dbPTM

TOE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOE1_HUMAN
UniProt AC	Q96GM8
Protein Name	Target of EGR1 protein 1
Gene Name	TOE1
Organism	Homo sapiens (Human).
Sequence Length	510
Subcellular Localization	Nucleus, nucleolus . Nucleus speckle . Localizes to nuclear speckles.
Protein Description	Inhibits cell growth rate and cell cycle. Induces CDKN1A expression as well as TGF-beta expression. Mediates the inhibitory growth effect of EGR1. Involved in the maturation of snRNAs and snRNA 3'-tail processing. [PubMed: 28092684]
Protein Sequence	MAADSDDGAVSAPAASDGGVSKSTTSGEELVVQVPVVDVQSNNFKEMWPSLLLAIKTANFVAVDTELSGLGDRKSLLNQCIEERYKAVCHAARTRSILSLGLACFKRQPDKGEHSYLAQVFNLTLLCMEEYVIEPKSVQFLIQHGFNFNQQYAQGIPYHKGNDKGDESQSQSVRTLFLELIRARRPLVLHNGLIDLVFLYQNFYAHLPESLGTFTADLCEMFPAGIYDTKYAAEFHARFVASYLEYAFRKCERENGKQRAAGSPHLTLEFCNYPSSMRDHIDYRCCLPPATHRPHPTSICDNFSAYGWCPLGPQCPQSHDIDLIIDTDEAAAEDKRRRRRRREKRKRALLNLPGTQTSGEAKDGPPKKQVCGDSIKPEETEQEVAADETRNLPHSKQGNKNDLEMGIKAARPEIADRATSEVPGSQASPNPVPGDGLHRAGFDAFMTGYVMAYVEVSQGPQPCSSGPWLPECHNKVYLSGKAVPLTVAKSQFSRSSKAHNQKMKLTWGSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAADSDDGA ------CCCCCCCCC	21.70	19413330
5	Phosphorylation	---MAADSDDGAVSA ---CCCCCCCCCCCC	32.64	29255136
11	Phosphorylation	DSDDGAVSAPAASDG CCCCCCCCCCCCCCC	28.18	22167270
16	Phosphorylation	AVSAPAASDGGVSKS CCCCCCCCCCCCCCC	38.60	23403867
21	Phosphorylation	AASDGGVSKSTTSGE CCCCCCCCCCCCCCC	24.94	23403867
33	Ubiquitination	SGEELVVQVPVVDVQ CCCCEEEEEEEEECC	26.73	22817900
37	Ubiquitination	LVVQVPVVDVQSNNF EEEEEEEEECCCCCH	4.96	22817900
74	Ubiquitination	LSGLGDRKSLLNQCI CCCCCCHHHHHHHHH	50.63	29967540
75	O-linked_Glycosylation	SGLGDRKSLLNQCIE CCCCCHHHHHHHHHH	38.70	30379171
84	Ubiquitination	LNQCIEERYKAVCHA HHHHHHHHHHHHHHH	26.01	-
96	Phosphorylation	CHAARTRSILSLGLA HHHHHHHHHHHHEEH	27.54	28450419
99	Phosphorylation	ARTRSILSLGLACFK HHHHHHHHHEEHHHH	20.79	28450419
106	Acetylation	SLGLACFKRQPDKGE HHEEHHHHCCCCCCC	50.43	26051181
114	Ubiquitination	RQPDKGEHSYLAQVF CCCCCCCCCHHHHHH	30.34	22817900
118	Ubiquitination	KGEHSYLAQVFNLTL CCCCCHHHHHHHHHE	8.68	22817900
160	Ubiquitination	AQGIPYHKGNDKGDE HCCCCCCCCCCCCCH	54.27	22817900
164	Acetylation	PYHKGNDKGDESQSQ CCCCCCCCCCHHHHH	72.72	26051181
164	Ubiquitination	PYHKGNDKGDESQSQ CCCCCCCCCCHHHHH	72.72	22817900
166	Ubiquitination	HKGNDKGDESQSQSV CCCCCCCCHHHHHHH	59.10	22817900
170	Ubiquitination	DKGDESQSQSVRTLF CCCCHHHHHHHHHHH	33.43	22817900
354	Ubiquitination	RALLNLPGTQTSGEA HHHHCCCCCCCCCCC	33.35	22505724
355	Phosphorylation	ALLNLPGTQTSGEAK HHHCCCCCCCCCCCC	27.08	21712546
357	Phosphorylation	LNLPGTQTSGEAKDG HCCCCCCCCCCCCCC	38.24	25159151
358	Phosphorylation	NLPGTQTSGEAKDGP CCCCCCCCCCCCCCC	25.48	25159151
368	Acetylation	AKDGPPKKQVCGDSI CCCCCCCCCCCCCCC	54.45	26051181
368	Ubiquitination	AKDGPPKKQVCGDSI CCCCCCCCCCCCCCC	54.45	29967540
374	Phosphorylation	KKQVCGDSIKPEETE CCCCCCCCCCHHHHH	20.14	23312004
376	Acetylation	QVCGDSIKPEETEQE CCCCCCCCHHHHHHH	50.78	26051181
376	Ubiquitination	QVCGDSIKPEETEQE CCCCCCCCHHHHHHH	50.78	29967540
401	Ubiquitination	HSKQGNKNDLEMGIK HHCCCCHHHHHHHHH	64.20	-
419	Phosphorylation	PEIADRATSEVPGSQ HHHHHHCCCCCCCCC	26.72	29255136
420	Phosphorylation	EIADRATSEVPGSQA HHHHHCCCCCCCCCC	35.30	30266825
425	Phosphorylation	ATSEVPGSQASPNPV CCCCCCCCCCCCCCC	19.26	23401153
428	Phosphorylation	EVPGSQASPNPVPGD CCCCCCCCCCCCCCC	19.99	23401153
435	Ubiquitination	SPNPVPGDGLHRAGF CCCCCCCCCCCCCCC	50.87	22505724
481	Acetylation	NKVYLSGKAVPLTVA CEEEECCCEEECCHH	42.72	26051181
481	Ubiquitination	NKVYLSGKAVPLTVA CEEEECCCEEECCHH	42.72	22505724
487	Ubiquitination	GKAVPLTVAKSQFSR CCEEECCHHHHHHCC	9.22	22505724
489	Ubiquitination	AVPLTVAKSQFSRSS EEECCHHHHHHCCCC	40.22	29967540
509	Phosphorylation	KMKLTWGSS------ CCCCEECCC------	25.16	21712546
510	Phosphorylation	MKLTWGSS------- CCCEECCC-------	40.06	22617229

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 TOE1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TOE1_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 TOE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APLP1_HUMAN	APLP1	physical	16169070
SUMO1_HUMAN	SUMO1	physical	16169070
RS3A_HUMAN	RPS3A	physical	16169070
SH3G3_HUMAN	SH3GL3	physical	16169070
PYM1_HUMAN	WIBG	physical	22939629
SF3B2_HUMAN	SF3B2	physical	22365833
SF3B3_HUMAN	SF3B3	physical	22365833
U2AF1_HUMAN	U2AF1	physical	22365833
RBM39_HUMAN	RBM39	physical	22365833
SRSF6_HUMAN	SRSF6	physical	22365833
LSM4_HUMAN	LSM4	physical	22365833
PRCC_HUMAN	PRCC	physical	22365833
RED_HUMAN	IK	physical	22365833
RBM8A_HUMAN	RBM8A	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
PP1A_HUMAN	PPP1CA	physical	22365833
AGGF1_HUMAN	AGGF1	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878

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 TOE1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-5, AND MASSSPECTROMETRY.	18691976 [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-5, AND MASSSPECTROMETRY.	19007248 [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-5, AND MASSSPECTROMETRY.	17081983 [Abstract]