dbPTM

ETS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ETS2_HUMAN
UniProt AC	P15036
Protein Name	Protein C-ets-2
Gene Name	ETS2
Organism	Homo sapiens (Human).
Sequence Length	469
Subcellular Localization	Nucleus.
Protein Description	Transcription factor activating transcription. Binds specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in gene promoters and stimulates transcription..
Protein Sequence	MNDFGIKNMDQVAPVANSYRGTLKRQPAFDTFDGSLFAVFPSLNEEQTLQEVPTGLDSISHDSANCELPLLTPCSKAVMSQALKATFSGFKKEQRRLGIPKNPWLWSEQQVCQWLLWATNEFSLVNVNLQRFGMNGQMLCNLGKERFLELAPDFVGDILWEHLEQMIKENQEKTEDQYEENSHLTSVPHWINSNTLGFGTEQAPYGMQTQNYPKGGLLDSMCPASTPSVLSSEQEFQMFPKSRLSSVSVTYCSVSQDFPGSNLNLLTNNSGTPKDHDSPENGADSFESSDSLLQSWNSQSSLLDVQRVPSFESFEDDCSQSLCLNKPTMSFKDYIQERSDPVEQGKPVIPAAVLAGFTGSGPIQLWQFLLELLSDKSCQSFISWTGDGWEFKLADPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTSGKRYVYRFVCDLQNLLGFTPEELHAILGVQPDTED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Sumoylation	-MNDFGIKNMDQVAP -CCCCCCCCHHHHHH	46.74	-
7	Ubiquitination	-MNDFGIKNMDQVAP -CCCCCCCCHHHHHH	46.74	-
7	Sumoylation	-MNDFGIKNMDQVAP -CCCCCCCCHHHHHH	46.74	-
18	Phosphorylation	QVAPVANSYRGTLKR HHHHCHHCCCCCCCC	13.38	25159151
19	Phosphorylation	VAPVANSYRGTLKRQ HHHCHHCCCCCCCCC	16.93	21712546
22	Phosphorylation	VANSYRGTLKRQPAF CHHCCCCCCCCCCCC	21.80	25159151
24	Sumoylation	NSYRGTLKRQPAFDT HCCCCCCCCCCCCCC	49.15	-
24	Sumoylation	NSYRGTLKRQPAFDT HCCCCCCCCCCCCCC	49.15	-
72	Phosphorylation	NCELPLLTPCSKAVM CCCCCCCCCCCHHHH	29.90	22128184
80	Phosphorylation	PCSKAVMSQALKATF CCCHHHHHHHHHHHH	13.00	28555341
84	Sumoylation	AVMSQALKATFSGFK HHHHHHHHHHHCCHH	48.69	-
84	Ubiquitination	AVMSQALKATFSGFK HHHHHHHHHHHCCHH	48.69	29967540
84	Sumoylation	AVMSQALKATFSGFK HHHHHHHHHHHCCHH	48.69	-
88	Phosphorylation	QALKATFSGFKKEQR HHHHHHHCCHHHHHH	38.68	25159151
91	Ubiquitination	KATFSGFKKEQRRLG HHHHCCHHHHHHHHC	59.95	29967540
92	Ubiquitination	ATFSGFKKEQRRLGI HHHCCHHHHHHHHCC	57.74	-
101	Sumoylation	QRRLGIPKNPWLWSE HHHHCCCCCCCCCCH	73.96	-
144	Ubiquitination	QMLCNLGKERFLELA CEEHHCCHHHHHHHC	49.21	21987572
173	Ubiquitination	MIKENQEKTEDQYEE HHHHCHHHHHHHHHH	47.66	29967540
220	Phosphorylation	PKGGLLDSMCPASTP CCCCCCCCCCCCCCC	23.43	24218572
224	Ubiquitination	LLDSMCPASTPSVLS CCCCCCCCCCCCCCC	22.55	29967540
225	Phosphorylation	LDSMCPASTPSVLSS CCCCCCCCCCCCCCC	26.45	24218572
226	Phosphorylation	DSMCPASTPSVLSSE CCCCCCCCCCCCCCH	22.99	-
228	Phosphorylation	MCPASTPSVLSSEQE CCCCCCCCCCCCHHH	35.46	-
231	Ubiquitination	ASTPSVLSSEQEFQM CCCCCCCCCHHHHHC	29.67	29967540
241	Ubiquitination	QEFQMFPKSRLSSVS HHHHCCCHHHCCCEE	36.62	21963094
246	Phosphorylation	FPKSRLSSVSVTYCS CCHHHCCCEEEEEEE	24.01	22817900
248	Phosphorylation	KSRLSSVSVTYCSVS HHHCCCEEEEEEEEC	15.64	-
255	Phosphorylation	SVTYCSVSQDFPGSN EEEEEEECCCCCCCC	14.03	25627689
278	Phosphorylation	GTPKDHDSPENGADS CCCCCCCCCCCCCCC	30.60	24144214
284	Ubiquitination	DSPENGADSFESSDS CCCCCCCCCCCCCHH	56.08	21987572
285	Phosphorylation	SPENGADSFESSDSL CCCCCCCCCCCCHHH	30.31	24144214
288	Phosphorylation	NGADSFESSDSLLQS CCCCCCCCCHHHHHH	37.12	24144214
289	Phosphorylation	GADSFESSDSLLQSW CCCCCCCCHHHHHHC	24.83	24144214
291	Phosphorylation	DSFESSDSLLQSWNS CCCCCCHHHHHHCCC	32.69	24144214
295	Phosphorylation	SSDSLLQSWNSQSSL CCHHHHHHCCCCCCC	28.35	17192257
298	Phosphorylation	SLLQSWNSQSSLLDV HHHHHCCCCCCCCCC	25.77	24719451
300	Phosphorylation	LQSWNSQSSLLDVQR HHHCCCCCCCCCCCC	23.83	24144214
301	Phosphorylation	QSWNSQSSLLDVQRV HHCCCCCCCCCCCCC	25.89	24144214
310	Phosphorylation	LDVQRVPSFESFEDD CCCCCCCCCHHCCCH	38.50	26657352
313	Phosphorylation	QRVPSFESFEDDCSQ CCCCCCHHCCCHHHH	31.74	20873877
313	Ubiquitination	QRVPSFESFEDDCSQ CCCCCCHHCCCHHHH	31.74	29967540
319	Phosphorylation	ESFEDDCSQSLCLNK HHCCCHHHHHCCCCC	29.78	20873877
321	Phosphorylation	FEDDCSQSLCLNKPT CCCHHHHHCCCCCCC	12.54	20873877
326	Ubiquitination	SQSLCLNKPTMSFKD HHHCCCCCCCCCHHH	28.99	21963094
328	Phosphorylation	SLCLNKPTMSFKDYI HCCCCCCCCCHHHHH	27.36	20873877
330	Phosphorylation	CLNKPTMSFKDYIQE CCCCCCCCHHHHHHH	31.46	20873877
332	Ubiquitination	NKPTMSFKDYIQERS CCCCCCHHHHHHHCC	42.17	21963094
381	Ubiquitination	SDKSCQSFISWTGDG CCCCCHHHEECCCCC	1.80	21963094
392	Sumoylation	TGDGWEFKLADPDEV CCCCEEEEECCHHHH	31.11	-
411	Ubiquitination	GKRKNKPKMNYEKLS HHCCCCCCCCHHHHH	41.19	24816145
416	Sumoylation	KPKMNYEKLSRGLRY CCCCCHHHHHHHHHH	41.21	-
416	Ubiquitination	KPKMNYEKLSRGLRY CCCCCHHHHHHHHHH	41.21	22505724
416	Sumoylation	KPKMNYEKLSRGLRY CCCCCHHHHHHHHHH	41.21	-
423	Phosphorylation	KLSRGLRYYYDKNII HHHHHHHHEECCCEE	16.06	-
427	Ubiquitination	GLRYYYDKNIIHKTS HHHHEECCCEEEECC	33.65	-
432	Ubiquitination	YDKNIIHKTSGKRYV ECCCEEEECCCCCCE	33.70	29967540
466	Ubiquitination	AILGVQPDTED---- HHHCCCCCCCC----	45.71	21963094
472	Ubiquitination	PDTED---------- CCCCC----------		21963094
551	Ubiquitination	----------------------------------------------------------------------------------------- -----------------------------------------------------------------------------------------		24816145
556	Ubiquitination	---------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------		22505724
572	Ubiquitination	-------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------		29967540

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
72	T	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
220	S	Phosphorylation	Kinase	CDK10	Q15131	PSP
225	S	Phosphorylation	Kinase	CDK10	Q15131	PSP
246	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
310	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
313	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
220	S	Phosphorylation	24218572
Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a phosphodegron that targets ETS2 for proteasomal degradation.
225	S	Phosphorylation	24218572
Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a phosphodegron that targets ETS2 for proteasomal degradation.

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 ETS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK10_HUMAN	CDK10	physical	11313931
ZMY11_HUMAN	ZMYND11	physical	12894593
FOS_HUMAN	FOS	physical	9334186
JUN_HUMAN	JUN	physical	9334186
ERG_HUMAN	ERG	physical	9334186
ETS1_HUMAN	ETS1	physical	9334186
CBP_HUMAN	CREBBP	physical	15572696
EP300_HUMAN	EP300	physical	15572696
CBP_HUMAN	CREBBP	physical	10358095
EP300_HUMAN	EP300	physical	10358095
CBP_HUMAN	CREBBP	physical	14722092
EP300_HUMAN	EP300	physical	14722092
P53_HUMAN	TP53	physical	18374905
XPO1_HUMAN	XPO1	physical	12860972
SRA1_HUMAN	SRA1	physical	20398657
TWST1_HUMAN	TWIST1	physical	18598946
TWST2_HUMAN	TWIST2	physical	18598946
RFWD2_HUMAN	RFWD2	physical	25117710
VPS51_HUMAN	VPS51	physical	26496610
CTDP1_HUMAN	CTDP1	physical	26496610
TF3C5_HUMAN	GTF3C5	physical	26496610
IMPCT_HUMAN	IMPACT	physical	26496610
RFWD2_HUMAN	RFWD2	physical	26496610
RM14_HUMAN	MRPL14	physical	26496610
ANKS6_HUMAN	ANKS6	physical	26496610
RFWD2_HUMAN	RFWD2	physical	26871468
DET1_HUMAN	DET1	physical	26871468
P53_HUMAN	TP53	physical	26871468

Drug and Disease Associations

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

Regulatory Network of ETS2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY.	18691976 [Abstract]

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