STAG2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STAG2_MOUSE
• UniProt AC: O35638
• Protein Name: Cohesin subunit SA-2
• Gene Name: Stag2
• Organism: Mus musculus (Mouse).
• Sequence Length: 1231
• 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 (By similarity)..
• Protein Sequence: MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKSGNGGGKPPSGSNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGLMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTRITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCAHYVILWQLAKITESTSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDSNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGMSSRGSTVRSKKSKPSTGKRKVVEGMQLALPEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQAEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF

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
1	Acetylation	-------MIAAPEIP -------CCCCCCCC	22.93	-
9	Phosphorylation	IAAPEIPTDFNLLQE CCCCCCCCCCCHHHH	59.91	25338131
17	Phosphorylation	DFNLLQESETHFSSD CCCHHHHCCCCCCCC	34.53	-
22	Phosphorylation	QESETHFSSDTDFED HHCCCCCCCCCCHHH	21.50	24224561
23	Phosphorylation	ESETHFSSDTDFEDI HCCCCCCCCCCHHHC	43.52	25338131
25	Phosphorylation	ETHFSSDTDFEDIEG CCCCCCCCCHHHCCC	44.53	24224561
270	Ubiquitination	RLELLLQKRKELQEN HHHHHHHHHHHHHHC	66.46	-
433	Phosphorylation	VAAGEFLYKKLFSRR HHHHHHHHHHHHCCC	16.05	-
594	Phosphorylation	NLLQLPQYFDLEIYT HHHCCCCEECEEEEE	9.34	26487105
600	Phosphorylation	QYFDLEIYTTGRLEK CEECEEEEECCCHHH	6.73	29895711
601	Phosphorylation	YFDLEIYTTGRLEKH EECEEEEECCCHHHH	28.56	29895711
602	Phosphorylation	FDLEIYTTGRLEKHL ECEEEEECCCHHHHH	11.88	29895711
607	Acetylation	YTTGRLEKHLDALLR EECCCHHHHHHHHHH	54.80	22826441
685	Phosphorylation	EPDEDDAYQVLSTLK CCCCCHHHHHHHHHH	13.22	30482847
689	Phosphorylation	DDAYQVLSTLKRITA CHHHHHHHHHHHHHH	32.60	30482847
965	Ubiquitination	TFGLDQLKTREAIAM HHCHHHHHHHHHHHH	39.64	-
1019	Phosphorylation	RQDKRTVYVYLEKFM CCCCCHHEEEHHHHH	5.24	29514104
1047	Phosphorylation	PLMSYRNSLLAGGDD HHHHHCCCHHCCCCC	18.76	25159016
1056	Phosphorylation	LAGGDDDTMSVISGM HCCCCCCHHHHHHHC	20.52	21082442
1058	Phosphorylation	GGDDDTMSVISGMSS CCCCCHHHHHHHCCC	20.56	25521595
1061	Phosphorylation	DDTMSVISGMSSRGS CCHHHHHHHCCCCCC	26.70	21082442
1064	Phosphorylation	MSVISGMSSRGSTVR HHHHHHCCCCCCCCC	22.02	21082442
1065	Phosphorylation	SVISGMSSRGSTVRS HHHHHCCCCCCCCCC	31.59	21082442
1068	Phosphorylation	SGMSSRGSTVRSKKS HHCCCCCCCCCCCCC	23.71	24759943
1069	Phosphorylation	GMSSRGSTVRSKKSK HCCCCCCCCCCCCCC	23.82	24759943
1072	Phosphorylation	SRGSTVRSKKSKPST CCCCCCCCCCCCCCC	39.85	-
1096	Phosphorylation	QLALPEESSSSDSMW EEECCCCCCCCCCCC	33.58	26643407
1097	Phosphorylation	LALPEESSSSDSMWL EECCCCCCCCCCCCC	36.82	26643407
1098	Phosphorylation	ALPEESSSSDSMWLS ECCCCCCCCCCCCCC	47.66	25266776
1099	Phosphorylation	LPEESSSSDSMWLSR CCCCCCCCCCCCCCH	35.34	26643407
1101	Phosphorylation	EESSSSDSMWLSREQ CCCCCCCCCCCCHHH	17.51	26643407
1105	Phosphorylation	SSDSMWLSREQTLHT CCCCCCCCHHHHCCC	20.47	26643407
1109	Phosphorylation	MWLSREQTLHTPVMM CCCCHHHHCCCCCCC	18.76	28833060
1112	Phosphorylation	SREQTLHTPVMMQTP CHHHHCCCCCCCCCC	22.23	28833060
1118	Phosphorylation	HTPVMMQTPQLTSTI CCCCCCCCCCCHHHH	8.63	28833060
1160	Phosphorylation	LDYNRRGTSLMEDDE CCCCCCCCCCCCCCC	19.51	21082442
1161	Phosphorylation	DYNRRGTSLMEDDEE CCCCCCCCCCCCCCC	28.66	26239621
1177	Phosphorylation	IVEDVMMSSEGRIED HHHHHHHCCCCCHHH	13.72	28833060
1178	Phosphorylation	VEDVMMSSEGRIEDL HHHHHHCCCCCHHHC	26.61	28833060

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

Oops, there are no upstream regulatory protein records of STAG2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STAG2_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 STAG2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC1A_HUMAN	SMC1A	physical	20360068
AL3A2_HUMAN	ALDH3A2	physical	20360068
CYTSB_HUMAN	SPECC1	physical	20360068
SMC3_HUMAN	SMC3	physical	20360068
HMGA1_HUMAN	HMGA1	physical	20360068
MYPT1_HUMAN	PPP1R12A	physical	20360068
PDS5B_HUMAN	PDS5B	physical	20360068
TMOD3_HUMAN	TMOD3	physical	20360068
RAD21_HUMAN	RAD21	physical	20360068
MISP_HUMAN	MISP	physical	20360068
WAPL_HUMAN	WAPAL	physical	20360068
CLUS_HUMAN	CLU	physical	20360068
STAG2_HUMAN	STAG2	physical	20360068
PDS5A_HUMAN	PDS5A	physical	20360068

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-1061 AND THR-1160, ANDMASS SPECTROMETRY.
PubMed: 17242355