MET16_HUMAN - dbPTM
MET16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MET16_HUMAN
UniProt AC Q86W50
Protein Name U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase {ECO:0000305}
Gene Name METTL16 {ECO:0000303|PubMed:27872311, ECO:0000312|HGNC:HGNC:28484}
Organism Homo sapiens (Human).
Sequence Length 562
Subcellular Localization Nucleus .
Protein Description RNA N6-methyltransferase that methylates adenosine residues of a subset of RNAs and plays a key role in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts. [PubMed: 28525753 Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs)]
Protein Sequence MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHVQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKSTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIIYDFCMCNPPFFANQLEAKGVNSRNPRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTYTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLASVMKELSLKASPLRSETAEGIVVVTTWIEKILTDLKVQHKRVPCGKEEVSLFLTAIENSWIHLRRKKRERVRQLREVPRAPEDVIQALEEKKPTPKESGNSQELARGPQERTPCGPALREGEAAAVEGPCPSQESLSQEENPEPTEDERSEEKGGVEVLESCQGSSNGAQDQEASEQFGSPVAERGKRLPGVAGQYLFKCLINVKKEVDDALVEMHWVEGQNRDLMNQLCTYIRNQIFRLVAVN
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
5Acetylation---MALSKSMHARNR
---CCCCCCHHHHHH		53.2825953088
16UbiquitinationARNRYKDKPPDFAYL
HHHHCCCCCCCHHHH		55.06-
26UbiquitinationDFAYLASKYPDFKQH
CHHHHHHHCCCHHHE		56.02-
43PhosphorylationINLNGRVSLNFKDPE
EECCCCEEECCCCHH		19.0828555341
47UbiquitinationGRVSLNFKDPEAVRA
CCEEECCCCHHHHHH		71.89-
47AcetylationGRVSLNFKDPEAVRA
CCEEECCCCHHHHHH		71.8925953088
58PhosphorylationAVRALTCTLLREDFG
HHHHHHHHHHHHHHC		24.48-
144UbiquitinationMCFNYAKKNVEQNNL
HHHHHHHHHHHHCCH		59.04-
156UbiquitinationNNLSDLIKVVKVPQK
CCHHHHHHHCCCCHH		48.55-
159UbiquitinationSDLIKVVKVPQKTLL
HHHHHHCCCCHHHHH		51.70-
163UbiquitinationKVVKVPQKTLLMDAL
HHCCCCHHHHHHHHH		34.76-
178PhosphorylationKEESEIIYDFCMCNP
HHHHHHHHHHHHCCC		14.5020049867
229UbiquitinationGGELEFVKRIIHDSL
CCCEEHHHHHHHHHH		43.11-
235PhosphorylationVKRIIHDSLQLKKRL
HHHHHHHHHHHHHHH		12.1223836654
239UbiquitinationIHDSLQLKKRLRWYS
HHHHHHHHHHHHHHH		23.92-
246PhosphorylationKKRLRWYSCMLGKKC
HHHHHHHHHHHCCCC		6.01-
251AcetylationWYSCMLGKKCSLAPL
HHHHHHCCCCCCCCC		46.7925953088
259UbiquitinationKCSLAPLKEELRIQG
CCCCCCCCHHHHHCC		48.35-
294PhosphorylationWSFYDDVTVPSPPSK
HHHCCCCCCCCCHHH		33.4227732954
297PhosphorylationYDDVTVPSPPSKRRK
CCCCCCCCCHHHCCC		45.1427422710
300PhosphorylationVTVPSPPSKRRKLEK
CCCCCCHHHCCCCCC		42.0227732954
325PhosphorylationASVMKELSLKASPLR
HHHHHHHCCCCCCCC		28.9923927012
3272-HydroxyisobutyrylationVMKELSLKASPLRSE
HHHHHCCCCCCCCCC		43.36-
329PhosphorylationKELSLKASPLRSETA
HHHCCCCCCCCCCCC		23.9123927012
333PhosphorylationLKASPLRSETAEGIV
CCCCCCCCCCCCCEE		47.1622199227
335PhosphorylationASPLRSETAEGIVVV
CCCCCCCCCCCEEEE		31.1222199227
412PhosphorylationALEEKKPTPKESGNS
HHHHCCCCCCCCCCH		56.7421712546
416PhosphorylationKKPTPKESGNSQELA
CCCCCCCCCCHHHHH		49.7720164059
419PhosphorylationTPKESGNSQELARGP
CCCCCCCHHHHHCCC		28.6729255136
430PhosphorylationARGPQERTPCGPALR
HCCCCCCCCCCHHHC		23.3721815630
450PhosphorylationAVEGPCPSQESLSQE
EEECCCCCHHHCCCC		53.9825159151
453PhosphorylationGPCPSQESLSQEENP
CCCCCHHHCCCCCCC		26.1925159151
455PhosphorylationCPSQESLSQEENPEP
CCCHHHCCCCCCCCC		44.8425159151
463PhosphorylationQEENPEPTEDERSEE
CCCCCCCCCCHHHHH		55.1728450419
468PhosphorylationEPTEDERSEEKGGVE
CCCCCHHHHHHCCCC		48.3228450419
493PhosphorylationGAQDQEASEQFGSPV
CCCCHHHHHHHCCCH		31.0425850435
498PhosphorylationEASEQFGSPVAERGK
HHHHHHCCCHHHHCC		19.9330576142
514PhosphorylationLPGVAGQYLFKCLIN
CCCHHHHHHHHHHHC		17.1221406692
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 MET16_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MET16_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 MET16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SYYC_HUMANYARSphysical
22939629
TCEA1_HUMANTCEA1physical
26344197
MET16_HUMANMETTL16physical
26472760
MEPCE_HUMANMEPCEphysical
26472760
IMA7_HUMANKPNA6physical
26472760
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 MET16_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-329, 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-329, AND MASSSPECTROMETRY.

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