MET2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MET2A_HUMAN
• UniProt AC: Q96IZ6
• Protein Name: Methyltransferase-like protein 2A
• Gene Name: METTL2A
• 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: MAGSYPEGAPAVLADKRQQFGSRFLRDPARVFHHNAWDNVEWSEEQAAAAERKVQENSIQRVCQEKQVDYEINAHKYWNDFYKIHENGFFKDRHWLFTEFPELAPSQNQNHLKDWFLENKSEVPECRNNEDGPGLIMEEQHKCSSKSLEHKTQTLPVEENVTQKISDLEICADEFPGSSATYRILEVGCGVGNTVFPILQTNNDPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDEEKSYPVPKGSLDIIILIFVLSAIVPDKMQKAINRLSRLLKPGGMMLLRDYGRYDMAQLRFKKGQCLSGNFYVRGDGTRVYFFTQEELDTLFTTAGLEKVQNLVDRRLQVNRGKQLTMYRVWIQCKYCKPLLSSTS

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	Phosphorylation	---MAGSYPEGAPAV ---CCCCCCCCCCCC	12.37	25072903
15 (in isoform 2)	Ubiquitination	-	42.37	21906983
16	Ubiquitination	APAVLADKRQQFGSR CCCCHHHHHHHHHHH	46.64	-
53	Ubiquitination	QAAAAERKVQENSIQ HHHHHHHHHHHHHHH	39.51	-
66	Acetylation	IQRVCQEKQVDYEIN HHHHHHHHCCCCEEE	29.73	-
66	Ubiquitination	IQRVCQEKQVDYEIN HHHHHHHHCCCCEEE	29.73	-
76	Ubiquitination	DYEINAHKYWNDFYK CCEEEHHHHHCCCHH	49.94	-
91	Ubiquitination	IHENGFFKDRHWLFT HHHCCCCCCCCEEEC	52.14	-
113	Methylation	SQNQNHLKDWFLENK CCCCCHHHHHHHHCC	45.41	-
113	Ubiquitination	SQNQNHLKDWFLENK CCCCCHHHHHHHHCC	45.41	-
120	Ubiquitination	KDWFLENKSEVPECR HHHHHHCCCCCCCCC	38.32	-
146	Ubiquitination	EQHKCSSKSLEHKTQ EEECCCCCCCCCCCC	42.65	-
147	Phosphorylation	QHKCSSKSLEHKTQT EECCCCCCCCCCCCC	40.72	-
151 (in isoform 1)	Ubiquitination	-	32.71	21906983
154	Phosphorylation	SLEHKTQTLPVEENV CCCCCCCCCCCCCCH	37.96	18669648
279	Phosphorylation	QKAINRLSRLLKPGG HHHHHHHHHHHCCCC	20.04	-
293	Phosphorylation	GMMLLRDYGRYDMAQ CEEEEEECCCCCCEE	9.32	22817900
348	Methylation	KVQNLVDRRLQVNRG HHHHHHHHHCCCCCC	33.46	-
369	Phosphorylation	RVWIQCKYCKPLLSS EEEEECCCCHHHHCC	17.21	21406692
371	Ubiquitination	WIQCKYCKPLLSSTS EEECCCCHHHHCCCC	35.29	-
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 MET2A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MET2A_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 MET2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MET2B_HUMAN	METTL2B	physical	28514442
ID4_HUMAN	ID4	physical	28514442
CPNE7_HUMAN	CPNE7	physical	28514442
NDUF7_HUMAN	NDUFAF7	physical	28514442
IF2M_HUMAN	MTIF2	physical	28514442
UBR4_HUMAN	UBR4	physical	28514442
NDUS1_HUMAN	NDUFS1	physical	28514442
NDUS6_HUMAN	NDUFS6	physical	28514442
TOP3A_HUMAN	TOP3A	physical	28514442
MCCA_HUMAN	MCCC1	physical	28514442
NDUF5_HUMAN	NDUFAF5	physical	28514442
UBR2_HUMAN	UBR2	physical	28514442

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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-154, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-154, AND MASS SPECTROMETRY.
PubMed: 19413330