YTDC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YTDC1_HUMAN
• UniProt AC: Q96MU7
• Protein Name: YTH domain-containing protein 1 {ECO:0000305}
• Gene Name: YTHDC1 {ECO:0000312|HGNC:HGNC:30626}
• Organism: Homo sapiens (Human).
• Sequence Length: 727
• Subcellular Localization: Nucleus . Nucleus speckle . Localizes to a novel subnuclear structure, the YT bodies.
• Protein Description: Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. [PubMed: 26318451]
• Protein Sequence: MAADSREEKDGELNVLDDILTEVPEQDDELYNPESEQDKNEKKGSKRKSDRMESTDTKRQKPSVHSRQLVSKPLSSSVSNNKRIVSTKGKSATEYKNEEYQRSERNKRLDADRKIRLSSSASREPYKNQPEKTCVRKRDPERRAKSPTPDGSERIGLEVDRRASRSSQSSKEEVNSEEYGSDHETGSSGSSDEQGNNTENEEEGVEEDVEEDEEVEEDAEEDEEVDEDGEEEEEEEEEEEEEEEEEEEEYEQDERDQKEEGNDYDTRSEASDSGSESVSFTDGSVRSGSGTDGSDEKKKERKRARGISPIVFDRSGSSASESYAGSEKKHEKLSSSVRAVRKDQTSKLKYVLQDARFFLIKSNNHENVSLAKAKGVWSTLPVNEKKLNLAFRSARSVILIFSVRESGKFQGFARLSSESHHGGSPIHWVLPAGMSAKMLGGVFKIDWICRRELPFTKSAHLTNPWNEHKPVKIGRDGQEIELECGTQLCLLFPPDESIDLYQVIHKMRHKRRMHSQPRSRGRPSRREPVRDVGRRRPEDYDIHNSRKKPRIDYPPEFHQRPGYLKDPRYQEVDRRFSGVRRDVFLNGSYNDYVREFHNMGPPPPWQGMPPYPGMEQPPHHPYYQHHAPPPQAHPPYSGHHPVPHEARYRDKRVHDYDMRVDDFLRRTQAVVSGRRSRPRERDRERERDRPRDNRRDRERDRGRDRERERERLCDRDRDRGERGRYRR

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
21	Phosphorylation	NVLDDILTEVPEQDD CCHHHHHHHCCCCCC	34.96	20873877
31	Phosphorylation	PEQDDELYNPESEQD CCCCCCCCCCCCCCC	26.99	28122231
35	Phosphorylation	DELYNPESEQDKNEK CCCCCCCCCCCCCCC	41.64	28387310
48	Acetylation	EKKGSKRKSDRMEST CCCCCHHHHHHHCCC	61.52	12433863
49	Phosphorylation	KKGSKRKSDRMESTD CCCCHHHHHHHCCCC	34.19	24719451
54	Phosphorylation	RKSDRMESTDTKRQK HHHHHHCCCCCCCCC	23.41	30576142
55	Phosphorylation	KSDRMESTDTKRQKP HHHHHCCCCCCCCCC	34.09	26074081
57	Phosphorylation	DRMESTDTKRQKPSV HHHCCCCCCCCCCCC	28.37	26074081
58	Acetylation	RMESTDTKRQKPSVH HHCCCCCCCCCCCCC	56.49	12433871
71	Phosphorylation	VHSRQLVSKPLSSSV CCHHHHHCCCCCCCC	36.83	20068231
72	Acetylation	HSRQLVSKPLSSSVS CHHHHHCCCCCCCCC	42.36	23954790
75	Phosphorylation	QLVSKPLSSSVSNNK HHHCCCCCCCCCCCC	29.15	20068231
76	Phosphorylation	LVSKPLSSSVSNNKR HHCCCCCCCCCCCCC	42.30	27732954
77	Phosphorylation	VSKPLSSSVSNNKRI HCCCCCCCCCCCCCE	26.62	20068231
79	Phosphorylation	KPLSSSVSNNKRIVS CCCCCCCCCCCCEEE	36.31	20068231
82	Acetylation	SSSVSNNKRIVSTKG CCCCCCCCCEEECCC	47.99	25953088
86	Phosphorylation	SNNKRIVSTKGKSAT CCCCCEEECCCCCHH	23.25	28655764
95	Phosphorylation	KGKSATEYKNEEYQR CCCCHHHHCCHHHHH	18.11	27642862
96	Sumoylation	GKSATEYKNEEYQRS CCCHHHHCCHHHHHH	52.21	-
96	Sumoylation	GKSATEYKNEEYQRS CCCHHHHCCHHHHHH	52.21	28112733
96	Acetylation	GKSATEYKNEEYQRS CCCHHHHCCHHHHHH	52.21	26051181
100	Phosphorylation	TEYKNEEYQRSERNK HHHCCHHHHHHHHHH	11.75	27642862
118	Phosphorylation	ADRKIRLSSSASREP HHHHHCCCCCCCCCC	16.64	30266825
119	Phosphorylation	DRKIRLSSSASREPY HHHHCCCCCCCCCCC	34.22	27273156
120	Phosphorylation	RKIRLSSSASREPYK HHHCCCCCCCCCCCC	27.21	23401153
122	Phosphorylation	IRLSSSASREPYKNQ HCCCCCCCCCCCCCC	38.84	25159151
126	Phosphorylation	SSASREPYKNQPEKT CCCCCCCCCCCCCCC	20.16	27273156
132	Acetylation	PYKNQPEKTCVRKRD CCCCCCCCCCCCCCC	54.64	25953088
146	Phosphorylation	DPERRAKSPTPDGSE CHHHHCCCCCCCHHH	32.78	29255136
148	Phosphorylation	ERRAKSPTPDGSERI HHHCCCCCCCHHHCC	40.89	29255136
152	Phosphorylation	KSPTPDGSERIGLEV CCCCCCHHHCCCHHH	30.96	30266825
164	Phosphorylation	LEVDRRASRSSQSSK HHHHHHHHCCCCCCH	30.77	25159151
264	Phosphorylation	QKEEGNDYDTRSEAS HHHCCCCCCCCHHCC	24.18	25850435
266	Phosphorylation	EEGNDYDTRSEASDS HCCCCCCCCHHCCCC	29.84	25850435
268	Phosphorylation	GNDYDTRSEASDSGS CCCCCCCHHCCCCCC	39.34	20873877
271	Phosphorylation	YDTRSEASDSGSESV CCCCHHCCCCCCCCE	28.40	24905233
273	Phosphorylation	TRSEASDSGSESVSF CCHHCCCCCCCCEEE	41.54	25849741
275	Phosphorylation	SEASDSGSESVSFTD HHCCCCCCCCEEECC	30.56	25849741
277	Phosphorylation	ASDSGSESVSFTDGS CCCCCCCCEEECCCC	25.43	25849741
279	Phosphorylation	DSGSESVSFTDGSVR CCCCCCEEECCCCCC	31.54	24905233
281	Phosphorylation	GSESVSFTDGSVRSG CCCCEEECCCCCCCC	31.76	24905233
287	Phosphorylation	FTDGSVRSGSGTDGS ECCCCCCCCCCCCCC	34.84	28176443
289	Phosphorylation	DGSVRSGSGTDGSDE CCCCCCCCCCCCCHH	39.50	24719451
291	Phosphorylation	SVRSGSGTDGSDEKK CCCCCCCCCCCHHHH	38.59	28985074
294	Phosphorylation	SGSGTDGSDEKKKER CCCCCCCCHHHHHHH	45.46	24719451
308	Phosphorylation	RKRARGISPIVFDRS HHHHCCCCCEEECCC	16.05	19664994
308 (in isoform 2)	Phosphorylation	-	16.05	22115753
315	Phosphorylation	SPIVFDRSGSSASES CCEEECCCCCCCCCC	44.89	25159151
315 (in isoform 2)	Phosphorylation	-	44.89	23663014
317	Phosphorylation	IVFDRSGSSASESYA EEECCCCCCCCCCCC	24.79	25159151
317 (in isoform 2)	Phosphorylation	-	24.79	23663014
318	Phosphorylation	VFDRSGSSASESYAG EECCCCCCCCCCCCC	39.06	25159151
318 (in isoform 2)	Phosphorylation	-	39.06	23663014
320	Phosphorylation	DRSGSSASESYAGSE CCCCCCCCCCCCCCH	29.08	25159151
320 (in isoform 2)	Phosphorylation	-	29.08	26434776
322	Phosphorylation	SGSSASESYAGSEKK CCCCCCCCCCCCHHH	20.14	22115753
322 (in isoform 2)	Phosphorylation	-	20.14	26434776
323	Phosphorylation	GSSASESYAGSEKKH CCCCCCCCCCCHHHH	15.78	22115753
323 (in isoform 2)	Phosphorylation	-	15.78	26434776
326	Phosphorylation	ASESYAGSEKKHEKL CCCCCCCCHHHHHHH	37.76	25159151
327 (in isoform 2)	Phosphorylation	-	66.27	26434776
328 (in isoform 2)	Phosphorylation	-	62.21	26434776
334	Phosphorylation	EKKHEKLSSSVRAVR HHHHHHHHHHHHHHH	31.47	20068231
335	Phosphorylation	KKHEKLSSSVRAVRK HHHHHHHHHHHHHHC	43.20	20068231
336	Phosphorylation	KHEKLSSSVRAVRKD HHHHHHHHHHHHHCC	16.55	21815630
345	Phosphorylation	RAVRKDQTSKLKYVL HHHHCCCCCCHHHHH	37.65	20068231
346	Phosphorylation	AVRKDQTSKLKYVLQ HHHCCCCCCHHHHHH	30.29	20068231
349	Acetylation	KDQTSKLKYVLQDAR CCCCCCHHHHHHHCE	36.73	25953088
372	Ubiquitination	HENVSLAKAKGVWST CCCEEEEEECCCEEC	56.79	-
372	Acetylation	HENVSLAKAKGVWST CCCEEEEEECCCEEC	56.79	25953088
385	Ubiquitination	STLPVNEKKLNLAFR ECCCCCHHHHHHHHH	58.31	-
385	Acetylation	STLPVNEKKLNLAFR ECCCCCHHHHHHHHH	58.31	25953088
393	Phosphorylation	KLNLAFRSARSVILI HHHHHHHHCCEEEEE	22.91	20860994
396	O-linked_Glycosylation	LAFRSARSVILIFSV HHHHHCCEEEEEEEE	17.15	30379171
396	Phosphorylation	LAFRSARSVILIFSV HHHHHCCEEEEEEEE	17.15	20860994
402	Phosphorylation	RSVILIFSVRESGKF CEEEEEEEECCCCCC	17.17	20860994
406	Phosphorylation	LIFSVRESGKFQGFA EEEEECCCCCCCCEE	36.40	18669648
408	Acetylation	FSVRESGKFQGFARL EEECCCCCCCCEEEC	43.74	25953088
416	Phosphorylation	FQGFARLSSESHHGG CCCEEECCCCCCCCC	26.89	23401153
417	Phosphorylation	QGFARLSSESHHGGS CCEEECCCCCCCCCC	47.94	22167270
419	Phosphorylation	FARLSSESHHGGSPI EEECCCCCCCCCCCC	23.80	22167270
424	Phosphorylation	SESHHGGSPIHWVLP CCCCCCCCCCEEEEE	25.85	22167270
435	Phosphorylation	WVLPAGMSAKMLGGV EEEECCCCHHHHCCE	24.66	22167270
469	Sumoylation	TNPWNEHKPVKIGRD CCCCCCCCCEECCCC	45.38	-
469	Sumoylation	TNPWNEHKPVKIGRD CCCCCCCCCEECCCC	45.38	-
469	Ubiquitination	TNPWNEHKPVKIGRD CCCCCCCCCEECCCC	45.38	-
469	Acetylation	TNPWNEHKPVKIGRD CCCCCCCCCEECCCC	45.38	26051181
472	Ubiquitination	WNEHKPVKIGRDGQE CCCCCCEECCCCCCE	48.23	-
472	Malonylation	WNEHKPVKIGRDGQE CCCCCCEECCCCCCE	48.23	26320211
497	Phosphorylation	LLFPPDESIDLYQVI EECCCCCCCCHHHHH	28.87	20068231
515	Phosphorylation	RHKRRMHSQPRSRGR HHHHHHCCCCCCCCC	32.32	26846344
519	Phosphorylation	RMHSQPRSRGRPSRR HHCCCCCCCCCCCCC	45.85	30576142
524	Phosphorylation	PRSRGRPSRREPVRD CCCCCCCCCCCCCCC	42.48	28634120
540	Phosphorylation	GRRRPEDYDIHNSRK CCCCCCCCCCCCCCC	18.35	28152594
545	Phosphorylation	EDYDIHNSRKKPRID CCCCCCCCCCCCCCC	31.17	26055452
553	Phosphorylation	RKKPRIDYPPEFHQR CCCCCCCCCCHHHCC	20.51	25884760
563	Phosphorylation	EFHQRPGYLKDPRYQ HHHCCCCCCCCCCHH	17.17	28152594
569	Phosphorylation	GYLKDPRYQEVDRRF CCCCCCCHHHHHHHH	17.89	27642862
577	Phosphorylation	QEVDRRFSGVRRDVF HHHHHHHCCCCCCEE	34.27	29496963
588	Phosphorylation	RDVFLNGSYNDYVRE CCEECCCCHHHHHHH	21.49	28450419
656	Phosphorylation	RDKRVHDYDMRVDDF CCCCCCCCCCCHHHH	9.21	-
667	Phosphorylation	VDDFLRRTQAVVSGR HHHHHHHHHHHHCCC	17.91	26074081
672	Phosphorylation	RRTQAVVSGRRSRPR HHHHHHHCCCCCCCC	21.71	26074081
676	Phosphorylation	AVVSGRRSRPRERDR HHHCCCCCCCCHHHH	45.32	26074081

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

Oops, there are no upstream regulatory protein records of YTDC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of YTDC1_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 YTDC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABL1_HUMAN	ABL1	physical	15175272
RBY1F_HUMAN	RBMY1F	physical	25416956
KHDR2_HUMAN	KHDRBS2	physical	25416956
SRC_HUMAN	SRC	physical	15175272

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

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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-424, ANDMASS SPECTROMETRY.
PubMed: 19413330

"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-308; SER-315; SER-317;SER-318; SER-320 AND SER-424, AND MASS SPECTROMETRY.
PubMed: 18669648

"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-308, AND MASSSPECTROMETRY.
PubMed: 18691976

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-308 ANDSER-577, AND MASS SPECTROMETRY.
PubMed: 19007248

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASSSPECTROMETRY.
PubMed: 17924679

"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASSSPECTROMETRY.
PubMed: 16565220

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASSSPECTROMETRY.
PubMed: 16964243

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-308; SER-315;SER-317; SER-318; SER-320; SER-322; TYR-323; SER-326 AND SER-515, ANDMASS SPECTROMETRY.
PubMed: 17081983

"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND THR-148, ANDMASS SPECTROMETRY.
PubMed: 16083285

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-148; SER-275;SER-308; SER-320 AND SER-326, AND MASS SPECTROMETRY.
PubMed: 15302935