MTA70_HUMAN - dbPTM
MTA70_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTA70_HUMAN
UniProt AC Q86U44
Protein Name N6-adenosine-methyltransferase catalytic subunit {ECO:0000305}
Gene Name METTL3 {ECO:0000312|HGNC:HGNC:17563}
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with speckles in interphase nuclei, suggesting that it may be associated with nuclear pre-mRNA splicing components (PubMed:9409616). In response to ultraviolet irradiation, colocalizes to DNA damage
Protein Description The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and haematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing. [PubMed: 22575960]
Protein Sequence MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGGPKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLLQKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRAEQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSKKVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVGGDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL
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
2Acetylation------MSDTWSSIQ
------CCCHHHHHH		43.6929348140
2Phosphorylation------MSDTWSSIQ
------CCCHHHHHH		43.6925159151
12AcetylationWSSIQAHKKQLDSLR
HHHHHHHHHHHHHHH		45.2725953088
17PhosphorylationAHKKQLDSLRERLQR
HHHHHHHHHHHHHHH		37.6128355574
27UbiquitinationERLQRRRKQDSGHLD
HHHHHHHHHHCCCCC		57.5629967540
30PhosphorylationQRRRKQDSGHLDLRN
HHHHHHHCCCCCCCC		26.1430266825
36MethylationDSGHLDLRNPEAALS
HCCCCCCCCHHHHHC		57.22115483191
43PhosphorylationRNPEAALSPTFRSDS
CCHHHHHCCCCCCCC		19.7119664994
45PhosphorylationPEAALSPTFRSDSPV
HHHHHCCCCCCCCCC		28.4530266825
48PhosphorylationALSPTFRSDSPVPTA
HHCCCCCCCCCCCCC		37.9423401153
50PhosphorylationSPTFRSDSPVPTAPT
CCCCCCCCCCCCCCC		29.1029255136
54PhosphorylationRSDSPVPTAPTSGGP
CCCCCCCCCCCCCCC		45.5721955146
57PhosphorylationSPVPTAPTSGGPKPS
CCCCCCCCCCCCCCC		37.2225159151
58PhosphorylationPVPTAPTSGGPKPST
CCCCCCCCCCCCCCC		40.4725159151
64PhosphorylationTSGGPKPSTASAVPE
CCCCCCCCCCCCCCH		42.6121955146
65PhosphorylationSGGPKPSTASAVPEL
CCCCCCCCCCCCCHH		32.9121955146
67PhosphorylationGPKPSTASAVPELAT
CCCCCCCCCCCHHHC		29.8621955146
74PhosphorylationSAVPELATDPELEKK
CCCCHHHCCHHHHHH		65.7920068231
80UbiquitinationATDPELEKKLLHHLS
HCCHHHHHHHHHHHH		62.4433845483
132SumoylationAQELIEVKRGLLQDD
HHHHHHHHCCCCCCC		28.14-
132SumoylationAQELIEVKRGLLQDD
HHHHHHHHCCCCCCC		28.14-
132UbiquitinationAQELIEVKRGLLQDD
HHHHHHHHCCCCCCC		28.1432015554
151PhosphorylationLVTYADHSKLSAMMG
EEEECCHHHHHHHHH		35.5228555341
152AcetylationVTYADHSKLSAMMGA
EEECCHHHHHHHHHH		42.9425953088
174PhosphorylationGEVAGTVTGQKRRAE
CCEECEECCCCCCCC		33.4628555341
175UbiquitinationEVAGTVTGQKRRAEQ
CEECEECCCCCCCCC		27.0321963094
177SumoylationAGTVTGQKRRAEQDS
ECEECCCCCCCCCCH		45.2429506078
196PhosphorylationAFASSLVSGLNSSAS
HHHHHHHHCCCCCCC		42.7421712546
200PhosphorylationSLVSGLNSSASEPAK
HHHHCCCCCCCCCCC		32.1221712546
201PhosphorylationLVSGLNSSASEPAKE
HHHCCCCCCCCCCCC		34.4428555341
203PhosphorylationSGLNSSASEPAKEPA
HCCCCCCCCCCCCCC		46.1729214152
204UbiquitinationGLNSSASEPAKEPAK
CCCCCCCCCCCCCCH		49.3321963094
211SumoylationEPAKEPAKKSRKHAA
CCCCCCCHHHHHHHH		63.1029506078
212SumoylationPAKEPAKKSRKHAAS
CCCCCCHHHHHHHHC		58.5629506078
215UbiquitinationEPAKKSRKHAASDVD
CCCHHHHHHHHCHHH		44.6929967540
215SumoylationEPAKKSRKHAASDVD
CCCHHHHHHHHCHHH		44.6929506078
219PhosphorylationKSRKHAASDVDLEIE
HHHHHHHCHHHHHHH		38.6625159151
227PhosphorylationDVDLEIESLLNQQST
HHHHHHHHHHCCCCC		43.7628387310
233PhosphorylationESLLNQQSTKEQQSK
HHHHCCCCCHHHHHH		31.5120873877
234PhosphorylationSLLNQQSTKEQQSKK
HHHCCCCCHHHHHHH		33.9720873877
235UbiquitinationLLNQQSTKEQQSKKV
HHCCCCCHHHHHHHH		59.7929967540
241UbiquitinationTKEQQSKKVSQEILE
CHHHHHHHHHHHHHH		52.9829967540
243PhosphorylationEQQSKKVSQEILELL
HHHHHHHHHHHHHHH		30.8625159151
252PhosphorylationEILELLNTTTAKEQS
HHHHHHCCCCHHHHH		26.0328555341
253PhosphorylationILELLNTTTAKEQSI
HHHHHCCCCHHHHHH		24.5527050516
256UbiquitinationLLNTTTAKEQSIVEK
HHCCCCHHHHHHHHH		54.9529967540
263UbiquitinationKEQSIVEKFRSRGRA
HHHHHHHHHHHCCCH		34.8729967540
281AcetylationEFCDYGTKEECMKAS
HHHCCCCHHHHHHHC		47.3425953088
305UbiquitinationHFRRIINKHTDESLG
HHHHHHHHCCCCCCC		37.16-
315PhosphorylationDESLGDCSFLNTCFH
CCCCCCCCCCCCEEC		37.1921712546
344PhosphorylationMDSEAPGSKDHTPSQ
CCCCCCCCCCCCCHH		33.5725159151
348PhosphorylationAPGSKDHTPSQELAL
CCCCCCCCCHHHEEE		34.4730266825
350PhosphorylationGSKDHTPSQELALTQ
CCCCCCCHHHEEEEE		37.1317525332
356PhosphorylationPSQELALTQSVGGDS
CHHHEEEEECCCCCC		17.1217525332
358PhosphorylationQELALTQSVGGDSSA
HHEEEEECCCCCCCH		19.9320873877
363PhosphorylationTQSVGGDSSADRLFP
EECCCCCCCHHHHCC		30.6020873877
364PhosphorylationQSVGGDSSADRLFPP
ECCCCCCCHHHHCCC		38.6420873877
459UbiquitinationVDEIIWVKTNQLQRI
CCEEEEEEHHHHHHH		27.1121963094
480UbiquitinationGHWLNHGKEHCLVGV
CCCCCCCCCCEEEEE		36.4129967540
488UbiquitinationEHCLVGVKGNPQGFN
CCEEEEECCCCCCCC		47.2221963094
513UbiquitinationEVRSTSHKPDEIYGM
EEHHCCCCCCHHHHH		54.66-
518PhosphorylationSHKPDEIYGMIERLS
CCCCCHHHHHHHHCC		9.9027642862
566UbiquitinationPDVVARFKQRYPDGI
HHHHHHHHHHCCCCC		28.45-
575PhosphorylationRYPDGIISKPKNL--
HCCCCCCCCCCCC--		40.7724719451
576UbiquitinationYPDGIISKPKNL---
CCCCCCCCCCCC---		49.9929967540
576AcetylationYPDGIISKPKNL---
CCCCCCCCCCCC---		49.9925953088
578UbiquitinationDGIISKPKNL-----
CCCCCCCCCC-----		74.70-
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 MTA70_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTA70_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 MTA70_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET14_HUMANMETTL14physical
22939629
ROBO2_HUMANROBO2physical
26496610
SE1L1_HUMANSEL1Lphysical
26496610
FL2D_HUMANWTAPphysical
26496610
RB15B_HUMANRBM15Bphysical
26496610
PPHLN_HUMANPPHLN1physical
26496610
MET14_HUMANMETTL14physical
26496610
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 MTA70_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-43, 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-43, 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-43; SER-219 AND SER-243,AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND THR-356, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.

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