dbPTM

MYPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYPT1_HUMAN
UniProt AC	O14974
Protein Name	Protein phosphatase 1 regulatory subunit 12A
Gene Name	PPP1R12A {ECO:0000312\|HGNC:HGNC:7618}
Organism	Homo sapiens (Human).
Sequence Length	1030
Subcellular Localization	Cytoplasm . Along actomyosin filaments and stress fibers.
Protein Description	Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity..
Protein Sequence	MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNASRIESLEQEKVDEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPLASVTNANTSSTQAAPVAVTTPTVSSGQATPTSPIKKFPTTATKISPKEEERKDESPATWRLGLRKTGSYGALAEITASKEGQKEKDTAGVTRSASSPRLSSSLDNKEKEKDSKGTRLAYVAPTIPRRLASTSDIEEKENRDSSSLRTSSSYTRRKWEDDLKKNSSVNEGSTYHKSCSFGRRQDDLISSSVPSTTSTPTVTSAAGLQKSLLSSTSTTTKITTGSSSAGTQSSTSNRLWAEDSTEKEKDSVPTAVTIPVAPTVVNAAASTTTLTTTTAGTVSSTTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETSREDEYKQKYSRTYDETYQRYRPVSTSSSTTPSSSLSTMSSSLYASSQLNRPNSLVGITSAYSRGITKENEREGEKREEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Acetylation	KMADAKQKRNEQLKR CHHHHHHHHHHHHHH	57.39	19813065
20	Phosphorylation	QLKRWIGSETDLEPP HHHHHHCCCCCCCCC	28.34	22516431
22	Phosphorylation	KRWIGSETDLEPPVV HHHHCCCCCCCCCCC	47.81	22516431
30	2-Hydroxyisobutyrylation	DLEPPVVKRQKTKVK CCCCCCCCCCCCEEE	49.71	-
49	Phosphorylation	AVFLAACSSGDTDEV CEEEEECCCCCHHHH	32.40	-
67	Hydroxylation	LHRGADINYANVDGL HHCCCCCCCCCCCHH	30.34	19245366
68	Phosphorylation	HRGADINYANVDGLT HCCCCCCCCCCCHHH	10.41	-
100	Hydroxylation	VENGANINQPDNEGW HHCCCCCCCCCCCCC	47.33	19245366
198	Phosphorylation	NDVRHAKSGGTALHV CCCCCCCCCCHHHHH	43.15	20068231
201	Phosphorylation	RHAKSGGTALHVAAA CCCCCCCHHHHHHHH	29.57	20068231
226	Hydroxylation	IQAGYDVNIKDYDGW HHCCCCCCCCCCCCC	32.47	19245366
234	Phosphorylation	IKDYDGWTPLHAAAH CCCCCCCCHHHHHHH	22.85	-
244	Ubiquitination	HAAAHWGKEEACRIL HHHHHCCHHHHHHHH	47.38	-
258	Sulfoxidation	LVDNLCDMEMVNKVG HHHCCCCHHHHHHHC	3.32	21406390
285	Ubiquitination	GYLEELQKKQNLLHS HHHHHHHHHHCHHCC	69.79	-
285 (in isoform 2)	Ubiquitination	-	69.79	-
286	Ubiquitination	YLEELQKKQNLLHSE HHHHHHHHHCHHCCC	31.30	-
292	Phosphorylation	KKQNLLHSEKRDKKS HHHCHHCCCCCCCCC	44.79	25159151
294	2-Hydroxyisobutyrylation	QNLLHSEKRDKKSPL HCHHCCCCCCCCCCC	69.76	-
299	Phosphorylation	SEKRDKKSPLIESTA CCCCCCCCCCCHHCC	30.58	19664994
304	Phosphorylation	KKSPLIESTANMDNN CCCCCCHHCCCCCCC	26.31	30266825
305	Phosphorylation	KSPLIESTANMDNNQ CCCCCHHCCCCCCCC	14.84	30266825
308	Sulfoxidation	LIESTANMDNNQSQK CCHHCCCCCCCCCCH	5.60	21406390
313	Phosphorylation	ANMDNNQSQKTFKNK CCCCCCCCCHHHCCC	35.45	30266825
315	Acetylation	MDNNQSQKTFKNKET CCCCCCCHHHCCCCC	62.26	25953088
316	Phosphorylation	DNNQSQKTFKNKETL CCCCCCHHHCCCCCE	32.00	28857561
332	Phosphorylation	IEPEKNASRIESLEQ ECCCCCHHHHHHHHH	43.09	29514088
336	Phosphorylation	KNASRIESLEQEKVD CCHHHHHHHHHHCCC	34.53	21815630
353	Phosphorylation	EEGKKDESSCSSEED HCCCCCCCCCCCCCC	46.94	30576142
354	Phosphorylation	EGKKDESSCSSEEDE CCCCCCCCCCCCCCC	18.90	30576142
356	Phosphorylation	KKDESSCSSEEDEED CCCCCCCCCCCCCCC	42.61	30576142
357	Phosphorylation	KDESSCSSEEDEEDD CCCCCCCCCCCCCCC	49.70	30576142
365	Phosphorylation	EEDEEDDSESEAETD CCCCCCCCHHHHCCC	56.17	27251275
367	Phosphorylation	DEEDDSESEAETDKT CCCCCCHHHHCCCCC	46.16	30576142
371	Phosphorylation	DSESEAETDKTKPLA CCHHHHCCCCCCCCC	50.25	30576142
374	Phosphorylation	SEAETDKTKPLASVT HHHCCCCCCCCCCCC	40.48	23684312
379	O-linked_Glycosylation	DKTKPLASVTNANTS CCCCCCCCCCCCCCC	36.84	32574038
379	Phosphorylation	DKTKPLASVTNANTS CCCCCCCCCCCCCCC	36.84	22199227
381	O-linked_Glycosylation	TKPLASVTNANTSST CCCCCCCCCCCCCCC	26.56	32574038
381	Phosphorylation	TKPLASVTNANTSST CCCCCCCCCCCCCCC	26.56	22199227
385	O-linked_Glycosylation	ASVTNANTSSTQAAP CCCCCCCCCCCCCCC	22.95	32574038
385	Phosphorylation	ASVTNANTSSTQAAP CCCCCCCCCCCCCCC	22.95	22199227
386	Phosphorylation	SVTNANTSSTQAAPV CCCCCCCCCCCCCCE	31.06	22199227
387	Phosphorylation	VTNANTSSTQAAPVA CCCCCCCCCCCCCEE	23.62	22199227
388	O-linked_Glycosylation	TNANTSSTQAAPVAV CCCCCCCCCCCCEEE	23.22	32574038
388	Phosphorylation	TNANTSSTQAAPVAV CCCCCCCCCCCCEEE	23.22	22199227
396	O-linked_Glycosylation	QAAPVAVTTPTVSSG CCCCEEEECCCCCCC	19.81	32574038
396	Phosphorylation	QAAPVAVTTPTVSSG CCCCEEEECCCCCCC	19.81	28348404
397	Phosphorylation	AAPVAVTTPTVSSGQ CCCEEEECCCCCCCC	15.46	28348404
399	Phosphorylation	PVAVTTPTVSSGQAT CEEEECCCCCCCCCC	30.81	30278072
401	Phosphorylation	AVTTPTVSSGQATPT EEECCCCCCCCCCCC	31.09	28348404
402	Phosphorylation	VTTPTVSSGQATPTS EECCCCCCCCCCCCC	30.50	30278072
406	Phosphorylation	TVSSGQATPTSPIKK CCCCCCCCCCCCCCC	21.15	30278072
408	Phosphorylation	SSGQATPTSPIKKFP CCCCCCCCCCCCCCC	42.66	25159151
409	Phosphorylation	SGQATPTSPIKKFPT CCCCCCCCCCCCCCC	26.32	30278072
416	O-linked_Glycosylation	SPIKKFPTTATKISP CCCCCCCCCCCCCCC	31.99	32574038
416	Phosphorylation	SPIKKFPTTATKISP CCCCCCCCCCCCCCC	31.99	23927012
417	Phosphorylation	PIKKFPTTATKISPK CCCCCCCCCCCCCCC	32.35	30266825
419	Phosphorylation	KKFPTTATKISPKEE CCCCCCCCCCCCCHH	27.15	30266825
420	Acetylation	KFPTTATKISPKEEE CCCCCCCCCCCCHHH	38.43	25953088
422	Phosphorylation	PTTATKISPKEEERK CCCCCCCCCCHHHCC	31.32	23927012
432	Phosphorylation	EEERKDESPATWRLG HHHCCCCCCCCHHHC	29.93	25159151
435	Phosphorylation	RKDESPATWRLGLRK CCCCCCCCHHHCCCC	17.94	25850435
442	Acetylation	TWRLGLRKTGSYGAL CHHHCCCCCCCCHHE	63.38	12650253
442	Methylation	TWRLGLRKTGSYGAL CHHHCCCCCCCCHHE	63.38	21115810
443	Phosphorylation	WRLGLRKTGSYGALA HHHCCCCCCCCHHEE	25.56	29255136
445	Phosphorylation	LGLRKTGSYGALAEI HCCCCCCCCHHEEEE	26.14	29255136
446	Phosphorylation	GLRKTGSYGALAEIT CCCCCCCCHHEEEEE	14.04	22322096
453	Phosphorylation	YGALAEITASKEGQK CHHEEEEECCCCCCC	19.18	22322096
455	Phosphorylation	ALAEITASKEGQKEK HEEEEECCCCCCCCC	23.69	23927012
456	Acetylation	LAEITASKEGQKEKD EEEEECCCCCCCCCC	64.50	12650269
460	Acetylation	TASKEGQKEKDTAGV ECCCCCCCCCCCCCC	77.05	12650285
464	O-linked_Glycosylation	EGQKEKDTAGVTRSA CCCCCCCCCCCCCCC	36.06	32574038
464	Phosphorylation	EGQKEKDTAGVTRSA CCCCCCCCCCCCCCC	36.06	26074081
468	Phosphorylation	EKDTAGVTRSASSPR CCCCCCCCCCCCCCC	20.28	26074081
470	Phosphorylation	DTAGVTRSASSPRLS CCCCCCCCCCCCCCH	24.12	22617229
472	Phosphorylation	AGVTRSASSPRLSSS CCCCCCCCCCCCHHC	41.96	28355574
473	Phosphorylation	GVTRSASSPRLSSSL CCCCCCCCCCCHHCC	17.47	25159151
477	O-linked_Glycosylation	SASSPRLSSSLDNKE CCCCCCCHHCCCCHH	21.11	32574038
477	Phosphorylation	SASSPRLSSSLDNKE CCCCCCCHHCCCCHH	21.11	29255136
478	Phosphorylation	ASSPRLSSSLDNKEK CCCCCCHHCCCCHHH	39.24	29255136
479	O-linked_Glycosylation	SSPRLSSSLDNKEKE CCCCCHHCCCCHHHH	36.04	32574038
479	Phosphorylation	SSPRLSSSLDNKEKE CCCCCHHCCCCHHHH	36.04	29255136
483	2-Hydroxyisobutyrylation	LSSSLDNKEKEKDSK CHHCCCCHHHHCCCC	70.59	-
489	Phosphorylation	NKEKEKDSKGTRLAY CHHHHCCCCCCEEEE	44.01	24719451
496	Phosphorylation	SKGTRLAYVAPTIPR CCCCEEEEECCCCCH	11.18	21945579
500	Phosphorylation	RLAYVAPTIPRRLAS EEEEECCCCCHHCCC	33.60	21945579
507	Phosphorylation	TIPRRLASTSDIEEK CCCHHCCCCCCHHHH	32.79	29255136
508	Phosphorylation	IPRRLASTSDIEEKE CCHHCCCCCCHHHHH	25.47	29255136
509	Phosphorylation	PRRLASTSDIEEKEN CHHCCCCCCHHHHHC	33.81	29255136
514	2-Hydroxyisobutyrylation	STSDIEEKENRDSSS CCCCHHHHHCCCCCC	47.72	-
514	Acetylation	STSDIEEKENRDSSS CCCCHHHHHCCCCCC	47.72	26051181
519	Phosphorylation	EEKENRDSSSLRTSS HHHHCCCCCCCCCCC	20.70	29214152
520	Phosphorylation	EKENRDSSSLRTSSS HHHCCCCCCCCCCCH	37.37	30576142
521	Phosphorylation	KENRDSSSLRTSSSY HHCCCCCCCCCCCHH	26.31	30576142
524	Phosphorylation	RDSSSLRTSSSYTRR CCCCCCCCCCHHHHH	37.95	26437602
525	Phosphorylation	DSSSLRTSSSYTRRK CCCCCCCCCHHHHHH	15.74	27134283
527	Phosphorylation	SSLRTSSSYTRRKWE CCCCCCCHHHHHHHH	30.23	26437602
528	Phosphorylation	SLRTSSSYTRRKWED CCCCCCHHHHHHHHH	13.25	30576142
529	Phosphorylation	LRTSSSYTRRKWEDD CCCCCHHHHHHHHHH	26.41	30576142
539	Methylation	KWEDDLKKNSSVNEG HHHHHHHHCCCCCCC	70.16	115973583
541	Phosphorylation	EDDLKKNSSVNEGST HHHHHHCCCCCCCCC	44.54	28348404
542	Phosphorylation	DDLKKNSSVNEGSTY HHHHHCCCCCCCCCC	38.05	28857561
547	Phosphorylation	NSSVNEGSTYHKSCS CCCCCCCCCCCCCCC	21.44	28857561
548	Phosphorylation	SSVNEGSTYHKSCSF CCCCCCCCCCCCCCC	40.27	-
549	Phosphorylation	SVNEGSTYHKSCSFG CCCCCCCCCCCCCCC	14.67	30576142
551	Methylation	NEGSTYHKSCSFGRR CCCCCCCCCCCCCCC	42.62	115973595
552	Phosphorylation	EGSTYHKSCSFGRRQ CCCCCCCCCCCCCCH	11.15	26437602
554	Phosphorylation	STYHKSCSFGRRQDD CCCCCCCCCCCCHHH	37.51	29496963
554 (in isoform 3)	Phosphorylation	-	37.51	27251275
562 (in isoform 3)	Phosphorylation	-	5.71	25849741
563 (in isoform 3)	Phosphorylation	-	4.89	29507054
564	O-linked_Glycosylation	RRQDDLISSSVPSTT CCHHHHHHCCCCCCC	24.69	32574038
564	Phosphorylation	RRQDDLISSSVPSTT CCHHHHHHCCCCCCC	24.69	30576142
565	O-linked_Glycosylation	RQDDLISSSVPSTTS CHHHHHHCCCCCCCC	28.50	32574038
566	O-linked_Glycosylation	QDDLISSSVPSTTST HHHHHHCCCCCCCCC	31.12	32574038
569	O-linked_Glycosylation	LISSSVPSTTSTPTV HHHCCCCCCCCCCCC	42.01	32574038
570	O-linked_Glycosylation	ISSSVPSTTSTPTVT HHCCCCCCCCCCCCC	20.78	32574038
571	O-linked_Glycosylation	SSSVPSTTSTPTVTS HCCCCCCCCCCCCCC	34.63	32574038
571	Phosphorylation	SSSVPSTTSTPTVTS HCCCCCCCCCCCCCC	34.63	22817900
572	O-linked_Glycosylation	SSVPSTTSTPTVTSA CCCCCCCCCCCCCCC	32.26	32574038
572	Phosphorylation	SSVPSTTSTPTVTSA CCCCCCCCCCCCCCC	32.26	30576142
573	O-linked_Glycosylation	SVPSTTSTPTVTSAA CCCCCCCCCCCCCCC	22.38	32574038
573	Phosphorylation	SVPSTTSTPTVTSAA CCCCCCCCCCCCCCC	22.38	25627689
575	Phosphorylation	PSTTSTPTVTSAAGL CCCCCCCCCCCCCHH	36.18	22817900
577	O-linked_Glycosylation	TTSTPTVTSAAGLQK CCCCCCCCCCCHHHH	18.35	32574038
578	O-linked_Glycosylation	TSTPTVTSAAGLQKS CCCCCCCCCCHHHHH	16.28	32574038
578	Phosphorylation	TSTPTVTSAAGLQKS CCCCCCCCCCHHHHH	16.28	30576142
585	O-linked_Glycosylation	SAAGLQKSLLSSTST CCCHHHHHHHCCCCC	22.91	32574038
585	Phosphorylation	SAAGLQKSLLSSTST CCCHHHHHHHCCCCC	22.91	22199227
588	Phosphorylation	GLQKSLLSSTSTTTK HHHHHHHCCCCCEEE	36.54	20068231
589	O-linked_Glycosylation	LQKSLLSSTSTTTKI HHHHHHCCCCCEEEE	26.75	32574038
589	Phosphorylation	LQKSLLSSTSTTTKI HHHHHHCCCCCEEEE	26.75	28348404
590	O-linked_Glycosylation	QKSLLSSTSTTTKIT HHHHHCCCCCEEEEE	27.07	32574038
590	Phosphorylation	QKSLLSSTSTTTKIT HHHHHCCCCCEEEEE	27.07	20068231
591	Phosphorylation	KSLLSSTSTTTKITT HHHHCCCCCEEEEEC	26.21	28348404
592	O-linked_Glycosylation	SLLSSTSTTTKITTG HHHCCCCCEEEEECC	38.28	32574038
592	Phosphorylation	SLLSSTSTTTKITTG HHHCCCCCEEEEECC	38.28	20068231
593	Phosphorylation	LLSSTSTTTKITTGS HHCCCCCEEEEECCC	26.34	20068231
594	O-linked_Glycosylation	LSSTSTTTKITTGSS HCCCCCEEEEECCCC	22.12	32574038
594	Phosphorylation	LSSTSTTTKITTGSS HCCCCCEEEEECCCC	22.12	20068231
597	Phosphorylation	TSTTTKITTGSSSAG CCCEEEEECCCCCCC	27.02	21406692
598	Phosphorylation	STTTKITTGSSSAGT CCEEEEECCCCCCCC	38.24	21406692
600	Phosphorylation	TTKITTGSSSAGTQS EEEEECCCCCCCCCC	21.01	21406692
601	O-linked_Glycosylation	TKITTGSSSAGTQSS EEEECCCCCCCCCCC	26.08	32574038
601	Phosphorylation	TKITTGSSSAGTQSS EEEECCCCCCCCCCC	26.08	18477460
602	Phosphorylation	KITTGSSSAGTQSST EEECCCCCCCCCCCC	32.20	21406692
605	Phosphorylation	TGSSSAGTQSSTSNR CCCCCCCCCCCCCCC	25.62	21406692
607	Phosphorylation	SSSAGTQSSTSNRLW CCCCCCCCCCCCCCC	35.11	21406692
608	Phosphorylation	SSAGTQSSTSNRLWA CCCCCCCCCCCCCCC	26.49	21406692
609	Phosphorylation	SAGTQSSTSNRLWAE CCCCCCCCCCCCCCC	34.96	21406692
609 (in isoform 4)	Phosphorylation	-	34.96	25159151
610	Phosphorylation	AGTQSSTSNRLWAED CCCCCCCCCCCCCCC	23.15	21406692
612 (in isoform 4)	Phosphorylation	-	31.23	25159151
618	O-linked_Glycosylation	NRLWAEDSTEKEKDS CCCCCCCCCCCCCCC	29.94	32574038
618	Phosphorylation	NRLWAEDSTEKEKDS CCCCCCCCCCCCCCC	29.94	28355574
619	Phosphorylation	RLWAEDSTEKEKDSV CCCCCCCCCCCCCCC	64.50	23403867
621 (in isoform 4)	Phosphorylation	-	70.88	25159151
631	O-linked_Glycosylation	DSVPTAVTIPVAPTV CCCCCEEEECCCCCC	19.66	32574038
631	Phosphorylation	DSVPTAVTIPVAPTV CCCCCEEEECCCCCC	19.66	-
637	O-linked_Glycosylation	VTIPVAPTVVNAAAS EEECCCCCCCCCCCC	27.61	32574038
645	O-linked_Glycosylation	VVNAAASTTTLTTTT CCCCCCCCCEEEEEC	21.05	32574038
645	Phosphorylation	VVNAAASTTTLTTTT CCCCCCCCCEEEEEC	21.05	-
647	Phosphorylation	NAAASTTTLTTTTAG CCCCCCCEEEEECCC	23.38	-
652	Phosphorylation	TTTLTTTTAGTVSST CCEEEEECCCCCCCC	22.46	-
668	Phosphorylation	EVRERRRSYLTPVRD HHHHHHHHHCCCCCC	23.76	27273156
669	Phosphorylation	VRERRRSYLTPVRDE HHHHHHHHCCCCCCC	16.88	28555341
671	Phosphorylation	ERRRSYLTPVRDEES HHHHHHCCCCCCCCC	16.11	25159151
678	Phosphorylation	TPVRDEESESQRKAR CCCCCCCCHHHHHHH	40.26	22516431
680	Phosphorylation	VRDEESESQRKARSR CCCCCCHHHHHHHHH	44.56	22516431
686	Phosphorylation	ESQRKARSRQARQSR HHHHHHHHHHHHHHH	33.34	23882029
692	Phosphorylation	RSRQARQSRRSTQGV HHHHHHHHHHHCCCC	24.90	15194681
695	Phosphorylation	QARQSRRSTQGVTLT HHHHHHHHCCCCCHH	24.79	29255136
696	Phosphorylation	ARQSRRSTQGVTLTD HHHHHHHCCCCCHHH	27.77	11384979
700	Phosphorylation	RRSTQGVTLTDLQEA HHHCCCCCHHHHHHH	30.66	30266825
702	Phosphorylation	STQGVTLTDLQEAEK HCCCCCHHHHHHHHH	25.87	23927012
710	Phosphorylation	DLQEAEKTIGRSRST HHHHHHHHHCCCHHH	21.85	20873877
716	Phosphorylation	KTIGRSRSTRTREQE HHHCCCHHHHHHHHH	24.40	26074081
717	Phosphorylation	TIGRSRSTRTREQEN HHCCCHHHHHHHHHH	34.64	26074081
719	Phosphorylation	GRSRSTRTREQENEE CCCHHHHHHHHHHHH	38.35	24719451
743	Acetylation	DKEKQEEKKESETSR HHHHHHHHHHHHHHH	62.17	7662857
746	O-linked_Glycosylation	KQEEKKESETSREDE HHHHHHHHHHHHHHH	55.87	32574038
748	Phosphorylation	EEKKESETSREDEYK HHHHHHHHHHHHHHH	42.22	25159151
749	Phosphorylation	EKKESETSREDEYKQ HHHHHHHHHHHHHHH	29.62	-
754	Phosphorylation	ETSREDEYKQKYSRT HHHHHHHHHHHHCCC	30.92	22817900
755	Acetylation	TSREDEYKQKYSRTY HHHHHHHHHHHCCCC	37.96	7662873
758	Phosphorylation	EDEYKQKYSRTYDET HHHHHHHHCCCCCHH	10.82	21945579
759	Phosphorylation	DEYKQKYSRTYDETY HHHHHHHCCCCCHHH	25.78	21945579
761	Phosphorylation	YKQKYSRTYDETYQR HHHHHCCCCCHHHHH	29.41	21945579
762	Phosphorylation	KQKYSRTYDETYQRY HHHHCCCCCHHHHHH	15.63	21945579
765	Phosphorylation	YSRTYDETYQRYRPV HCCCCCHHHHHHCCC	23.27	21945579
766	Phosphorylation	SRTYDETYQRYRPVS CCCCCHHHHHHCCCC	6.74	21945579
769	Phosphorylation	YDETYQRYRPVSTSS CCHHHHHHCCCCCCC	12.07	-
773	O-linked_Glycosylation	YQRYRPVSTSSSTTP HHHHCCCCCCCCCCC	25.84	32574038
774	O-linked_Glycosylation	QRYRPVSTSSSTTPS HHHCCCCCCCCCCCC	32.63	32574038
775	O-linked_Glycosylation	RYRPVSTSSSTTPSS HHCCCCCCCCCCCCC	18.13	32574038
776	O-linked_Glycosylation	YRPVSTSSSTTPSSS HCCCCCCCCCCCCCC	31.62	32574038
777	O-linked_Glycosylation	RPVSTSSSTTPSSSL CCCCCCCCCCCCCCH	35.75	32574038
778	O-linked_Glycosylation	PVSTSSSTTPSSSLS CCCCCCCCCCCCCHH	44.68	32574038
779	O-linked_Glycosylation	VSTSSSTTPSSSLST CCCCCCCCCCCCHHH	24.11	32574038
781	O-linked_Glycosylation	TSSSTTPSSSLSTMS CCCCCCCCCCHHHHC	30.39	32574038
781	Phosphorylation	TSSSTTPSSSLSTMS CCCCCCCCCCHHHHC	30.39	-
782	O-linked_Glycosylation	SSSTTPSSSLSTMSS CCCCCCCCCHHHHCC	36.18	32574038
783	O-linked_Glycosylation	SSTTPSSSLSTMSSS CCCCCCCCHHHHCCH	30.58	32574038
785	O-linked_Glycosylation	TTPSSSLSTMSSSLY CCCCCCHHHHCCHHH	24.82	32574038
786	O-linked_Glycosylation	TPSSSLSTMSSSLYA CCCCCHHHHCCHHHH	26.77	32574038
788	O-linked_Glycosylation	SSSLSTMSSSLYASS CCCHHHHCCHHHHHH	19.50	32574038
789	O-linked_Glycosylation	SSLSTMSSSLYASSQ CCHHHHCCHHHHHHC	17.34	32574038
790	O-linked_Glycosylation	SLSTMSSSLYASSQL CHHHHCCHHHHHHCC	20.35	32574038
790	Phosphorylation	SLSTMSSSLYASSQL CHHHHCCHHHHHHCC	20.35	-
792	Phosphorylation	STMSSSLYASSQLNR HHHCCHHHHHHCCCC	13.34	-
794	O-linked_Glycosylation	MSSSLYASSQLNRPN HCCHHHHHHCCCCCC	12.69	32574038
794	Phosphorylation	MSSSLYASSQLNRPN HCCHHHHHHCCCCCC	12.69	-
795	O-linked_Glycosylation	SSSLYASSQLNRPNS CCHHHHHHCCCCCCC	30.43	32574038
795	Phosphorylation	SSSLYASSQLNRPNS CCHHHHHHCCCCCCC	30.43	-
802	O-linked_Glycosylation	SQLNRPNSLVGITSA HCCCCCCCCCHHHHH	27.41	32574038
802	Phosphorylation	SQLNRPNSLVGITSA HCCCCCCCCCHHHHH	27.41	26657352
807	O-linked_Glycosylation	PNSLVGITSAYSRGI CCCCCHHHHHHHCCC	11.02	32574038
808	O-linked_Glycosylation	NSLVGITSAYSRGIT CCCCHHHHHHHCCCC	24.24	32574038
810	Phosphorylation	LVGITSAYSRGITKE CCHHHHHHHCCCCHH	9.92	-
811	Phosphorylation	VGITSAYSRGITKEN CHHHHHHHCCCCHHH	24.60	-
835	O-linked_Glycosylation	EKEGEDKSQPKSIRE HHCCCCCCCCHHHHH	65.13	32574038
839	Phosphorylation	EDKSQPKSIRERRRP CCCCCCHHHHHHCCC	33.29	-
852	Phosphorylation	RPREKRRSTGVSFWT CCHHHHHHCCCCCCC	33.28	30266825
853	Phosphorylation	PREKRRSTGVSFWTQ CHHHHHHCCCCCCCC	39.53	30266825
856	Phosphorylation	KRRSTGVSFWTQDSD HHHHCCCCCCCCCCC	19.19	30266825
859	Phosphorylation	STGVSFWTQDSDENE HCCCCCCCCCCCCCH	22.08	23459991
862	Phosphorylation	VSFWTQDSDENEQEQ CCCCCCCCCCCHHHH	36.69	22167270
871	Phosphorylation	ENEQEQQSDTEEGSN CCHHHHHCCCCCCCC	46.31	22167270
873	Phosphorylation	EQEQQSDTEEGSNKK HHHHHCCCCCCCCCC	40.98	22167270
877	Phosphorylation	QSDTEEGSNKKETQT HCCCCCCCCCCCCCC	49.08	30266825
882	Phosphorylation	EGSNKKETQTDSISR CCCCCCCCCCCCCCC	45.72	21945579
884	Phosphorylation	SNKKETQTDSISRYE CCCCCCCCCCCCCCC	38.85	21945579
886	Phosphorylation	KKETQTDSISRYETS CCCCCCCCCCCCCCC	26.33	21945579
888	Phosphorylation	ETQTDSISRYETSST CCCCCCCCCCCCCCC	32.53	21945579
890	Phosphorylation	QTDSISRYETSSTSA CCCCCCCCCCCCCCC	19.44	21945579
892	Phosphorylation	DSISRYETSSTSAGD CCCCCCCCCCCCCHH	21.02	21945579
893	Phosphorylation	SISRYETSSTSAGDR CCCCCCCCCCCCHHH	21.48	21945579
894	Phosphorylation	ISRYETSSTSAGDRY CCCCCCCCCCCHHHH	33.53	21945579
895	Phosphorylation	SRYETSSTSAGDRYD CCCCCCCCCCHHHHH	23.51	21945579
896	Phosphorylation	RYETSSTSAGDRYDS CCCCCCCCCHHHHHH	32.00	21945579
901	Phosphorylation	STSAGDRYDSLLGRS CCCCHHHHHHHHCCC	18.02	21945579
903	Phosphorylation	SAGDRYDSLLGRSGS CCHHHHHHHHCCCCC	19.29	21945579
908	Phosphorylation	YDSLLGRSGSYSYLE HHHHHCCCCCCHHHC	30.23	23927012
910	Phosphorylation	SLLGRSGSYSYLEER HHHCCCCCCHHHCCC	16.50	22322096
911	Phosphorylation	LLGRSGSYSYLEERK HHCCCCCCHHHCCCC	12.59	21945579
912	Phosphorylation	LGRSGSYSYLEERKP HCCCCCCHHHCCCCC	25.57	21945579
913	Phosphorylation	GRSGSYSYLEERKPY CCCCCCHHHCCCCCC	15.20	21945579
920	Phosphorylation	YLEERKPYSSRLEKD HHCCCCCCCCCCCCC	23.47	-
921	Phosphorylation	LEERKPYSSRLEKDD HCCCCCCCCCCCCCC	19.94	-
922	Phosphorylation	EERKPYSSRLEKDDS CCCCCCCCCCCCCCC	34.73	-
926	Acetylation	PYSSRLEKDDSTDFK CCCCCCCCCCCHHHH	72.00	26051181
929	Phosphorylation	SRLEKDDSTDFKKLY CCCCCCCCHHHHHHH	39.76	28348404
936	Phosphorylation	STDFKKLYEQILAEN CHHHHHHHHHHHHHH	18.05	20068231
945	Acetylation	QILAENEKLKAQLHD HHHHHHHHHHHHHHH	67.86	26051181
945	Ubiquitination	QILAENEKLKAQLHD HHHHHHHHHHHHHHH	67.86	-
947	Malonylation	LAENEKLKAQLHDTN HHHHHHHHHHHHHCC	45.19	26320211
953	Phosphorylation	LKAQLHDTNMELTDL HHHHHHHCCHHHHHH	26.22	24247654
955	Sulfoxidation	AQLHDTNMELTDLKL HHHHHCCHHHHHHHH	4.92	30846556
961	2-Hydroxyisobutyrylation	NMELTDLKLQLEKAT CHHHHHHHHHHHHHH	36.68	-
978	Phosphorylation	QERFADRSLLEMEKR HHHHHCHHHHHHHHH	37.54	21815630
984	Acetylation	RSLLEMEKRERRALE HHHHHHHHHHHHHHH	59.24	26051181
984	Malonylation	RSLLEMEKRERRALE HHHHHHHHHHHHHHH	59.24	26320211
995	Phosphorylation	RALERRISEMEEELK HHHHHHHHHHHHHHH	29.13	29255136
997	Sulfoxidation	LERRISEMEEELKML HHHHHHHHHHHHHCC	6.66	21406390
1002	"N6,N6-dimethyllysine"	SEMEEELKMLPDLKA HHHHHHHHCCCCCHH	41.49	-
1002	Methylation	SEMEEELKMLPDLKA HHHHHHHHCCCCCHH	41.49	-
1008	"N6,N6-dimethyllysine"	LKMLPDLKADNQRLK HHCCCCCHHHHHHHC	62.16	-
1008	Methylation	LKMLPDLKADNQRLK HHCCCCCHHHHHHHC	62.16	-
1029	Phosphorylation	IRVISKLSK------ HHHHHHHCC------	39.80	-

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
141	T	Phosphorylation	Kinase	MYLK	Q15746	GPS
445	S	Phosphorylation	Kinase	NUAK1	O60285	Uniprot
472	S	Phosphorylation	Kinase	NUAK1	O60285	Uniprot
473	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
692	S	Phosphorylation	Kinase	PKG	-	Uniprot
692	S	Phosphorylation	Kinase	PKA	-	Uniprot
692	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
692	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
695	S	Phosphorylation	Kinase	PKG	-	Uniprot
695	S	Phosphorylation	Kinase	PKA	-	Uniprot
695	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
695	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
696	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
696	T	Phosphorylation	Kinase	MRCK-SUBFAMILY	-	GPS
696	T	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
696	T	Phosphorylation	Kinase	RAF1	P04049	Uniprot
696	T	Phosphorylation	Kinase	CDC42BP	Q9Y5S2	Uniprot
696	T	Phosphorylation	Kinase	DAPK3	O43293	Uniprot
852	S	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
852	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
852	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
852	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
853	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
853	T	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
910	S	Phosphorylation	Kinase	NUAK1	O60285	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:19744480

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
445	S	Phosphorylation	18669648
Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2.
472	S	Phosphorylation	20354225
Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2.
473	S	Phosphorylation	18477460
Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1.
695	S	Phosphorylation	15194681
In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1.
696	T	Phosphorylation	11719507
In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1.
696	T	Phosphorylation	11719507
May be phosphorylated at Thr-696 by DMPK; may inhibit the myosin phosphatase activity.
696	T	Phosphorylation	11719507
Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696.
910	S	Phosphorylation	20354225
Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2.

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 MYPT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC7_HUMAN	HDAC7	physical	17369396
RHOA_HUMAN	RHOA	physical	22939629
LATS1_HUMAN	LATS1	physical	22641346
AASD1_HUMAN	AARSD1	physical	22863883
ARP3_HUMAN	ACTR3	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
CUL1_HUMAN	CUL1	physical	22863883
P3H1_HUMAN	P3H1	physical	22863883
NRDC_HUMAN	NRD1	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
NUDT5_HUMAN	NUDT5	physical	22863883
NUSAP_HUMAN	NUSAP1	physical	22863883
OSGEP_HUMAN	OSGEP	physical	22863883
PFD1_HUMAN	PFDN1	physical	22863883
PFD5_HUMAN	PFDN5	physical	22863883
TRUA_HUMAN	PUS1	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
TPP2_HUMAN	TPP2	physical	22863883
TRI47_HUMAN	TRIM47	physical	22863883
TTL12_HUMAN	TTLL12	physical	22863883

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.

Regulatory Network of MYPT1_HUMAN

Related Literatures of Post-Translational Modification

Hydroxylation
Reference	PubMed
"MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, isa substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)."; Webb J.D., Muranyi A., Pugh C.W., Ratcliffe P.J., Coleman M.L.; Biochem. J. 420:327-333(2009). Cited for: PROTEIN SEQUENCE OF 63-76; 95-105 AND 217-228, FUNCTION, ANDHYDROXYLATION AT ASN-67; ASN-100 AND ASN-226 BY HIF1AN.	19245366 [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-445; SER-507; SER-871AND SER-910, AND MASS SPECTROMETRY.	19690332 [Abstract]
"New roles for the LKB1-NUAK pathway in controlling myosin phosphatasecomplexes and cell adhesion."; Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M.,Aizawa S., Prescott A.R., Alessi D.R.; Sci. Signal. 3:RA25-RA25(2010). Cited for: FUNCTION, INTERACTION WITH PPP1CB AND 14-3-3, DOMAIN KVKF MOTIF, ANDPHOSPHORYLATION AT SER-445; SER-472 AND SER-910.	20354225 [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 THR-443; SER-445 ANDTYR-446, 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-299; SER-422; SER-445;SER-473; SER-477; SER-507; SER-862 AND SER-871, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-445, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-507 ANDSER-910, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Myosin phosphatase-targeting subunit 1 regulates mitosis byantagonizing polo-like kinase 1."; Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M.,Hartshorne D.J., Matsumura F.; Dev. Cell 14:787-797(2008). Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-432; SER-473AND SER-601, PHOSPHORYLATION BY PLK1, AND MUTAGENESIS OF SER-473.	18477460 [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 SER-507, AND MASSSPECTROMETRY.	17924679 [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 SER-422, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Rho-kinase--mediated contraction of isolated stress fibers."; Katoh K., Kano Y., Amano M., Onishi H., Kaibuchi K., Fujiwara K.; J. Cell Biol. 153:569-584(2001). Cited for: PHOSPHORYLATION AT SER-852.	11331307 [Abstract]
"Solution structure of the inhibitory phosphorylation domain of myosinphosphatase targeting subunit 1."; Mori S., Iwaoka R., Eto M., Ohki S.-Y.; Proteins 77:732-735(2009). Cited for: STRUCTURE BY NMR OF 658-714, AND PHOSPHORYLATION AT THR-696.	19701943 [Abstract]
"Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocytedifferentiation."; Lock F.E., Hotchin N.A.; PLoS ONE 4:E8190-E8190(2009). Cited for: PHOSPHORYLATION AT THR-696.	19997641 [Abstract]
"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 THR-696, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Cdc42-MRCK and Rho-ROCK signalling cooperate in myosinphosphorylation and cell invasion."; Wilkinson S., Paterson H.F., Marshall C.J.; Nat. Cell Biol. 7:255-261(2005). Cited for: PHOSPHORYLATION AT THR-696.	15723050 [Abstract]
"Phosphorylation of the myosin-binding subunit of myosin phosphataseby Raf-1 and inhibition of phosphatase activity."; Broustas C.G., Grammatikakis N., Eto M., Dent P., Brautigan D.L.,Kasid U.; J. Biol. Chem. 277:3053-3059(2002). Cited for: PHOSPHORYLATION AT THR-696 BY RAF1, AND INTERACTION WITH RAF1.	11719507 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-890; TYR-901 ANDTYR-911, AND MASS SPECTROMETRY.	15144186 [Abstract]

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