ATF4_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATF4_RAT
• UniProt AC: Q9ES19
• Protein Name: Cyclic AMP-dependent transcription factor ATF-4
• Gene Name: Atf4 {ECO:0000312|RGD:621863}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 347
• Subcellular Localization: Cytoplasm . Cell membrane . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Colocalizes with GABBR1 in hippocampal neuron dendritic membranes (PubMed:10924501). Colocalizes with NEK6 in the centrosome (By similarity).
• Protein Description: Transcriptional activator. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (By similarity). Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to ER stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis by regulating the transcriptional induction of BBC3/PUMA. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes (By similarity)..
• Protein Sequence: MTEMSFLNSEVLAGDLMSPFDQSGLGAEESLGLLDDYLEVAKHFKPHGFSSDKAGSSEWLAMDGLVSASDTGKEDAFSGTDWMLEKMDLKEFDFDALFRMDDLETMPDELLATLDDTCDLFAPLVQETNKEPPQTVNPIGHLPESVIKVDQAAPFTFLQPLPCSPGFLSSTPDHSFSLELGSEVDISEGDRKPDSAAYITLTPQCVKEEDTPSDSDSGICMSPESYLGSPQHSPSTSRAPPDSLPSPGVPRGSRPKPYDPPGVSVTAKVKTEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKEKADSLAKEIQYLKDLIEEVRKARGKKRVP

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
211	Phosphorylation	QCVKEEDTPSDSDSG HHHCCCCCCCCCCCC	28.15	-
213	Phosphorylation	VKEEDTPSDSDSGIC HCCCCCCCCCCCCCC	52.41	-
217	Phosphorylation	DTPSDSDSGICMSPE CCCCCCCCCCCCCHH	33.73	-
222	Phosphorylation	SDSGICMSPESYLGS CCCCCCCCHHHHCCC	22.54	-
229	Phosphorylation	SPESYLGSPQHSPST CHHHHCCCCCCCCCC	20.84	-
233	Phosphorylation	YLGSPQHSPSTSRAP HCCCCCCCCCCCCCC	18.46	-
234	Hydroxylation	LGSPQHSPSTSRAPP CCCCCCCCCCCCCCC	39.23	-
243	Phosphorylation	TSRAPPDSLPSPGVP CCCCCCCCCCCCCCC	48.21	26437020
246	Phosphorylation	APPDSLPSPGVPRGS CCCCCCCCCCCCCCC	39.31	26437020
307	Acetylation	EALTGECKELEKKNE HHHHHHHHHHHHHHH	62.12	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ATF4_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
211	T	Phosphorylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
211	T	ubiquitylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
213	S	Phosphorylation	Phosphorylation at Ser-213 by CK2 decreases its stability.	-
217	S	Phosphorylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
217	S	ubiquitylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
222	S	Phosphorylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
222	S	ubiquitylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
229	S	Phosphorylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
229	S	ubiquitylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
233	S	Phosphorylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
233	S	ubiquitylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
243	S	Phosphorylation	Phosphorylation at Ser-243 by RPS6KA3/RSK2 in osteoblasts enhances transactivation activity and promotes osteoblast differentiation (By similarity).	-
246	S	Phosphorylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-
246	S	ubiquitylation	Phosphorylated on the betaTrCP degron motif at Ser-217, followed by phosphorylation at Thr-211, Ser-222, Ser-229, Ser-233 and Ser-246, promoting interaction with BTRC and ubiquitination.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ATF4_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NF2L2_MOUSE	Nfe2l2	physical	11274184

Drug and Disease Associations

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