NUMA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NUMA1_HUMAN
• UniProt AC: Q14980
• Protein Name: Nuclear mitotic apparatus protein 1 {ECO:0000312|HGNC:HGNC:8059}
• Gene Name: NUMA1 {ECO:0000312|HGNC:HGNC:8059}
• Organism: Homo sapiens (Human).
• Sequence Length: 2115
• Subcellular Localization: Nucleus . Nucleus, nucleoplasm . Nucleus matrix . Chromosome . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cell cortex . Cell membrane ; Lipid-anchor ; C
• Protein Description: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division. [PubMed: 7769006]
• Protein Sequence: MTLHATRGAALLSWVNSLHVADPVEAVLQLQDCSIFIKIIDRIHGTEEGQQILKQPVSERLDFVCSFLQKNRKHPSSPECLVSAQKVLEGSELELAKMTMLLLYHSTMSSKSPRDWEQFEYKIQAELAVILKFVLDHEDGLNLNEDLENFLQKAPVPSTCSSTFPEELSPPSHQAKREIRFLELQKVASSSSGNNFLSGSPASPMGDILQTPQFQMRRLKKQLADERSNRDELELELAENRKLLTEKDAQIAMMQQRIDRLALLNEKQAASPLEPKELEELRDKNESLTMRLHETLKQCQDLKTEKSQMDRKINQLSEENGDLSFKLREFASHLQQLQDALNELTEEHSKATQEWLEKQAQLEKELSAALQDKKCLEEKNEILQGKLSQLEEHLSQLQDNPPQEKGEVLGDVLQLETLKQEAATLAANNTQLQARVEMLETERGQQEAKLLAERGHFEEEKQQLSSLITDLQSSISNLSQAKEELEQASQAHGARLTAQVASLTSELTTLNATIQQQDQELAGLKQQAKEKQAQLAQTLQQQEQASQGLRHQVEQLSSSLKQKEQQLKEVAEKQEATRQDHAQQLATAAEEREASLRERDAALKQLEALEKEKAAKLEILQQQLQVANEARDSAQTSVTQAQREKAELSRKVEELQACVETARQEQHEAQAQVAELELQLRSEQQKATEKERVAQEKDQLQEQLQALKESLKVTKGSLEEEKRRAADALEEQQRCISELKAETRSLVEQHKRERKELEEERAGRKGLEARLQQLGEAHQAETEVLRRELAEAMAAQHTAESECEQLVKEVAAWRERYEDSQQEEAQYGAMFQEQLMTLKEECEKARQELQEAKEKVAGIESHSELQISRQQNELAELHANLARALQQVQEKEVRAQKLADDLSTLQEKMAATSKEVARLETLVRKAGEQQETASRELVKEPARAGDRQPEWLEEQQGRQFCSTQAALQAMEREAEQMGNELERLRAALMESQGQQQEERGQQEREVARLTQERGRAQADLALEKAARAELEMRLQNALNEQRVEFATLQEALAHALTEKEGKDQELAKLRGLEAAQIKELEELRQTVKQLKEQLAKKEKEHASGSGAQSEAAGRTEPTGPKLEALRAEVSKLEQQCQKQQEQADSLERSLEAERASRAERDSALETLQGQLEEKAQELGHSQSALASAQRELAAFRTKVQDHSKAEDEWKAQVARGRQEAERKNSLISSLEEEVSILNRQVLEKEGESKELKRLVMAESEKSQKLEERLRLLQAETASNSARAAERSSALREEVQSLREEAEKQRVASENLRQELTSQAERAEELGQELKAWQEKFFQKEQALSTLQLEHTSTQALVSELLPAKHLCQQLQAEQAAAEKRHREELEQSKQAAGGLRAELLRAQRELGELIPLRQKVAEQERTAQQLRAEKASYAEQLSMLKKAHGLLAEENRGLGERANLGRQFLEVELDQAREKYVQELAAVRADAETRLAEVQREAQSTARELEVMTAKYEGAKVKVLEERQRFQEERQKLTAQVEQLEVFQREQTKQVEELSKKLADSDQASKVQQQKLKAVQAQGGESQQEAQRLQAQLNELQAQLSQKEQAAEHYKLQMEKAKTHYDAKKQQNQELQEQLRSLEQLQKENKELRAEAERLGHELQQAGLKTKEAEQTCRHLTAQVRSLEAQVAHADQQLRDLGKFQVATDALKSREPQAKPQLDLSIDSLDLSCEEGTPLSITSKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFTPIPARSQAPLESSLDSLGDVFLDSGRKTRSARRRTTQIINITMTKKLDVEEPDSANSSFYSTRSAPASQASLRATSSTQSLARLGSPDYGNSALLSLPGYRPTTRSSARRSQAGVSSGAPPGRNSFYMGTCQDEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESRPSLSLGTITDEEMKTGDPQETLRRASMQPIQIAEGTGITTRQQRKRVSLEPHQGPGTPESKKATSCFPRPMTPRDRHEGRKQSTTEAQKKAAPASTKQADRRQSMAFSILNTPKKLGNSLLRRGASKKALSKASPNTRSGTRRSPRIATTTASAATAAAIGATPRAKGKAKH

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	Phosphorylation	------MTLHATRGA ------CCCCCHHHH	38.26	20068231
6	Phosphorylation	--MTLHATRGAALLS --CCCCCHHHHHHHH	20.91	20068231
42	Methylation	IFIKIIDRIHGTEEG HHHHHHHHHCCCHHH	16.64	115485773
46	Phosphorylation	IIDRIHGTEEGQQIL HHHHHCCCHHHHHHH	19.39	20068231
54	Acetylation	EEGQQILKQPVSERL HHHHHHHHCCHHHHH	54.94	26051181
54	Ubiquitination	EEGQQILKQPVSERL HHHHHHHHCCHHHHH	54.94	21890473
70	Acetylation	FVCSFLQKNRKHPSS HHHHHHHHCCCCCCC	61.95	25953088
73	Acetylation	SFLQKNRKHPSSPEC HHHHHCCCCCCCHHH	70.07	27452117
73	Ubiquitination	SFLQKNRKHPSSPEC HHHHHCCCCCCCHHH	70.07	-
76	Phosphorylation	QKNRKHPSSPECLVS HHCCCCCCCHHHHHH	59.24	25159151
77	Phosphorylation	KNRKHPSSPECLVSA HCCCCCCCHHHHHHH	29.21	25159151
80	Glutathionylation	KHPSSPECLVSAQKV CCCCCHHHHHHHHHH	5.30	22555962
80	S-nitrosylation	KHPSSPECLVSAQKV CCCCCHHHHHHHHHH	5.30	22178444
83	Phosphorylation	SSPECLVSAQKVLEG CCHHHHHHHHHHHCC	16.42	26552605
91	Phosphorylation	AQKVLEGSELELAKM HHHHHCCCHHHHHHH	29.63	-
99	Phosphorylation	ELELAKMTMLLLYHS HHHHHHHHHHHHHHH	12.17	25907765
104	Phosphorylation	KMTMLLLYHSTMSSK HHHHHHHHHHHCCCC	8.16	25907765
106	Phosphorylation	TMLLLYHSTMSSKSP HHHHHHHHHCCCCCC	16.55	20860994
107	Phosphorylation	MLLLYHSTMSSKSPR HHHHHHHHCCCCCCC	14.04	25907765
109	Phosphorylation	LLYHSTMSSKSPRDW HHHHHHCCCCCCCCH	34.40	25907765
110	Phosphorylation	LYHSTMSSKSPRDWE HHHHHCCCCCCCCHH	26.74	20860994
111	Acetylation	YHSTMSSKSPRDWEQ HHHHCCCCCCCCHHH	58.11	25953088
112	Phosphorylation	HSTMSSKSPRDWEQF HHHCCCCCCCCHHHH	27.41	25849741
153	Ubiquitination	DLENFLQKAPVPSTC HHHHHHHHCCCCCCC	57.72	-
158	Phosphorylation	LQKAPVPSTCSSTFP HHHCCCCCCCCCCCC	42.13	23927012
159	Phosphorylation	QKAPVPSTCSSTFPE HHCCCCCCCCCCCCH	15.44	23927012
161	Phosphorylation	APVPSTCSSTFPEEL CCCCCCCCCCCCHHH	32.28	23927012
162	Phosphorylation	PVPSTCSSTFPEELS CCCCCCCCCCCHHHC	35.89	23927012
163	Phosphorylation	VPSTCSSTFPEELSP CCCCCCCCCCHHHCC	27.24	23927012
169	Phosphorylation	STFPEELSPPSHQAK CCCCHHHCCCCHHHH	37.74	29255136
169 (in isoform 2)	Phosphorylation	-	37.74	21406692
172	Phosphorylation	PEELSPPSHQAKREI CHHHCCCCHHHHHHH	31.45	30266825
176	Acetylation	SPPSHQAKREIRFLE CCCCHHHHHHHHHHH	43.95	25953088
176	Ubiquitination	SPPSHQAKREIRFLE CCCCHHHHHHHHHHH	43.95	-
189	Phosphorylation	LELQKVASSSSGNNF HHHHHHHCCCCCCCC	33.47	20068231
190	Phosphorylation	ELQKVASSSSGNNFL HHHHHHCCCCCCCCC	20.84	20068231
191	Phosphorylation	LQKVASSSSGNNFLS HHHHHCCCCCCCCCC	39.51	20068231
192	Phosphorylation	QKVASSSSGNNFLSG HHHHCCCCCCCCCCC	47.70	22199227
198	Phosphorylation	SSGNNFLSGSPASPM CCCCCCCCCCCCCCC	32.84	23401153
200	Phosphorylation	GNNFLSGSPASPMGD CCCCCCCCCCCCCHH	17.57	25159151
203	Phosphorylation	FLSGSPASPMGDILQ CCCCCCCCCCHHHHC	20.85	25159151
211	Phosphorylation	PMGDILQTPQFQMRR CCHHHHCCHHHHHHH	18.66	25159151
247	Acetylation	NRKLLTEKDAQIAMM HHHCCCHHHHHHHHH	53.80	26051181
247	Ubiquitination	NRKLLTEKDAQIAMM HHHCCCHHHHHHHHH	53.80	-
267	2-Hydroxyisobutyrylation	RLALLNEKQAASPLE HHHHHCHHHCCCCCC	44.13	-
267	Acetylation	RLALLNEKQAASPLE HHHHHCHHHCCCCCC	44.13	26051181
267	Ubiquitination	RLALLNEKQAASPLE HHHHHCHHHCCCCCC	44.13	21906983
267 (in isoform 1)	Ubiquitination	-	44.13	21906983
267 (in isoform 2)	Ubiquitination	-	44.13	21906983
267	Ubiquitination	RLALLNEKQAASPLE HHHHHCHHHCCCCCC	44.13	21906983
271	Phosphorylation	LNEKQAASPLEPKEL HCHHHCCCCCCHHHH	32.79	23401153
284	Acetylation	ELEELRDKNESLTMR HHHHHHHHCHHHHHH	57.06	25953088
284	Ubiquitination	ELEELRDKNESLTMR HHHHHHHHCHHHHHH	57.06	-
289	Phosphorylation	RDKNESLTMRLHETL HHHCHHHHHHHHHHH	14.99	17081983
297	Acetylation	MRLHETLKQCQDLKT HHHHHHHHHHHHHHH	57.35	26051181
297	Ubiquitination	MRLHETLKQCQDLKT HHHHHHHHHHHHHHH	57.35	-
303	Acetylation	LKQCQDLKTEKSQMD HHHHHHHHHHHHHHH	64.03	23749302
303	Ubiquitination	LKQCQDLKTEKSQMD HHHHHHHHHHHHHHH	64.03	-
311	Dimethylation	TEKSQMDRKINQLSE HHHHHHHHHHHHHHH	36.09	-
311	Methylation	TEKSQMDRKINQLSE HHHHHHHHHHHHHHH	36.09	24411725
312	Ubiquitination	EKSQMDRKINQLSEE HHHHHHHHHHHHHHH	41.57	-
324	Phosphorylation	SEENGDLSFKLREFA HHHCCCHHHHHHHHH	25.69	24719451
326	2-Hydroxyisobutyrylation	ENGDLSFKLREFASH HCCCHHHHHHHHHHH	43.17	-
326	Ubiquitination	ENGDLSFKLREFASH HCCCHHHHHHHHHHH	43.17	21890473
358	Ubiquitination	ATQEWLEKQAQLEKE HHHHHHHHHHHHHHH	49.08	21890473
364	Ubiquitination	EKQAQLEKELSAALQ HHHHHHHHHHHHHHH	72.97	21890473
373	Acetylation	LSAALQDKKCLEEKN HHHHHHCHHHHHHHH	32.21	25953088
374	Acetylation	SAALQDKKCLEEKNE HHHHHCHHHHHHHHH	52.95	26051181
379	Acetylation	DKKCLEEKNEILQGK CHHHHHHHHHHHHHH	50.97	19608861
379	Ubiquitination	DKKCLEEKNEILQGK CHHHHHHHHHHHHHH	50.97	-
386	Ubiquitination	KNEILQGKLSQLEEH HHHHHHHHHHHHHHH	31.82	21890473
386 (in isoform 1)	Ubiquitination	-	31.82	21906983
386 (in isoform 2)	Ubiquitination	-	31.82	21906983
386	Ubiquitination	KNEILQGKLSQLEEH HHHHHHHHHHHHHHH	31.82	21906983
388	Phosphorylation	EILQGKLSQLEEHLS HHHHHHHHHHHHHHH	35.88	17525332
395	Phosphorylation	SQLEEHLSQLQDNPP HHHHHHHHHHCCCCC	30.65	23401153
405	Ubiquitination	QDNPPQEKGEVLGDV CCCCCHHHCCHHHHH	55.94	-
419	Ubiquitination	VLQLETLKQEAATLA HHHHHHHHHHHHHHH	54.21	-
437	Ubiquitination	TQLQARVEMLETERG HHHHHHHHHHHHHHH	32.28	21906983
438	Sulfoxidation	QLQARVEMLETERGQ HHHHHHHHHHHHHHH	3.61	21406390
441	Phosphorylation	ARVEMLETERGQQEA HHHHHHHHHHHHHHH	27.33	20860994
449	2-Hydroxyisobutyrylation	ERGQQEAKLLAERGH HHHHHHHHHHHHCCC	43.19	-
449	Ubiquitination	ERGQQEAKLLAERGH HHHHHHHHHHHHCCC	43.19	-
531	Acetylation	LKQQAKEKQAQLAQT HHHHHHHHHHHHHHH	50.67	25953088
531	Ubiquitination	LKQQAKEKQAQLAQT HHHHHHHHHHHHHHH	50.67	-
558	Phosphorylation	HQVEQLSSSLKQKEQ HHHHHHHHHHHHHHH	48.56	25627689
561	Acetylation	EQLSSSLKQKEQQLK HHHHHHHHHHHHHHH	62.36	25953088
561	Ubiquitination	EQLSSSLKQKEQQLK HHHHHHHHHHHHHHH	62.36	-
561 (in isoform 2)	Ubiquitination	-	62.36	-
572	Ubiquitination	QQLKEVAEKQEATRQ HHHHHHHHHHHHHHH	61.52	21906983
573	Acetylation	QLKEVAEKQEATRQD HHHHHHHHHHHHHHH	43.64	25953088
587	Phosphorylation	DHAQQLATAAEEREA HHHHHHHHHHHHHHH	34.69	-
595	Phosphorylation	AAEEREASLRERDAA HHHHHHHHHHHHHHH	24.17	-
604	Acetylation	RERDAALKQLEALEK HHHHHHHHHHHHHHH	48.38	25953088
604	Ubiquitination	RERDAALKQLEALEK HHHHHHHHHHHHHHH	48.38	21890473
611	Acetylation	KQLEALEKEKAAKLE HHHHHHHHHHHHHHH	66.42	26051181
616	2-Hydroxyisobutyrylation	LEKEKAAKLEILQQQ HHHHHHHHHHHHHHH	52.06	-
616	Acetylation	LEKEKAAKLEILQQQ HHHHHHHHHHHHHHH	52.06	25953088
616	Ubiquitination	LEKEKAAKLEILQQQ HHHHHHHHHHHHHHH	52.06	21890473
633	Phosphorylation	VANEARDSAQTSVTQ HHHHHHHHHHHHHHH	19.40	21712546
636	Phosphorylation	EARDSAQTSVTQAQR HHHHHHHHHHHHHHH	25.53	24505115
637	Phosphorylation	ARDSAQTSVTQAQRE HHHHHHHHHHHHHHH	15.87	24505115
645	2-Hydroxyisobutyrylation	VTQAQREKAELSRKV HHHHHHHHHHHHHHH	49.72	-
697	Acetylation	KERVAQEKDQLQEQL HHHHHHHHHHHHHHH	38.40	26051181
697	Ubiquitination	KERVAQEKDQLQEQL HHHHHHHHHHHHHHH	38.40	-
708	Acetylation	QEQLQALKESLKVTK HHHHHHHHHHHCCCC	48.55	26051181
708	Succinylation	QEQLQALKESLKVTK HHHHHHHHHHHCCCC	48.55	23954790
708	Ubiquitination	QEQLQALKESLKVTK HHHHHHHHHHHCCCC	48.55	-
710	Phosphorylation	QLQALKESLKVTKGS HHHHHHHHHCCCCCC	31.72	24173317
712	Acetylation	QALKESLKVTKGSLE HHHHHHHCCCCCCHH	58.08	25953088
714	Phosphorylation	LKESLKVTKGSLEEE HHHHHCCCCCCHHHH	28.27	24173317
717	Phosphorylation	SLKVTKGSLEEEKRR HHCCCCCCHHHHHHH	33.88	24173317
737	Phosphorylation	EEQQRCISELKAETR HHHHHHHHHHHHHHH	40.27	26074081
740	Acetylation	QRCISELKAETRSLV HHHHHHHHHHHHHHH	39.87	25953088
740	Ubiquitination	QRCISELKAETRSLV HHHHHHHHHHHHHHH	39.87	-
751	2-Hydroxyisobutyrylation	RSLVEQHKRERKELE HHHHHHHHHHHHHHH	56.50	-
751	Acetylation	RSLVEQHKRERKELE HHHHHHHHHHHHHHH	56.50	25953088
755	Ubiquitination	EQHKRERKELEEERA HHHHHHHHHHHHHHH	63.00	-
782	Phosphorylation	GEAHQAETEVLRREL HHHHHHHHHHHHHHH	34.12	25690035
801	Phosphorylation	AAQHTAESECEQLVK HHHHHCHHHHHHHHH	45.11	28348404
803	Glutathionylation	QHTAESECEQLVKEV HHHCHHHHHHHHHHH	5.86	22555962
817	Phosphorylation	VAAWRERYEDSQQEE HHHHHHHHCHHHHHH	21.23	27732954
820	Phosphorylation	WRERYEDSQQEEAQY HHHHHCHHHHHHHHH	23.09	17525332
827	Phosphorylation	SQQEEAQYGAMFQEQ HHHHHHHHHHHHHHH	17.56	27080861
855	Ubiquitination	ELQEAKEKVAGIESH HHHHHHHHHHCCCCC	36.36	21890473
861	Phosphorylation	EKVAGIESHSELQIS HHHHCCCCCCHHHHH	30.32	25002506
863	Phosphorylation	VAGIESHSELQISRQ HHCCCCCCHHHHHHH	49.64	25002506
868	Phosphorylation	SHSELQISRQQNELA CCCHHHHHHHHHHHH	15.86	25002506
891	Acetylation	ALQQVQEKEVRAQKL HHHHHHHHHHHHHHH	44.40	19608861
891	Malonylation	ALQQVQEKEVRAQKL HHHHHHHHHHHHHHH	44.40	26320211
891	Ubiquitination	ALQQVQEKEVRAQKL HHHHHHHHHHHHHHH	44.40	-
891 (in isoform 1)	Ubiquitination	-	44.40	21906983
891 (in isoform 2)	Ubiquitination	-	44.40	21906983
897	2-Hydroxyisobutyrylation	EKEVRAQKLADDLST HHHHHHHHHHHHHHH	44.66	-
897	Acetylation	EKEVRAQKLADDLST HHHHHHHHHHHHHHH	44.66	26051181
897	Ubiquitination	EKEVRAQKLADDLST HHHHHHHHHHHHHHH	44.66	-
903	Phosphorylation	QKLADDLSTLQEKMA HHHHHHHHHHHHHHH	33.78	20860994
908	2-Hydroxyisobutyrylation	DLSTLQEKMAATSKE HHHHHHHHHHHCHHH	22.37	-
908	Ubiquitination	DLSTLQEKMAATSKE HHHHHHHHHHHCHHH	22.37	21890473
908 (in isoform 1)	Ubiquitination	-	22.37	21906983
908 (in isoform 2)	Ubiquitination	-	22.37	21906983
914	Ubiquitination	EKMAATSKEVARLET HHHHHCHHHHHHHHH	52.43	-
934	Phosphorylation	GEQQETASRELVKEP HHHHHHHHHHHHHCH	33.44	25159151
939	Ubiquitination	TASRELVKEPARAGD HHHHHHHHCHHCCCC	71.28	-
962	O-linked_Glycosylation	QQGRQFCSTQAALQA HHHHHHHHHHHHHHH	25.50	30059200
963	O-linked_Glycosylation	QGRQFCSTQAALQAM HHHHHHHHHHHHHHH	24.33	30059200
963	Phosphorylation	QGRQFCSTQAALQAM HHHHHHHHHHHHHHH	24.33	17525332
977	Sulfoxidation	MEREAEQMGNELERL HHHHHHHHHHHHHHH	4.72	21406390
989	Sulfoxidation	ERLRAALMESQGQQQ HHHHHHHHHHHHHHH	3.90	21406390
991	Phosphorylation	LRAALMESQGQQQEE HHHHHHHHHHHHHHH	26.16	-
1024	Acetylation	QADLALEKAARAELE HHHHHHHHHHHHHHH	48.47	26051181
1024	Ubiquitination	QADLALEKAARAELE HHHHHHHHHHHHHHH	48.47	-
1047	Phosphorylation	EQRVEFATLQEALAH HHHHHHHHHHHHHHH	34.00	22327364
1059	2-Hydroxyisobutyrylation	LAHALTEKEGKDQEL HHHHHHHHCCCHHHH	67.54	-
1059	Ubiquitination	LAHALTEKEGKDQEL HHHHHHHHCCCHHHH	67.54	-
1068	2-Hydroxyisobutyrylation	GKDQELAKLRGLEAA CCHHHHHHHHCCHHH	51.87	-
1068	Ubiquitination	GKDQELAKLRGLEAA CCHHHHHHHHCCHHH	51.87	-
1078	Ubiquitination	GLEAAQIKELEELRQ CCHHHHHHHHHHHHH	44.13	-
1088	Acetylation	EELRQTVKQLKEQLA HHHHHHHHHHHHHHH	53.99	25953088
1091	2-Hydroxyisobutyrylation	RQTVKQLKEQLAKKE HHHHHHHHHHHHHHH	40.70	-
1099	Acetylation	EQLAKKEKEHASGSG HHHHHHHHHHCCCCC	64.77	25953088
1103	Phosphorylation	KKEKEHASGSGAQSE HHHHHHCCCCCCCCH	35.09	25159151
1105	Phosphorylation	EKEHASGSGAQSEAA HHHHCCCCCCCCHHC	28.58	25159151
1109	Phosphorylation	ASGSGAQSEAAGRTE CCCCCCCCHHCCCCC	28.77	-
1121	Acetylation	RTEPTGPKLEALRAE CCCCCCHHHHHHHHH	61.37	23954790
1121	Ubiquitination	RTEPTGPKLEALRAE CCCCCCHHHHHHHHH	61.37	-
1131	Acetylation	ALRAEVSKLEQQCQK HHHHHHHHHHHHHHH	62.31	25953088
1131	Ubiquitination	ALRAEVSKLEQQCQK HHHHHHHHHHHHHHH	62.31	-
1138	Acetylation	KLEQQCQKQQEQADS HHHHHHHHHHHHHHH	62.67	26051181
1138	Ubiquitination	KLEQQCQKQQEQADS HHHHHHHHHHHHHHH	62.67	-
1145	Phosphorylation	KQQEQADSLERSLEA HHHHHHHHHHHHHHH	34.84	25849741
1149	Phosphorylation	QADSLERSLEAERAS HHHHHHHHHHHHHHH	22.61	25159151
1162	Phosphorylation	ASRAERDSALETLQG HHHHHHHHHHHHHHH	40.76	29214152
1174	Ubiquitination	LQGQLEEKAQELGHS HHHHHHHHHHHHCCC	46.09	-
1183	Phosphorylation	QELGHSQSALASAQR HHHCCCHHHHHHHHH	28.41	28674419
1187	Phosphorylation	HSQSALASAQRELAA CCHHHHHHHHHHHHH	26.28	20068231
1203	Phosphorylation	RTKVQDHSKAEDEWK HHHHCCCCCCHHHHH	41.68	27251275
1204	Acetylation	TKVQDHSKAEDEWKA HHHCCCCCCHHHHHH	52.99	26051181
1210	2-Hydroxyisobutyrylation	SKAEDEWKAQVARGR CCCHHHHHHHHHHHH	27.22	-
1210	Acetylation	SKAEDEWKAQVARGR CCCHHHHHHHHHHHH	27.22	26051181
1210	Ubiquitination	SKAEDEWKAQVARGR CCCHHHHHHHHHHHH	27.22	-
1223	Ubiquitination	GRQEAERKNSLISSL HHHHHHHHHHHHHHH	42.25	-
1225	Phosphorylation	QEAERKNSLISSLEE HHHHHHHHHHHHHHH	30.07	29255136
1228	Phosphorylation	ERKNSLISSLEEEVS HHHHHHHHHHHHHHH	33.88	30278072
1229	Phosphorylation	RKNSLISSLEEEVSI HHHHHHHHHHHHHHH	32.57	30278072
1235	Phosphorylation	SSLEEEVSILNRQVL HHHHHHHHHHHHHHH	25.33	23927012
1244	2-Hydroxyisobutyrylation	LNRQVLEKEGESKEL HHHHHHHHCCCCHHH	67.85	-
1261	2-Hydroxyisobutyrylation	LVMAESEKSQKLEER HHHHCHHHHHHHHHH	68.42	-
1261	Acetylation	LVMAESEKSQKLEER HHHHCHHHHHHHHHH	68.42	25953088
1262	Phosphorylation	VMAESEKSQKLEERL HHHCHHHHHHHHHHH	28.61	20068231
1264	Acetylation	AESEKSQKLEERLRL HCHHHHHHHHHHHHH	66.03	25953088
1278	Phosphorylation	LLQAETASNSARAAE HHHHHHHHHHHHHHH	38.44	25159151
1280	Phosphorylation	QAETASNSARAAERS HHHHHHHHHHHHHHH	19.35	25159151
1287	Phosphorylation	SARAAERSSALREEV HHHHHHHHHHHHHHH	16.09	21406692
1287 (in isoform 2)	Phosphorylation	-	16.09	21406692
1288	Phosphorylation	ARAAERSSALREEVQ HHHHHHHHHHHHHHH	37.23	21406692
1330	Ubiquitination	EELGQELKAWQEKFF HHHHHHHHHHHHHHH	46.99	21890473
1330 (in isoform 1)	Ubiquitination	-	46.99	21906983
1330 (in isoform 2)	Ubiquitination	-	46.99	21906983
1335	Ubiquitination	ELKAWQEKFFQKEQA HHHHHHHHHHHHHHH	36.06	21890473
1339	Ubiquitination	WQEKFFQKEQALSTL HHHHHHHHHHHHHHH	46.79	-
1364	Ubiquitination	VSELLPAKHLCQQLQ HHHHHCHHHHHHHHH	34.86	-
1367	Glutathionylation	LLPAKHLCQQLQAEQ HHCHHHHHHHHHHHH	2.13	22555962
1379	2-Hydroxyisobutyrylation	AEQAAAEKRHREELE HHHHHHHHHHHHHHH	49.10	-
1379	Acetylation	AEQAAAEKRHREELE HHHHHHHHHHHHHHH	49.10	25953088
1379	Ubiquitination	AEQAAAEKRHREELE HHHHHHHHHHHHHHH	49.10	-
1389	Ubiquitination	REELEQSKQAAGGLR HHHHHHHHHHHHHHH	43.58	-
1430	Acetylation	AQQLRAEKASYAEQL HHHHHHHHHHHHHHH	41.47	25953088
1430	Ubiquitination	AQQLRAEKASYAEQL HHHHHHHHHHHHHHH	41.47	21890473
1432	Phosphorylation	QLRAEKASYAEQLSM HHHHHHHHHHHHHHH	35.62	29449344
1433	Phosphorylation	LRAEKASYAEQLSML HHHHHHHHHHHHHHH	21.01	29449344
1438	Phosphorylation	ASYAEQLSMLKKAHG HHHHHHHHHHHHHHC	23.05	20068231
1441	2-Hydroxyisobutyrylation	AEQLSMLKKAHGLLA HHHHHHHHHHHCHHH	38.99	-
1441	Ubiquitination	AEQLSMLKKAHGLLA HHHHHHHHHHHCHHH	38.99	-
1441 (in isoform 2)	Ubiquitination	-	38.99	-
1442	2-Hydroxyisobutyrylation	EQLSMLKKAHGLLAE HHHHHHHHHHCHHHH	41.47	-
1442	Ubiquitination	EQLSMLKKAHGLLAE HHHHHHHHHHCHHHH	41.47	-
1452	Methylation	GLLAEENRGLGERAN CHHHHHCCCHHHHCC	45.02	115485757
1475	Ubiquitination	ELDQAREKYVQELAA HHHHHHHHHHHHHHH	45.21	21890473
1476	Phosphorylation	LDQAREKYVQELAAV HHHHHHHHHHHHHHH	11.56	24114839
1489	Phosphorylation	AVRADAETRLAEVQR HHHCCHHHHHHHHHH	32.48	21406692
1489 (in isoform 2)	Phosphorylation	-	32.48	21406692
1500	Phosphorylation	EVQREAQSTARELEV HHHHHHHHHHHHHHH	30.96	29978859
1501	Phosphorylation	VQREAQSTARELEVM HHHHHHHHHHHHHHH	20.04	29978859
1509	Phosphorylation	ARELEVMTAKYEGAK HHHHHHHHHHCCCCC	25.77	-
1511	2-Hydroxyisobutyrylation	ELEVMTAKYEGAKVK HHHHHHHHCCCCCCH	34.37	-
1511	Acetylation	ELEVMTAKYEGAKVK HHHHHHHHCCCCCCH	34.37	19608861
1511	Ubiquitination	ELEVMTAKYEGAKVK HHHHHHHHCCCCCCH	34.37	21890473
1516	Acetylation	TAKYEGAKVKVLEER HHHCCCCCCHHHHHH	54.14	25953088
1518	Ubiquitination	KYEGAKVKVLEERQR HCCCCCCHHHHHHHH	40.16	-
1559 (in isoform 2)	Ubiquitination	-	24.12	21906983
1566	Acetylation	ADSDQASKVQQQKLK CCCHHHHHHHHHHHH	47.26	25953088
1571	2-Hydroxyisobutyrylation	ASKVQQQKLKAVQAQ HHHHHHHHHHHHHHC	47.84	-
1571	Acetylation	ASKVQQQKLKAVQAQ HHHHHHHHHHHHHHC	47.84	25953088
1573	Ubiquitination	KVQQQKLKAVQAQGG HHHHHHHHHHHHCCC	54.25	21906983
1573 (in isoform 1)	Ubiquitination	-	54.25	21906983
1582	Phosphorylation	VQAQGGESQQEAQRL HHHCCCHHHHHHHHH	40.20	25849741
1601	Phosphorylation	NELQAQLSQKEQAAE HHHHHHHHHHHHHHH	27.42	25849741
1603	Ubiquitination	LQAQLSQKEQAAEHY HHHHHHHHHHHHHHH	48.71	-
1624	2-Hydroxyisobutyrylation	AKTHYDAKKQQNQEL HHHHHHHHHHHHHHH	48.49	-
1624	Acetylation	AKTHYDAKKQQNQEL HHHHHHHHHHHHHHH	48.49	22361529
1625	Ubiquitination	KTHYDAKKQQNQELQ HHHHHHHHHHHHHHH	59.86	-
1643	Acetylation	RSLEQLQKENKELRA HHHHHHHHHCHHHHH	72.37	25953088
1643	Ubiquitination	RSLEQLQKENKELRA HHHHHHHHHCHHHHH	72.37	-
1665	Ubiquitination	ELQQAGLKTKEAEQT HHHHCCCCHHHHHHH	57.54	-
1682	Phosphorylation	HLTAQVRSLEAQVAH HHHHHHHHHHHHHHH	31.53	25849741
1694 (in isoform 2)	Ubiquitination	-	3.70	21906983
1699	2-Hydroxyisobutyrylation	QQLRDLGKFQVATDA HHHHHHCCHHHHHHH	39.66	-
1699	Acetylation	QQLRDLGKFQVATDA HHHHHHCCHHHHHHH	39.66	25953088
1699	Sumoylation	QQLRDLGKFQVATDA HHHHHHCCHHHHHHH	39.66	28112733
1699	Ubiquitination	QQLRDLGKFQVATDA HHHHHHCCHHHHHHH	39.66	21890473
1704	Phosphorylation	LGKFQVATDALKSRE HCCHHHHHHHHHCCC	23.97	20860994
1708	2-Hydroxyisobutyrylation	QVATDALKSREPQAK HHHHHHHHCCCCCCC	49.54	-
1708	Ubiquitination	QVATDALKSREPQAK HHHHHHHHCCCCCCC	49.54	21890473
1708 (in isoform 1)	Ubiquitination	-	49.54	21906983
1709	Phosphorylation	VATDALKSREPQAKP HHHHHHHCCCCCCCC	42.60	30108239
1715	Acetylation	KSREPQAKPQLDLSI HCCCCCCCCCCCEEE	28.22	26051181
1715	Ubiquitination	KSREPQAKPQLDLSI HCCCCCCCCCCCEEE	28.22	-
1721	Phosphorylation	AKPQLDLSIDSLDLS CCCCCCEEEEEECCC	24.82	25159151
1724	Phosphorylation	QLDLSIDSLDLSCEE CCCEEEEEECCCCCC	23.32	30266825
1728	Phosphorylation	SIDSLDLSCEEGTPL EEEEECCCCCCCCCC	21.10	30266825
1733	Phosphorylation	DLSCEEGTPLSITSK CCCCCCCCCCEEEEC	25.08	30266825
1736	Phosphorylation	CEEGTPLSITSKLPR CCCCCCCEEEECCCC	25.64	30108239
1738	Phosphorylation	EGTPLSITSKLPRTQ CCCCCEEEECCCCCC	19.21	20873877
1739	Phosphorylation	GTPLSITSKLPRTQP CCCCEEEECCCCCCC	30.44	20873877
1740	Ubiquitination	TPLSITSKLPRTQPD CCCEEEECCCCCCCC	54.59	-
1743 (in isoform 2)	Phosphorylation	-	57.33	21406692
1744	Phosphorylation	ITSKLPRTQPDGTSV EEECCCCCCCCCCCC	42.38	29255136
1749	Phosphorylation	PRTQPDGTSVPGEPA CCCCCCCCCCCCCCC	33.65	29255136
1750	Phosphorylation	RTQPDGTSVPGEPAS CCCCCCCCCCCCCCC	31.66	29255136
1752 (in isoform 2)	Ubiquitination	-	40.99	-
1755	Phosphorylation	GTSVPGEPASPISQR CCCCCCCCCCCHHHC	43.91	19081932
1757	Phosphorylation	SVPGEPASPISQRLP CCCCCCCCCHHHCCC	33.22	19664994
1760	Phosphorylation	GEPASPISQRLPPKV CCCCCCHHHCCCCCC	16.78	29255136
1762	Phosphorylation	PASPISQRLPPKVES CCCCHHHCCCCCCCC	42.23	19081932
1766	Sumoylation	ISQRLPPKVESLESL HHHCCCCCCCCCCHH	57.61	-
1766	Acetylation	ISQRLPPKVESLESL HHHCCCCCCCCCCHH	57.61	26051181
1766	Sumoylation	ISQRLPPKVESLESL HHHCCCCCCCCCCHH	57.61	25114211
1766	Ubiquitination	ISQRLPPKVESLESL HHHCCCCCCCCCCHH	57.61	2189047
1769	Phosphorylation	RLPPKVESLESLYFT CCCCCCCCCCHHCCC	40.19	29255136
1772	Phosphorylation	PKVESLESLYFTPIP CCCCCCCHHCCCCCC	33.39	21945579
1774	Phosphorylation	VESLESLYFTPIPAR CCCCCHHCCCCCCCC	18.06	21945579
1776	Phosphorylation	SLESLYFTPIPARSQ CCCHHCCCCCCCCCC	13.52	21945579
1782	Phosphorylation	FTPIPARSQAPLESS CCCCCCCCCCCCCHH	32.57	23927012
1788	Phosphorylation	RSQAPLESSLDSLGD CCCCCCCHHHHHHCH	43.83	25159151
1789	Phosphorylation	SQAPLESSLDSLGDV CCCCCCHHHHHHCHH	27.16	23927012
1792	Phosphorylation	PLESSLDSLGDVFLD CCCHHHHHHCHHHHH	39.27	30266825
1800	Phosphorylation	LGDVFLDSGRKTRSA HCHHHHHCCCCCHHH	42.52	25463755
1802	Methylation	DVFLDSGRKTRSARR HHHHHCCCCCHHHCH	40.92	115386543
1803	Methylation	VFLDSGRKTRSARRR HHHHCCCCCHHHCHH	52.38	23748837
1804	Phosphorylation	FLDSGRKTRSARRRT HHHCCCCCHHHCHHC	28.61	26055452
1804 (in isoform 2)	Phosphorylation	-	28.61	21406692
1806	Phosphorylation	DSGRKTRSARRRTTQ HCCCCCHHHCHHCCE	31.21	21712546
1811	Phosphorylation	TRSARRRTTQIINIT CHHHCHHCCEEEEEE	22.65	27273156
1812	Phosphorylation	RSARRRTTQIINITM HHHCHHCCEEEEEEE	18.89	26055452
1818	Phosphorylation	TTQIINITMTKKLDV CCEEEEEEEECCCCC	17.82	20860994
1820	Phosphorylation	QIINITMTKKLDVEE EEEEEEEECCCCCCC	19.17	20860994
1821	Acetylation	IINITMTKKLDVEEP EEEEEEECCCCCCCC	40.28	25953088
1821	Ubiquitination	IINITMTKKLDVEEP EEEEEEECCCCCCCC	40.28	-
1822	Sumoylation	INITMTKKLDVEEPD EEEEEECCCCCCCCC	40.53	28112733
1822	Ubiquitination	INITMTKKLDVEEPD EEEEEECCCCCCCCC	40.53	-
1830	Phosphorylation	LDVEEPDSANSSFYS CCCCCCCCCCCCCCC	39.81	25159151
1833	Phosphorylation	EEPDSANSSFYSTRS CCCCCCCCCCCCCCC	22.88	23401153
1834	Phosphorylation	EPDSANSSFYSTRSA CCCCCCCCCCCCCCC	28.19	25159151
1836	Phosphorylation	DSANSSFYSTRSAPA CCCCCCCCCCCCCCC	15.87	21712546
1837	O-linked_Glycosylation	SANSSFYSTRSAPAS CCCCCCCCCCCCCCC	18.48	30059200
1837	Phosphorylation	SANSSFYSTRSAPAS CCCCCCCCCCCCCCC	18.48	25159151
1838	Phosphorylation	ANSSFYSTRSAPASQ CCCCCCCCCCCCCCH	19.77	26055452
1838 (in isoform 2)	Phosphorylation	-	19.77	21406692
1839 (in isoform 2)	Phosphorylation	-	25.53	21406692
1840	O-linked_Glycosylation	SSFYSTRSAPASQAS CCCCCCCCCCCCHHH	38.40	30059200
1840	Phosphorylation	SSFYSTRSAPASQAS CCCCCCCCCCCCHHH	38.40	25159151
1840 (in isoform 2)	Phosphorylation	-	38.40	21406692
1844	O-linked_Glycosylation	STRSAPASQASLRAT CCCCCCCCHHHHHCC	25.81	30059200
1844	Phosphorylation	STRSAPASQASLRAT CCCCCCCCHHHHHCC	25.81	26055452
1847	O-linked_Glycosylation	SAPASQASLRATSST CCCCCHHHHHCCCCC	15.68	30059200
1847	Phosphorylation	SAPASQASLRATSST CCCCCHHHHHCCCCC	15.68	23401153
1849	Methylation	PASQASLRATSSTQS CCCHHHHHCCCCCHH	33.07	115485781
1851	Phosphorylation	SQASLRATSSTQSLA CHHHHHCCCCCHHHH	19.44	25849741
1852	Phosphorylation	QASLRATSSTQSLAR HHHHHCCCCCHHHHH	30.33	29255136
1853	Phosphorylation	ASLRATSSTQSLARL HHHHCCCCCHHHHHH	26.55	23401153
1854	Phosphorylation	SLRATSSTQSLARLG HHHCCCCCHHHHHHC	23.19	29255136
1856	Phosphorylation	RATSSTQSLARLGSP HCCCCCHHHHHHCCC	24.88	26329039
1859	Methylation	SSTQSLARLGSPDYG CCCHHHHHHCCCCCC	44.89	115485765
1862	Phosphorylation	QSLARLGSPDYGNSA HHHHHHCCCCCCCCC	21.13	25159151
1865	Phosphorylation	ARLGSPDYGNSALLS HHHCCCCCCCCCCCC	22.91	21712546
1868	Phosphorylation	GSPDYGNSALLSLPG CCCCCCCCCCCCCCC	18.87	26055452
1872	Phosphorylation	YGNSALLSLPGYRPT CCCCCCCCCCCCCCC	33.11	25159151
1876	Phosphorylation	ALLSLPGYRPTTRSS CCCCCCCCCCCCCHH	16.10	27732954
1879	Phosphorylation	SLPGYRPTTRSSARR CCCCCCCCCCHHHHH	26.33	23312004
1880	Phosphorylation	LPGYRPTTRSSARRS CCCCCCCCCHHHHHH	31.10	24732914
1882	Phosphorylation	GYRPTTRSSARRSQA CCCCCCCHHHHHHHC	26.68	26434776
1883	Phosphorylation	YRPTTRSSARRSQAG CCCCCCHHHHHHHCC	23.62	26434776
1887	Phosphorylation	TRSSARRSQAGVSSG CCHHHHHHHCCCCCC	20.87	29255136
1892	Phosphorylation	RRSQAGVSSGAPPGR HHHHCCCCCCCCCCC	23.33	22210691
1893	Phosphorylation	RSQAGVSSGAPPGRN HHHCCCCCCCCCCCC	36.25	27251275
1901	Phosphorylation	GAPPGRNSFYMGTCQ CCCCCCCCCCCEECC	19.18	21815630
1903	Phosphorylation	PPGRNSFYMGTCQDE CCCCCCCCCEECCCC	8.41	20873877
1906	Phosphorylation	RNSFYMGTCQDEPEQ CCCCCCEECCCCHHH	7.17	28985074
1935	Acetylation	RVCPPHLKTCYPLES CCCCCCCCCCCCCCC	33.25	25953088
1935	Ubiquitination	RVCPPHLKTCYPLES CCCCCCCCCCCCCCC	33.25	-
1936	Phosphorylation	VCPPHLKTCYPLESR CCCCCCCCCCCCCCC	24.51	26552605
1938	Phosphorylation	PPHLKTCYPLESRPS CCCCCCCCCCCCCCC	18.98	29396449
1942	Phosphorylation	KTCYPLESRPSLSLG CCCCCCCCCCCCCCC	58.11	23663014
1945	Phosphorylation	YPLESRPSLSLGTIT CCCCCCCCCCCCCCC	29.49	29255136
1947	Phosphorylation	LESRPSLSLGTITDE CCCCCCCCCCCCCHH	29.14	29255136
1950	Phosphorylation	RPSLSLGTITDEEMK CCCCCCCCCCHHHHC	26.46	29255136
1952	Phosphorylation	SLSLGTITDEEMKTG CCCCCCCCHHHHCCC	36.88	29255136
1957	Ubiquitination	TITDEEMKTGDPQET CCCHHHHCCCCHHHH	53.27	-
1958	Phosphorylation	ITDEEMKTGDPQETL CCHHHHCCCCHHHHH	45.57	20068231
1964	Phosphorylation	KTGDPQETLRRASMQ CCCCHHHHHHHHHCC	21.95	20068231
1969	Phosphorylation	QETLRRASMQPIQIA HHHHHHHHCCCEEEE	19.01	22167270
1970	Sulfoxidation	ETLRRASMQPIQIAE HHHHHHHCCCEEEEC	5.54	21406390
1979	Phosphorylation	PIQIAEGTGITTRQQ CEEEECCCCCCCHHH	19.54	24732914
1982	Phosphorylation	IAEGTGITTRQQRKR EECCCCCCCHHHCCC	19.78	24732914
1983	Phosphorylation	AEGTGITTRQQRKRV ECCCCCCCHHHCCCC	25.26	24732914
1986 (in isoform 2)	Phosphorylation	-	49.96	21406692
1988	Acetylation	ITTRQQRKRVSLEPH CCCHHHCCCCCCCCC	53.46	7825189
1989 (in isoform 2)	Phosphorylation	-	25.99	21406692
1991	Phosphorylation	RQQRKRVSLEPHQGP HHHCCCCCCCCCCCC	30.92	20201521
2000	Phosphorylation	EPHQGPGTPESKKAT CCCCCCCCCCHHCCC	27.32	29255136
2003	Phosphorylation	QGPGTPESKKATSCF CCCCCCCHHCCCCCC	40.43	22167270
2004	Acetylation	GPGTPESKKATSCFP CCCCCCHHCCCCCCC	44.77	25953088
2004	Ubiquitination	GPGTPESKKATSCFP CCCCCCHHCCCCCCC	44.77	-
2007	Phosphorylation	TPESKKATSCFPRPM CCCHHCCCCCCCCCC	34.60	23403867
2008	Phosphorylation	PESKKATSCFPRPMT CCHHCCCCCCCCCCC	20.72	22167270
2014 (in isoform 2)	Phosphorylation	-	9.46	21406692
2015	Phosphorylation	SCFPRPMTPRDRHEG CCCCCCCCCCCCCCC	20.18	22167270
2026	Phosphorylation	RHEGRKQSTTEAQKK CCCCCCCCCHHHHHH	40.09	26657352
2027	Phosphorylation	HEGRKQSTTEAQKKA CCCCCCCCHHHHHHH	26.60	21406692
2028	Phosphorylation	EGRKQSTTEAQKKAA CCCCCCCHHHHHHHC	34.27	21406692
2047	Phosphorylation	KQADRRQSMAFSILN HHHHHHHHHHHHHHC	15.40	23401153
2051	Phosphorylation	RRQSMAFSILNTPKK HHHHHHHHHHCCCHH	19.34	25159151
2055	Phosphorylation	MAFSILNTPKKLGNS HHHHHHCCCHHHHHH	32.80	29255136
2057	Acetylation	FSILNTPKKLGNSLL HHHHCCCHHHHHHHH	59.60	30583725
2062	Phosphorylation	TPKKLGNSLLRRGAS CCHHHHHHHHHCCCC	27.29	23401153
2069	Phosphorylation	SLLRRGASKKALSKA HHHHCCCCHHHHHCC	37.20	26074081
2070	Acetylation	LLRRGASKKALSKAS HHHCCCCHHHHHCCC	41.34	130153
2071	Acetylation	LRRGASKKALSKASP HHCCCCHHHHHCCCC	52.65	130157
2074	Phosphorylation	GASKKALSKASPNTR CCCHHHHHCCCCCCC	30.91	26055452
2077	Phosphorylation	KKALSKASPNTRSGT HHHHHCCCCCCCCCC	23.55	26055452
2080	Phosphorylation	LSKASPNTRSGTRRS HHCCCCCCCCCCCCC	29.60	23403867
2084	Phosphorylation	SPNTRSGTRRSPRIA CCCCCCCCCCCCCCC	24.93	-
2087	Phosphorylation	TRSGTRRSPRIATTT CCCCCCCCCCCCCHH	18.42	26552605
2092	Phosphorylation	RRSPRIATTTASAAT CCCCCCCCHHHHHHH	23.47	29255136
2093	O-linked_Glycosylation	RSPRIATTTASAATA CCCCCCCHHHHHHHH	16.02	30059200
2093	Phosphorylation	RSPRIATTTASAATA CCCCCCCHHHHHHHH	16.02	29255136
2094	Phosphorylation	SPRIATTTASAATAA CCCCCCHHHHHHHHH	17.79	27251275
2096	Phosphorylation	RIATTTASAATAAAI CCCCHHHHHHHHHHH	19.15	29255136
2099	Phosphorylation	TTTASAATAAAIGAT CHHHHHHHHHHHCCC	19.29	29255136
2106	Phosphorylation	TAAAIGATPRAKGKA HHHHHCCCCCCCCCC	14.22	29255136
2114	Methylation	PRAKGKAKH------ CCCCCCCCC------	54.02	116252697

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
1047	T	Phosphorylation	Kinase	PLK1	P53350	Uniprot
1769	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
1772	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
1774	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
1776	T	Phosphorylation	Kinase	CDK2	P24941	PSP
1789	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
1804	T	Phosphorylation	Kinase	AURKA	O14965	GPS
1811	T	Phosphorylation	Kinase	AURKA	O14965	GPS
1811	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
1812	T	Phosphorylation	Kinase	AURKA	O14965	GPS
1834	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
1883	S	Phosphorylation	Kinase	AURA	O14965	PSP
1887	S	Phosphorylation	Kinase	AURKA	O14965	GPS
1969	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
1969	S	Phosphorylation	Kinase	AURKA	O14965	GPS
1991	S	Phosphorylation	Kinase	AURKA	O14965	GPS
2015	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
2047	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
2047	S	Phosphorylation	Kinase	AURKA	O14965	GPS
2055	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
2055	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
2084	T	Phosphorylation	Kinase	AURKA	O14965	GPS
2087	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
2087	S	Phosphorylation	Kinase	AURKA	O14965	GPS
2106	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1047	T	Phosphorylation	Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization.	22327364
1769	S	Phosphorylation	Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization.	16964243
1772	S	Phosphorylation	Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization.	18669648
1789	S	Phosphorylation	Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization.	18669648
1834	S	Phosphorylation	Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization.	18669648
2015	T	Phosphorylation	Probably also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase.	7769006
2055	T	Phosphorylation	In anaphase, dephosphorylated on Thr-2055 by phosphatase PPP2CA; this dephosphorylation stimulates its membrane association and with the dynein-dynactin complex its enrichment at the cell cortex, and hence robust spindle elongation.	7769006
2055	T	Phosphorylation	In metaphase, phosphorylation on Thr-2055 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning.	7769006
2055	T	Phosphorylation	Phosphorylation and dephosphorylation on Thr-2055 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase.	7769006
2087	S	Phosphorylation	Probably also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase.	7769006

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NUMA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
41_HUMAN	EPB41	physical	10189366
YETS4_HUMAN	YEATS4	physical	10913114
GPSM2_HUMAN	GPSM2	physical	11781568
TNKS1_HUMAN	TNKS	physical	12080061
E41L2_HUMAN	EPB41L2	physical	12239178
E41L1_HUMAN	EPB41L1	physical	10594058
EMIL1_HUMAN	EMILIN1	physical	17609108
RAE1L_HUMAN	RAE1	physical	17172455
NUP98_HUMAN	NUP98	physical	17172455
DYL1_HUMAN	DYNLL1	physical	17172455
DVL1_HUMAN	DVL1	physical	24469800
DVL2_HUMAN	DVL2	physical	24469800
DVL3_HUMAN	DVL3	physical	24469800
GMCL1_HUMAN	GMCL1	physical	25416956
CCD57_HUMAN	CCDC57	physical	25416956
BRD4_HUMAN	BRD4	physical	26344197
EIF3H_HUMAN	EIF3H	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RTF1_HUMAN	RTF1	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
ZCH18_HUMAN	ZC3H18	physical	26344197
DYHC1_HUMAN	DYNC1H1	physical	26195665
IMB1_HUMAN	KPNB1	physical	26195665

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

"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-379; LYS-891 AND LYS-1511,AND MASS SPECTROMETRY.
PubMed: 19608861

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 SER-203; SER-1225; SER-1757;SER-1769; THR-1776; SER-1788; SER-1800; SER-1840; THR-2055 ANDTHR-2106, AND MASS SPECTROMETRY.
PubMed: 19690332

"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-1757, AND MASSSPECTROMETRY.
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-169; SER-198; SER-203;THR-211; SER-1721; SER-1724; SER-1728; SER-1757; SER-1769; SER-1772;TYR-1774; THR-1776; SER-1788; SER-1789; SER-1792; SER-1800; THR-1804;SER-1830; SER-1833; SER-1834; TYR-1836; SER-1837; SER-1840; SER-1862;SER-1872; SER-1887; SER-1969; SER-1991 AND THR-2000, AND MASSSPECTROMETRY.
PubMed: 18669648

"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND MASSSPECTROMETRY.
PubMed: 19367720

"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 SER-1757 AND SER-1969, ANDMASS SPECTROMETRY.
PubMed: 18220336

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND MASSSPECTROMETRY.
PubMed: 18187866

"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-200; SER-271; SER-1280;SER-1757; SER-1830; SER-1840; SER-1847; SER-1862; SER-1887; SER-2074;SER-2077 AND THR-2106, AND MASS SPECTROMETRY.
PubMed: 19007248

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-395; SER-820;THR-963; SER-1601; SER-1757 AND SER-1760, AND MASS SPECTROMETRY.
PubMed: 17525332

"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-1757 AND SER-2077, ANDMASS SPECTROMETRY.
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-169; SER-172; SER-200;SER-203; THR-211; SER-1262; SER-1721; SER-1724; THR-1733; SER-1757;SER-1769; SER-1772; THR-1776; SER-1830; SER-1833; SER-1834; SER-1862;SER-1872; SER-1945 AND THR-2000, AND MASS SPECTROMETRY.
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-1757; SER-1769;THR-1776; SER-1840; SER-1847; THR-2055 AND THR-2106, 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-169; SER-1721; SER-1724;SER-1728; THR-1733; SER-1757; SER-1862 AND THR-2000, AND MASSSPECTROMETRY.
PubMed: 17081983

"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-1757 AND SER-1853, ANDMASS SPECTROMETRY.
PubMed: 15302935

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1774, AND MASSSPECTROMETRY.
PubMed: 15592455