dbPTM

STAG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STAG2_HUMAN
UniProt AC	Q8N3U4
Protein Name	Cohesin subunit SA-2
Gene Name	STAG2
Organism	Homo sapiens (Human).
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..
Protein Sequence	MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKGGNGGGKPPSGPNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGMMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTKITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCTHYVILWQLAKITESSSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDNNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGISSRGSTVRSKKSKPSTGKRKVVEGMQLSLTEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQTEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MIAAPEIP -------CCCCCCCC	22.93	20068231
9	Phosphorylation	IAAPEIPTDFNLLQE CCCCCCCCCCCHHHH	59.91	30108239
17	Phosphorylation	DFNLLQESETHFSSD CCCHHHHCCCCCCCC	34.53	30108239
19	Phosphorylation	NLLQESETHFSSDTD CHHHHCCCCCCCCCC	37.18	30108239
22	Phosphorylation	QESETHFSSDTDFED HHCCCCCCCCCCHHH	21.50	30108239
23	Phosphorylation	ESETHFSSDTDFEDI HCCCCCCCCCCHHHC	43.52	25159151
25	Phosphorylation	ETHFSSDTDFEDIEG CCCCCCCCCHHHCCC	44.53	30108239
48	Acetylation	KTCKKGKKGPAEKGK CCCCCCCCCCCCCCC	77.96	26051181
53	Acetylation	GKKGPAEKGKGGNGG CCCCCCCCCCCCCCC	68.94	26051181
55	Acetylation	KGPAEKGKGGNGGGK CCCCCCCCCCCCCCC	74.78	26051181
62	Acetylation	KGGNGGGKPPSGPNR CCCCCCCCCCCCCCC	57.96	25953088
132	Phosphorylation	SGCKGVVTAEMFRHM CCCCCHHHHHHHHHH	17.94	21406692
142	Phosphorylation	MFRHMQNSEIIRKMT HHHHHCCHHHHHHHH	17.18	20068231
149	Phosphorylation	SEIIRKMTEEFDEDS HHHHHHHHHHHCCCC	35.08	-
156	Phosphorylation	TEEFDEDSGDYPLTM HHHHCCCCCCCCCCC	31.36	-
159	Phosphorylation	FDEDSGDYPLTMAGP HCCCCCCCCCCCCCH	12.03	-
162	Phosphorylation	DSGDYPLTMAGPQWK CCCCCCCCCCCHHHH	10.64	-
169	Ubiquitination	TMAGPQWKKFKSSFC CCCCHHHHHHHHHHH	42.98	-
173	Phosphorylation	PQWKKFKSSFCEFIG HHHHHHHHHHHHHHH	31.60	-
174	Phosphorylation	QWKKFKSSFCEFIGV HHHHHHHHHHHHHHH	34.21	-
270	Acetylation	RLELLLQKRKELQEN HHHHHHHHHHHHHHC	66.46	25953088
270	Ubiquitination	RLELLLQKRKELQEN HHHHHHHHHHHHHHC	66.46	21890473
272	Ubiquitination	ELLLQKRKELQENQD HHHHHHHHHHHHCHH	70.57	-
358	Ubiquitination	LQGLYYNKELNSKLE HHHHHHCHHHHHHHH	47.67	-
362	Phosphorylation	YYNKELNSKLELFTS HHCHHHHHHHHHHHH	51.77	22210691
363	Ubiquitination	YNKELNSKLELFTSR HCHHHHHHHHHHHHH	44.93	21890473
363	Ubiquitination	YNKELNSKLELFTSR HCHHHHHHHHHHHHH	44.93	21890473
363	Ubiquitination	YNKELNSKLELFTSR HCHHHHHHHHHHHHH	44.93	21890473
363 (in isoform 2)	Ubiquitination	-	44.93	-
377	Phosphorylation	RFKDRIVSMTLDKEY HHHHHHHHCCCCCCH	12.04	30576142
379	Phosphorylation	KDRIVSMTLDKEYDV HHHHHHCCCCCCHHH	25.05	30576142
433	Phosphorylation	VAAGEFLYKKLFSRR HHHHHHHHHHHHCCC	16.05	25884760
449	Ubiquitination	PEEDGMMKRRGRQGP HHHCCHHHCCCCCCC	30.01	-
449 (in isoform 2)	Ubiquitination	-	30.01	-
528	Phosphorylation	LIEIMLCTIRQAAEC HHHHHHHHHHHHHHC	18.42	24043423
551	Acetylation	GKRVLTAKEKKTQLD CCCCCCHHHHCCCCC	65.90	25953088
562	Ubiquitination	TQLDDRTKITELFAV CCCCCCHHHHHHHHH	48.82	-
562 (in isoform 2)	Ubiquitination	-	48.82	-
602	Phosphorylation	FDLEIYTTGRLEKHL ECEEEEECCCHHHHH	11.88	-
607	Ubiquitination	YTTGRLEKHLDALLR EECCCHHHHHHHHHH	54.80	21890473
607	Ubiquitination	YTTGRLEKHLDALLR EECCCHHHHHHHHHH	54.80	21890473
607	Acetylation	YTTGRLEKHLDALLR EECCCHHHHHHHHHH	54.80	19608861
607	Ubiquitination	YTTGRLEKHLDALLR EECCCHHHHHHHHHH	54.80	19608861
622	Acetylation	QIRNIVEKHTDTDVL HHHHHHHHCCCHHHH	40.69	25953088
622	Ubiquitination	QIRNIVEKHTDTDVL HHHHHHHHCCCHHHH	40.69	-
622 (in isoform 2)	Ubiquitination	-	40.69	-
634	Ubiquitination	DVLEACSKTYHALCN HHHHHHHHHHHHHHC	53.65	-
664	Ubiquitination	LIDELADKFNRLLED HHHHHHHHHHHHHHH	38.64	21890473
664	Ubiquitination	LIDELADKFNRLLED HHHHHHHHHHHHHHH	38.64	21890473
664	Acetylation	LIDELADKFNRLLED HHHHHHHHHHHHHHH	38.64	26051181
664	Ubiquitination	LIDELADKFNRLLED HHHHHHHHHHHHHHH	38.64	21890473
664 (in isoform 2)	Ubiquitination	-	38.64	-
685	Phosphorylation	EPDEDDAYQVLSTLK CCCCCHHHHHHHHHH	13.22	-
692	Ubiquitination	YQVLSTLKRITAFHN HHHHHHHHHHHHCCC	41.67	21906983
705	Ubiquitination	HNAHDLSKWDLFACN CCCCCCHHHCHHHHC	52.61	-
705 (in isoform 2)	Ubiquitination	-	52.61	-
714	Acetylation	DLFACNYKLLKTGIE CHHHHCHHHHHHCHH	33.09	26051181
714	Ubiquitination	DLFACNYKLLKTGIE CHHHHCHHHHHHCHH	33.09	-
714 (in isoform 2)	Ubiquitination	-	33.09	-
737	Phosphorylation	VIHALQCTHYVILWQ HHHHHHHCHHHHHHH	11.86	22067460
749	Phosphorylation	LWQLAKITESSSTKE HHHHHHHHCCCCCHH	29.16	21406692
751	Phosphorylation	QLAKITESSSTKEDL HHHHHHCCCCCHHHH	22.42	21406692
752	Phosphorylation	LAKITESSSTKEDLL HHHHHCCCCCHHHHH	35.48	21406692
753	Phosphorylation	AKITESSSTKEDLLR HHHHCCCCCHHHHHH	53.42	21406692
754	Phosphorylation	KITESSSTKEDLLRL HHHCCCCCHHHHHHH	40.16	21406692
755	Acetylation	ITESSSTKEDLLRLK HHCCCCCHHHHHHHH	51.70	26051181
755	Ubiquitination	ITESSSTKEDLLRLK HHCCCCCHHHHHHHH	51.70	21906983
755 (in isoform 2)	Ubiquitination	-	51.70	-
843	Phosphorylation	EQDDDNNSADGQQED ECCCCCCCCCCCCCC	33.71	20363803
860	Ubiquitination	SKIEALHKRRNLLAA HHHHHHHHHHHHHHH	54.63	-
874	Phosphorylation	AFCKLIVYTVVEMNT HHHHHHHHHHHHHCC	6.19	28270605
875	Phosphorylation	FCKLIVYTVVEMNTA HHHHHHHHHHHHCCH	13.74	28270605
881	Phosphorylation	YTVVEMNTAADIFKQ HHHHHHCCHHHHHHH	23.16	28270605
889	Phosphorylation	AADIFKQYMKYYNDY HHHHHHHHHHHHCHH	9.00	-
891	Ubiquitination	DIFKQYMKYYNDYGD HHHHHHHHHHCHHHH	39.38	-
892	Phosphorylation	IFKQYMKYYNDYGDI HHHHHHHHHCHHHHH	7.32	18083107
893	Phosphorylation	FKQYMKYYNDYGDII HHHHHHHHCHHHHHH	8.95	18083107
896	Phosphorylation	YMKYYNDYGDIIKET HHHHHCHHHHHHHHH	17.04	22817900
901	Acetylation	NDYGDIIKETMSKTR CHHHHHHHHHHHHCC	47.68	26051181
901	Ubiquitination	NDYGDIIKETMSKTR CHHHHHHHHHHHHCC	47.68	-
901 (in isoform 2)	Ubiquitination	-	47.68	-
903	Phosphorylation	YGDIIKETMSKTRQI HHHHHHHHHHHCCCC	23.03	29759185
905	Phosphorylation	DIIKETMSKTRQIDK HHHHHHHHHCCCCCH	37.99	29759185
912	Acetylation	SKTRQIDKIQCAKTL HHCCCCCHHHHHHHH	35.98	25953088
912	Ubiquitination	SKTRQIDKIQCAKTL HHCCCCCHHHHHHHH	35.98	-
941	Phosphorylation	NGYNFDRSSSTFSGI CCCCCCCCCCCCHHH	30.41	21406692
942	Phosphorylation	GYNFDRSSSTFSGIK CCCCCCCCCCCHHHH	34.00	21406692
943	Phosphorylation	YNFDRSSSTFSGIKE CCCCCCCCCCHHHHH	34.42	21406692
944	Phosphorylation	NFDRSSSTFSGIKEL CCCCCCCCCHHHHHH	24.62	21406692
946	Phosphorylation	DRSSSTFSGIKELAR CCCCCCCHHHHHHHH	39.43	21406692
949	Acetylation	SSTFSGIKELARRFA CCCCHHHHHHHHHHH	50.64	26051181
949	Ubiquitination	SSTFSGIKELARRFA CCCCHHHHHHHHHHH	50.64	-
949 (in isoform 2)	Ubiquitination	-	50.64	-
965	Ubiquitination	TFGLDQLKTREAIAM HHCHHHHHHHHHHHH	39.64	21890473
965	Ubiquitination	TFGLDQLKTREAIAM HHCHHHHHHHHHHHH	39.64	21890473
965	Ubiquitination	TFGLDQLKTREAIAM HHCHHHHHHHHHHHH	39.64	2189047
965 (in isoform 2)	Ubiquitination	-	39.64	-
1017	Phosphorylation	LLRQDKRTVYVYLEK HHCCCCCHHEEEHHH	23.17	22210691
1019	Phosphorylation	RQDKRTVYVYLEKFM CCCCCHHEEEHHHHH	5.24	28152594
1021	Phosphorylation	DKRTVYVYLEKFMTF CCCHHEEEHHHHHHH	7.46	22210691
1047	Phosphorylation	PLMSYRNSLLAGGDD HHHHHCCCHHCCCCC	18.76	25262027
1056	Phosphorylation	LAGGDDDTMSVISGI HCCCCCCHHHHHHHC	20.52	30266825
1057	Sulfoxidation	AGGDDDTMSVISGIS CCCCCCHHHHHHHCC	3.76	21406390
1058	Phosphorylation	GGDDDTMSVISGISS CCCCCHHHHHHHCCC	20.56	22167270
1061	Phosphorylation	DDTMSVISGISSRGS CCHHHHHHHCCCCCC	28.11	22167270
1064	Phosphorylation	MSVISGISSRGSTVR HHHHHHCCCCCCCCC	19.94	22167270
1065	Phosphorylation	SVISGISSRGSTVRS HHHHHCCCCCCCCCC	38.45	22167270
1066	Methylation	VISGISSRGSTVRSK HHHHCCCCCCCCCCC	35.97	5172523
1068	Phosphorylation	SGISSRGSTVRSKKS HHCCCCCCCCCCCCC	23.71	23090842
1069	Phosphorylation	GISSRGSTVRSKKSK HCCCCCCCCCCCCCC	23.82	23090842
1071	Methylation	SSRGSTVRSKKSKPS CCCCCCCCCCCCCCC	42.73	115387683
1075	Phosphorylation	STVRSKKSKPSTGKR CCCCCCCCCCCCCCC	54.24	23898821
1078	Phosphorylation	RSKKSKPSTGKRKVV CCCCCCCCCCCCCCE	54.23	23898821
1079	Phosphorylation	SKKSKPSTGKRKVVE CCCCCCCCCCCCCEE	56.07	23898821
1091	Phosphorylation	VVEGMQLSLTEESSS CEECEEEEECCCCCC	19.16	27251275
1093	Phosphorylation	EGMQLSLTEESSSSD ECEEEEECCCCCCCC	34.04	27251275
1096	Phosphorylation	QLSLTEESSSSDSMW EEEECCCCCCCCCCC	29.32	27251275
1097	Phosphorylation	LSLTEESSSSDSMWL EEECCCCCCCCCCCC	36.82	27690223
1099	Phosphorylation	LTEESSSSDSMWLSR ECCCCCCCCCCCCCH	35.34	21601212
1105	Phosphorylation	SSDSMWLSREQTLHT CCCCCCCCHHHHCCC	20.47	26074081
1109	Phosphorylation	MWLSREQTLHTPVMM CCCCHHHHCCCCCCC	18.76	30266825
1112	Phosphorylation	SREQTLHTPVMMQTP CHHHHCCCCCCCCCC	22.23	30266825
1118	Phosphorylation	HTPVMMQTPQLTSTI CCCCCCCCCCCHHHH	8.63	25159151
1122	Phosphorylation	MMQTPQLTSTIMREP CCCCCCCHHHHHCCC	20.69	29978859
1123	Phosphorylation	MQTPQLTSTIMREPK CCCCCCHHHHHCCCC	25.24	29978859
1124	Phosphorylation	QTPQLTSTIMREPKR CCCCCHHHHHCCCCC	17.35	29978859
1137	Phosphorylation	KRLRPEDSFMSVYPM CCCCCCCCCCCCCCC	22.61	26552605
1140	Phosphorylation	RPEDSFMSVYPMQTE CCCCCCCCCCCCCCC	19.25	26552605
1142	Phosphorylation	EDSFMSVYPMQTEHH CCCCCCCCCCCCCCC	5.91	26552605
1146	Phosphorylation	MSVYPMQTEHHQTPL CCCCCCCCCCCCCCC	30.91	26552605
1151	Phosphorylation	MQTEHHQTPLDYNRR CCCCCCCCCCCCCCC	22.82	25159151
1155	Phosphorylation	HHQTPLDYNRRGTSL CCCCCCCCCCCCCCC	20.46	26552605
1158	Methylation	TPLDYNRRGTSLMED CCCCCCCCCCCCCCC	49.45	115917913
1160	Phosphorylation	LDYNRRGTSLMEDDE CCCCCCCCCCCCCCC	19.51	23401153
1161	Phosphorylation	DYNRRGTSLMEDDEE CCCCCCCCCCCCCCC	28.66	30266825
1177	Phosphorylation	IVEDVMMSSEGRIED HHHHHHHCCCCCHHH	13.72	25159151
1178	Phosphorylation	VEDVMMSSEGRIEDL HHHHHHCCCCCHHHC	26.61	21712546
1181 (in isoform 2)	Phosphorylation	-	25.68	29116813
1193	Phosphorylation	NEGMDFDTMDIDLPP CCCCCCCCCCCCCCC	19.41	15737063
1197 (in isoform 2)	Phosphorylation	-	49.19	29116813
1198	Phosphorylation	FDTMDIDLPPSKNRR CCCCCCCCCCCCCHH	7.40	27251275
1198 (in isoform 2)	Phosphorylation	-	7.40	29116813
1219	Phosphorylation	PDFFDPASIMDESVL CCCCCHHHHCCHHHH	24.67	26270265
1224	Phosphorylation	PASIMDESVLGVSMF HHHHCCHHHHCCCCC	20.55	15737063
1229	Phosphorylation	DESVLGVSMF----- CHHHHCCCCC-----	16.81	-

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 STAG2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STAG2_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 STAG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSU72_HUMAN	SSU72	physical	20818333
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
RAD21_HUMAN	RAD21	physical	17962804
SMC3_HUMAN	SMC3	physical	17962804
SMC1A_HUMAN	SMC1A	physical	10931856
SMC3_HUMAN	SMC3	physical	10931856
RAD21_HUMAN	RAD21	physical	10931856
BZW2_HUMAN	BZW2	physical	26344197
COPE_HUMAN	COPE	physical	26344197
EXOS2_HUMAN	EXOSC2	physical	26344197
EXOS9_HUMAN	EXOSC9	physical	26344197
PDS5A_HUMAN	PDS5A	physical	26344197
RAD21_HUMAN	RAD21	physical	26344197
SMC1A_HUMAN	SMC1A	physical	26344197
SMC1B_HUMAN	SMC1B	physical	26344197
SMC3_HUMAN	SMC3	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 STAG2_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-607, 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-1058; SER-1061 ANDTHR-1112, AND MASS SPECTROMETRY.	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-1058; SER-1061 ANDSER-1065, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, AND MASSSPECTROMETRY.	17081983 [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-1061, AND MASSSPECTROMETRY.	15302935 [Abstract]