MET2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MET2B_HUMAN
• UniProt AC: Q6P1Q9
• Protein Name: Methyltransferase-like protein 2B
• Gene Name: METTL2B
• Organism: Homo sapiens (Human).
• Sequence Length: 378
• Protein Description: Probable S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of some tRNAs..
• Protein Sequence: MAGSYPEGAPAILADKRQQFGSRFLSDPARVFHHNAWDNVEWSEEQAAAAERKVQENSIQRVCQEKQVDYEINAHKYWNDFYKIHENGFFKDRHWLFTEFPELAPSQNQNHLKDWFLENKSEVCECRNNEDGPGLIMEEQHKCSSKSLEHKTQTPPVEENVTQKISDLEICADEFPGSSATYRILEVGCGVGNTVFPILQTNNDPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDEEKSYPVPKGSLDIIILIFVLSAVVPDKMQKAINRLSRLLKPGGMVLLRDYGRYDMAQLRFKKGQCLSGNFYVRGDGTRVYFFTQEELDTLFTTAGLEKVQNLVDRRLQVNRGKQLTMYRVWIQCKYCKPLLSSTS

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
2	Acetylation	------MAGSYPEGA ------CCCCCCCCC	18.68	22814378
4	Phosphorylation	----MAGSYPEGAPA ----CCCCCCCCCCC	28.16	25159151
5 (in isoform 2)	Phosphorylation	-	12.37	24043423
5	Phosphorylation	---MAGSYPEGAPAI ---CCCCCCCCCCCC	12.37	23186163
16	Ubiquitination	APAILADKRQQFGSR CCCCHHHHHHHHHHH	46.64	-
26	Phosphorylation	QFGSRFLSDPARVFH HHHHHHCCCHHHHHC	38.54	21815630
53	Ubiquitination	QAAAAERKVQENSIQ HHHHHHHHHHHHHHH	39.51	29967540
66	Acetylation	IQRVCQEKQVDYEIN HHHHHHHHCCCCEEE	29.73	23749302
66	Ubiquitination	IQRVCQEKQVDYEIN HHHHHHHHCCCCEEE	29.73	29967540
70	Phosphorylation	CQEKQVDYEINAHKY HHHHCCCCEEEHHHH	21.61	27642862
76	Ubiquitination	DYEINAHKYWNDFYK CCEEEHHHHHCCCHH	49.94	29967540
86 (in isoform 2)	Ubiquitination	-	63.62	21906983
91	Ubiquitination	IHENGFFKDRHWLFT HHHCCCCCCCCEEEC	52.14	27667366
113	Ubiquitination	SQNQNHLKDWFLENK CCCCCHHHHHHHCCH	45.41	29967540
113	Methylation	SQNQNHLKDWFLENK CCCCCHHHHHHHCCH	45.41	23644510
120	Ubiquitination	KDWFLENKSEVCECR HHHHHCCHHHEEECC	38.32	29967540
146	Ubiquitination	EQHKCSSKSLEHKTQ EEECCCCCCCCCCCC	42.65	22817900
147	Phosphorylation	QHKCSSKSLEHKTQT EECCCCCCCCCCCCC	40.72	23911959
151	Ubiquitination	SSKSLEHKTQTPPVE CCCCCCCCCCCCCCC	32.71	21963094
151 (in isoform 1)	Ubiquitination	-	32.71	21906983
152	Phosphorylation	SKSLEHKTQTPPVEE CCCCCCCCCCCCCCC	39.31	30266825
154	Phosphorylation	SLEHKTQTPPVEENV CCCCCCCCCCCCCCH	34.49	30266825
162	Phosphorylation	PPVEENVTQKISDLE CCCCCCHHHHHCCCE	35.41	29396449
264	Phosphorylation	IILIFVLSAVVPDKM HHHHHHHHCCCCHHH	17.45	-
279	Phosphorylation	QKAINRLSRLLKPGG HHHHHHHHHHHCCCC	20.04	-
283	Ubiquitination	NRLSRLLKPGGMVLL HHHHHHHCCCCEEEE	46.32	-
348	Methylation	KVQNLVDRRLQVNRG HHHHHHHHHCCCCCC	33.46	-
369	Phosphorylation	RVWIQCKYCKPLLSS EEEEECCCCHHHHCC	17.21	21406692
371	Ubiquitination	WIQCKYCKPLLSSTS EEECCCCHHHHCCCC	35.29	29967540
375	Phosphorylation	KYCKPLLSSTS---- CCCHHHHCCCC----	38.97	21406692
376	Phosphorylation	YCKPLLSSTS----- CCHHHHCCCC-----	32.41	21406692
377	Phosphorylation	CKPLLSSTS------ CHHHHCCCC------	34.77	21406692
378	Phosphorylation	KPLLSSTS------- HHHHCCCC-------	39.92	21406692

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MET2B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MET2B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MET2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049

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.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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 THR-154, AND MASSSPECTROMETRY.
PubMed: 19690332

"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 THR-154, AND MASSSPECTROMETRY.
PubMed: 18669648