dbPTM

SET_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SET_HUMAN
UniProt AC	Q01105
Protein Name	Protein SET
Gene Name	SET
Organism	Homo sapiens (Human).
Sequence Length	290
Subcellular Localization	Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus, nucleoplasm. In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavag
Protein Description	Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher..
Protein Sequence	MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEGEEDDDDDEEEEGLEDIDEEGDEDEGEEDEDDDEGEEGEEDEGEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Phosphorylation	-	20.51	28348404
2	Methylation	------MAPKRQSPL ------CCCCCCCCC	20.51	-
7	Phosphorylation	-MAPKRQSPLPPQKK -CCCCCCCCCCCCCC	32.22	29255136
7 (in isoform 2)	Acetylation	-	32.22	-
7 (in isoform 2)	Ubiquitination	-	32.22	-
9 (in isoform 2)	Phosphorylation	-	13.48	17245428
10 (in isoform 2)	Acetylation	-	32.43	-
10 (in isoform 2)	Ubiquitination	-	32.43	-
11 (in isoform 2)	Acetylation	-	67.32	19608861
15 (in isoform 2)	Phosphorylation	-	53.98	28731282
23 (in isoform 2)	Phosphorylation	-	29.67	30266825
24 (in isoform 2)	Phosphorylation	-	36.78	30266825
27	Phosphorylation	PALGPEETSASAGLP CCCCCCCCCCCCCCC	28.12	30108239
28	Phosphorylation	ALGPEETSASAGLPK CCCCCCCCCCCCCCC	24.41	23401153
30	Phosphorylation	GPEETSASAGLPKKG CCCCCCCCCCCCCCC	23.72	25159151
39	Acetylation	GLPKKGEKEQQEAIE CCCCCCHHHHHHHHH	70.28	18530485
55 (in isoform 2)	Ubiquitination	-	4.98	21890473
57	Methylation	EVQNEIDRLNEQASE HHHHHHHHHHHHHHH	45.11	115916501
59 (in isoform 2)	Acetylation	-	39.98	-
60	Ubiquitination	NEIDRLNEQASEEIL HHHHHHHHHHHHHHH	52.71	21890473
61	Ubiquitination	EIDRLNEQASEEILK HHHHHHHHHHHHHHH	49.46	21890473
61	Acetylation	EIDRLNEQASEEILK HHHHHHHHHHHHHHH	49.46	19608861
61	Ubiquitination	EIDRLNEQASEEILK HHHHHHHHHHHHHHH	49.46	19608861
61	Ubiquitination	EIDRLNEQASEEILK HHHHHHHHHHHHHHH	49.46	21890473
63	Phosphorylation	DRLNEQASEEILKVE HHHHHHHHHHHHHHH	35.14	19664994
68	Acetylation	QASEEILKVEQKYNK HHHHHHHHHHHHHHH	49.76	26822725
68	Ubiquitination	QASEEILKVEQKYNK HHHHHHHHHHHHHHH	49.76	21906983
68 (in isoform 1)	Ubiquitination	-	49.76	21890473
70 (in isoform 2)	Ubiquitination	-	39.50	21890473
72	Acetylation	EILKVEQKYNKLRQP HHHHHHHHHHHHHCC	36.97	25953088
72	2-Hydroxyisobutyrylation	EILKVEQKYNKLRQP HHHHHHHHHHHHHCC	36.97	-
83	Methylation	LRQPFFQKRSELIAK HHCCHHHHHHHHHHH	53.38	7406531
83	Acetylation	LRQPFFQKRSELIAK HHCCHHHHHHHHHHH	53.38	7406531
83	Ubiquitination	LRQPFFQKRSELIAK HHCCHHHHHHHHHHH	53.38	83
83	2-Hydroxyisobutyrylation	LRQPFFQKRSELIAK HHCCHHHHHHHHHHH	53.38	-
83 (in isoform 1)	Ubiquitination	-	53.38	21890473
90	Acetylation	KRSELIAKIPNFWVT HHHHHHHHCCCEEEE	52.26	156055
90	Ubiquitination	KRSELIAKIPNFWVT HHHHHHHHCCCEEEE	52.26	-
106	Phosphorylation	FVNHPQVSALLGEED ECCCHHHHHHCCCCC	14.14	-
109	Ubiquitination	HPQVSALLGEEDEEA CHHHHHHCCCCCHHH	8.97	21890473
110	Ubiquitination	PQVSALLGEEDEEAL HHHHHHCCCCCHHHH	36.78	21890473
110	Acetylation	PQVSALLGEEDEEAL HHHHHHCCCCCHHHH	36.78	19608861
110	Ubiquitination	PQVSALLGEEDEEAL HHHHHHCCCCCHHHH	36.78	19608861
110	Ubiquitination	PQVSALLGEEDEEAL HHHHHHCCCCCHHHH	36.78	21890473
119	Phosphorylation	EDEEALHYLTRVEVT CCHHHHHHHEEEEEE	15.60	19608861
119 (in isoform 2)	Ubiquitination	-	15.60	21890473
126	Phosphorylation	YLTRVEVTEFEDIKS HHEEEEEEEEECCCC	22.81	23403867
127	Ubiquitination	LTRVEVTEFEDIKSG HEEEEEEEEECCCCC	52.82	21890473
128	Ubiquitination	TRVEVTEFEDIKSGY EEEEEEEEECCCCCE	8.15	21890473
128	Acetylation	TRVEVTEFEDIKSGY EEEEEEEEECCCCCE	8.15	19608861
128	Ubiquitination	TRVEVTEFEDIKSGY EEEEEEEEECCCCCE	8.15	19608861
128	Ubiquitination	TRVEVTEFEDIKSGY EEEEEEEEECCCCCE	8.15	21890473
131	Ubiquitination	EVTEFEDIKSGYRID EEEEEECCCCCEEEE	2.77	21890473
132	Methylation	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	22634955
132	Acetylation	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	22634955
132	Ubiquitination	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	22053931
132	2-Hydroxyisobutyrylation	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	-
132	Malonylation	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	26320211
132	Ubiquitination	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	21890473
132 (in isoform 1)	Ubiquitination	-	50.58	21890473
132	Ubiquitination	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	21890473
133	Phosphorylation	TEFEDIKSGYRIDFY EEEECCCCCEEEEEE	41.20	22167270
135	Phosphorylation	FEDIKSGYRIDFYFD EECCCCCEEEEEEEC	16.10	23403867
137 (in isoform 2)	Ubiquitination	-	3.02	21890473
140	Phosphorylation	SGYRIDFYFDENPYF CCEEEEEEECCCCCH	13.33	27259358
141 (in isoform 2)	Ubiquitination	-	10.83	21890473
144	Ubiquitination	IDFYFDENPYFENKV EEEEECCCCCHHCCE	38.11	21890473
145	Ubiquitination	DFYFDENPYFENKVL EEEECCCCCHHCCEE	32.89	21890473
145	Ubiquitination	DFYFDENPYFENKVL EEEECCCCCHHCCEE	32.89	21890473
146	Phosphorylation	FYFDENPYFENKVLS EEECCCCCHHCCEEC	34.80	27273156
149	Ubiquitination	DENPYFENKVLSKEF CCCCCHHCCEECEEE	29.81	21890473
150	Acetylation	ENPYFENKVLSKEFH CCCCHHCCEECEEEE	37.04	19608861
150	Ubiquitination	ENPYFENKVLSKEFH CCCCHHCCEECEEEE	37.04	21890473
150	2-Hydroxyisobutyrylation	ENPYFENKVLSKEFH CCCCHHCCEECEEEE	37.04	-
150	Ubiquitination	ENPYFENKVLSKEFH CCCCHHCCEECEEEE	37.04	21890473
150 (in isoform 1)	Ubiquitination	-	37.04	21890473
150	Ubiquitination	ENPYFENKVLSKEFH CCCCHHCCEECEEEE	37.04	21890473
154	Acetylation	FENKVLSKEFHLNES HHCCEECEEEECCCC	61.30	23954790
154	Ubiquitination	FENKVLSKEFHLNES HHCCEECEEEECCCC	61.30	21890473
154 (in isoform 2)	Ubiquitination	-	61.30	21890473
154	2-Hydroxyisobutyrylation	FENKVLSKEFHLNES HHCCEECEEEECCCC	61.30	-
154 (in isoform 1)	Ubiquitination	-	61.30	21890473
159 (in isoform 2)	Ubiquitination	-	32.58	21890473
161	Phosphorylation	KEFHLNESGDPSSKS EEEECCCCCCCCCCC	47.63	30266825
165	Phosphorylation	LNESGDPSSKSTEIK CCCCCCCCCCCCEEE	55.95	30266825
166	Phosphorylation	NESGDPSSKSTEIKW CCCCCCCCCCCEEEE	35.69	30266825
167	Acetylation	ESGDPSSKSTEIKWK CCCCCCCCCCEEEEC	66.78	23954790
167	Ubiquitination	ESGDPSSKSTEIKWK CCCCCCCCCCEEEEC	66.78	-
167	2-Hydroxyisobutyrylation	ESGDPSSKSTEIKWK CCCCCCCCCCEEEEC	66.78	-
167	Malonylation	ESGDPSSKSTEIKWK CCCCCCCCCCEEEEC	66.78	26320211
167 (in isoform 1)	Ubiquitination	-	66.78	21890473
172	Acetylation	SSKSTEIKWKSGKDL CCCCCEEEECCCCCH	42.19	19608861
172	Ubiquitination	SSKSTEIKWKSGKDL CCCCCEEEECCCCCH	42.19	2189047
172	2-Hydroxyisobutyrylation	SSKSTEIKWKSGKDL CCCCCEEEECCCCCH	42.19	-
172 (in isoform 1)	Ubiquitination	-	42.19	21890473
175	Phosphorylation	STEIKWKSGKDLTKR CCEEEECCCCCHHHH	50.38	-
181	Ubiquitination	KSGKDLTKRSSQTQN CCCCCHHHHHHHHHC	58.54	-
183	Phosphorylation	GKDLTKRSSQTQNKA CCCHHHHHHHHHCHH	28.49	30576142
184	Phosphorylation	KDLTKRSSQTQNKAS CCHHHHHHHHHCHHH	41.08	-
186	O-linked_Glycosylation	LTKRSSQTQNKASRK HHHHHHHHHCHHHHH	35.74	30379171
189	Ubiquitination	RSSQTQNKASRKRQH HHHHHHCHHHHHHHH	37.61	-
191	Phosphorylation	SQTQNKASRKRQHEE HHHHCHHHHHHHHCC	39.69	-
201	Phosphorylation	RQHEEPESFFTWFTD HHHCCCHHHHHHCCC	36.05	22468782
207	Phosphorylation	ESFFTWFTDHSDAGA HHHHHHCCCCCCCCH	25.10	22468782
210	Phosphorylation	FTWFTDHSDAGADEL HHHCCCCCCCCHHHH	31.78	22468782

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
9	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
9	S	Phosphorylation	Kinase	PIK3CG	P48736	PSP
93	S	Phosphorylation	Kinase	PIK3CG	P48736	PSP
171	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
11	K	Acetylation	19608861
Isoform 2 is acetylated on Lys-11.
15	S	Phosphorylation	20068231
Isoform 2 is phosphorylated on Ser-15 and Ser-24.
24	S	Phosphorylation	20068231
Isoform 2 is phosphorylated on Ser-15 and Ser-24.

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 SET_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THAP7_HUMAN	THAP7	physical	16189514
NDKA_HUMAN	NME1	physical	12628186
CD5R1_HUMAN	CDK5R1	physical	11741927
SETBP_HUMAN	SETBP1	physical	11231286
GRAA_HUMAN	GZMA	physical	11555662
AN32A_HUMAN	ANP32A	physical	11909973
HMGB2_HUMAN	HMGB2	physical	11909973
TAF1A_HUMAN	TAF1A	physical	11163245
AN32A_HUMAN	ANP32A	physical	11163245
TREX1_HUMAN	TREX1	physical	16818237
G3P_HUMAN	GAPDH	physical	16474839
CCNB1_HUMAN	CCNB1	physical	16474839
H31_HUMAN	HIST1H3A	physical	19358706
H2B1A_HUMAN	HIST1H2BA	physical	19358706
A4_HUMAN	APP	physical	16162853
APBB1_HUMAN	APBB1	physical	15592452
XPO1_HUMAN	XPO1	physical	15239126
NUP88_HUMAN	NUP88	physical	15239126
SET_HUMAN	SET	physical	10490631
SET_HUMAN	SET	physical	10390352
H31_HUMAN	HIST1H3A	physical	15100215
GCR_HUMAN	NR3C1	physical	18096310
PTPA_HUMAN	PPP2R4	physical	21419339
H11_HUMAN	HIST1H1A	physical	21940793
P53_HUMAN	TP53	physical	21911363
SMAP_HUMAN	C11orf58	physical	22939629
IRF1_HUMAN	IRF1	physical	23134341
THAP7_HUMAN	THAP7	physical	21988832
FRIH_HUMAN	FTH1	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
HS105_HUMAN	HSPH1	physical	22863883
PUR6_HUMAN	PAICS	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SPT5H_HUMAN	SUPT5H	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
THAP7_HUMAN	THAP7	physical	25416956
F111B_HUMAN	FAM111B	physical	25416956
VPS72_HUMAN	VPS72	physical	26344197
ELAV1_HUMAN	ELAVL1	physical	11565755
TIF1B_HUMAN	TRIM28	physical	25818296
REPI1_HUMAN	REPIN1	physical	28514442
ZDBF2_HUMAN	ZDBF2	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
HSP7E_HUMAN	HSPA14	physical	28514442
TSYL2_HUMAN	TSPYL2	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 SET_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-83; LYS-132; LYS-150 ANDLYS-172, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-7, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.	19007248 [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-7, AND MASSSPECTROMETRY.	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-7 (ISOFORM 1) AND SER-15(ISOFORM 2), AND MASS SPECTROMETRY.	17081983 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-154, AND MASSSPECTROMETRY.	18781797 [Abstract]

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