dbPTM

ATF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATF1_HUMAN
UniProt AC	P18846
Protein Name	Cyclic AMP-dependent transcription factor ATF-1
Gene Name	ATF1
Organism	Homo sapiens (Human).
Sequence Length	271
Subcellular Localization	Nucleus.
Protein Description	This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation..
Protein Sequence	MEDSHKSTTSETAPQPGSAVQGAHISHIAQQVSSLSESEESQDSSDSIGSSQKAHGILARRPSYRKILKDLSSEDTRGRKGDGENSGVSAAVTSMSVPTPIYQTSSGQYIAIAPNGALQLASPGTDGVQGLQTLTMTNSGSTQQGTTILQYAQTSDGQQILVPSNQVVVQTASGDMQTYQIRTTPSATSLPQTVVMTSPVTLTSQTTKTDDPQLKREIRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKTLKDLYSNKSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	ETAPQPGSAVQGAHI CCCCCCCCCCCHHHH	31.76	30576142
33	Phosphorylation	SHIAQQVSSLSESEE HHHHHHHHCCCCCHH	22.63	30576142
36	Phosphorylation	AQQVSSLSESEESQD HHHHHCCCCCHHCCC	40.81	8414969
38	Phosphorylation	QVSSLSESEESQDSS HHHCCCCCHHCCCCC	43.20	30576142
41	Phosphorylation	SLSESEESQDSSDSI CCCCCHHCCCCCCCC	34.92	30576142
47	Phosphorylation	ESQDSSDSIGSSQKA HCCCCCCCCCCHHHH	30.69	22817900
50	Phosphorylation	DSSDSIGSSQKAHGI CCCCCCCCHHHHHHH	28.11	22817900
51	Phosphorylation	SSDSIGSSQKAHGIL CCCCCCCHHHHHHHH	30.41	22817900
63	Phosphorylation	GILARRPSYRKILKD HHHHCCHHHHHHHHH	35.44	27273156
64	Phosphorylation	ILARRPSYRKILKDL HHHCCHHHHHHHHHC	20.71	26074081
69	Acetylation	PSYRKILKDLSSEDT HHHHHHHHHCCCCCC	61.16	25953088
69	Ubiquitination	PSYRKILKDLSSEDT HHHHHHHHHCCCCCC	61.16	33845483
72	Phosphorylation	RKILKDLSSEDTRGR HHHHHHCCCCCCCCC	41.64	21815630
73	Ubiquitination	KILKDLSSEDTRGRK HHHHHCCCCCCCCCC	46.95	-
73	Phosphorylation	KILKDLSSEDTRGRK HHHHHCCCCCCCCCC	46.95	21712546
76	Phosphorylation	KDLSSEDTRGRKGDG HHCCCCCCCCCCCCC	30.85	26270265
77	Ubiquitination	DLSSEDTRGRKGDGE HCCCCCCCCCCCCCC	56.06	24816145
80	Ubiquitination	SEDTRGRKGDGENSG CCCCCCCCCCCCCCC	65.27	-
104	Ubiquitination	VPTPIYQTSSGQYIA CCCCEEECCCCCEEE	14.11	-
114	Ubiquitination	GQYIAIAPNGALQLA CCEEEECCCCCEEEC	33.40	21963094
118	Ubiquitination	AIAPNGALQLASPGT EECCCCCEEECCCCC	4.55	-
121	Ubiquitination	PNGALQLASPGTDGV CCCCEEECCCCCCCC	10.75	21963094
125	Ubiquitination	LQLASPGTDGVQGLQ EEECCCCCCCCCEEE	32.72	21890473
128	Ubiquitination	ASPGTDGVQGLQTLT CCCCCCCCCEEEEEE	4.55	-
140	Ubiquitination	TLTMTNSGSTQQGTT EEEECCCCCCCCCEE	36.46	24816145
154	O-linked_Glycosylation	TILQYAQTSDGQQIL EEEEEEECCCCCEEE	22.18	20068230
159	Ubiquitination	AQTSDGQQILVPSNQ EECCCCCEEEEECCE	36.19	23000965
164	O-linked_Glycosylation	GQQILVPSNQVVVQT CCEEEEECCEEEEEE	32.20	20068230
166	Ubiquitination	QILVPSNQVVVQTAS EEEEECCEEEEEECC	33.45	21890473
169	Ubiquitination	VPSNQVVVQTASGDM EECCEEEEEECCCCC	4.38	22817900
183	Phosphorylation	MQTYQIRTTPSATSL CEEEEEEECCCCCCC	44.69	25159151
183	O-linked_Glycosylation	MQTYQIRTTPSATSL CEEEEEEECCCCCCC	44.69	20068230
184	Phosphorylation	QTYQIRTTPSATSLP EEEEEEECCCCCCCC	12.85	24732914
186	Phosphorylation	YQIRTTPSATSLPQT EEEEECCCCCCCCCE	41.93	21712546
188	Phosphorylation	IRTTPSATSLPQTVV EEECCCCCCCCCEEE	34.82	21712546
189	Phosphorylation	RTTPSATSLPQTVVM EECCCCCCCCCEEEE	37.46	24732914
189	O-linked_Glycosylation	RTTPSATSLPQTVVM EECCCCCCCCCEEEE	37.46	23301498
189	O-linked_Glycosylation	RTTPSATSLPQTVVM EECCCCCCCCCEEEE	37.46	20068230
193	Phosphorylation	SATSLPQTVVMTSPV CCCCCCCEEEEECCE	17.09	24732914
197	O-linked_Glycosylation	LPQTVVMTSPVTLTS CCCEEEEECCEEEEE	20.47	20068230
197	Phosphorylation	LPQTVVMTSPVTLTS CCCEEEEECCEEEEE	20.47	25159151
198	O-linked_Glycosylation	PQTVVMTSPVTLTSQ CCEEEEECCEEEEEC	10.16	20068230
198	Phosphorylation	PQTVVMTSPVTLTSQ CCEEEEECCEEEEEC	10.16	25159151
201	O-linked_Glycosylation	VVMTSPVTLTSQTTK EEEECCEEEEECCCC	27.92	20068230
201	Phosphorylation	VVMTSPVTLTSQTTK EEEECCEEEEECCCC	27.92	24732914
203	Phosphorylation	MTSPVTLTSQTTKTD EECCEEEEECCCCCC	14.93	24732914
203	O-linked_Glycosylation	MTSPVTLTSQTTKTD EECCEEEEECCCCCC	14.93	20068230
204	Phosphorylation	TSPVTLTSQTTKTDD ECCEEEEECCCCCCC	28.74	24732914
206	Phosphorylation	PVTLTSQTTKTDDPQ CEEEEECCCCCCCHH	29.99	24732914
206	O-linked_Glycosylation	PVTLTSQTTKTDDPQ CEEEEECCCCCCCHH	29.99	20068230
207	O-linked_Glycosylation	VTLTSQTTKTDDPQL EEEEECCCCCCCHHH	25.06	20068230
207	Phosphorylation	VTLTSQTTKTDDPQL EEEEECCCCCCCHHH	25.06	24732914
208	Sumoylation	TLTSQTTKTDDPQLK EEEECCCCCCCHHHH	54.03	28112733
208	Ubiquitination	TLTSQTTKTDDPQLK EEEECCCCCCCHHHH	54.03	21963094
209	Phosphorylation	LTSQTTKTDDPQLKR EEECCCCCCCHHHHH	43.47	24732914
215	Sumoylation	KTDDPQLKREIRLMK CCCCHHHHHHHHHHH	42.62	28112733
215	Ubiquitination	KTDDPQLKREIRLMK CCCCHHHHHHHHHHH	42.62	21963094
216	Ubiquitination	TDDPQLKREIRLMKN CCCHHHHHHHHHHHH	53.84	21963094
223	Ubiquitination	REIRLMKNREAAREC HHHHHHHHHHHHHHH	32.81	21963094
234	Ubiquitination	ARECRRKKKEYVKCL HHHHHHHHHHHHHHH	49.37	24816145
234	Sumoylation	ARECRRKKKEYVKCL HHHHHHHHHHHHHHH	49.37	-
239	Ubiquitination	RKKKEYVKCLENRVA HHHHHHHHHHHHHHH	32.00	32015554
242	Ubiquitination	KEYVKCLENRVAVLE HHHHHHHHHHHHHHH	53.08	24816145
244	Methylation	YVKCLENRVAVLENQ HHHHHHHHHHHHHHC	14.38	-
253	Ubiquitination	AVLENQNKTLIEELK HHHHHCCHHHHHHHH	34.64	23000965
260	Ubiquitination	KTLIEELKTLKDLYS HHHHHHHHHHHHHHH	55.90	21963094
261	Ubiquitination	TLIEELKTLKDLYSN HHHHHHHHHHHHHHC	52.22	23000965
263	Acetylation	IEELKTLKDLYSNKS HHHHHHHHHHHHCCC	51.42	26051181
263	Ubiquitination	IEELKTLKDLYSNKS HHHHHHHHHHHHCCC	51.42	33845483
266	Phosphorylation	LKTLKDLYSNKSV-- HHHHHHHHHCCCC--	21.97	23312004
267	Phosphorylation	KTLKDLYSNKSV--- HHHHHHHHCCCC---	45.11	21712546
268	Ubiquitination	TLKDLYSNKSV---- HHHHHHHCCCC----	27.37	21890473
270	Phosphorylation	KDLYSNKSV------ HHHHHCCCC------	36.99	29214152
271	Ubiquitination	DLYSNKSV------- HHHHCCCC-------	10.98	22817900

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
36	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
36	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
36	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
36	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
41	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
41	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
47	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
47	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
50	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
50	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
51	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
51	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
63	S	Phosphorylation	Kinase	CDK3	Q00526	Uniprot
63	S	Phosphorylation	Kinase	CAMK1	Q14012	Uniprot
63	S	Phosphorylation	Kinase	RPS6KA4	O75676	Uniprot
63	S	Phosphorylation	Kinase	MSK1	O75582	PSP
198	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
63	S	Phosphorylation	8621702
Phosphorylated at Ser-63 by RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli.
63	S	Phosphorylation	8621702
The CDK3-mediated phosphorylation at Ser-63 promotes its transactivation and transcriptional activities.
198	S	Phosphorylation	18669648
Phosphorylated at Ser-198 by HIPK2 in response to genotoxic stress.

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 ATF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSK21_HUMAN	CSNK2A1	physical	9685505
CSK2B_HUMAN	CSNK2B	physical	9685505
FOSL2_HUMAN	FOSL2	physical	22939629
SRA1_HUMAN	SRA1	physical	20398657
JUNB_HUMAN	JUNB	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612160	Angiomatoid fibrous histiocytoma (AFH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00852	Pseudoephedrine

Regulatory Network of ATF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Transcriptional regulation of ferritin and antioxidant genes by HIPK2under genotoxic stress."; Hailemariam K., Iwasaki K., Huang B.W., Sakamoto K., Tsuji Y.; J. Cell Sci. 123:3863-3871(2010). Cited for: FUNCTION AS REPRESSOR, PHOSPHORYLATION AT SER-198 BY HIPK2, ANDINTERACTION WITH HIPK2.	20980392 [Abstract]
"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-198, AND MASSSPECTROMETRY.	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-198, AND MASSSPECTROMETRY.	18669648 [Abstract]

show

show

show