCCCHHHHCCCCH		42.28-
570PhosphorylationGYTDEKNSLWREMCS
CCCCCCCHHHHHHHH		40.1424719451
577PhosphorylationSLWREMCSTLRLQLN
HHHHHHHHHHHHHCC		29.21-
578PhosphorylationLWREMCSTLRLQLNN
HHHHHHHHHHHHCCC		15.80-
632PhosphorylationSDTQLNRYIEKLTNE
CHHHHHHHHHHHHHH		16.6229083192
664PhosphorylationDGVDLMESYVDRTGD
CCHHHHHHHCCCCCC		19.25-
665PhosphorylationGVDLMESYVDRTGDV
CHHHHHHHCCCCCCC		7.9622817900
727PhosphorylationRSKLDPSSKPLAQVF
HHHCCCCCCCHHHHH		43.6224719451
743PhosphorylationSCNFCGKSISYSCSA
CCCCCCCEEEEECCC		11.3126074081
745PhosphorylationNFCGKSISYSCSAVP
CCCCCEEEEECCCCC		20.3426074081
746PhosphorylationFCGKSISYSCSAVPH
CCCCEEEEECCCCCC		16.4226074081
747PhosphorylationCGKSISYSCSAVPHQ
CCCEEEEECCCCCCC		8.5326074081
749PhosphorylationKSISYSCSAVPHQGR
CEEEEECCCCCCCCC		26.7626074081
756MethylationSAVPHQGRGFSQYGV
CCCCCCCCCCCCCCC		36.09115483299
759PhosphorylationPHQGRGFSQYGVSGS
CCCCCCCCCCCCCCC		25.8923927012
761PhosphorylationQGRGFSQYGVSGSPT
CCCCCCCCCCCCCCC		20.4923927012
764PhosphorylationGFSQYGVSGSPTKSK
CCCCCCCCCCCCCCC		29.2322167270
766PhosphorylationSQYGVSGSPTKSKVT
CCCCCCCCCCCCCCC		23.1419664994
768PhosphorylationYGVSGSPTKSKVTSC
CCCCCCCCCCCCCCC		50.0422167270
769MalonylationGVSGSPTKSKVTSCP
CCCCCCCCCCCCCCC		52.2226320211
770PhosphorylationVSGSPTKSKVTSCPG
CCCCCCCCCCCCCCC		34.5329978859
773PhosphorylationSPTKSKVTSCPGCRK
CCCCCCCCCCCCCCC		28.48-
774PhosphorylationPTKSKVTSCPGCRKP
CCCCCCCCCCCCCCC		22.69-
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 MIO_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIO_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 MIO_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRAGA_HUMANRRAGAphysical
23723238
RRAGC_HUMANRRAGCphysical
23723238
CAST1_HUMANGATSL3physical
26972053
CAST2_HUMANGATSL2physical
26972053
AIPL1_HUMANAIPL1physical
27173435
FR1OP_HUMANFGFR1OPphysical
27173435
PDE5A_HUMANPDE5Aphysical
27173435
BLM_HUMANBLMphysical
27173435
SPT5H_HUMANSUPT5Hphysical
27173435
WDR24_HUMANWDR24physical
27173435
PATZ1_HUMANPATZ1physical
27173435
FKB15_HUMANFKBP15physical
27173435
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 MIO_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-766, 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-766, 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-766, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND MASSSPECTROMETRY.

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