dbPTM

ENSA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ENSA_HUMAN
UniProt AC	O43768
Protein Name	Alpha-endosulfine
Gene Name	ENSA
Organism	Homo sapiens (Human).
Sequence Length	121
Subcellular Localization	Cytoplasm.
Protein Description	Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents..
Protein Sequence	MSQKQEEENPAEETGEEKQDTQEKEGILPERAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGPDKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSQKQEEEN ------CCHHHHCCC	46.19	21406692
2	Phosphorylation	------MSQKQEEEN ------CCHHHHCCC	46.19	29255136
2 (in isoform 3)	Phosphorylation	-	46.19	27251275
4	Ubiquitination	----MSQKQEEENPA ----CCHHHHCCCHH	52.98	33845483
14	Phosphorylation	EENPAEETGEEKQDT CCCHHHHCCCHHHHH	41.20	21815630
21	Phosphorylation	TGEEKQDTQEKEGIL CCCHHHHHHHHCCCC	35.81	23186163
24	Ubiquitination	EKQDTQEKEGILPER HHHHHHHHCCCCHHH	51.96	24816145
34	Ubiquitination	ILPERAEEAKLKAKY CCHHHHHHHHHHHCC	50.55	24816145
36	Ubiquitination	PERAEEAKLKAKYPS HHHHHHHHHHHCCCC	54.52	32142685
38	Ubiquitination	RAEEAKLKAKYPSLG HHHHHHHHHCCCCCC	41.97	24816145
40	Acetylation	EEAKLKAKYPSLGQK HHHHHHHCCCCCCCC	56.99	25953088
40	Ubiquitination	EEAKLKAKYPSLGQK HHHHHHHCCCCCCCC	56.99	32142685
41	Phosphorylation	EAKLKAKYPSLGQKP HHHHHHCCCCCCCCC	11.69	22115753
43	Phosphorylation	KLKAKYPSLGQKPGG HHHHCCCCCCCCCCC	41.88	23401153
43	Ubiquitination	KLKAKYPSLGQKPGG HHHHCCCCCCCCCCC	41.88	32015554
43 (in isoform 3)	Phosphorylation	-	41.88	27251275
47	Acetylation	KYPSLGQKPGGSDFL CCCCCCCCCCCCHHH	43.78	25953088
47	Ubiquitination	KYPSLGQKPGGSDFL CCCCCCCCCCCCHHH	43.78	32015554
51	Phosphorylation	LGQKPGGSDFLMKRL CCCCCCCCHHHHHHH	30.98	27794612
52	Ubiquitination	GQKPGGSDFLMKRLQ CCCCCCCHHHHHHHH	43.93	32015554
55	Sulfoxidation	PGGSDFLMKRLQKGQ CCCCHHHHHHHHHCC	2.10	21406390
56	Methylation	GGSDFLMKRLQKGQK CCCHHHHHHHHHCCC	52.70	-
56	Ubiquitination	GGSDFLMKRLQKGQK CCCHHHHHHHHHCCC	52.70	23000965
59	Acetylation	DFLMKRLQKGQKYFD HHHHHHHHHCCCHHC	52.44	19608861
59	Ubiquitination	DFLMKRLQKGQKYFD HHHHHHHHHCCCHHC	52.44	21890473
59 (in isoform 5)	Ubiquitination	-	52.44	21890473
59 (in isoform 6)	Ubiquitination	-	52.44	21890473
59 (in isoform 7)	Phosphorylation	-	52.44	-
60	Ubiquitination	FLMKRLQKGQKYFDS HHHHHHHHCCCHHCC	68.82	23000965
63	Acetylation	KRLQKGQKYFDSGDY HHHHHCCCHHCCCCH	57.46	23954790
63	Phosphorylation	KRLQKGQKYFDSGDY HHHHHCCCHHCCCCH	57.46	32645325
63	Ubiquitination	KRLQKGQKYFDSGDY HHHHHCCCHHCCCCH	57.46	23000965
63 (in isoform 1)	Ubiquitination	-	57.46	21890473
63 (in isoform 2)	Ubiquitination	-	57.46	21890473
63 (in isoform 3)	Phosphorylation	-	57.46	-
63 (in isoform 9)	Phosphorylation	-	57.46	-
64	Phosphorylation	RLQKGQKYFDSGDYN HHHHCCCHHCCCCHH	12.53	22167270
67	Phosphorylation	KGQKYFDSGDYNMAK HCCCHHCCCCHHHHH	24.54	19664994
70	Phosphorylation	KYFDSGDYNMAKAKM CHHCCCCHHHHHHHH	15.46	25463755
70	Ubiquitination	KYFDSGDYNMAKAKM CHHCCCCHHHHHHHH	15.46	21890473
72	Sulfoxidation	FDSGDYNMAKAKMKN HCCCCHHHHHHHHHC	3.09	30846556
74	Acetylation	SGDYNMAKAKMKNKQ CCCHHHHHHHHHCCC	37.46	25953088
74	Ubiquitination	SGDYNMAKAKMKNKQ CCCHHHHHHHHHCCC	37.46	32015554
76	Ubiquitination	DYNMAKAKMKNKQLP CHHHHHHHHHCCCCC	50.10	29967540
76 (in isoform 7)	Phosphorylation	-	50.10	25159151
79	Phosphorylation	MAKAKMKNKQLPSAG HHHHHHHCCCCCCCC	33.53	32142685
79 (in isoform 7)	Phosphorylation	-	33.53	22496350
80	Ubiquitination	AKAKMKNKQLPSAGP HHHHHHCCCCCCCCC	47.93	29967540
80 (in isoform 3)	Phosphorylation	-	47.93	25159151
80 (in isoform 9)	Phosphorylation	-	47.93	25159151
82 (in isoform 7)	Phosphorylation	-	3.75	25159151
83	Phosphorylation	KMKNKQLPSAGPDKN HHHCCCCCCCCCCCC	21.46	32142685
83 (in isoform 3)	Phosphorylation	-	21.46	22496350
83 (in isoform 9)	Phosphorylation	-	21.46	22496350
84	O-linked_Glycosylation	MKNKQLPSAGPDKNL HHCCCCCCCCCCCCC	55.22	OGP
84	Phosphorylation	MKNKQLPSAGPDKNL HHCCCCCCCCCCCCC	55.22	20068231
85	Ubiquitination	KNKQLPSAGPDKNLV HCCCCCCCCCCCCCC	31.43	29967540
86	Ubiquitination	NKQLPSAGPDKNLVT CCCCCCCCCCCCCCC	34.96	21890473
86 (in isoform 3)	Phosphorylation	-	34.96	25159151
86 (in isoform 7)	Ubiquitination	-	34.96	21890473
86 (in isoform 9)	Phosphorylation	-	34.96	25159151
89	Acetylation	LPSAGPDKNLVTGDH CCCCCCCCCCCCCCC	56.14	25953088
89	Ubiquitination	LPSAGPDKNLVTGDH CCCCCCCCCCCCCCC	56.14	29967540
90	Ubiquitination	PSAGPDKNLVTGDHI CCCCCCCCCCCCCCC	47.31	21890473
90 (in isoform 3)	Ubiquitination	-	47.31	21890473
90 (in isoform 4)	Phosphorylation	-	47.31	22496350
92	Ubiquitination	AGPDKNLVTGDHIPT CCCCCCCCCCCCCCC	8.64	29967540
93	O-linked_Glycosylation	GPDKNLVTGDHIPTP CCCCCCCCCCCCCCC	39.81	31373491
93	Phosphorylation	GPDKNLVTGDHIPTP CCCCCCCCCCCCCCC	39.81	26074081
93 (in isoform 4)	Phosphorylation	-	39.81	27155012
96	Ubiquitination	KNLVTGDHIPTPQDL CCCCCCCCCCCCCCC	29.31	29967540
97 (in isoform 4)	Ubiquitination	-	4.90	21890473
99	O-linked_Glycosylation	VTGDHIPTPQDLPQR CCCCCCCCCCCCCCH	32.74	30838711
99	Phosphorylation	VTGDHIPTPQDLPQR CCCCCCCCCCCCCCH	32.74	25159151
100 (in isoform 3)	Phosphorylation	-	21.97	27251275
101	Ubiquitination	GDHIPTPQDLPQRKS CCCCCCCCCCCCHHH	68.31	29967540
103	Ubiquitination	HIPTPQDLPQRKSSL CCCCCCCCCCHHHHH	3.07	29967540
104 (in isoform 6)	Phosphorylation	-	39.97	25849741
105	Phosphorylation	PTPQDLPQRKSSLVT CCCCCCCCHHHHHHH	73.13	32142685
105	Ubiquitination	PTPQDLPQRKSSLVT CCCCCCCCHHHHHHH	73.13	29967540
105 (in isoform 6)	Phosphorylation	-	73.13	25849741
107	Ubiquitination	PQDLPQRKSSLVTSK CCCCCCHHHHHHHHH	38.87	29967540
108	Phosphorylation	QDLPQRKSSLVTSKL CCCCCHHHHHHHHHH	30.97	27273156
108 (in isoform 2)	Phosphorylation	-	30.97	25849741
108 (in isoform 6)	Phosphorylation	-	30.97	17924679
109	Phosphorylation	DLPQRKSSLVTSKLA CCCCHHHHHHHHHHC	29.87	23927012
109 (in isoform 2)	Phosphorylation	-	29.87	25849741
109 (in isoform 6)	Phosphorylation	-	29.87	19651622
110	Ubiquitination	LPQRKSSLVTSKLAG CCCHHHHHHHHHHCC	6.68	24816145
112	Phosphorylation	QRKSSLVTSKLAGGQ CHHHHHHHHHHCCCC	25.99	30266825
112 (in isoform 2)	Phosphorylation	-	25.99	17924679
113	Phosphorylation	RKSSLVTSKLAGGQV HHHHHHHHHHCCCCC	20.42	23927012
113 (in isoform 2)	Phosphorylation	-	20.42	19651622
114	Acetylation	KSSLVTSKLAGGQVE HHHHHHHHHCCCCCC	32.75	25953088
114	Ubiquitination	KSSLVTSKLAGGQVE HHHHHHHHHCCCCCC	32.75	24816145
115 (in isoform 3)	Phosphorylation	-	5.54	27251275
119	Ubiquitination	TSKLAGGQVE----- HHHHCCCCCC-----	34.94	29967540
121	Phosphorylation	KLAGGQVE------- HHCCCCCC-------	47.20	32142685
123	Ubiquitination	AGGQVE--------- CCCCCC---------		29967540
124 (in isoform 3)	Phosphorylation	-		27251275
124 (in isoform 9)	Phosphorylation	-		25849741
125	Phosphorylation	GQVE----------- CCCC-----------		32142685
125 (in isoform 3)	Phosphorylation	-		27251275
125 (in isoform 9)	Phosphorylation	-		25849741
126	Ubiquitination	QVE------------ CCC------------		24816145
128 (in isoform 9)	Phosphorylation	-		17924679
129 (in isoform 9)	Phosphorylation	-		19651622
130	Ubiquitination	---------------- ----------------		24816145
131 (in isoform 4)	Phosphorylation	-		25849741
132 (in isoform 4)	Phosphorylation	-		25849741
135 (in isoform 4)	Phosphorylation	-		17924679
136 (in isoform 4)	Phosphorylation	-		19651622

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
67	S	Phosphorylation	Kinase	MASTL	Q96GX5	PSP
109	S	Phosphorylation	Kinase	PKACA	P17612	PSP
109	S	Phosphorylation	Kinase	PKG1	Q13976	PSP
109	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
67	S	Phosphorylation		9653196
Phosphorylation at Ser-67 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A (By similarity).

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 ENSA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM3_HUMAN	MCM3	physical	17353931
OFD1_HUMAN	OFD1	physical	28514442
RPP25_HUMAN	RPP25	physical	28514442
DPP9_HUMAN	DPP9	physical	28514442
PEX6_HUMAN	PEX6	physical	28514442
UBB_HUMAN	UBB	physical	28514442
QSOX1_HUMAN	QSOX1	physical	28514442
UBP4_HUMAN	USP4	physical	28514442
CBX5_HUMAN	CBX5	physical	28514442
IREB2_HUMAN	IREB2	physical	28514442
DD19B_HUMAN	DDX19B	physical	28514442
POP7_HUMAN	POP7	physical	28514442
AT12A_HUMAN	ATP12A	physical	28514442
RIC8B_HUMAN	RIC8B	physical	28514442
PPME1_HUMAN	PPME1	physical	28514442
MTMR4_HUMAN	MTMR4	physical	28514442
PGTA_HUMAN	RABGGTA	physical	28514442
SCPDL_HUMAN	SCCPDH	physical	28514442

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 ENSA_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-63, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Membrane-induced folding of the cAMP-regulated phosphoproteinendosulfine-alpha."; Boettcher J.M., Hartman K.L., Ladror D.T., Qi Z., Woods W.S.,George J.M., Rienstra C.M.; Biochemistry 47:12357-12364(2008). Cited for: INTERACTION WITH SNCA, PHOSPHORYLATION AT SER-109, AND MUTAGENESIS OFSER-109.	18973346 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND TYR-70, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-109; THR-112AND SER-113, AND MASS SPECTROMETRY.	17924679 [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-2, AND MASSSPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70, AND MASSSPECTROMETRY.	19534553 [Abstract]

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