dbPTM

SMC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMC3_HUMAN
UniProt AC	Q9UQE7
Protein Name	Structural maintenance of chromosomes protein 3
Gene Name	SMC3
Organism	Homo sapiens (Human).
Sequence Length	1217
Subcellular Localization	Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except
Protein Description	Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement..
Protein Sequence	MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	VIIQGFRSYRDQTIV HHHHCHHHCCCCCEE	23.43	26074081
14	Phosphorylation	IIQGFRSYRDQTIVD HHHCHHHCCCCCEEC	17.60	26074081
18	Phosphorylation	FRSYRDQTIVDPFSS HHHCCCCCEECCCCC	27.53	24719451
24	Phosphorylation	QTIVDPFSSKHNVIV CCEECCCCCCCCEEE	43.81	25599653
25	Phosphorylation	TIVDPFSSKHNVIVG CEECCCCCCCCEEEC	38.01	25599653
26	2-Hydroxyisobutyrylation	IVDPFSSKHNVIVGR EECCCCCCCCEEECC	37.69	-
26	Ubiquitination	IVDPFSSKHNVIVGR EECCCCCCCCEEECC	37.69	21906983
69	Phosphorylation	LALLHEGTGPRVISA HHHHHCCCCHHHHHE	40.82	22496350
72	Methylation	LHEGTGPRVISAFVE HHCCCCHHHHHEEEE	39.48	5168447
85	Phosphorylation	VEIIFDNSDNRLPID EEECCCCCCCCCCCC	37.80	22067460
93	2-Hydroxyisobutyrylation	DNRLPIDKEEVSLRR CCCCCCCHHHHHHHH	57.40	-
105	Acetylation	LRRVIGAKKDQYFLD HHHHHCCCCCCHHCC	52.23	18614053
106	Acetylation	RRVIGAKKDQYFLDK HHHHCCCCCCHHCCC	49.91	18614053
106	Ubiquitination	RRVIGAKKDQYFLDK HHHHCCCCCCHHCCC	49.91	18614053
109	Phosphorylation	IGAKKDQYFLDKKMV HCCCCCCHHCCCCCC	19.08	-
113	Sumoylation	KDQYFLDKKMVTKND CCCHHCCCCCCCHHH	44.94	-
113	Acetylation	KDQYFLDKKMVTKND CCCHHCCCCCCCHHH	44.94	26051181
113	Sumoylation	KDQYFLDKKMVTKND CCCHHCCCCCCCHHH	44.94	-
113	Ubiquitination	KDQYFLDKKMVTKND CCCHHCCCCCCCHHH	44.94	22817900
114	Ubiquitination	DQYFLDKKMVTKNDV CCHHCCCCCCCHHHH	37.97	22817900
117	Phosphorylation	FLDKKMVTKNDVMNL HCCCCCCCHHHHHHH	22.19	24719451
118	Acetylation	LDKKMVTKNDVMNLL CCCCCCCHHHHHHHH	39.48	26051181
118	Ubiquitination	LDKKMVTKNDVMNLL CCCCCCCHHHHHHHH	39.48	21906983
122	Sulfoxidation	MVTKNDVMNLLESAG CCCHHHHHHHHHHCC	3.05	21406390
133	Phosphorylation	ESAGFSRSNPYYIVK HHCCCCCCCCEEEEE	40.74	28152594
136	Phosphorylation	GFSRSNPYYIVKQGK CCCCCCCEEEEECCC	15.29	28152594
137	Phosphorylation	FSRSNPYYIVKQGKI CCCCCCEEEEECCCC	10.65	28152594
140	2-Hydroxyisobutyrylation	SNPYYIVKQGKINQM CCCEEEEECCCCCCC	43.72	-
140	Acetylation	SNPYYIVKQGKINQM CCCEEEEECCCCCCC	43.72	19608861
140	Ubiquitination	SNPYYIVKQGKINQM CCCEEEEECCCCCCC	43.72	21906983
143	Ubiquitination	YYIVKQGKINQMATA EEEEECCCCCCCCCC	35.67	21906983
147	Sulfoxidation	KQGKINQMATAPDSQ ECCCCCCCCCCCCHH	2.86	21406390
149	Phosphorylation	GKINQMATAPDSQRL CCCCCCCCCCCHHHH	33.12	20860994
155	Methylation	ATAPDSQRLKLLREV CCCCCHHHHHHHHHH	37.43	5168467
172	Ubiquitination	TRVYDERKEESISLM CCCCCCCHHHHHHHH	64.88	29967540
175	Phosphorylation	YDERKEESISLMKET CCCCHHHHHHHHHHC	20.69	20068231
177	Phosphorylation	ERKEESISLMKETEG CCHHHHHHHHHHCCC	31.52	20068231
180	2-Hydroxyisobutyrylation	EESISLMKETEGKRE HHHHHHHHHCCCHHH	67.77	-
180	Ubiquitination	EESISLMKETEGKRE HHHHHHHHHCCCHHH	67.77	21906983
185	Ubiquitination	LMKETEGKREKINEL HHHHCCCHHHHHHHH	51.67	22817900
188	Acetylation	ETEGKREKINELLKY HCCCHHHHHHHHHHH	55.66	25953088
188	Ubiquitination	ETEGKREKINELLKY HCCCHHHHHHHHHHH	55.66	23000965
194	Ubiquitination	EKINELLKYIEERLH HHHHHHHHHHHHHHH	57.73	23000965
207	2-Hydroxyisobutyrylation	LHTLEEEKEELAQYQ HHCHHHHHHHHHHHH	60.82	-
207	Acetylation	LHTLEEEKEELAQYQ HHCHHHHHHHHHHHH	60.82	25953088
207	Ubiquitination	LHTLEEEKEELAQYQ HHCHHHHHHHHHHHH	60.82	29967540
213	Phosphorylation	EKEELAQYQKWDKMR HHHHHHHHHHHHHHH	13.37	17360941
215	Acetylation	EELAQYQKWDKMRRA HHHHHHHHHHHHHHH	53.04	19608861
215	Ubiquitination	EELAQYQKWDKMRRA HHHHHHHHHHHHHHH	53.04	22817900
218	Ubiquitination	AQYQKWDKMRRALEY HHHHHHHHHHHHHHH	32.94	22817900
225	Phosphorylation	KMRRALEYTIYNQEL HHHHHHHHHHHHHHH	10.17	28152594
226	Phosphorylation	MRRALEYTIYNQELN HHHHHHHHHHHHHHH	13.96	28152594
236	Methylation	NQELNETRAKLDELS HHHHHHHHHHHHHHH	24.44	5168455
238	Acetylation	ELNETRAKLDELSAK HHHHHHHHHHHHHHH	53.86	25953088
238	Ubiquitination	ELNETRAKLDELSAK HHHHHHHHHHHHHHH	53.86	29967540
243	Phosphorylation	RAKLDELSAKRETSG HHHHHHHHHHHHCCC	29.69	21815630
245	2-Hydroxyisobutyrylation	KLDELSAKRETSGEK HHHHHHHHHHCCCHH	47.60	-
245	Acetylation	KLDELSAKRETSGEK HHHHHHHHHHCCCHH	47.60	26051181
245	Methylation	KLDELSAKRETSGEK HHHHHHHHHHCCCHH	47.60	-
245	Ubiquitination	KLDELSAKRETSGEK HHHHHHHHHHCCCHH	47.60	24816145
266	Acetylation	AQQDARDKMEDIERQ HHHHHHHHHHHHHHH	38.34	26051181
272	Methylation	DKMEDIERQVRELKT HHHHHHHHHHHHHHH	40.40	5168443
279	Phosphorylation	RQVRELKTKISAMKE HHHHHHHHHHHHHHH	46.35	26074081
280	2-Hydroxyisobutyrylation	QVRELKTKISAMKEE HHHHHHHHHHHHHHH	32.83	-
282	Phosphorylation	RELKTKISAMKEEKE HHHHHHHHHHHHHHH	24.70	26074081
285	2-Hydroxyisobutyrylation	KTKISAMKEEKEQLS HHHHHHHHHHHHHHH	63.54	-
285	Acetylation	KTKISAMKEEKEQLS HHHHHHHHHHHHHHH	63.54	25953088
285	Ubiquitination	KTKISAMKEEKEQLS HHHHHHHHHHHHHHH	63.54	24816145
292	Phosphorylation	KEEKEQLSAERQEQI HHHHHHHHHHHHHHH	27.98	25159151
304	Ubiquitination	EQIKQRTKLELKAKD HHHHHHHHHHHHHHH	42.00	23503661
308	Ubiquitination	QRTKLELKAKDLQDE HHHHHHHHHHHHHHH	43.97	23503661
310	Acetylation	TKLELKAKDLQDELA HHHHHHHHHHHHHHC	58.34	26051181
310	Ubiquitination	TKLELKAKDLQDELA HHHHHHHHHHHHHHC	58.34	23503661
323	Methylation	LAGNSEQRKRLLKER HCCCHHHHHHHHHHH	23.24	5168423
336	Acetylation	ERQKLLEKIEEKQKE HHHHHHHHHHHHHHH	56.22	23236377
336	Malonylation	ERQKLLEKIEEKQKE HHHHHHHHHHHHHHH	56.22	26320211
340	Acetylation	LLEKIEEKQKELAET HHHHHHHHHHHHHHC	54.61	25953088
347	Phosphorylation	KQKELAETEPKFNSV HHHHHHHCCCCCHHH	52.56	20068231
350	2-Hydroxyisobutyrylation	ELAETEPKFNSVKEK HHHHCCCCCHHHHHH	51.44	-
350	Acetylation	ELAETEPKFNSVKEK HHHHCCCCCHHHHHH	51.44	26051181
350	Ubiquitination	ELAETEPKFNSVKEK HHHHCCCCCHHHHHH	51.44	29967540
378	Ubiquitination	ERTDLYAKQGRGSQF HHHHHHHHCCCCCCC	39.46	29967540
383	Phosphorylation	YAKQGRGSQFTSKEE HHHCCCCCCCCCHHH	22.29	27174698
386	O-linked_Glycosylation	QGRGSQFTSKEERDK CCCCCCCCCHHHHHH	31.11	28510447
386	Phosphorylation	QGRGSQFTSKEERDK CCCCCCCCCHHHHHH	31.11	27174698
387	O-linked_Glycosylation	GRGSQFTSKEERDKW CCCCCCCCHHHHHHH	39.08	28510447
387	Phosphorylation	GRGSQFTSKEERDKW CCCCCCCCHHHHHHH	39.08	27174698
388	Acetylation	RGSQFTSKEERDKWI CCCCCCCHHHHHHHH	61.61	26051181
388	Ubiquitination	RGSQFTSKEERDKWI CCCCCCCHHHHHHHH	61.61	24816145
400	Acetylation	KWIKKELKSLDQAIN HHHHHHHHHHHHHHH	50.49	25953088
400	Malonylation	KWIKKELKSLDQAIN HHHHHHHHHHHHHHH	50.49	26320211
409	Acetylation	LDQAINDKKRQIAAI HHHHHHHHHHHHHHH	45.42	25953088
409	Methylation	LDQAINDKKRQIAAI HHHHHHHHHHHHHHH	45.42	-
418	Acetylation	RQIAAIHKDLEDTEA HHHHHHHCCHHCHHH	58.87	26051181
427	Acetylation	LEDTEANKEKNLEQY HHCHHHHHHHCHHHH	76.69	26051181
427	Methylation	LEDTEANKEKNLEQY HHCHHHHHHHCHHHH	76.69	-
429	Methylation	DTEANKEKNLEQYNK CHHHHHHHCHHHHHH	69.32	-
436	Acetylation	KNLEQYNKLDQDLNE HCHHHHHHHHHHHHH	48.81	26051181
436	Ubiquitination	KNLEQYNKLDQDLNE HCHHHHHHHHHHHHH	48.81	29967540
445	Acetylation	DQDLNEVKARVEELD HHHHHHHHHHHHHHH	25.05	25953088
445	Methylation	DQDLNEVKARVEELD HHHHHHHHHHHHHHH	25.05	-
445	Ubiquitination	DQDLNEVKARVEELD HHHHHHHHHHHHHHH	25.05	32015554
453	Methylation	ARVEELDRKYYEVKN HHHHHHHHHHHHHCC	41.31	115917249
459	Acetylation	DRKYYEVKNKKDELQ HHHHHHHCCCHHHHH	51.62	25953088
459	Ubiquitination	DRKYYEVKNKKDELQ HHHHHHHCCCHHHHH	51.62	33845483
486	2-Hydroxyisobutyrylation	EQQALAAKREDLEKK HHHHHHHHHHHHHHH	51.19	-
486	Methylation	EQQALAAKREDLEKK HHHHHHHHHHHHHHH	51.19	-
486	Ubiquitination	EQQALAAKREDLEKK HHHHHHHHHHHHHHH	51.19	21906983
503	2-Hydroxyisobutyrylation	LLRAATGKAILNGID HHHHHHHHHHHHCHH	28.09	-
503	Ubiquitination	LLRAATGKAILNGID HHHHHHHHHHHHCHH	28.09	29967540
514	Acetylation	NGIDSINKVLDHFRR HCHHHHHHHHHHHHH	42.37	25953088
560	Phosphorylation	TAGNRLFYHIVDSDE ECCCEEEEEEECCCC	8.67	25884760
565	Phosphorylation	LFYHIVDSDEVSTKI EEEEEECCCCCHHHH	25.44	-
592	Acetylation	VTFLPLNKLDVRDTA EEEEECCCCCCCCCC	54.47	26051181
592	Ubiquitination	VTFLPLNKLDVRDTA EEEEECCCCCCCCCC	54.47	21906983
600	Phosphorylation	LDVRDTAYPETNDAI CCCCCCCCCCCCCCH	12.05	-
612	Ubiquitination	DAIPMISKLRYNPRF CCHHHHHHHCCCCCH	26.51	22817900
615	Phosphorylation	PMISKLRYNPRFDKA HHHHHHCCCCCHHHH	39.70	20860994
621	Acetylation	RYNPRFDKAFKHVFG CCCCCHHHHHHHHHC	53.67	26051181
629	Acetylation	AFKHVFGKTLICRSM HHHHHHCCHHHHCCH	28.79	25953088
635	Phosphorylation	GKTLICRSMEVSTQL CCHHHHCCHHHHHHH	18.19	21406692
636	Sulfoxidation	KTLICRSMEVSTQLA CHHHHCCHHHHHHHH	2.81	28183972
639	Phosphorylation	ICRSMEVSTQLARAF HHCCHHHHHHHHHHH	9.34	21406692
640	Phosphorylation	CRSMEVSTQLARAFT HCCHHHHHHHHHHHC	32.55	21406692
644	Methylation	EVSTQLARAFTMDCI HHHHHHHHHHCCCEE	38.53	5168459
647	Phosphorylation	TQLARAFTMDCITLE HHHHHHHCCCEEEEE	15.89	26126808
665	Phosphorylation	VSHRGALTGGYYDTR CCCCCCCCCCCCHHH	28.20	28152594
668	Phosphorylation	RGALTGGYYDTRKSR CCCCCCCCCHHHHHH	10.26	28152594
669	Phosphorylation	GALTGGYYDTRKSRL CCCCCCCCHHHHHHH	17.70	28152594
671	Phosphorylation	LTGGYYDTRKSRLEL CCCCCCHHHHHHHHH	24.71	28152594
674	Phosphorylation	GYYDTRKSRLELQKD CCCHHHHHHHHHHHH	38.51	20815410
684	Acetylation	ELQKDVRKAEEELGE HHHHHHHHHHHHHHH	61.06	26051181
695	Ubiquitination	ELGELEAKLNENLRR HHHHHHHHHHHHHHH	42.33	29967540
731	Phosphorylation	QQRKFKASRDSILSE HHHHHHHHHHHHHHH	36.89	20068231
734	Phosphorylation	KFKASRDSILSEMKM HHHHHHHHHHHHHHH	25.07	28348404
737	Phosphorylation	ASRDSILSEMKMLKE HHHHHHHHHHHHHHH	33.69	20068231
740	2-Hydroxyisobutyrylation	DSILSEMKMLKEKRQ HHHHHHHHHHHHHHH	36.71	-
740	Acetylation	DSILSEMKMLKEKRQ HHHHHHHHHHHHHHH	36.71	25953088
751	Acetylation	EKRQQSEKTFMPKQR HHHHHHCCCCCHHHH	52.92	25953088
751	Ubiquitination	EKRQQSEKTFMPKQR HHHHHHCCCCCHHHH	52.92	24816145
756	2-Hydroxyisobutyrylation	SEKTFMPKQRSLQSL HCCCCCHHHHHHHHH	46.70	-
773	Phosphorylation	SLHAMESTRESLKAE HHHHHHHHHHHHHHH	25.75	-
778	Acetylation	ESTRESLKAELGTDL HHHHHHHHHHHCHHH	49.44	26051181
783	Phosphorylation	SLKAELGTDLLSQLS HHHHHHCHHHHHHCC	35.78	30108239
787	Phosphorylation	ELGTDLLSQLSLEDQ HHCHHHHHHCCHHHH	36.05	17525332
790	Phosphorylation	TDLLSQLSLEDQKRV HHHHHHCCHHHHHHH	23.29	30108239
795	2-Hydroxyisobutyrylation	QLSLEDQKRVDALND HCCHHHHHHHHHHHH	67.71	-
795	Acetylation	QLSLEDQKRVDALND HCCHHHHHHHHHHHH	67.71	24431735
795	Ubiquitination	QLSLEDQKRVDALND HCCHHHHHHHHHHHH	67.71	21906983
820	Acetylation	QLLNERIKLEGIITR HHHHHHHHHHHHHHH	46.86	25953088
820	Malonylation	QLLNERIKLEGIITR HHHHHHHHHHHHHHH	46.86	26320211
830	Phosphorylation	GIITRVETYLNENLR HHHHHHHHHHCHHHH	30.37	28509920
831	Phosphorylation	IITRVETYLNENLRK HHHHHHHHHCHHHHH	8.27	29978859
851	Methylation	EQELNELRETEGGTV HHHHHHHHHCCCCEE	42.48	115917253
862	Phosphorylation	GGTVLTATTSELEAI CCEEEEEEHHHHHHH	26.14	22210691
863	Phosphorylation	GTVLTATTSELEAIN CEEEEEEHHHHHHHH	20.10	22210691
864	Phosphorylation	TVLTATTSELEAINK EEEEEEHHHHHHHHH	35.51	22210691
871	Ubiquitination	SELEAINKRVKDTMA HHHHHHHHHHHHHHH	53.08	32015554
874	2-Hydroxyisobutyrylation	EAINKRVKDTMARSE HHHHHHHHHHHHCCH	52.06	-
880	Phosphorylation	VKDTMARSEDLDNSI HHHHHHCCHHHCCCC	26.40	28111955
886	Phosphorylation	RSEDLDNSIDKTEAG CCHHHCCCCCHHHHH	31.65	25159151
889	Acetylation	DLDNSIDKTEAGIKE HHCCCCCHHHHHHHH	46.74	25953088
889	Ubiquitination	DLDNSIDKTEAGIKE HHCCCCCHHHHHHHH	46.74	29967540
890	Phosphorylation	LDNSIDKTEAGIKEL HCCCCCHHHHHHHHH	27.59	30108239
895	Acetylation	DKTEAGIKELQKSME CHHHHHHHHHHHHHH	51.99	25953088
899	Acetylation	AGIKELQKSMERWKN HHHHHHHHHHHHHHH	65.48	26051181
909	Acetylation	ERWKNMEKEHMDAIN HHHHHHHHHHHHHHC	42.00	26051181
919	Phosphorylation	MDAINHDTKELEKMT HHHHCCCHHHHHHHH	20.90	30576142
920	Acetylation	DAINHDTKELEKMTN HHHCCCHHHHHHHHH	67.37	26051181
924	Acetylation	HDTKELEKMTNRQGM CCHHHHHHHHHHCCC	64.74	25953088
924	Ubiquitination	HDTKELEKMTNRQGM CCHHHHHHHHHHCCC	64.74	30230243
926	Phosphorylation	TKELEKMTNRQGMLL HHHHHHHHHHCCCCH	38.01	-
956	Acetylation	LPQEAFEKYQTLSLK CCHHHHHHHHHCCHH	35.88	23954790
956	Ubiquitination	LPQEAFEKYQTLSLK CCHHHHHHHHHCCHH	35.88	23000965
959	Phosphorylation	EAFEKYQTLSLKQLF HHHHHHHHCCHHHHH	18.41	23532336
963	Acetylation	KYQTLSLKQLFRKLE HHHHCCHHHHHHHHH	41.39	25953088
963	Ubiquitination	KYQTLSLKQLFRKLE HHHHCCHHHHHHHHH	41.39	23000965
968	Acetylation	SLKQLFRKLEQCNTE CHHHHHHHHHHHCHH	49.38	23749302
968	Ubiquitination	SLKQLFRKLEQCNTE CHHHHHHHHHHHCHH	49.38	23000965
974	Phosphorylation	RKLEQCNTELKKYSH HHHHHHCHHHHHCCC	50.77	30377224
977	Acetylation	EQCNTELKKYSHVNK HHHCHHHHHCCCCCH	43.35	26051181
977	Ubiquitination	EQCNTELKKYSHVNK HHHCHHHHHCCCCCH	43.35	32015554
978	2-Hydroxyisobutyrylation	QCNTELKKYSHVNKK HHCHHHHHCCCCCHH	65.69	-
979	Phosphorylation	CNTELKKYSHVNKKA HCHHHHHCCCCCHHH	11.47	22817900
980	Phosphorylation	NTELKKYSHVNKKAL CHHHHHCCCCCHHHH	29.82	22210691
984	2-Hydroxyisobutyrylation	KKYSHVNKKALDQFV HHCCCCCHHHHHHHC	38.03	-
984	Ubiquitination	KKYSHVNKKALDQFV HHCCCCCHHHHHHHC	38.03	22817900
985	Ubiquitination	KYSHVNKKALDQFVN HCCCCCHHHHHHHCC	49.32	22817900
994	Phosphorylation	LDQFVNFSEQKEKLI HHHHCCHHHHHHHHH	33.63	28842319
997	2-Hydroxyisobutyrylation	FVNFSEQKEKLIKRQ HCCHHHHHHHHHHHH	53.41	-
997	Acetylation	FVNFSEQKEKLIKRQ HCCHHHHHHHHHHHH	53.41	26051181
997	Methylation	FVNFSEQKEKLIKRQ HCCHHHHHHHHHHHH	53.41	-
997	Ubiquitination	FVNFSEQKEKLIKRQ HCCHHHHHHHHHHHH	53.41	21906983
999	Ubiquitination	NFSEQKEKLIKRQEE CHHHHHHHHHHHHHH	63.65	22817900
1002	Ubiquitination	EQKEKLIKRQEELDR HHHHHHHHHHHHHHH	59.47	22817900
1009	Methylation	KRQEELDRGYKSIME HHHHHHHHHHHHHHH	64.07	115917241
1012	Ubiquitination	EELDRGYKSIMELMN HHHHHHHHHHHHHHH	36.01	21906983
1013	Phosphorylation	ELDRGYKSIMELMNV HHHHHHHHHHHHHHH	20.77	20068231
1025	Ubiquitination	MNVLELRKYEAIQLT HHHHHHHHHHHHHCH	61.13	23000965
1026	Phosphorylation	NVLELRKYEAIQLTF HHHHHHHHHHHHCHH	12.26	28152594
1034	Acetylation	EAIQLTFKQVSKNFS HHHHCHHHHHHHCHH	44.55	25953088
1034	Ubiquitination	EAIQLTFKQVSKNFS HHHHCHHHHHHHCHH	44.55	23000965
1038	Acetylation	LTFKQVSKNFSEVFQ CHHHHHHHCHHHHHH	64.25	26051181
1038	Ubiquitination	LTFKQVSKNFSEVFQ CHHHHHHHCHHHHHH	64.25	23000965
1046	Acetylation	NFSEVFQKLVPGGKA CHHHHHHHHCCCCEE	39.73	26051181
1046	Ubiquitination	NFSEVFQKLVPGGKA CHHHHHHHHCCCCEE	39.73	21906983
1052	Malonylation	QKLVPGGKATLVMKK HHHCCCCEEEEEEEE	44.08	26320211
1058	Ubiquitination	GKATLVMKKGDVEGS CEEEEEEEECCCCCC	46.23	22817900
1059	Ubiquitination	KATLVMKKGDVEGSQ EEEEEEEECCCCCCC	42.10	21906983
1065	Phosphorylation	KKGDVEGSQSQDEGE EECCCCCCCCCCCCC	17.10	22167270
1067	Phosphorylation	GDVEGSQSQDEGEGS CCCCCCCCCCCCCCC	41.10	29255136
1074	Phosphorylation	SQDEGEGSGESERGS CCCCCCCCCCCCCCC	34.78	23401153
1077	Phosphorylation	EGEGSGESERGSGSQ CCCCCCCCCCCCCCC	35.80	23927012
1079	Methylation	EGSGESERGSGSQSS CCCCCCCCCCCCCCC	54.58	115917245
1081	Phosphorylation	SGESERGSGSQSSVP CCCCCCCCCCCCCCC	41.30	22167270
1083	Phosphorylation	ESERGSGSQSSVPSV CCCCCCCCCCCCCCH	28.69	22167270
1085	Phosphorylation	ERGSGSQSSVPSVDQ CCCCCCCCCCCCHHH	34.69	22167270
1086	Phosphorylation	RGSGSQSSVPSVDQF CCCCCCCCCCCHHHC	30.34	22167270
1089	Phosphorylation	GSQSSVPSVDQFTGV CCCCCCCCHHHCCCE	35.85	23927012
1094	Phosphorylation	VPSVDQFTGVGIRVS CCCHHHCCCEEEEEE	25.89	20873877
1105	2-Hydroxyisobutyrylation	IRVSFTGKQGEMREM EEEEEECCCCCCHHH	52.66	-
1105	Acetylation	IRVSFTGKQGEMREM EEEEEECCCCCCHHH	52.66	25953088
1105	Ubiquitination	IRVSFTGKQGEMREM EEEEEECCCCCCHHH	52.66	21906983
1116	Phosphorylation	MREMQQLSGGQKSLV CHHHHHHCCHHHHHH	36.22	20068231
1185	Ubiquitination	ELLESADKFYGVKFR HHHHHCCHHCCCCCC	39.95	22817900
1190	Acetylation	ADKFYGVKFRNKVSH CCHHCCCCCCCCCCE	33.95	19608861
1190	Ubiquitination	ADKFYGVKFRNKVSH CCHHCCCCCCCCCCE	33.95	22817900
1194	Ubiquitination	YGVKFRNKVSHIDVI CCCCCCCCCCEEEEE	40.64	22817900
1207	Ubiquitination	VITAEMAKDFVEDDT EEEHHHHHHHHHCCC	50.84	29967540

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
1067	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
1067	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
1083	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
105	K	Acetylation	18614053
Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion.
106	K	Acetylation	18614053
Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion.
1083	S	Phosphorylation	20068231
Phosphorylated at Ser-1083 in a SPO11-dependent manner.

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 SMC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC1A_HUMAN	SMC1A	physical	12759374
SYCP3_HUMAN	SYCP3	physical	12759374
REC8_HUMAN	REC8	physical	12759374
SMC1A_HUMAN	SMC1A	physical	9789013
NUMA1_HUMAN	NUMA1	physical	11590136
TBB5_HUMAN	TUBB	physical	11590136
MAD3_HUMAN	MXD3	physical	9528857
MAD4_HUMAN	MXD4	physical	9528857
MAD1_HUMAN	MXD1	physical	9528857
MXI1_HUMAN	MXI1	physical	9528857
KIFA3_HUMAN	KIFAP3	physical	9506951
WFDC5_HUMAN	WFDC5	physical	19906707
PDS5A_HUMAN	PDS5A	physical	19906707
RPGR_HUMAN	RPGR	physical	16043481
RAD21_HUMAN	RAD21	physical	17113138
SMC1A_HUMAN	SMC1A	physical	17113138
STAG1_HUMAN	STAG1	physical	17113138
STAG2_HUMAN	STAG2	physical	17113138
PDS5A_HUMAN	PDS5A	physical	17113138
PDS5B_HUMAN	PDS5B	physical	17113138
SMC1A_HUMAN	SMC1A	physical	17349791
RAD21_HUMAN	RAD21	physical	17349791
STAG1_HUMAN	STAG1	physical	17349791
STAG2_HUMAN	STAG2	physical	17349791
PDS5A_HUMAN	PDS5A	physical	17349791
PDS5B_HUMAN	PDS5B	physical	17349791
WAPL_HUMAN	WAPAL	physical	17349791
CDCA5_HUMAN	CDCA5	physical	17349791
RAD21_HUMAN	RAD21	physical	15855230
STAG1_HUMAN	STAG1	physical	15855230
STAG2_HUMAN	STAG2	physical	15855230
PDS5A_HUMAN	PDS5A	physical	15855230
PDS5B_HUMAN	PDS5B	physical	15855230
SMC1A_HUMAN	SMC1A	physical	10931856
RAD21_HUMAN	RAD21	physical	10931856
STAG1_HUMAN	STAG1	physical	10931856
STAG2_HUMAN	STAG2	physical	10931856
CTCF_HUMAN	CTCF	physical	21880767
SMC1A_HUMAN	SMC1A	physical	21880767
RAD21_HUMAN	RAD21	physical	21880767
SPT5H_HUMAN	SUPT5H	physical	21880767
RAD21_HUMAN	RAD21	physical	16802858
CDCA5_HUMAN	CDCA5	physical	21111234
RAD21_HUMAN	RAD21	physical	21111234
PDS5A_HUMAN	PDS5A	physical	21111234
WAPL_HUMAN	WAPAL	physical	21111234
COPG1_HUMAN	COPG1	physical	26344197
IMB1_HUMAN	KPNB1	physical	26344197
MARE2_HUMAN	MAPRE2	physical	26344197
MSH6_HUMAN	MSH6	physical	26344197
PDS5A_HUMAN	PDS5A	physical	26344197
RAD21_HUMAN	RAD21	physical	26344197
SMCA2_HUMAN	SMARCA2	physical	26344197
SMCA4_HUMAN	SMARCA4	physical	26344197
STAG1_HUMAN	STAG1	physical	26344197
WAPL_HUMAN	WAPAL	physical	17113138
SMC1B_HUMAN	SMC1B	physical	12759374
CLCB_HUMAN	CLTB	physical	26496610
RAD21_HUMAN	RAD21	physical	26496610
RL37A_HUMAN	RPL37A	physical	26496610
SMC1A_HUMAN	SMC1A	physical	26496610
IQGA1_HUMAN	IQGAP1	physical	26496610
HERC2_HUMAN	HERC2	physical	26496610
UBP13_HUMAN	USP13	physical	26496610
CE170_HUMAN	CEP170	physical	26496610
STAG1_HUMAN	STAG1	physical	26496610
SMC2_HUMAN	SMC2	physical	26496610
STAG2_HUMAN	STAG2	physical	26496610
FND3A_HUMAN	FNDC3A	physical	26496610
PDS5B_HUMAN	PDS5B	physical	26496610
WAPL_HUMAN	WAPAL	physical	26496610
ARHGC_HUMAN	ARHGEF12	physical	26496610
GNL3L_HUMAN	GNL3L	physical	26496610
TM165_HUMAN	TMEM165	physical	26496610
NEUL4_HUMAN	NEURL4	physical	26496610
CDCA5_HUMAN	CDCA5	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
NS1BP_HUMAN	IVNS1ABP	physical	27173435
SMC1A_HUMAN	SMC1A	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610759	Cornelia de Lange syndrome 3 (CDLS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SMC3_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-105; LYS-106; LYS-140;LYS-215; LYS-336 AND LYS-1190, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Acetylation of Smc3 by Eco1 is required for S phase sister chromatidcohesion in both human and yeast."; Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X.,Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.; Mol. Cell 31:143-151(2008). Cited for: ACETYLATION AT LYS-105 AND LYS-106, AND MUTAGENESIS OF LYS-105 ANDLYS-106.	18614053 [Abstract]
Phosphorylation
Reference	PubMed
"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-1065 AND SER-1067, ANDMASS 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 SER-1081, AND MASSSPECTROMETRY.	18691976 [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-1067, AND MASSSPECTROMETRY.	19367720 [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 SER-787; SER-1065; SER-1067AND SER-1083, AND MASS SPECTROMETRY.	17525332 [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-1065; SER-1067; SER-1074AND SER-1083, AND MASS SPECTROMETRY.	15302935 [Abstract]

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