ATF2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATF2_RAT
• UniProt AC: Q00969
• Protein Name: Cyclic AMP-dependent transcription factor ATF-2
• Gene Name: Atf2
• Organism: Rattus norvegicus (Rat).
• 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: MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTNDEKEIPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRAQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDLSVPSSPHTEAIQHSSVSTSNGVSSTSKTEAGATSVLTQMADQSTEPALSQIVMAPSSQAQPSGS

Overview of Protein Modification Sites with Functional and Structural Information

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	28432305
51	Phosphorylation	SVIVADQTPTPTRFL CEEEECCCCCCCHHH	29.67	12196528
53	Phosphorylation	IVADQTPTPTRFLKN EEECCCCCCCHHHHC	40.45	12196528
55	Phosphorylation	ADQTPTPTRFLKNCE ECCCCCCCHHHHCHH	36.21	23712012
72	Phosphorylation	GLFNELASPFENEFK CCHHHHCCCCHHHHH	42.62	23984901
87	Acetylation	KASEDDIKKMPLDLS HCCHHHHHHCCCCCC	50.44	22902405
94	Phosphorylation	KKMPLDLSPLATPII HHCCCCCCCCCCHHH	19.96	23712012
98	Phosphorylation	LDLSPLATPIIRSKI CCCCCCCCHHHHHCC	23.78	22108457
103	Phosphorylation	LATPIIRSKIEEPSV CCCHHHHHCCCCCCC	27.81	-
109	Phosphorylation	RSKIEEPSVVETTHQ HHCCCCCCCEEECCC	41.91	28432305
113	Phosphorylation	EEPSVVETTHQDSPL CCCCCEEECCCCCCC	20.26	28432305
114	Phosphorylation	EPSVVETTHQDSPLP CCCCEEECCCCCCCC	12.20	28432305
118	Phosphorylation	VETTHQDSPLPHPES EEECCCCCCCCCCCC	23.05	28432305
125	Phosphorylation	SPLPHPESTTNDEKE CCCCCCCCCCCCCCC	45.01	28432305
126	Phosphorylation	PLPHPESTTNDEKEI CCCCCCCCCCCCCCC	28.14	28432305
127	Phosphorylation	LPHPESTTNDEKEIP CCCCCCCCCCCCCCC	50.37	28432305
235	Phosphorylation	VPLVRPVTMVPSVPG ECEEEECEECCCCCC	18.35	28432305
239	Phosphorylation	RPVTMVPSVPGIPGP EECEECCCCCCCCCC	29.54	28432305
247	Phosphorylation	VPGIPGPSSPQPVQS CCCCCCCCCCCCCCC	61.64	27097102
248	Phosphorylation	PGIPGPSSPQPVQSE CCCCCCCCCCCCCCH	30.59	27097102
254	Phosphorylation	SSPQPVQSEAKMRLK CCCCCCCCHHHHHHH	39.49	28432305
289	Phosphorylation	SGLVRAQSEESRPQS CCCCCCCCCCCCCCC	42.20	27097102
292	Phosphorylation	VRAQSEESRPQSLQQ CCCCCCCCCCCCCCC	45.25	27097102
296	Phosphorylation	SEESRPQSLQQPATS CCCCCCCCCCCCCCC	30.72	27097102
302	Phosphorylation	QSLQQPATSTTETPA CCCCCCCCCCCCCCC	33.03	23984901
303	Phosphorylation	SLQQPATSTTETPAS CCCCCCCCCCCCCCC	35.12	23984901
304	Phosphorylation	LQQPATSTTETPASP CCCCCCCCCCCCCCC	25.05	23984901
305	Phosphorylation	QQPATSTTETPASPA CCCCCCCCCCCCCCC	37.31	27097102
307	Phosphorylation	PATSTTETPASPAHT CCCCCCCCCCCCCCC	23.28	27097102
310	Phosphorylation	STTETPASPAHTTPQ CCCCCCCCCCCCCCC	24.67	27097102
314	Phosphorylation	TPASPAHTTPQTQNT CCCCCCCCCCCCCCC	42.13	27097102
315	Phosphorylation	PASPAHTTPQTQNTS CCCCCCCCCCCCCCC	11.97	27097102
318	Phosphorylation	PAHTTPQTQNTSGRR CCCCCCCCCCCCCHH	25.62	23984901
321	Phosphorylation	TTPQTQNTSGRRRRA CCCCCCCCCCHHHHH	23.81	23984901
322	Phosphorylation	TPQTQNTSGRRRRAA CCCCCCCCCHHHHHC	37.54	27097102
339	Acetylation	DPDEKRRKFLERNRA CCHHHHHHHHHHHHH	59.33	-
349	Phosphorylation	ERNRAAASRCRQKRK HHHHHHHHHHHHHHH	27.47	-
356	Acetylation	SRCRQKRKVWVQSLE HHHHHHHHHHHHHHH	47.70	-
419	Phosphorylation	HTADKDDSSEDLSVP CCCCCCCCCCCCCCC	45.84	30181290
420	Phosphorylation	TADKDDSSEDLSVPS CCCCCCCCCCCCCCC	41.97	30181290
424	Phosphorylation	DDSSEDLSVPSSPHT CCCCCCCCCCCCCCC	44.28	30181290
427	Phosphorylation	SEDLSVPSSPHTEAI CCCCCCCCCCCCHHC	55.11	30181290
428	Phosphorylation	EDLSVPSSPHTEAIQ CCCCCCCCCCCHHCC	18.03	30181290
431	Phosphorylation	SVPSSPHTEAIQHSS CCCCCCCCHHCCCCC	30.42	30181290
437	Phosphorylation	HTEAIQHSSVSTSNG CCHHCCCCCCCCCCC	18.96	30181290
438	Phosphorylation	TEAIQHSSVSTSNGV CHHCCCCCCCCCCCC	20.26	30181290
440	Phosphorylation	AIQHSSVSTSNGVSS HCCCCCCCCCCCCCC	28.24	30181290
441	Phosphorylation	IQHSSVSTSNGVSST CCCCCCCCCCCCCCC	24.85	30181290
472	Phosphorylation	QSTEPALSQIVMAPS CCCCCHHHHHEECCC	21.70	-
480	Phosphorylation	QIVMAPSSQAQPSGS HHEECCCHHCCCCCC	28.60	-

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	Q64617	Uniprot
44	S	Phosphorylation	Kinase	VRK1	-	Uniprot
55	T	Phosphorylation	Kinase	VRK1	-	Uniprot
103	S	Phosphorylation	Kinase	PRKCA	P05696	Uniprot
103	S	Phosphorylation	Kinase	PRKCB	P68403	Uniprot
322	S	Phosphorylation	Kinase	PRKCA	P05696	Uniprot
322	S	Phosphorylation	Kinase	PRKCB	P68403	Uniprot
349	S	Phosphorylation	Kinase	PRKCA	P05696	Uniprot
349	S	Phosphorylation	Kinase	PRKCB	P68403	Uniprot
472	S	Phosphorylation	Kinase	ATM	-	Uniprot
480	S	Phosphorylation	Kinase	ATM	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	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.	22673903
51	T	Phosphorylation	Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.	22673903
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.	22673903
53	T	Acetylation	Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.	22673903
53	T	Phosphorylation	Phosphorylation at Thr-51 or Thr-53 enhances acetylation of histones H2B and H4.	22673903
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.	22673903
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.

Oops, there are no SNP-PTM records of ATF2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEBPA_HUMAN	CEBPA	physical	9139739
CEBPB_HUMAN	CEBPB	physical	9139739

Drug and Disease Associations

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