NEP1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NEP1_SCHPO
• UniProt AC: Q10107
• Protein Name: Ribosomal RNA small subunit methyltransferase mra1 {ECO:0000305}
• Gene Name: mra1 {ECO:0000303|PubMed:9133664}
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 359
• Subcellular Localization: Nucleus, nucleolus .
• Protein Description: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates the pseudouridine corresponding to position 1189 (Psi1189) in S.cerevisiae 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity). Essential for cell growth. It also has a key role in promoting the mating function. [PubMed: 9133664]
• Protein Sequence: MPTYSKRKSRGSLEVSEKTNQPKFIKRSQSSETITSGETASELMQDEKEQSNGAVGSIEDEELQRLRENQASVEALSKKPESIDRELGVEALEIDNVVKSDEEKEDPNGASSKTVKARPLPAGSVHRVTTHMAPIPARSIGSHDTTTQRLIVVLDQACLEIYKVGKAKDAKYQLLNCDDHQGILKKLNRNIAQARPDITHQCLLTLLDSPLNKAGRLQVYIHTAKKVLIEVNPSVRIPRTFKRFSGLMVQLLHKLSIRSVNGNEKLLKVIKNPVTDYLPPNCRKATLSFDAPTVPPRKYLETLQPNQSVCIAIGAMAHGPDDFSDGWVDEKISISDYPLSASIACSKFLHSMEDFLGIV

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
9	Phosphorylation	PTYSKRKSRGSLEVS CCCCCCCCCCCCCCC	42.95	29996109
12	Phosphorylation	SKRKSRGSLEVSEKT CCCCCCCCCCCCHHC	49.23	28889911
16	Phosphorylation	SRGSLEVSEKTNQPK CCCCCCCCHHCCCCC	47.88	21712547
28	Phosphorylation	QPKFIKRSQSSETIT CCCEEECCCCCCEEC	13.17	21712547
30	Phosphorylation	KFIKRSQSSETITSG CEEECCCCCCEECCC	27.40	28889911
31	Phosphorylation	FIKRSQSSETITSGE EEECCCCCCEECCCH	23.77	28889911
33	Phosphorylation	KRSQSSETITSGETA ECCCCCCEECCCHHH	16.74	28889911
35	Phosphorylation	SQSSETITSGETASE CCCCCEECCCHHHHH	29.87	21712547
36	Phosphorylation	QSSETITSGETASEL CCCCEECCCHHHHHH	14.23	28889911
39	Phosphorylation	ETITSGETASELMQD CEECCCHHHHHHHHH	41.42	24763107
41	Phosphorylation	ITSGETASELMQDEK ECCCHHHHHHHHHHH	2.70	28889911
51	Phosphorylation	MQDEKEQSNGAVGSI HHHHHHHCCCCCCCC	45.42	29996109
57	Phosphorylation	QSNGAVGSIEDEELQ HCCCCCCCCCHHHHH	2.76	28889911
72	Phosphorylation	RLRENQASVEALSKK HHHHCHHHHHHHHCC	10.20	29996109
77	Phosphorylation	QASVEALSKKPESID HHHHHHHHCCCHHHC	5.29	29996109
82	Phosphorylation	ALSKKPESIDRELGV HHHCCCHHHCHHHCC	23.23	25720772
100	Phosphorylation	EIDNVVKSDEEKEDP EEEEEECCCCCCCCC	42.30	28889911
124	Phosphorylation	ARPLPAGSVHRVTTH EEECCCCCEEEEEEE	14.39	25720772
142	Phosphorylation	IPARSIGSHDTTTQR CCCHHCCCCCCCHHH	29.35	29996109
340	Phosphorylation	SISDYPLSASIACSK CCCCCCHHHHHHHHH	39.71	18257517
351	Phosphorylation	ACSKFLHSMEDFLGI HHHHHHHHHHHHHCC	37.80	25720772

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

Oops, there are no upstream regulatory protein records of NEP1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NEP1_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NEP1_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of NEP1_SCHPO !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-340 ANDSER-351, AND MASS SPECTROMETRY.
PubMed: 18257517