dbPTM

ATF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATF2_MOUSE
UniProt AC	P16951
Protein Name	Cyclic AMP-dependent transcription factor ATF-2
Gene Name	Atf2
Organism	Mus musculus (Mouse).
Sequence Length	487
Subcellular Localization	Nucleus. Cytoplasm. Mitochondrion outer membrane. Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress
Protein Description	Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type (By similarity)..
Protein Sequence	MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDLSVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPPSQAQPSGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	HKHKHEMTLKFGPAR EECCCEEEEEECCCC	24.66	-
44	Phosphorylation	FGPARNDSVIVADQT ECCCCCCCEEEECCC	19.79	21082442
51	Phosphorylation	SVIVADQTPTPTRFL CEEEECCCCCCCHHH	29.67	27087446
53	Phosphorylation	IVADQTPTPTRFLKN EEECCCCCCCHHHHC	40.45	27087446
55	Phosphorylation	ADQTPTPTRFLKNCE ECCCCCCCHHHHCHH	36.21	27742792
72	Phosphorylation	GLFNELASPFENEFK CCHHHHCCCCHHHHH	42.62	27087446
94	Phosphorylation	KKMPLDLSPLATPII HHCCCCCCCCCCHHH	19.96	25521595
98	Phosphorylation	LDLSPLATPIIRSKI CCCCCCCCHHHHHCC	23.78	21082442
103	Phosphorylation	LATPIIRSKIEEPSV CCCHHHHHCCCCCCC	27.81	-
109	Phosphorylation	RSKIEEPSVVETTHQ HHCCCCCCCEEECCC	41.91	26643407
113	Phosphorylation	EEPSVVETTHQDSPL CCCCCEEECCCCCCC	20.26	26745281
114	Phosphorylation	EPSVVETTHQDSPLP CCCCEEECCCCCCCC	12.20	27087446
118	Phosphorylation	VETTHQDSPLPHPES EEECCCCCCCCCCCC	23.05	25266776
118 (in isoform 2)	Phosphorylation	-	23.05	29514104
125	Phosphorylation	SPLPHPESTTSDEKE CCCCCCCCCCCCCCC	41.24	26745281
126	Phosphorylation	PLPHPESTTSDEKEV CCCCCCCCCCCCCCC	28.76	26745281
127	Phosphorylation	LPHPESTTSDEKEVP CCCCCCCCCCCCCCC	43.38	26745281
128	Phosphorylation	PHPESTTSDEKEVPL CCCCCCCCCCCCCCC	43.81	28066266
235	Phosphorylation	VPLVRPVTMVPSVPG ECEEEECEECCCCCC	18.35	29233185
239	Phosphorylation	RPVTMVPSVPGIPGP EECEECCCCCCCCCC	29.54	29233185
247	Phosphorylation	VPGIPGPSSPQPVQS CCCCCCCCCCCCCCC	61.64	25159016
248	Phosphorylation	PGIPGPSSPQPVQSE CCCCCCCCCCCCCCH	30.59	22942356
254	Phosphorylation	SSPQPVQSEAKMRLK CCCCCCCCHHHHHHH	39.49	25159016
265	Phosphorylation	MRLKAALTQQHPPVT HHHHHHHHCCCCCCC	22.81	-
272	Phosphorylation	TQQHPPVTNGDTVKG HCCCCCCCCCCCCCC	38.98	-
272	O-linked_Glycosylation	TQQHPPVTNGDTVKG HCCCCCCCCCCCCCC	38.98	22517741
287	Phosphorylation	HGSGLVRTQSEESRP CCCCCCCCCCCCCCC	29.03	25159016
289	Phosphorylation	SGLVRTQSEESRPQS CCCCCCCCCCCCCCC	42.59	21082442
292	Phosphorylation	VRTQSEESRPQSLQQ CCCCCCCCCCCCCCC	45.25	25159016
296	Phosphorylation	SEESRPQSLQQPATS CCCCCCCCCCCCCCC	30.72	25159016
302	Phosphorylation	QSLQQPATSTTETPA CCCCCCCCCCCCCCC	33.03	25159016
303	Phosphorylation	SLQQPATSTTETPAS CCCCCCCCCCCCCCC	35.12	25159016
304	Phosphorylation	LQQPATSTTETPASP CCCCCCCCCCCCCCC	25.05	25159016
305	Phosphorylation	QQPATSTTETPASPA CCCCCCCCCCCCCCC	37.31	25159016
307	Phosphorylation	PATSTTETPASPAHT CCCCCCCCCCCCCCC	23.28	25159016
310	Phosphorylation	STTETPASPAHTTPQ CCCCCCCCCCCCCCC	24.67	27087446
314	Phosphorylation	TPASPAHTTPQTQNT CCCCCCCCCCCCCCC	42.13	25159016
315	Phosphorylation	PASPAHTTPQTQNTS CCCCCCCCCCCCCCC	11.97	25159016
318	Phosphorylation	PAHTTPQTQNTSGRR CCCCCCCCCCCCCHH	25.62	25159016
321	Phosphorylation	TTPQTQNTSGRRRRA CCCCCCCCCCHHHHH	23.81	25159016
322	Phosphorylation	TPQTQNTSGRRRRAA CCCCCCCCCHHHHHC	37.54	25159016
339	Acetylation	DPDEKRRKFLERNRA CCHHHHHHHHHHHHH	59.33	-
349	Phosphorylation	ERNRAAASRCRQKRK HHHHHHHHHHHHHHH	27.47	-
356	Acetylation	SRCRQKRKVWVQSLE HHHHHHHHHHHHHHH	47.70	-
391	Ubiquitination	RNEVAQLKQLLLAHK HHHHHHHHHHHHHCC	27.16	-
409	Phosphorylation	VTAMQKKSGYHTADK CEEEHHHCCCCCCCC	52.17	26643407
411	Phosphorylation	AMQKKSGYHTADKDD EEHHHCCCCCCCCCC	11.77	26643407
413	Phosphorylation	QKKSGYHTADKDDSS HHHCCCCCCCCCCCC	28.24	26643407
419	Phosphorylation	HTADKDDSSEDLSVP CCCCCCCCCCCCCCC	45.84	26643407
420	Phosphorylation	TADKDDSSEDLSVPS CCCCCCCCCCCCCCC	41.97	26643407
424	Phosphorylation	DDSSEDLSVPSSPHT CCCCCCCCCCCCCCC	44.28	26643407
427	Phosphorylation	SEDLSVPSSPHTEAI CCCCCCCCCCCCHHC	55.11	26643407
428	Phosphorylation	EDLSVPSSPHTEAIQ CCCCCCCCCCCHHCC	18.03	26643407
431	Phosphorylation	SVPSSPHTEAIQHSS CCCCCCCCHHCCCCC	30.42	26643407
437	Phosphorylation	HTEAIQHSSVSTSNG CCHHCCCCCCCCCCC	18.96	26643407
438	Phosphorylation	TEAIQHSSVSTSNGV CHHCCCCCCCCCCCC	20.26	26643407
440	Phosphorylation	AIQHSSVSTSNGVSS HCCCCCCCCCCCCCC	28.24	26643407
441	Phosphorylation	IQHSSVSTSNGVSST CCCCCCCCCCCCCCC	24.85	26643407
442	Phosphorylation	QHSSVSTSNGVSSTS CCCCCCCCCCCCCCH	24.87	26643407
446	Phosphorylation	VSTSNGVSSTSKAEA CCCCCCCCCCHHHHH	29.33	26643407
447	Phosphorylation	STSNGVSSTSKAEAV CCCCCCCCCHHHHHH	34.00	26643407
448	Phosphorylation	TSNGVSSTSKAEAVA CCCCCCCCHHHHHHH	27.09	26643407
449	Phosphorylation	SNGVSSTSKAEAVAT CCCCCCCHHHHHHHH	31.64	26643407
472	Phosphorylation	QSTEPALSQIVMAPP CCCCCHHHHHEECCH	21.70	-
480	Phosphorylation	QIVMAPPSQAQPSGS HHEECCHHHCCCCCC	36.77	-

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
34	T	Phosphorylation	Kinase	PRKCH	P23298	Uniprot
51	T	Phosphorylation	Kinase	MAPK11	Q9WUI1	Uniprot
51	T	Phosphorylation	Kinase	P38A	P47811	PSP
51	T	Phosphorylation	Kinase	MAPK9	P45984	GPS
51	T	Phosphorylation	Kinase	P38A	Q16539	PSP
51	T	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
51	T	Phosphorylation	Kinase	JNK1	P45983	PSP
53	T	Phosphorylation	Kinase	ERK2	P63085	PSP
53	T	Phosphorylation	Kinase	MAPK9	P45984	GPS
53	T	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
53	T	Phosphorylation	Kinase	JNK1	P45983	PSP
53	T	Phosphorylation	Kinase	ERK1	Q63844	PSP
53	T	Phosphorylation	Kinase	ERK1	P27361	PSP
53	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
53	T	Phosphorylation	Kinase	MAPK11	Q9WUI1	Uniprot
53	T	Phosphorylation	Kinase	MAPK12	O08911	Uniprot
53	T	Phosphorylation	Kinase	P38A	Q16539	PSP
53	T	Phosphorylation	Kinase	P38A	P47811	PSP
53	T	Phosphorylation	Kinase	PLK3	Q60806	Uniprot
55	T	Phosphorylation	Kinase	VRK1	Q80X41	Uniprot
103	S	Phosphorylation	Kinase	PRKCB	P68404	Uniprot
103	S	Phosphorylation	Kinase	PRKCA	P20444	Uniprot
322	S	Phosphorylation	Kinase	PRKCB	P68404	Uniprot
322	S	Phosphorylation	Kinase	PRKCA	P20444	Uniprot
349	S	Phosphorylation	Kinase	PRKCB	P68404	Uniprot
349	S	Phosphorylation	Kinase	PRKCA	P20444	Uniprot
472	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot
480	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	S	Phosphorylation	-
Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its transcriptional activity.
51	T	Acetylation	-
Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.
51	T	Phosphorylation	-
Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.
51	T	Phosphorylation	-
Phosphorylation of Thr-51 by MAPK14 and MAPK11, and at Thr-53 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity.
53	T	Acetylation	-
Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.
53	T	Phosphorylation	-
Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.
53	T	Phosphorylation	-
Phosphorylation of Thr-51 by MAPK14 and MAPK11, and at Thr-53 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity.
55	T	Phosphorylation	-
Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its transcriptional activity.
103	S	Phosphorylation	-
Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its transcriptional activity.
472	S	Phosphorylation	-
ATM-mediated phosphorylation at Ser-472 and Ser-480 stimulates its function in DNA damage response.
480	S	Phosphorylation	-
ATM-mediated phosphorylation at Ser-472 and Ser-480 stimulates its function in DNA damage response.

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 ATF2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BARX2_MOUSE	Barx2	physical	20211142
ATF2_MOUSE	Atf2	physical	12052888
EP300_MOUSE	Ep300	physical	10327051
JDP2_MOUSE	Jdp2	physical	11231009
SSXT_MOUSE	Ss18	physical	22439931
TLE1_MOUSE	Tle1	physical	22439931
BRCA1_MOUSE	Brca1	physical	17700520
PO2F1_MOUSE	Pou2f1	physical	17700520

Drug and Disease Associations

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

Regulatory Network of ATF2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND THR-53, AND MASSSPECTROMETRY.	17242355 [Abstract]

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