dbPTM

STAG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STAG1_HUMAN
UniProt AC	Q8WVM7
Protein Name	Cohesin subunit SA-1
Gene Name	STAG1
Organism	Homo sapiens (Human).
Sequence Length	1258
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 PLK1, except at
Protein Description	Component of cohesin complex, a complex 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..
Protein Sequence	MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGEGEPVTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRNSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEAMSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLPMLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEACSKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLKRLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGSPSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQPLVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLIIYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQIDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNQKGQEYPPPNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTEQMMERREDVWLPLISYRNSLVTGGEDDRMSVNSGSSSSKTSSVRNKKGRPPLHKKRVEDESLDNTWLNRTDTMIQTPGPLPAPQLTSTVLRENSRPMGDQIQEPESEHGSEPDFLHNPQMQISWLGQPKLEDLNRKDRTGMNYMKVRTGVRHAVRGLMEEDAEPIFEDVMMSSRSQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MITSELPVLQ -----CCCCCCCCEE	28.18	30108239
4	Phosphorylation	----MITSELPVLQD ----CCCCCCCCEEC	42.69	30108239
12	Phosphorylation	ELPVLQDSTNETTAH CCCCEECCCCCCCCC	21.85	25159151
13	Phosphorylation	LPVLQDSTNETTAHS CCCEECCCCCCCCCC	45.42	25159151
16	Phosphorylation	LQDSTNETTAHSDAG EECCCCCCCCCCCCC	31.21	25159151
17	Phosphorylation	QDSTNETTAHSDAGS ECCCCCCCCCCCCCC	19.05	25159151
20	Phosphorylation	TNETTAHSDAGSELE CCCCCCCCCCCCCCC	27.05	25159151
24	Phosphorylation	TAHSDAGSELEETEV CCCCCCCCCCCCCCC	40.50	25159151
29	Phosphorylation	AGSELEETEVKGKRK CCCCCCCCCCCCCCC	36.38	24043423
45	Phosphorylation	GRPGRPPSTNKKPRK CCCCCCCCCCCCCCC	47.50	28348404
46	Phosphorylation	RPGRPPSTNKKPRKS CCCCCCCCCCCCCCC	57.75	22067460
57	Acetylation	PRKSPGEKSRIEAGI CCCCCCCHHHHHHHC	51.45	26051181
65	Methylation	SRIEAGIRGAGRGRA HHHHHHCCCCCCCCC	28.17	115917909
152	Phosphorylation	AEIIRKMTEEFDEDS HHHHHHHHHCCCCCC	35.08	-
159	Phosphorylation	TEEFDEDSGDYPLTM HHCCCCCCCCCCCCC	31.36	-
162	Phosphorylation	FDEDSGDYPLTMPGP CCCCCCCCCCCCCCH	12.03	-
165	Phosphorylation	DSGDYPLTMPGPQWK CCCCCCCCCCCHHHH	19.47	-
172	Acetylation	TMPGPQWKKFRSNFC CCCCHHHHHHHHHHH	36.47	26051181
273	Ubiquitination	RLELLLQKRKELQEN HHHHHHHHHHHHHHC	66.46	21890473
273	Ubiquitination	RLELLLQKRKELQEN HHHHHHHHHHHHHHC	66.46	21890473
290	Phosphorylation	EIENMMNSIFKGIFV HHHHHHHHHHHHHHH	16.11	24719451
333	Methylation	FLNDSYLKYVGWTLH HCCHHHHHHHHEEEC	29.65	-
356	Phosphorylation	KCLKALQSLYTNREL HHHHHHHHHHHCCCH	24.97	21406692
358	Phosphorylation	LKALQSLYTNRELFP HHHHHHHHHCCCHHH	13.76	21406692
359	Phosphorylation	KALQSLYTNRELFPK HHHHHHHHCCCHHHH	32.85	21406692
366	Ubiquitination	TNRELFPKLELFTNR HCCCHHHHHHHHHHH	47.46	21890473
366	Ubiquitination	TNRELFPKLELFTNR HCCCHHHHHHHHHHH	47.46	21890473
380	Phosphorylation	RFKDRIVSMTLDKEY HHHHHHHHCCCCCCH	12.04	30576142
382	Phosphorylation	KDRIVSMTLDKEYDV HHHHHHCCCCCCHHH	25.05	30576142
453	Acetylation	QAEEALAKRRGRNSP HHHHHHHHHCCCCCC	43.40	25953088
453	Ubiquitination	QAEEALAKRRGRNSP HHHHHHHHHCCCCCC	43.40	-
523	Phosphorylation	AMSDRQESALIELMV HCCHHHHHHHHHHHH	21.75	30631047
568	Phosphorylation	IDDRNKLTEHFIITL CCCCCHHHHHHHHHH	29.08	25159151
574	Phosphorylation	LTEHFIITLPMLLSK HHHHHHHHHHHHHHH	21.72	20068231
580	Phosphorylation	ITLPMLLSKYSADAE HHHHHHHHHCCCCHH	26.11	20068231
618	Methylation	KHLDALLKQIKFVVE HHHHHHHHHHHHHHH	51.32	-
621	Acetylation	DALLKQIKFVVEKHV HHHHHHHHHHHHHHC	29.61	22649355
626	Acetylation	QIKFVVEKHVESDVL HHHHHHHHHCCHHHH	41.14	26051181
639	Phosphorylation	VLEACSKTYSILCSE HHHHHHHHHHHHCCC	13.25	28851738
640	Phosphorylation	LEACSKTYSILCSEE HHHHHHHHHHHCCCC	9.46	28851738
641	Phosphorylation	EACSKTYSILCSEEY HHHHHHHHHHCCCCC	17.83	28851738
645	Phosphorylation	KTYSILCSEEYTIQN HHHHHHCCCCCCHHC	29.98	28851738
648	Phosphorylation	SILCSEEYTIQNRVD HHHCCCCCCHHCCHH	12.70	28851738
689	Phosphorylation	EADDDDIYNVLSTLK CCCHHHHHHHHHHHH	13.25	18452278
694	Phosphorylation	DIYNVLSTLKRLTSF HHHHHHHHHHHHHCC	31.94	18452278
700	O-linked_Glycosylation	STLKRLTSFHNAHDL HHHHHHHCCCCHHCC	29.15	30059200
753	Phosphorylation	LWQLVKITDGSPSKE HHHHHCCCCCCCCHH	28.70	23186163
756	Phosphorylation	LVKITDGSPSKEDLL HHCCCCCCCCHHHHH	28.89	29255136
758	Phosphorylation	KITDGSPSKEDLLVL CCCCCCCCHHHHHHH	50.83	29255136
759	Acetylation	ITDGSPSKEDLLVLR CCCCCCCHHHHHHHH	59.64	26051181
759	Ubiquitination	ITDGSPSKEDLLVLR CCCCCCCHHHHHHHH	59.64	-
781	Phosphorylation	AVCQQCLSNVNTPVK HHHHHHHHCCCCCHH	46.49	-
847	Phosphorylation	DQDEENQSMEGDEED CCCHHCCCCCCCHHH	30.31	26657352
864	Ubiquitination	NKIEALHKRRNLLAA HHHHHHHHHHHHHHH	54.63	-
893	Phosphorylation	AADIFKHYMKYYNDY HHHHHHHHHHHHCHH	8.90	22817900
896	Phosphorylation	IFKHYMKYYNDYGDI HHHHHHHHHCHHHHH	7.32	22817900
897	Phosphorylation	FKHYMKYYNDYGDII HHHHHHHHCHHHHHH	8.95	22817900
900	Phosphorylation	YMKYYNDYGDIIKET HHHHHCHHHHHHHHH	17.04	18083107
905	Ubiquitination	NDYGDIIKETLSKTR CHHHHHHHHHHHHCC	45.01	-
905	Acetylation	NDYGDIIKETLSKTR CHHHHHHHHHHHHCC	45.01	26051181
916	Ubiquitination	SKTRQIDKIQCAKTL HHCCCCCHHHHHHHH	35.98	-
962	Phosphorylation	LARRFALTFGLDQIK HHHHHHHHHCCHHHH	16.54	20068231
1021	Phosphorylation	LLRQDKKTVHSYLEK HHHCCHHHHHHHHHH	29.23	29449344
1024	Phosphorylation	QDKKTVHSYLEKFLT CCHHHHHHHHHHHHH	27.38	29449344
1025	Phosphorylation	DKKTVHSYLEKFLTE CHHHHHHHHHHHHHH	12.19	29449344
1031	Phosphorylation	SYLEKFLTEQMMERR HHHHHHHHHHHHHHC	27.57	24719451
1051	Phosphorylation	PLISYRNSLVTGGED HHHEECCCCCCCCCC	18.41	23927012
1054	Phosphorylation	SYRNSLVTGGEDDRM EECCCCCCCCCCCCC	44.77	29255136
1062	Phosphorylation	GGEDDRMSVNSGSSS CCCCCCCCCCCCCCC	21.02	23401153
1065	Phosphorylation	DDRMSVNSGSSSSKT CCCCCCCCCCCCCCC	37.59	23401153
1067	Phosphorylation	RMSVNSGSSSSKTSS CCCCCCCCCCCCCCC	27.20	29255136
1068	Phosphorylation	MSVNSGSSSSKTSSV CCCCCCCCCCCCCCC	42.00	23927012
1069	Phosphorylation	SVNSGSSSSKTSSVR CCCCCCCCCCCCCCC	37.24	23927012
1070	Phosphorylation	VNSGSSSSKTSSVRN CCCCCCCCCCCCCCC	41.73	23927012
1072	Phosphorylation	SGSSSSKTSSVRNKK CCCCCCCCCCCCCCC	28.34	20068231
1073	Phosphorylation	GSSSSKTSSVRNKKG CCCCCCCCCCCCCCC	30.49	20068231
1074	Phosphorylation	SSSSKTSSVRNKKGR CCCCCCCCCCCCCCC	30.26	20068231
1093	Phosphorylation	KKRVEDESLDNTWLN CCCCCCCCCCCCCCC	54.03	25159151
1097	Phosphorylation	EDESLDNTWLNRTDT CCCCCCCCCCCCCCC	30.88	23186163
1102	Phosphorylation	DNTWLNRTDTMIQTP CCCCCCCCCCCCCCC	34.45	27732954
1104	Phosphorylation	TWLNRTDTMIQTPGP CCCCCCCCCCCCCCC	18.63	27732954
1108	Phosphorylation	RTDTMIQTPGPLPAP CCCCCCCCCCCCCCC	21.20	27499020
1118	Phosphorylation	PLPAPQLTSTVLREN CCCCCCHHHHHHHHC	19.66	28122231
1119	Phosphorylation	LPAPQLTSTVLRENS CCCCCHHHHHHHHCC	25.72	22210691
1120	Phosphorylation	PAPQLTSTVLRENSR CCCCHHHHHHHHCCC	20.51	24719451
1126	Phosphorylation	STVLRENSRPMGDQI HHHHHHCCCCCCCCC	32.77	26657352
1138	Phosphorylation	DQIQEPESEHGSEPD CCCCCCCCCCCCCCC	45.68	22115753
1138 (in isoform 2)	Phosphorylation	-	45.68	23663014
1142 (in isoform 2)	Phosphorylation	-	48.11	23663014
1142	Phosphorylation	EPESEHGSEPDFLHN CCCCCCCCCCCCCCC	48.11	22115753
1155	Phosphorylation	HNPQMQISWLGQPKL CCCCCCEEECCCCCH	10.19	21406692
1161	Sumoylation	ISWLGQPKLEDLNRK EEECCCCCHHHCCCC	57.53	28112733
1171	Phosphorylation	DLNRKDRTGMNYMKV HCCCCCCCCCHHHHH	51.41	-
1204	Phosphorylation	IFEDVMMSSRSQLED HHHHHHHHCHHHHHH	12.42	27732954
1205	Phosphorylation	FEDVMMSSRSQLEDM HHHHHHHCHHHHHHC	20.32	27732954
1251	Phosphorylation	AAIIEDDSGFGMPMF CEEEECCCCCCCCCC	48.63	29802988

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
Oops, there are no upstream regulatory protein records of STAG1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STAG1_HUMAN !!

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 STAG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC1A_HUMAN	SMC1A	physical	11076961
SMC3_HUMAN	SMC3	physical	11076961
RAD21_HUMAN	RAD21	physical	11076961
RAD21_HUMAN	RAD21	physical	17113138
SMC1A_HUMAN	SMC1A	physical	17113138
SMC3_HUMAN	SMC3	physical	17113138
PDS5A_HUMAN	PDS5A	physical	17113138
PDS5B_HUMAN	PDS5B	physical	17113138
WFDC5_HUMAN	WFDC5	physical	17112726
RAD21_HUMAN	RAD21	physical	17112726
SMC1A_HUMAN	SMC1A	physical	17112726
SMC3_HUMAN	SMC3	physical	17112726
RAD21_HUMAN	RAD21	physical	17962804
SMC3_HUMAN	SMC3	physical	17962804
TERF1_HUMAN	TERF1	physical	17962804
TINF2_HUMAN	TINF2	physical	17962804
SMC1A_HUMAN	SMC1A	physical	10931856
SMC3_HUMAN	SMC3	physical	10931856
RAD21_HUMAN	RAD21	physical	10931856
EXOS9_HUMAN	EXOSC9	physical	26344197
RAD21_HUMAN	RAD21	physical	26344197
SMC1A_HUMAN	SMC1A	physical	26344197
SMC1B_HUMAN	SMC1B	physical	26344197
WAPL_HUMAN	WAPAL	physical	17113138

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 STAG1_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-621, 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-24, 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-1062; SER-1065 ANDSER-1067, AND MASS SPECTROMETRY.	18669648 [Abstract]