dbPTM

SMC1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMC1A_HUMAN
UniProt AC	Q14683
Protein Name	Structural maintenance of chromosomes protein 1A
Gene Name	SMC1A
Organism	Homo sapiens (Human).
Sequence Length	1233
Subcellular Localization	Nucleus . Chromosome . Chromosome, centromere, kinetochore . 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
Protein Description	Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms 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. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint..
Protein Sequence	MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MGFLKLIEIENF ---CCCEEEEEEECC	45.19	21890473
13	Acetylation	LIEIENFKSYKGRQI EEEEECCCCCCCCEE	65.54	26051181
13	Ubiquitination	LIEIENFKSYKGRQI EEEEECCCCCCCCEE	65.54	21906983
16	Ubiquitination	IENFKSYKGRQIIGP EECCCCCCCCEEECC	55.50	-
28	Phosphorylation	IGPFQRFTAIIGPNG ECCCCCEEEEECCCC	21.09	20068231
36	Phosphorylation	AIIGPNGSGKSNLMD EEECCCCCCHHCHHH	50.08	21406692
39	Phosphorylation	GPNGSGKSNLMDAIS CCCCCCHHCHHHHHH	38.43	28122231
52	Ubiquitination	ISFVLGEKTSNLRVK HHHHHCCCCCCCCCC	56.29	21890473
72	Acetylation	IHGAPVGKPAANRAF HCCCCCCCHHHHHHE	31.55	25953088
72	Ubiquitination	IHGAPVGKPAANRAF HCCCCCCCHHHHHHE	31.55	-
85	Phosphorylation	AFVSMVYSEEGAEDR HEEEEECCCCCCCCC	20.12	-
92	Methylation	SEEGAEDRTFARVIV CCCCCCCCEEEEEEC	24.21	5172423
102	Phosphorylation	ARVIVGGSSEYKINN EEEECCCCCCEEECC	17.67	25693802
103	Phosphorylation	RVIVGGSSEYKINNK EEECCCCCCEEECCE	48.50	25693802
105	Nitration	IVGGSSEYKINNKVV ECCCCCCEEECCEEE	21.08	-
105	Phosphorylation	IVGGSSEYKINNKVV ECCCCCCEEECCEEE	21.08	25693802
106	Acetylation	VGGSSEYKINNKVVQ CCCCCCEEECCEEEE	34.60	25953088
106	Ubiquitination	VGGSSEYKINNKVVQ CCCCCCEEECCEEEE	34.60	21890473
110	Ubiquitination	SEYKINNKVVQLHEY CCEEECCEEEEHHHH	39.02	21906983
117	Phosphorylation	KVVQLHEYSEELEKL EEEEHHHHHHHHHHH	15.61	-
123	Ubiquitination	EYSEELEKLGILIKA HHHHHHHHHCHHHHH	65.72	-
129	Acetylation	EKLGILIKARNFLVF HHHCHHHHHCCEEHH	37.54	25953088
129	Ubiquitination	EKLGILIKARNFLVF HHHCHHHHHCCEEHH	37.54	-
149	Methylation	SIAMKNPKERTALFE HHHCCCHHHHHHHHH	70.04	-
149	Ubiquitination	SIAMKNPKERTALFE HHHCCCHHHHHHHHH	70.04	-
152	Phosphorylation	MKNPKERTALFEEIS CCCHHHHHHHHHHHH	28.89	-
160	Methylation	ALFEEISRSGELAQE HHHHHHHHHCHHHHH	55.10	5172427
161	Phosphorylation	LFEEISRSGELAQEY HHHHHHHHCHHHHHH	29.81	-
168	Phosphorylation	SGELAQEYDKRKKEM HCHHHHHHHHHHHHH	18.06	22817900
170	Acetylation	ELAQEYDKRKKEMVK HHHHHHHHHHHHHHH	66.28	26051181
170	Ubiquitination	ELAQEYDKRKKEMVK HHHHHHHHHHHHHHH	66.28	21906983
177	Ubiquitination	KRKKEMVKAEEDTQF HHHHHHHHHHHHHCC	49.09	21906983
182	Phosphorylation	MVKAEEDTQFNYHRK HHHHHHHHCCCHHHH	38.04	24719451
186	Phosphorylation	EEDTQFNYHRKKNIA HHHHCCCHHHHHCHH	12.32	24719451
189	Ubiquitination	TQFNYHRKKNIAAER HCCCHHHHHCHHHHH	36.54	-
190	Ubiquitination	QFNYHRKKNIAAERK CCCHHHHHCHHHHHH	54.25	-
213	Ubiquitination	ADRYQRLKDEVVRAQ HHHHHHHHHHHHHHH	54.77	-
237	Acetylation	HNEVEIEKLNKELAS CCHHHHHHHHHHHHH	64.12	26051181
237	Ubiquitination	HNEVEIEKLNKELAS CCHHHHHHHHHHHHH	64.12	-
240	Ubiquitination	VEIEKLNKELASKNK HHHHHHHHHHHHCCC	65.62	-
258	Acetylation	KDKKRMDKVEDELKE HHHHHHHHHHHHHHH	37.87	26051181
264	Acetylation	DKVEDELKEKKKELG HHHHHHHHHHHHHHH	66.49	26051181
272	Acetylation	EKKKELGKMMREQQQ HHHHHHHHHHHHHHH	41.99	25953088
282	Acetylation	REQQQIEKEIKEKDS HHHHHHHHHHHHHHH	67.38	23749302
289	Phosphorylation	KEIKEKDSELNQKRP HHHHHHHHHHHHHCC	55.86	22673903
294	Ubiquitination	KDSELNQKRPQYIKA HHHHHHHHCCHHHHH	66.04	-
300	Ubiquitination	QKRPQYIKAKENTSH HHCCHHHHHHCCCHH	48.77	-
318	Phosphorylation	KLEAAKKSLQNAQKH HHHHHHHHHHHHHHH	34.18	24719451
324	Acetylation	KSLQNAQKHYKKRKG HHHHHHHHHHHHHCC	46.63	25953088
326	Phosphorylation	LQNAQKHYKKRKGDM HHHHHHHHHHHCCCH	25.82	24719451
358	Phosphorylation	EERMEEESQSQGRDL HHHHHHHHHHCCCCC	38.11	23401153
360	Phosphorylation	RMEEESQSQGRDLTL HHHHHHHHCCCCCCC	43.83	29255136
366	Phosphorylation	QSQGRDLTLEENQVK HHCCCCCCCCHHHHH	36.09	22167270
373	Acetylation	TLEENQVKKYHRLKE CCCHHHHHHHHHHHH	37.54	25953088
373	Ubiquitination	TLEENQVKKYHRLKE CCCHHHHHHHHHHHH	37.54	-
383	Phosphorylation	HRLKEEASKRAATLA HHHHHHHHHHHHHHH	26.42	21955146
395	Acetylation	TLAQELEKFNRDQKA HHHHHHHHHCHHHHH	61.64	26051181
395	Ubiquitination	TLAQELEKFNRDQKA HHHHHHHHHCHHHHH	61.64	-
401	Ubiquitination	EKFNRDQKADQDRLD HHHCHHHHHHHCCCC	59.21	-
406	Methylation	DQKADQDRLDLEERK HHHHHHCCCCHHHHH	25.19	115917233
433	Acetylation	REIEENQKRIEKLEE HHHHHHHHHHHHHHH	67.91	25953088
433	Ubiquitination	REIEENQKRIEKLEE HHHHHHHHHHHHHHH	67.91	-
437	Acetylation	ENQKRIEKLEEYITT HHHHHHHHHHHHHHH	59.85	23749302
437	Ubiquitination	ENQKRIEKLEEYITT HHHHHHHHHHHHHHH	59.85	19608861
441	Phosphorylation	RIEKLEEYITTSKQS HHHHHHHHHHHCHHH	8.32	-
446	Ubiquitination	EEYITTSKQSLEEQK HHHHHHCHHHHHHHH	41.64	-
448	Phosphorylation	YITTSKQSLEEQKKL HHHHCHHHHHHHHHH	41.29	26437602
454	"N6,N6-dimethyllysine"	QSLEEQKKLEGELTE HHHHHHHHHCCHHHH	52.01	-
454	Methylation	QSLEEQKKLEGELTE HHHHHHHHHCCHHHH	52.01	-
460	Phosphorylation	KKLEGELTEEVEMAK HHHCCHHHHHHHHHH	26.29	29083192
465	Sulfoxidation	ELTEEVEMAKRRIDE HHHHHHHHHHHHHHH	6.86	21406390
467	Ubiquitination	TEEVEMAKRRIDEIN HHHHHHHHHHHHHHH	40.68	-
475	Ubiquitination	RRIDEINKELNQVME HHHHHHHHHHHHHHH	70.05	-
500	Ubiquitination	ESSRQQRKAEIMESI HHHHHHHHHHHHHHH	46.14	-
506	Phosphorylation	RKAEIMESIKRLYPG HHHHHHHHHHHHCCC	18.94	23909892
508	Ubiquitination	AEIMESIKRLYPGSV HHHHHHHHHHCCCCH	45.70	21890473
511	Phosphorylation	MESIKRLYPGSVYGR HHHHHHHCCCCHHHH	15.02	20068231
514	Phosphorylation	IKRLYPGSVYGRLID HHHHCCCCHHHHHHH	13.99	20068231
516	Phosphorylation	RLYPGSVYGRLIDLC HHCCCCHHHHHHHHC	9.75	20068231
523	Glutathionylation	YGRLIDLCQPTQKKY HHHHHHHCCCCCCCH	3.95	22555962
528	Acetylation	DLCQPTQKKYQIAVT HHCCCCCCCHHHHHH	56.79	25953088
528	Ubiquitination	DLCQPTQKKYQIAVT HHCCCCCCCHHHHHH	56.79	-
529	Ubiquitination	LCQPTQKKYQIAVTK HCCCCCCCHHHHHHH	32.35	-
530	Phosphorylation	CQPTQKKYQIAVTKV CCCCCCCHHHHHHHH	16.52	21403953
536	Acetylation	KYQIAVTKVLGKNMD CHHHHHHHHHCCCCC	28.94	19608861
536	Ubiquitination	KYQIAVTKVLGKNMD CHHHHHHHHHCCCCC	28.94	21890473
540	Acetylation	AVTKVLGKNMDAIIV HHHHHHCCCCCEEEE	44.96	23954790
540	Malonylation	AVTKVLGKNMDAIIV HHHHHHCCCCCEEEE	44.96	26320211
540	Ubiquitination	AVTKVLGKNMDAIIV HHHHHHCCCCCEEEE	44.96	21890473
542	Sulfoxidation	TKVLGKNMDAIIVDS HHHHCCCCCEEEECC	4.14	21406390
551	Acetylation	AIIVDSEKTGRDCIQ EEEECCHHHHHHHHH	61.30	26051181
561	Acetylation	RDCIQYIKEQRGEPE HHHHHHHHHHCCCCC	42.75	26051181
561	Ubiquitination	RDCIQYIKEQRGEPE HHHHHHHHHHCCCCC	42.75	-
575	Nitration	ETFLPLDYLEVKPTD CCCCCCCCEEECCCH	16.67	-
575	Phosphorylation	ETFLPLDYLEVKPTD CCCCCCCCEEECCCH	16.67	-
579	Acetylation	PLDYLEVKPTDEKLR CCCCEEECCCHHHHH	32.59	23954790
579	Ubiquitination	PLDYLEVKPTDEKLR CCCCEEECCCHHHHH	32.59	21906983
584	Ubiquitination	EVKPTDEKLRELKGA EECCCHHHHHHHCCC	56.50	-
592	Acetylation	LRELKGAKLVIDVIR HHHHCCCEEEEEEHH	52.54	25953088
600	Phosphorylation	LVIDVIRYEPPHIKK EEEEEHHCCCHHHHH	22.97	22067460
606	Ubiquitination	RYEPPHIKKALQYAC HCCCHHHHHHHHHHH	29.03	21890473
607	Ubiquitination	YEPPHIKKALQYACG CCCHHHHHHHHHHHC	54.44	-
611	Phosphorylation	HIKKALQYACGNALV HHHHHHHHHHCCEEE	12.52	28152594
637	Acetylation	FGGHQRHKTVALDGT CCCCCCCCEEEECCC	47.05	27452117
637	Malonylation	FGGHQRHKTVALDGT CCCCCCCCEEEECCC	47.05	26320211
637	Ubiquitination	FGGHQRHKTVALDGT CCCCCCCCEEEECCC	47.05	21890473
638	Phosphorylation	GGHQRHKTVALDGTL CCCCCCCEEEECCCE	12.60	20068231
644	Phosphorylation	KTVALDGTLFQKSGV CEEEECCCEEECCCC	24.86	-
648	Acetylation	LDGTLFQKSGVISGG ECCCEEECCCCCCCC	41.67	19608861
648	Ubiquitination	LDGTLFQKSGVISGG ECCCEEECCCCCCCC	41.67	21890473
649	Phosphorylation	DGTLFQKSGVISGGA CCCEEECCCCCCCCH	27.75	21406692
653	Phosphorylation	FQKSGVISGGASDLK EECCCCCCCCHHHHH	28.86	21406692
657	Phosphorylation	GVISGGASDLKAKAR CCCCCCHHHHHHHHH	46.91	21406692
660	Acetylation	SGGASDLKAKARRWD CCCHHHHHHHHHHHC	53.48	25953088
660	Ubiquitination	SGGASDLKAKARRWD CCCHHHHHHHHHHHC	53.48	21906983
669	Acetylation	KARRWDEKAVDKLKE HHHHHCHHHHHHHHH	51.76	25953088
669	Ubiquitination	KARRWDEKAVDKLKE HHHHHCHHHHHHHHH	51.76	-
686	Acetylation	ERLTEELKEQMKAKR HHHHHHHHHHHHHHH	49.53	26051181
686	Ubiquitination	ERLTEELKEQMKAKR HHHHHHHHHHHHHHH	49.53	-
689	Sulfoxidation	TEELKEQMKAKRKEA HHHHHHHHHHHHHHH	4.83	21406390
692	Ubiquitination	LKEQMKAKRKEAELR HHHHHHHHHHHHHHH	59.49	-
699	Methylation	KRKEAELRQVQSQAH HHHHHHHHHHHHHHH	26.57	115917237
703	Phosphorylation	AELRQVQSQAHGLQM HHHHHHHHHHHHHHH	30.40	-
713	Acetylation	HGLQMRLKYSQSDLE HHHHHHHHCCHHHHH	32.27	19608861
713	Malonylation	HGLQMRLKYSQSDLE HHHHHHHHCCHHHHH	32.27	26320211
713	Methylation	HGLQMRLKYSQSDLE HHHHHHHHCCHHHHH	32.27	22634487
713	Ubiquitination	HGLQMRLKYSQSDLE HHHHHHHHCCHHHHH	32.27	19608861
714	Phosphorylation	GLQMRLKYSQSDLEQ HHHHHHHCCHHHHHH	19.28	28152594
715	Phosphorylation	LQMRLKYSQSDLEQT HHHHHHCCHHHHHHH	22.94	28152594
717	Phosphorylation	MRLKYSQSDLEQTKT HHHHCCHHHHHHHHH	37.92	28152594
722	O-linked_Glycosylation	SQSDLEQTKTRHLAL CHHHHHHHHHHHHHH	25.63	23301498
722	Phosphorylation	SQSDLEQTKTRHLAL CHHHHHHHHHHHHHH	25.63	20068231
723	Acetylation	QSDLEQTKTRHLALN HHHHHHHHHHHHHHH	43.16	26051181
723	Ubiquitination	QSDLEQTKTRHLALN HHHHHHHHHHHHHHH	43.16	-
734	Ubiquitination	LALNLQEKSKLESEL HHHHHHHHHHHHHHH	39.67	-
735	Phosphorylation	ALNLQEKSKLESELA HHHHHHHHHHHHHHH	41.54	24719451
736	Acetylation	LNLQEKSKLESELAN HHHHHHHHHHHHHHH	68.30	25953088
736	Ubiquitination	LNLQEKSKLESELAN HHHHHHHHHHHHHHH	68.30	21890473
781	Glutathionylation	DEVFEEFCREIGVRN HHHHHHHHHHHCCCC	4.28	22555962
796	Acetylation	IREFEEEKVKRQNEI HHHHHHHHHHHHHHH	57.23	25953088
805	Ubiquitination	KRQNEIAKKRLEFEN HHHHHHHHHHHHHHC	44.05	-
806	Ubiquitination	RQNEIAKKRLEFENQ HHHHHHHHHHHHHCH	53.87	-
814	Ubiquitination	RLEFENQKTRLGIQL HHHHHCHHHEEEEEE	47.39	-
834	Acetylation	QLKEDQDKVHMWEQT CCHHHHHHHHHHHHH	28.54	26051181
841	Phosphorylation	KVHMWEQTVKKDENE HHHHHHHHHCCCHHH	23.83	18452278
861	Acetylation	KEEQRHMKIIDETMA HHHHHHHHHHHHHHH	30.31	25953088
867	Sulfoxidation	MKIIDETMAQLQDLK HHHHHHHHHHHHHHH	1.79	21406390
874	Acetylation	MAQLQDLKNQHLAKK HHHHHHHHHHHHHHH	63.95	26051181
874	Ubiquitination	MAQLQDLKNQHLAKK HHHHHHHHHHHHHHH	63.95	-
881	Ubiquitination	KNQHLAKKSEVNDKN HHHHHHHHHHHCCCC	46.36	-
887	Acetylation	KKSEVNDKNHEMEEI HHHHHCCCCHHHHHH	55.81	26051181
897	Acetylation	EMEEIRKKLGGANKE HHHHHHHHHCCCCHH	42.38	21339330
903	Acetylation	KKLGGANKEMTHLQK HHHCCCCHHHHHHHH	48.61	26051181
903	Ubiquitination	KKLGGANKEMTHLQK HHHCCCCHHHHHHHH	48.61	-
910	Acetylation	KEMTHLQKEVTAIET HHHHHHHHHHHHHHH	61.59	23749302
918	Acetylation	EVTAIETKLEQKRSD HHHHHHHHHHHHHCH	36.92	26051181
918	Ubiquitination	EVTAIETKLEQKRSD HHHHHHHHHHHHHCH	36.92	-
934	Ubiquitination	HNLLQACKMQDIKLP HHHHHHHHHCCCCCC	42.48	-
939	Ubiquitination	ACKMQDIKLPLSKGT HHHHCCCCCCCCCCC	52.95	-
944	Ubiquitination	DIKLPLSKGTMDDIS CCCCCCCCCCHHHCH	67.11	21906983
946	Phosphorylation	KLPLSKGTMDDISQE CCCCCCCCHHHCHHH	22.59	30278072
947	Sulfoxidation	LPLSKGTMDDISQEE CCCCCCCHHHCHHHC	6.25	28183972
951	Phosphorylation	KGTMDDISQEEGSSQ CCCHHHCHHHCCCCC	38.24	23401153
956	Phosphorylation	DISQEEGSSQGEDSV HCHHHCCCCCCCCCC	23.83	22167270
957	Phosphorylation	ISQEEGSSQGEDSVS CHHHCCCCCCCCCCC	53.73	22167270
962	Phosphorylation	GSSQGEDSVSGSQRI CCCCCCCCCCHHHHH	17.55	22167270
964	Phosphorylation	SQGEDSVSGSQRISS CCCCCCCCHHHHHHH	36.36	25159151
966	Phosphorylation	GEDSVSGSQRISSIY CCCCCCHHHHHHHHH	14.58	25159151
970	Phosphorylation	VSGSQRISSIYAREA CCHHHHHHHHHHHHH	16.93	30266825
971	Phosphorylation	SGSQRISSIYAREAL CHHHHHHHHHHHHHH	19.76	30266825
973	Phosphorylation	SQRISSIYAREALIE HHHHHHHHHHHHHEE	11.10	30266825
1000	Ubiquitination	AQAEEEIKQEMNTLQ HHHHHHHHHHHHHHH	43.41	-
1009	Ubiquitination	EMNTLQQKLNEQQSV HHHHHHHHHHHHHHH	40.08	-
1015	Phosphorylation	QKLNEQQSVLQRIAA HHHHHHHHHHHHHHC	25.21	20068231
1026	Acetylation	RIAAPNMKAMEKLES HHHCCCHHHHHHHHH	51.74	25953088
1026	Ubiquitination	RIAAPNMKAMEKLES HHHCCCHHHHHHHHH	51.74	-
1030	Ubiquitination	PNMKAMEKLESVRDK CCHHHHHHHHHHHHH	44.46	21906983
1033	Phosphorylation	KAMEKLESVRDKFQE HHHHHHHHHHHHHHH	32.65	22067460
1037	Acetylation	KLESVRDKFQETSDE HHHHHHHHHHHCHHH	38.08	25953088
1037	Ubiquitination	KLESVRDKFQETSDE HHHHHHHHHHHCHHH	38.08	21906983
1041	Phosphorylation	VRDKFQETSDEFEAA HHHHHHHCHHHHHHH	30.60	28555341
1050	Ubiquitination	DEFEAARKRAKKAKQ HHHHHHHHHHHHHHH	52.56	-
1056	Ubiquitination	RKRAKKAKQAFEQIK HHHHHHHHHHHHHHH	51.55	-
1063	Ubiquitination	KQAFEQIKKERFDRF HHHHHHHHHHHHHHH	48.56	-
1115	Glutathionylation	LDGINYNCVAPGKRF CCCCCCCCCCCCCCC	1.63	22555962
1120	Acetylation	YNCVAPGKRFRPMDN CCCCCCCCCCCCCCC	47.51	25953088
1120	Ubiquitination	YNCVAPGKRFRPMDN CCCCCCCCCCCCCCC	47.51	-
1129	Phosphorylation	FRPMDNLSGGEKTVA CCCCCCCCCHHHHHH	51.51	-
1133	Methylation	DNLSGGEKTVAALAL CCCCCHHHHHHHHHH	52.12	-
1188	Phosphorylation	NFQAIVISLKEEFYT CEEEEEEEEHHHHHH	23.61	24719451
1196	Ubiquitination	LKEEFYTKAESLIGV EHHHHHHHHHHHCCC	38.48	21890473
1214	Ubiquitination	QGDCVISKVLTFDLT CCCEEEEEEEEEECC	30.09	-
1217	Phosphorylation	CVISKVLTFDLTKYP EEEEEEEEEECCCCC	20.35	-
1221	Phosphorylation	KVLTFDLTKYPDANP EEEEEECCCCCCCCC	30.31	-
1222	Acetylation	VLTFDLTKYPDANPN EEEEECCCCCCCCCC	63.18	26051181
1222	Ubiquitination	VLTFDLTKYPDANPN EEEEECCCCCCCCCC	63.18	21890473

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
957	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
957	S	Phosphorylation	Kinase	ATR	Q13535	PSP
966	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
966	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
957	S	Phosphorylation	11877377
Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation.
966	S	Phosphorylation	11877377
Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation.

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 SMC1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC3_HUMAN	SMC3	physical	11877376
SYCP3_HUMAN	SYCP3	physical	12759374
SMC3_HUMAN	SMC3	physical	12759374
SMC3_HUMAN	SMC3	physical	11590136
RAD21_HUMAN	RAD21	physical	11590136
NUMA1_HUMAN	NUMA1	physical	11590136
SMC1A_HUMAN	SMC1A	physical	18832153
RAE1L_HUMAN	RAE1	physical	18832153
AIRE_HUMAN	AIRE	physical	20085707
RPGR_HUMAN	RPGR	physical	16043481
ATR_HUMAN	ATR	physical	15640246
CTCF_HUMAN	CTCF	physical	18219272
KDM1B_HUMAN	KDM1B	physical	20670891
EHMT2_HUMAN	EHMT2	physical	20670891
WFDC5_HUMAN	WFDC5	physical	17112726
STAG2_HUMAN	STAG2	physical	17112726
RAD21_HUMAN	RAD21	physical	17112726
PDS5B_HUMAN	PDS5B	physical	17112726
PDS5A_HUMAN	PDS5A	physical	17112726
BRCA1_HUMAN	BRCA1	physical	11877377
SMC3_HUMAN	SMC3	physical	22939629
SMC2_HUMAN	SMC2	physical	22939629
MCM7_HUMAN	MCM7	physical	16438930
SMC1A_HUMAN	SMC1A	physical	16438930
RFC1_HUMAN	RFC1	physical	16438930
DPOLA_HUMAN	POLA1	physical	16438930
ARMX3_HUMAN	ARMCX3	physical	22863883
KI13A_HUMAN	KIF13A	physical	22863883
NDC80_HUMAN	NDC80	physical	26344197
PDS5A_HUMAN	PDS5A	physical	26344197
PDS5B_HUMAN	PDS5B	physical	26344197
PLK1_HUMAN	PLK1	physical	26344197
DPOE1_HUMAN	POLE	physical	26344197
RAD21_HUMAN	RAD21	physical	26344197
SMC2_HUMAN	SMC2	physical	26344197
SMC3_HUMAN	SMC3	physical	26344197
BPTF_HUMAN	BPTF	physical	26496610
GANC_HUMAN	GANC	physical	26496610
PEX1_HUMAN	PEX1	physical	26496610
RAD21_HUMAN	RAD21	physical	26496610
HLTF_HUMAN	HLTF	physical	26496610
ARK72_HUMAN	AKR7A2	physical	26496610
SAP30_HUMAN	SAP30	physical	26496610
UBP13_HUMAN	USP13	physical	26496610
SMC3_HUMAN	SMC3	physical	26496610
STAG1_HUMAN	STAG1	physical	26496610
STAG2_HUMAN	STAG2	physical	26496610
PDS5B_HUMAN	PDS5B	physical	26496610
WAPL_HUMAN	WAPAL	physical	26496610
PDS5A_HUMAN	PDS5A	physical	26496610
KCTD2_HUMAN	KCTD2	physical	26496610
OSBL3_HUMAN	OSBPL3	physical	26496610
PRP19_HUMAN	PRPF19	physical	26496610
P33MX_HUMAN	KIAA1191	physical	26496610
MTUS1_HUMAN	MTUS1	physical	26496610
HAUS3_HUMAN	HAUS3	physical	26496610
GCC1_HUMAN	GCC1	physical	26496610
NUF2_HUMAN	NUF2	physical	26496610
MGME1_HUMAN	MGME1	physical	26496610
CDCA5_HUMAN	CDCA5	physical	26496610
LS14B_HUMAN	LSM14B	physical	26496610
DDI1_HUMAN	DDI1	physical	26496610
BRD4_HUMAN	BRD4	physical	24945803
HSF1_HUMAN	HSF1	physical	27173435

Drug and Disease Associations

Kegg Disease
OMIM Disease
300590	Cornelia de Lange syndrome 2 (CDLS2)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SMC1A_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-282; LYS-437; LYS-536;LYS-648 AND LYS-713, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND MASSSPECTROMETRY.	19690332 [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-360; SER-957 ANDSER-970, AND MASS SPECTROMETRY.	18669648 [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-358; SER-360; SER-951;SER-957 AND SER-966, 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-360; SER-957 ANDSER-962, AND MASS SPECTROMETRY.	15302935 [Abstract]
"MSH2 and ATR form a signaling module and regulate two branches of thedamage response to DNA methylation."; Wang Y., Qin J.; Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003). Cited for: PHOSPHORYLATION AT SER-966, AND MUTAGENESIS OF SER-966.	14657349 [Abstract]
"SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint."; Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.; Genes Dev. 16:571-582(2002). Cited for: PROTEIN SEQUENCE OF 945-984, FUNCTION, INTERACTION WITH BRCA1,PHOSPHORYLATION AT SER-957 AND SER-966, AND MUTAGENESIS OF SER-957 ANDSER-966.	11877377 [Abstract]

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