dbPTM

SF3B1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SF3B1_HUMAN
UniProt AC	O75533
Protein Name	Splicing factor 3B subunit 1
Gene Name	SF3B1
Organism	Homo sapiens (Human).
Sequence Length	1304
Subcellular Localization	Nucleus . Nucleus speckle. During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm.
Protein Description	Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. [PubMed: 27720643 SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA]
Protein Sequence	MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYELDYIL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MAKIAKTHEDIEA --CCCCCCCHHHHHH	54.62	-
21	Ubiquitination	QIREIQGKKAALDEA HHHHHHCHHHHHHHH	23.90	-
22	Ubiquitination	IREIQGKKAALDEAQ HHHHHCHHHHHHHHC	45.79	-
35	Phosphorylation	AQGVGLDSTGYYDQE HCCCCCCCCCCCCCC	28.86	26552605
36	Phosphorylation	QGVGLDSTGYYDQEI CCCCCCCCCCCCCCC	28.95	28796482
38	Phosphorylation	VGLDSTGYYDQEIYG CCCCCCCCCCCCCCC	12.17	28796482
39	Phosphorylation	GLDSTGYYDQEIYGG CCCCCCCCCCCCCCC	16.70	28796482
44	Phosphorylation	GYYDQEIYGGSDSRF CCCCCCCCCCCCCCC	18.06	28796482
47	Phosphorylation	DQEIYGGSDSRFAGY CCCCCCCCCCCCHHC	28.22	28796482
49	Phosphorylation	EIYGGSDSRFAGYVT CCCCCCCCCCHHCEE	30.87	28796482
54	Phosphorylation	SDSRFAGYVTSIAAT CCCCCHHCEEEEEEE	9.34	27251275
56	Phosphorylation	SRFAGYVTSIAATEL CCCHHCEEEEEEEEC	13.11	28796482
57	Phosphorylation	RFAGYVTSIAATELE CCHHCEEEEEEEECC	10.53	27251275
61	Phosphorylation	YVTSIAATELEDDDD CEEEEEEEECCCCCC	31.89	26657352
70	Phosphorylation	LEDDDDDYSSSTSLL CCCCCCCCCCHHHHC	19.90	28796482
71	Phosphorylation	EDDDDDYSSSTSLLG CCCCCCCCCHHHHCC	25.47	28796482
72	Phosphorylation	DDDDDYSSSTSLLGQ CCCCCCCCHHHHCCC	31.26	26657352
73	Phosphorylation	DDDDYSSSTSLLGQK CCCCCCCHHHHCCCC	18.97	28796482
74	Phosphorylation	DDDYSSSTSLLGQKK CCCCCCHHHHCCCCC	25.91	28796482
75	Phosphorylation	DDYSSSTSLLGQKKP CCCCCHHHHCCCCCC	24.44	26552605
81	Acetylation	TSLLGQKKPGYHAPV HHHCCCCCCCCCCCH	35.47	26051181
81	Ubiquitination	TSLLGQKKPGYHAPV HHHCCCCCCCCCCCH	35.47	-
84	Phosphorylation	LGQKKPGYHAPVALL CCCCCCCCCCCHHHH	11.88	27259358
97	Phosphorylation	LLNDIPQSTEQYDPF HHCCCCCCCCCCCCC	28.67	28555341
98	Phosphorylation	LNDIPQSTEQYDPFA HCCCCCCCCCCCCCH	23.12	28796482
101	Phosphorylation	IPQSTEQYDPFAEHR CCCCCCCCCCCHHCC	21.25	28796482
119	Phosphorylation	IADREDEYKKHRRTM CCCCHHHHHHHCCEE	37.34	26074081
125	Phosphorylation	EYKKHRRTMIISPER HHHHHCCEEEECHHH	16.81	30266825
126	Sulfoxidation	YKKHRRTMIISPERL HHHHCCEEEECHHHC	2.13	21406390
129	Phosphorylation	HRRTMIISPERLDPF HCCEEEECHHHCCCC	15.13	19664994
141	2-Hydroxyisobutyrylation	DPFADGGKTPDPKMN CCCCCCCCCCCCCCC	63.51	-
141	Acetylation	DPFADGGKTPDPKMN CCCCCCCCCCCCCCC	63.51	19608861
141	Ubiquitination	DPFADGGKTPDPKMN CCCCCCCCCCCCCCC	63.51	19608861
142	Phosphorylation	PFADGGKTPDPKMNA CCCCCCCCCCCCCCH	35.88	29255136
146	Ubiquitination	GGKTPDPKMNARTYM CCCCCCCCCCHHHHH	52.76	-
151	Phosphorylation	DPKMNARTYMDVMRE CCCCCHHHHHHHHHH	22.31	29978859
152	Phosphorylation	PKMNARTYMDVMREQ CCCCHHHHHHHHHHH	5.93	28796482
157	Citrullination	RTYMDVMREQHLTKE HHHHHHHHHHHCCHH	40.03	-
157	Citrullination	RTYMDVMREQHLTKE HHHHHHHHHHHCCHH	40.03	-
163	2-Hydroxyisobutyrylation	MREQHLTKEEREIRQ HHHHHCCHHHHHHHH	65.03	-
175	2-Hydroxyisobutyrylation	IRQQLAEKAKAGELK HHHHHHHHHHCCCCE	49.97	-
175	Acetylation	IRQQLAEKAKAGELK HHHHHHHHHHCCCCE	49.97	25953088
175	Ubiquitination	IRQQLAEKAKAGELK HHHHHHHHHHCCCCE	49.97	-
182	Ubiquitination	KAKAGELKVVNGAAA HHHCCCCEEECCCCC	39.57	20972266
182 (in isoform 1)	Ubiquitination	-	39.57	20972266
190	Phosphorylation	VVNGAAASQPPSKRK EECCCCCCCCCCCCC	38.19	25159151
194	Phosphorylation	AAASQPPSKRKRRWD CCCCCCCCCCCCCHH	52.34	29255136
195	2-Hydroxyisobutyrylation	AASQPPSKRKRRWDQ CCCCCCCCCCCCHHC	68.65	-
195	Acetylation	AASQPPSKRKRRWDQ CCCCCCCCCCCCHHC	68.65	25953088
195	Methylation	AASQPPSKRKRRWDQ CCCCCCCCCCCCHHC	68.65	-
195	Ubiquitination	AASQPPSKRKRRWDQ CCCCCCCCCCCCHHC	68.65	-
203	Phosphorylation	RKRRWDQTADQTPGA CCCCHHCCCCCCCCC	29.72	29255136
207	Phosphorylation	WDQTADQTPGATPKK HHCCCCCCCCCCCCC	25.00	29255136
211	Phosphorylation	ADQTPGATPKKLSSW CCCCCCCCCCCCCCC	41.37	29255136
213	2-Hydroxyisobutyrylation	QTPGATPKKLSSWDQ CCCCCCCCCCCCCCC	63.09	-
213	Acetylation	QTPGATPKKLSSWDQ CCCCCCCCCCCCCCC	63.09	26051181
213	Ubiquitination	QTPGATPKKLSSWDQ CCCCCCCCCCCCCCC	63.09	-
214	Sumoylation	TPGATPKKLSSWDQA CCCCCCCCCCCCCCC	55.60	-
214	Acetylation	TPGATPKKLSSWDQA CCCCCCCCCCCCCCC	55.60	25953088
214	Sumoylation	TPGATPKKLSSWDQA CCCCCCCCCCCCCCC	55.60	28112733
214	Ubiquitination	TPGATPKKLSSWDQA CCCCCCCCCCCCCCC	55.60	-
216	Phosphorylation	GATPKKLSSWDQAET CCCCCCCCCCCCCCC	37.96	23927012
217	Phosphorylation	ATPKKLSSWDQAETP CCCCCCCCCCCCCCC	45.14	23927012
223	Phosphorylation	SSWDQAETPGHTPSL CCCCCCCCCCCCCCC	37.27	22167270
227	Phosphorylation	QAETPGHTPSLRWDE CCCCCCCCCCCCCCC	22.08	22167270
229	Phosphorylation	ETPGHTPSLRWDETP CCCCCCCCCCCCCCC	31.55	22167270
231	Methylation	PGHTPSLRWDETPGR CCCCCCCCCCCCCCC	43.04	115916605
235	Phosphorylation	PSLRWDETPGRAKGS CCCCCCCCCCCCCCC	28.68	25159151
240	Ubiquitination	DETPGRAKGSETPGA CCCCCCCCCCCCCCC	62.70	-
242	Phosphorylation	TPGRAKGSETPGATP CCCCCCCCCCCCCCC	37.28	30266825
244	Phosphorylation	GRAKGSETPGATPGS CCCCCCCCCCCCCCC	28.81	29255136
248	Phosphorylation	GSETPGATPGSKIWD CCCCCCCCCCCCCCC	33.81	29255136
251	Phosphorylation	TPGATPGSKIWDPTP CCCCCCCCCCCCCCC	23.36	30266825
252	Acetylation	PGATPGSKIWDPTPS CCCCCCCCCCCCCCC	54.45	26051181
257	Phosphorylation	GSKIWDPTPSHTPAG CCCCCCCCCCCCCCC	34.64	23401153
259	Phosphorylation	KIWDPTPSHTPAGAA CCCCCCCCCCCCCCC	42.33	23401153
261	Phosphorylation	WDPTPSHTPAGAATP CCCCCCCCCCCCCCC	21.12	25159151
267	Phosphorylation	HTPAGAATPGRGDTP CCCCCCCCCCCCCCC	26.24	23927012
273	Phosphorylation	ATPGRGDTPGHATPG CCCCCCCCCCCCCCC	33.71	29255136
278	Phosphorylation	GDTPGHATPGHGGAT CCCCCCCCCCCCCCC	24.91	29255136
285	Phosphorylation	TPGHGGATSSARKNR CCCCCCCCCHHHCCC	26.87	23401153
286	Phosphorylation	PGHGGATSSARKNRW CCCCCCCCHHHCCCC	22.82	23927012
287	Phosphorylation	GHGGATSSARKNRWD CCCCCCCHHHCCCCC	27.95	25159151
290	Methylation	GATSSARKNRWDETP CCCCHHHCCCCCCCC	51.05	23748837
296	Phosphorylation	RKNRWDETPKTERDT HCCCCCCCCCCCCCC	27.84	23401153
298	Acetylation	NRWDETPKTERDTPG CCCCCCCCCCCCCCC	71.13	26051181
299	Phosphorylation	RWDETPKTERDTPGH CCCCCCCCCCCCCCC	37.14	22167270
303	Phosphorylation	TPKTERDTPGHGSGW CCCCCCCCCCCCCCC	37.07	22167270
308	Phosphorylation	RDTPGHGSGWAETPR CCCCCCCCCCCCCCC	26.03	30266825
313	Phosphorylation	HGSGWAETPRTDRGG CCCCCCCCCCCCCCC	15.43	23927012
316	Phosphorylation	GWAETPRTDRGGDSI CCCCCCCCCCCCCCC	31.11	23927012
318	Methylation	AETPRTDRGGDSIGE CCCCCCCCCCCCCCC	50.83	115916609
322	Phosphorylation	RTDRGGDSIGETPTP CCCCCCCCCCCCCCC	35.45	23401153
326	Phosphorylation	GGDSIGETPTPGASK CCCCCCCCCCCCCCC	27.52	29255136
328	Phosphorylation	DSIGETPTPGASKRK CCCCCCCCCCCCCCC	41.60	29255136
332	O-linked_Glycosylation	ETPTPGASKRKSRWD CCCCCCCCCCCCCCC	38.62	23301498
332	Phosphorylation	ETPTPGASKRKSRWD CCCCCCCCCCCCCCC	38.62	29255136
333	2-Hydroxyisobutyrylation	TPTPGASKRKSRWDE CCCCCCCCCCCCCCC	64.41	-
333	Acetylation	TPTPGASKRKSRWDE CCCCCCCCCCCCCCC	64.41	25953088
333	Ubiquitination	TPTPGASKRKSRWDE CCCCCCCCCCCCCCC	64.41	21890473
336	Phosphorylation	PGASKRKSRWDETPA CCCCCCCCCCCCCCH	42.51	27732954
341	Phosphorylation	RKSRWDETPASQMGG CCCCCCCCCHHHCCC	22.98	29255136
344	Phosphorylation	RWDETPASQMGGSTP CCCCCCHHHCCCCCC	23.15	23401153
349	Phosphorylation	PASQMGGSTPVLTPG CHHHCCCCCCCCCCC	24.65	29255136
350	Phosphorylation	ASQMGGSTPVLTPGK HHHCCCCCCCCCCCC	22.23	29255136
354	Phosphorylation	GGSTPVLTPGKTPIG CCCCCCCCCCCCCCC	30.17	22167270
358	Phosphorylation	PVLTPGKTPIGTPAM CCCCCCCCCCCCCCC	26.50	28634298
362	Phosphorylation	PGKTPIGTPAMNMAT CCCCCCCCCCCCCCC	14.48	25002506
369	Phosphorylation	TPAMNMATPTPGHIM CCCCCCCCCCCCCCC	19.54	25627689
371	Phosphorylation	AMNMATPTPGHIMSM CCCCCCCCCCCCCCC	37.23	25002506
377	Phosphorylation	PTPGHIMSMTPEQLQ CCCCCCCCCCHHHHH	20.92	25159151
379	Phosphorylation	PGHIMSMTPEQLQAW CCCCCCCCHHHHHHH	19.16	25159151
400	Phosphorylation	DERNRPLSDEELDAM HCCCCCCCHHHHHHH	45.73	30266825
412	Phosphorylation	DAMFPEGYKVLPPPA HHHCCCCCCCCCCCC	9.03	23403867
413	Sumoylation	AMFPEGYKVLPPPAG HHCCCCCCCCCCCCC	48.42	-
413	Acetylation	AMFPEGYKVLPPPAG HHCCCCCCCCCCCCC	48.42	25953088
413	Sumoylation	AMFPEGYKVLPPPAG HHCCCCCCCCCCCCC	48.42	25114211
413	Ubiquitination	AMFPEGYKVLPPPAG HHCCCCCCCCCCCCC	48.42	-
421	Phosphorylation	VLPPPAGYVPIRTPA CCCCCCCCCCCCCCC	12.73	30183078
426	Phosphorylation	AGYVPIRTPARKLTA CCCCCCCCCCCCCCC	23.24	30266825
430	Sumoylation	PIRTPARKLTATPTP CCCCCCCCCCCCCCC	52.90	28112733
432	Phosphorylation	RTPARKLTATPTPLG CCCCCCCCCCCCCCC	31.36	30266825
434	Phosphorylation	PARKLTATPTPLGGM CCCCCCCCCCCCCCC	23.59	29255136
436	Phosphorylation	RKLTATPTPLGGMTG CCCCCCCCCCCCCCC	27.13	29255136
442	Phosphorylation	PTPLGGMTGFHMQTE CCCCCCCCCCEEECC	39.71	30266825
448	Phosphorylation	MTGFHMQTEDRTMKS CCCCEEECCCCCCCC	32.07	23927012
454	Ubiquitination	QTEDRTMKSVNDQPS ECCCCCCCCCCCCCC	51.11	21890473
455	Phosphorylation	TEDRTMKSVNDQPSG CCCCCCCCCCCCCCC	18.48	28348404
461	Phosphorylation	KSVNDQPSGNLPFLK CCCCCCCCCCCCCCC	34.38	27174698
468	Acetylation	SGNLPFLKPDDIQYF CCCCCCCCHHHCCHH	46.94	26051181
468	Sumoylation	SGNLPFLKPDDIQYF CCCCCCCCHHHCCHH	46.94	-
468	Ubiquitination	SGNLPFLKPDDIQYF CCCCCCCCHHHCCHH	46.94	21890473
474	Phosphorylation	LKPDDIQYFDKLLVD CCHHHCCHHHHEEEC	17.68	27174698
477	Ubiquitination	DDIQYFDKLLVDVDE HHCCHHHHEEECCCC	33.55	-
485	Phosphorylation	LLVDVDESTLSPEEQ EEECCCCCCCCHHHH	30.13	30266825
486	Phosphorylation	LVDVDESTLSPEEQK EECCCCCCCCHHHHH	29.25	30266825
488	Phosphorylation	DVDESTLSPEEQKER CCCCCCCCHHHHHHH	30.29	29255136
493	Acetylation	TLSPEEQKERKIMKL CCCHHHHHHHHHHHH	63.87	26051181
493	Ubiquitination	TLSPEEQKERKIMKL CCCHHHHHHHHHHHH	63.87	21890473
499	Sumoylation	QKERKIMKLLLKIKN HHHHHHHHHHHHHHC	39.18	-
499	Acetylation	QKERKIMKLLLKIKN HHHHHHHHHHHHHHC	39.18	25953088
499	Sumoylation	QKERKIMKLLLKIKN HHHHHHHHHHHHHHC	39.18	-
499	Ubiquitination	QKERKIMKLLLKIKN HHHHHHHHHHHHHHC	39.18	21890473
508	Phosphorylation	LLKIKNGTPPMRKAA HHHHHCCCCCHHHHH	33.34	-
517	Methylation	PMRKAALRQITDKAR CHHHHHHHHHHHHHH	22.56	115916613
541	Phosphorylation	QILPLLMSPTLEDQE HHHHHHHCCCCCHHH	18.07	-
554	Acetylation	QERHLLVKVIDRILY HHHHHHHHHHHHHHH	33.18	19608861
554	Ubiquitination	QERHLLVKVIDRILY HHHHHHHHHHHHHHH	33.18	21906983
558	Methylation	LLVKVIDRILYKLDD HHHHHHHHHHHHHHH	15.08	115916617
562	Acetylation	VIDRILYKLDDLVRP HHHHHHHHHHHHHHH	41.83	19608861
608	Phosphorylation	AKAAGLATMISTMRP HHHHCHHHHHHHCCC	21.78	20068231
611	Phosphorylation	AGLATMISTMRPDID HCHHHHHHHCCCCCC	12.82	20068231
612	Phosphorylation	GLATMISTMRPDIDN CHHHHHHHCCCCCCC	13.28	20068231
623	Phosphorylation	DIDNMDEYVRNTTAR CCCCHHHHHHHHHHH	10.63	20068231
656	Acetylation	KAVCKSKKSWQARHT HHHHCCCCCHHHHHH	65.11	26051181
700	2-Hydroxyisobutyrylation	GLVDEQQKVRTISAL CCCCHHHHHHHHHHH	33.12	-
700	Acetylation	GLVDEQQKVRTISAL CCCCHHHHHHHHHHH	33.12	25953088
700	Ubiquitination	GLVDEQQKVRTISAL CCCCHHHHHHHHHHH	33.12	21890473
733	Ubiquitination	SVLKPLWKGIRQHRG HHHHHHHHHHHHHCC	52.74	-
757	Sulfoxidation	IGYLIPLMDAEYANY HHHHHHHCCHHHHCC	3.73	28183972
761	Phosphorylation	IPLMDAEYANYYTRE HHHCCHHHHCCCHHH	11.23	-
764	Phosphorylation	MDAEYANYYTREVML CCHHHHCCCHHHHHH	9.68	-
785	2-Hydroxyisobutyrylation	QSPDEEMKKIVLKVV CCCCHHHHHHHHHHH	42.50	-
785	Acetylation	QSPDEEMKKIVLKVV CCCCHHHHHHHHHHH	42.50	26051181
785	Ubiquitination	QSPDEEMKKIVLKVV CCCCHHHHHHHHHHH	42.50	21890473
790	Acetylation	EMKKIVLKVVKQCCG HHHHHHHHHHHHHHC	33.80	25953088
790	Malonylation	EMKKIVLKVVKQCCG HHHHHHHHHHHHHHC	33.80	26320211
790	Ubiquitination	EMKKIVLKVVKQCCG HHHHHHHHHHHHHHC	33.80	-
793	Acetylation	KIVLKVVKQCCGTDG HHHHHHHHHHHCCCC	40.37	26051181
793	Ubiquitination	KIVLKVVKQCCGTDG HHHHHHHHHHHCCCC	40.37	21890473
805	Phosphorylation	TDGVEANYIKTEILP CCCCHHHEEEHHCCC	15.73	25367160
808	Phosphorylation	VEANYIKTEILPPFF CHHHEEEHHCCCHHH	20.78	19664995
816	Acetylation	EILPPFFKHFWQHRM HCCCHHHHHHHHHHH	37.97	25953088
816	Ubiquitination	EILPPFFKHFWQHRM HCCCHHHHHHHHHHH	37.97	21890473
843	2-Hydroxyisobutyrylation	TTVELANKVGAAEII HHHHHHHHHCHHHHH	36.12	-
851	Phosphorylation	VGAAEIISRIVDDLK HCHHHHHHHHHHHHH	22.93	20068231
858	2-Hydroxyisobutyrylation	SRIVDDLKDEAEQYR HHHHHHHHHHHHHHH	61.59	-
858	Acetylation	SRIVDDLKDEAEQYR HHHHHHHHHHHHHHH	61.59	26051181
858	Ubiquitination	SRIVDDLKDEAEQYR HHHHHHHHHHHHHHH	61.59	-
866	2-Hydroxyisobutyrylation	DEAEQYRKMVMETIE HHHHHHHHHHHHHHH	30.80	-
866	Ubiquitination	DEAEQYRKMVMETIE HHHHHHHHHHHHHHH	30.80	-
871	Phosphorylation	YRKMVMETIEKIMGN HHHHHHHHHHHHHHH	19.15	29759185
874	Ubiquitination	MVMETIEKIMGNLGA HHHHHHHHHHHHCCC	33.86	-
876	Sulfoxidation	METIEKIMGNLGAAD HHHHHHHHHHCCCCC	4.27	28183972
926	Acetylation	NALGKRVKPYLPQIC HHHHHCCCCCHHHHH	31.79	26051181
926	Ubiquitination	NALGKRVKPYLPQIC HHHHHCCCCCHHHHH	31.79	-
956	Phosphorylation	QQAADLISRTAVVMK HHHHHHHHHHHHHHH	30.76	24850871
963	2-Hydroxyisobutyrylation	SRTAVVMKTCQEEKL HHHHHHHHHHHHHHH	34.24	-
963	Acetylation	SRTAVVMKTCQEEKL HHHHHHHHHHHHHHH	34.24	25953088
963	Ubiquitination	SRTAVVMKTCQEEKL HHHHHHHHHHHHHHH	34.24	-
1008	Acetylation	VNVIGMHKMTPPIKD HHHHCHHCCCCCHHH	35.26	25953088
1008	Ubiquitination	VNVIGMHKMTPPIKD HHHHCHHCCCCCHHH	35.26	21890473
1014	Ubiquitination	HKMTPPIKDLLPRLT HCCCCCHHHHHHHHH	48.36	21890473
1021	Phosphorylation	KDLLPRLTPILKNRH HHHHHHHHHHHHCHH	15.01	27050516
1025	Acetylation	PRLTPILKNRHEKVQ HHHHHHHHCHHHHHH	53.29	25953088
1025	Ubiquitination	PRLTPILKNRHEKVQ HHHHHHHHCHHHHHH	53.29	21890473
1030	2-Hydroxyisobutyrylation	ILKNRHEKVQENCID HHHCHHHHHHHHHHH	42.99	-
1030	Acetylation	ILKNRHEKVQENCID HHHCHHHHHHHHHHH	42.99	26051181
1030	Ubiquitination	ILKNRHEKVQENCID HHHCHHHHHHHHHHH	42.99	-
1035	Glutathionylation	HEKVQENCIDLVGRI HHHHHHHHHHHHHHH	2.23	22555962
1045	Methylation	LVGRIADRGAEYVSA HHHHHHHCCCHHCCH	36.88	115916597
1059	S-nitrosylation	AREWMRICFELLELL HHHHHHHHHHHHHHH	1.21	22178444
1059	S-palmitoylation	AREWMRICFELLELL HHHHHHHHHHHHHHH	1.21	29575903
1067	Acetylation	FELLELLKAHKKAIR HHHHHHHHHHHHHHH	62.15	25825284
1080	Phosphorylation	IRRATVNTFGYIAKA HHHHCCHHHHHHHHH	17.69	28152594
1083	Phosphorylation	ATVNTFGYIAKAIGP HCCHHHHHHHHHHCH	8.10	28152594
1102	Acetylation	ATLLNNLKVQERQNR HHHHHHHCHHHHHCC	43.95	26051181
1102	Ubiquitination	ATLLNNLKVQERQNR HHHHHHHCHHHHHCC	43.95	21890473
1136	Phosphorylation	LPALMNEYRVPELNV HHHHHHHCCCCCHHH	16.35	22817900
1170	Phosphorylation	KDYIYAVTPLLEDAL CHHEEEECHHHHHHH	10.47	-
1180	Methylation	LEDALMDRDLVHRQT HHHHHCCCCHHHHHH	25.79	115916601
1269	Phosphorylation	RDVYWKIYNSIYIGS HHHHHHHHCCEEECC	10.10	28152594
1271	Phosphorylation	VYWKIYNSIYIGSQD HHHHHHCCEEECCCC	10.37	28152594
1273	Phosphorylation	WKIYNSIYIGSQDAL HHHHCCEEECCCCCC	10.07	28152594
1288	Phosphorylation	IAHYPRIYNDDKNTY EECCCEEEECCCCEE	17.51	28152594
1292	2-Hydroxyisobutyrylation	PRIYNDDKNTYIRYE CEEEECCCCEEEEEE	54.79	-
1292	Acetylation	PRIYNDDKNTYIRYE CEEEECCCCEEEEEE	54.79	26051181
1292	Ubiquitination	PRIYNDDKNTYIRYE CEEEECCCCEEEEEE	54.79	21890473
1294	Phosphorylation	IYNDDKNTYIRYELD EEECCCCEEEEEEEE	26.51	28152594
1295	Phosphorylation	YNDDKNTYIRYELDY EECCCCEEEEEEEEE	7.87	28152594
1302	Phosphorylation	YIRYELDYIL----- EEEEEEEECC-----	19.42	-

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
142	T	Phosphorylation	Kinase	CDK2	P24941	PSP
211	T	Phosphorylation	Kinase	CDK2	P24941	PSP
244	T	Phosphorylation	Kinase	CDK2	P24941	PSP
248	T	Phosphorylation	Kinase	CDK2	P24941	PSP
273	T	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
313	T	Phosphorylation	Kinase	CDK2	P24941	PSP
354	T	Phosphorylation	Kinase	CDK2	P24941	PSP
426	T	Phosphorylation	Kinase	CDK2	P24941	PSP
434	T	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
434	T	Phosphorylation	Kinase	DYR1B	Q9Y463	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
244	T	Phosphorylation	12105215
Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis.
248	T	Phosphorylation	12105215
Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis.
313	T	Phosphorylation	12105215
Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis.

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 SF3B1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SF3B2_HUMAN	SF3B2	physical	10490618
SF3B3_HUMAN	SF3B3	physical	10490618
PP1R8_HUMAN	PPP1R8	physical	12105215
SF3B2_HUMAN	SF3B2	physical	12234937
SF3B3_HUMAN	SF3B3	physical	12234937
DDX42_HUMAN	DDX42	physical	12234937
SF3B4_HUMAN	SF3B4	physical	12234937
SF3B6_HUMAN	SF3B6	physical	12234937
SF3B5_HUMAN	SF3B5	physical	12234937
PHF5A_HUMAN	PHF5A	physical	12234937
SF3B3_HUMAN	SF3B3	physical	22939629
SF3B2_HUMAN	SF3B2	physical	22939629
SF3B5_HUMAN	SF3B5	physical	22939629
SF3B4_HUMAN	SF3B4	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
SMD3_HUMAN	SNRPD3	physical	22939629
U5S1_HUMAN	EFTUD2	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
SFPQ_HUMAN	SFPQ	physical	22939629
TRA2B_HUMAN	TRA2B	physical	22939629
TADBP_HUMAN	TARDBP	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
THOC1_HUMAN	THOC1	physical	22939629
SNUT2_HUMAN	USP39	physical	22939629
SSRP1_HUMAN	SSRP1	physical	22939629
UBP2L_HUMAN	UBAP2L	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
SYEP_HUMAN	EPRS	physical	22939629
SON_HUMAN	SON	physical	22939629
TR112_HUMAN	TRMT112	physical	22939629
SURF4_HUMAN	SURF4	physical	22939629
TMED9_HUMAN	TMED9	physical	22939629
SSRG_HUMAN	SSR3	physical	22939629
TCPZ_HUMAN	CCT6A	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
TPM1_HUMAN	TPM1	physical	22939629
TIF1A_HUMAN	TRIM24	physical	22939629
TIM13_HUMAN	TIMM13	physical	22939629
TBA1B_HUMAN	TUBA1B	physical	22939629
SSBP_HUMAN	SSBP1	physical	22939629
TOX4_HUMAN	TOX4	physical	22939629
TFPI1_HUMAN	TFPI	physical	22939629
SF3B6_HUMAN	SF3B6	physical	22365833
SPF45_HUMAN	RBM17	physical	22365833
PLRG1_HUMAN	PLRG1	physical	22365833
SNIP1_HUMAN	SNIP1	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
RL23A_HUMAN	RPL23A	physical	22751105
RL18A_HUMAN	RPL18A	physical	22751105
RL3_HUMAN	RPL3	physical	22751105
RL10_HUMAN	RPL10	physical	22751105
RS2_HUMAN	RPS2	physical	22751105
CAZA1_HUMAN	CAPZA1	physical	26344197
CCD97_HUMAN	CCDC97	physical	26344197
COPA_HUMAN	COPA	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
COPG1_HUMAN	COPG1	physical	26344197
IMA1_HUMAN	KPNA2	physical	26344197
LONM_HUMAN	LONP1	physical	26344197
PHF5A_HUMAN	PHF5A	physical	26344197
PRPF3_HUMAN	PRPF3	physical	26344197
PRP31_HUMAN	PRPF31	physical	26344197
PRP4_HUMAN	PRPF4	physical	26344197
SNUT1_HUMAN	SART1	physical	26344197
SF3A1_HUMAN	SF3A1	physical	26344197
SF3A2_HUMAN	SF3A2	physical	26344197
SF3A3_HUMAN	SF3A3	physical	26344197
SF3B2_HUMAN	SF3B2	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
SF3B4_HUMAN	SF3B4	physical	26344197
SF3B5_HUMAN	SF3B5	physical	26344197
SF3B6_HUMAN	SF3B6	physical	26344197
U520_HUMAN	SNRNP200	physical	26344197
RU2A_HUMAN	SNRPA1	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
SMD2_HUMAN	SNRPD2	physical	26344197

Drug and Disease Associations

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

Regulatory Network of SF3B1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-554 AND LYS-562,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-129; THR-207; THR-211;THR-223; THR-227; THR-326; SER-332; THR-341; SER-349; THR-350;SER-400; THR-434 AND THR-436, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-194; THR-207; THR-211;THR-267; THR-273; SER-322; THR-326; THR-328; SER-349; THR-350; THR-354AND SER-488, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-129; THR-142; SER-194;THR-207; THR-211; THR-223; THR-227; THR-235; THR-326; THR-328; SER-332AND SER-488, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 THR-211; THR-354 ANDSER-488, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-344; THR-350 ANDTHR-354, AND MASS SPECTROMETRY.	15302935 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223; THR-227; THR-257;THR-261; THR-267; THR-299 AND THR-432, AND MASS SPECTROMETRY.	18220336 [Abstract]
"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 THR-142; THR-223 ANDTHR-244, AND MASS SPECTROMETRY.	17924679 [Abstract]
"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 THR-207; THR-211; THR-326AND THR-328, AND MASS SPECTROMETRY.	16964243 [Abstract]
"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 THR-211; THR-223; THR-296;THR-299; THR-316 AND THR-326, AND MASS SPECTROMETRY.	17081983 [Abstract]
"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 THR-235, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Phosphorylation-dependent interaction between the splicing factorsSAP155 and NIPP1."; Boudrez A., Beullens M., Waelkens E., Stalmans W., Bollen M.; J. Biol. Chem. 277:31834-31841(2002). Cited for: INTERACTION WITH PPP1R8, PHOSPHORYLATION AT THR-244; THR-248 ANDTHR-313, AND MUTAGENESIS OF THR-223; THR-227; THR-235; THR-244;THR-248; THR-257; THR-261; THR-267; THR-273; THR-278; THR-296; THR-303AND THR-313.	12105215 [Abstract]

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