STAG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STAG1_MOUSE
• UniProt AC: Q9D3E6
• Protein Name: Cohesin subunit SA-1
• Gene Name: Stag1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1258
• Subcellular Localization: Nucleus . Chromosome. 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 centromeres, where coh
• 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 (By similarity)..
• Protein Sequence: MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGDGDPVTLFEVVKLGKSAMQSVVDDWIELYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRNSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEAMSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLPMLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEACSKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLKRLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGSPSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQPLVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLIIYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQIDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNQKGQEYPPPNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTEQMMERREDVWLPLISYRNSLVTGGEDDRMSVNSGSSSSKTSSVRSKKGRPPLHRKRVEDESLDNTWLNRTDTMIQTPGPLPTPQLTSTVLRENSRPMGEQIQEPESEHGSEPDFLHNPQMQISWLGQPKLEDLNRKDRTGMNYMKVRAGVRHAVRGLMEEDAEPIFEDVMMSSRSQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF

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
4	Phosphorylation	----MITSELPVLQD ----CCCCCCCCEEC	42.69	23984901
12	Phosphorylation	ELPVLQDSTNETTAH CCCCEECCCCCCCCC	21.85	23429704
13	Phosphorylation	LPVLQDSTNETTAHS CCCEECCCCCCCCCC	45.42	23737553
16	Phosphorylation	LQDSTNETTAHSDAG EECCCCCCCCCCCCC	31.21	21149613
17	Phosphorylation	QDSTNETTAHSDAGS ECCCCCCCCCCCCCC	19.05	21149613
20	Phosphorylation	TNETTAHSDAGSELE CCCCCCCCCCCCCCC	27.05	23429704
24	Phosphorylation	TAHSDAGSELEETEV CCCCCCCCCCCCCCC	40.50	23429704
29	Phosphorylation	AGSELEETEVKGKRK CCCCCCCCCCCCCCC	36.38	21149613
45	Phosphorylation	GRPGRPPSTNKKPRK CCCCCCCCCCCCCCC	47.50	29472430
46	Phosphorylation	RPGRPPSTNKKPRKS CCCCCCCCCCCCCCC	57.75	29472430
273	Ubiquitination	RLELLLQKRKELQEN HHHHHHHHHHHHHHC	66.46	-
756	Phosphorylation	LVKITDGSPSKEDLL HHCCCCCCCCHHHHH	28.89	28066266
758	Phosphorylation	KITDGSPSKEDLLVL CCCCCCCCHHHHHHH	50.83	28066266
962	Phosphorylation	LARRFALTFGLDQIK HHHHHHHHHCCHHHH	16.54	28059163
1051	Phosphorylation	PLISYRNSLVTGGED HHHEECCCCCCCCCC	18.41	25168779
1054	Phosphorylation	SYRNSLVTGGEDDRM EECCCCCCCCCCCCC	44.77	28066266
1061	Oxidation	TGGEDDRMSVNSGSS CCCCCCCCCCCCCCC	7.25	17242355
1062	Phosphorylation	GGEDDRMSVNSGSSS CCCCCCCCCCCCCCC	21.02	27149854
1065	Phosphorylation	DDRMSVNSGSSSSKT CCCCCCCCCCCCCCH	37.59	22817900
1067	Phosphorylation	RMSVNSGSSSSKTSS CCCCCCCCCCCCHHC	27.20	21183079
1068	Phosphorylation	MSVNSGSSSSKTSSV CCCCCCCCCCCHHCC	42.00	22817900
1069	Phosphorylation	SVNSGSSSSKTSSVR CCCCCCCCCCHHCCC	37.24	22817900
1070	Phosphorylation	VNSGSSSSKTSSVRS CCCCCCCCCHHCCCC	41.73	22817900
1072	Phosphorylation	SGSSSSKTSSVRSKK CCCCCCCHHCCCCCC	28.34	22817900
1093	Phosphorylation	RKRVEDESLDNTWLN CCCCCCCCCCCCCCC	54.03	28066266
1108	Phosphorylation	RTDTMIQTPGPLPTP CCCCCCCCCCCCCCC	21.20	29514104
1126	Phosphorylation	STVLRENSRPMGEQI HHHHHHCCCCCCCCC	32.77	22817900
1138	Phosphorylation	EQIQEPESEHGSEPD CCCCCCCCCCCCCCC	45.68	21183079
1142	Phosphorylation	EPESEHGSEPDFLHN CCCCCCCCCCCCCCC	48.11	21183079
1251	Phosphorylation	AAIIEDDSGFGMPMF CEEEECCCCCCCCCC	48.63	29514104

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of STAG1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STAG1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of STAG1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of STAG1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1069 AND SER-1070, ANDMASS SPECTROMETRY.
PubMed: 17242355