MET16_MOUSE - dbPTM
MET16_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MET16_MOUSE
UniProt AC Q9CQG2
Protein Name U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase {ECO:0000250|UniProtKB:Q86W50}
Gene Name Mettl16 {ECO:0000312|MGI:MGI:1914743}
Organism Mus musculus (Mouse).
Sequence Length 553
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: 29262316 Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs) (By similarity In contrast to the METTL3-METTL14 heterodimer, only able to methylate a limited number of RNAs: requires both a 5'UACAGAGAA-3' nonamer sequence and a specific RNA structure (By similarity In presence of S-adenosyl-L-methionine, binds the 3'-UTR region of MAT2A mRNA and specifically N6-methylates the first hairpin of MAT2A mRNA, impairing MAT2A expression]
Protein Sequence MALSKSMHARNRYKDKPPDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSIDIPLERLIPTVPLRLNYIHWVEDLIGHQDSDKTTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPQKTLLMDALKEESEIVYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDDVTVPSPPSKRRKLEKPRKPITFVVLESVMKELSLKASSLGSETAEGIVVVTTWIEKILTDLKVQHKRIPCGREEVSLFLTAIENSWIHLRRKRRERVRQLREVPRAPEDVILALEERKSTPKELSSGQDVAHSPQESALCGLDVPGGEAAADGGHCLSQKLLCQEETPEATEDERDEERGGMEAMESCKGSSNGAQDGEASEKGDRLDGAAGRYLFKCLVNIKKEAGDAVVEMHWVEGQNRDLMNQLCTYVRNQILRLVAS
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
22PhosphorylationDKPPDFAYLASKYPD
CCCCCHHHHHHHCCC
11.64-
27PhosphorylationFAYLASKYPDFKQHI
HHHHHHHCCCHHHHE
12.92-
67PhosphorylationLREDFGLSIDIPLER
HHHHHCCCCEEEHHH
20.7021743459
294PhosphorylationWSFYDDVTVPSPPSK
HHCCCCCCCCCCHHH
33.4226643407
297PhosphorylationYDDVTVPSPPSKRRK
CCCCCCCCCHHHCCC
45.1426643407
300PhosphorylationVTVPSPPSKRRKLEK
CCCCCCHHHCCCCCC
42.0226643407
325PhosphorylationESVMKELSLKASSLG
HHHHHHHCHHHHHCC
28.9928059163
329PhosphorylationKELSLKASSLGSETA
HHHCHHHHHCCCCCC
25.22-
411PhosphorylationLALEERKSTPKELSS
HHHHHCCCCCCCCCC
57.0526160508
412PhosphorylationALEERKSTPKELSSG
HHHHCCCCCCCCCCC
41.2226160508
417PhosphorylationKSTPKELSSGQDVAH
CCCCCCCCCCCCCCC
33.2527742792
418PhosphorylationSTPKELSSGQDVAHS
CCCCCCCCCCCCCCC
53.7727742792
425PhosphorylationSGQDVAHSPQESALC
CCCCCCCCCCHHCCC
20.6725521595
429PhosphorylationVAHSPQESALCGLDV
CCCCCCHHCCCCCCC
22.6927742792
450PhosphorylationADGGHCLSQKLLCQE
CCCCCCCCHHCEECC
30.5725619855
459PhosphorylationKLLCQEETPEATEDE
HCEECCCCCCCCCCH
26.1925521595
463PhosphorylationQEETPEATEDERDEE
CCCCCCCCCCHHHHH
42.1627087446
493PhosphorylationGAQDGEASEKGDRLD
CCCCCCCCCCCCCCC
35.2223684622

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MET16_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MET16_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MET16_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-450, AND MASSSPECTROMETRY.

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