dbPTM

ATF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATF2_HUMAN
UniProt AC	P15336
Protein Name	Cyclic AMP-dependent transcription factor ATF-2
Gene Name	ATF2
Organism	Homo sapiens (Human).
Sequence Length	505
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..
Protein Sequence	MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQSTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDISVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPSSQSQPSGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13 (in isoform 4)	Phosphorylation	-	10.83	28634120
44	Phosphorylation	TNEDHLAVHKHKHEM CCCCCEEEEECCCEE	8.54	15105425
46	Ubiquitination	EDHLAVHKHKHEMTL CCCEEEEECCCEEEE	47.99	-
48	Ubiquitination	HLAVHKHKHEMTLKF CEEEEECCCEEEEEE	46.17	21890473
48	Ubiquitination	HLAVHKHKHEMTLKF CEEEEECCCEEEEEE	46.17	21890473
51	Phosphorylation	VHKHKHEMTLKFGPA EEECCCEEEEEECCC	5.49	18669648
52	Phosphorylation	HKHKHEMTLKFGPAR EECCCEEEEEECCCC	24.66	22304920
53	Phosphorylation	KHKHEMTLKFGPARN ECCCEEEEEECCCCC	4.11	18669648
55	Phosphorylation	KHEMTLKFGPARNDS CCEEEEEECCCCCCC	18.65	18669648
62	Phosphorylation	FGPARNDSVIVADQT ECCCCCCCEEEECCC	19.79	22322096
69	Phosphorylation	SVIVADQTPTPTRFL CEEEECCCCCCCHHH	29.67	22322096
71	Phosphorylation	IVADQTPTPTRFLKN EEECCCCCCCHHHHC	40.45	22322096
73	Phosphorylation	ADQTPTPTRFLKNCE ECCCCCCCHHHHCHH	36.21	29255136
77	Ubiquitination	PTPTRFLKNCEEVGL CCCCHHHHCHHHCCC	57.76	-
90	Phosphorylation	GLFNELASPFENEFK CCHHHHCCCCHHHHH	42.62	25159151
94	Phosphorylation	ELASPFENEFKKASE HHCCCCHHHHHHCCH	61.45	18669648
97	Acetylation	SPFENEFKKASEDDI CCCHHHHHHCCHHHH	41.05	24179875
97	Ubiquitination	SPFENEFKKASEDDI CCCHHHHHHCCHHHH	41.05	-
98	Phosphorylation	PFENEFKKASEDDIK CCHHHHHHCCHHHHH	63.57	18669648
100	Phosphorylation	ENEFKKASEDDIKKM HHHHHHCCHHHHHHC	50.90	23312004
105	Acetylation	KASEDDIKKMPLDLS HCCHHHHHHCCCCCC	50.44	25953088
112	O-linked_Glycosylation	KKMPLDLSPLATPII HHCCCCCCCCCCHHH	19.96	30059200
112	Phosphorylation	KKMPLDLSPLATPII HHCCCCCCCCCCHHH	19.96	29255136
116	Phosphorylation	LDLSPLATPIIRSKI CCCCCCCCHHHHHCC	23.78	23927012
121	Phosphorylation	LATPIIRSKIEEPSV CCCHHHHHCCCCCCC	27.81	22817900
127	Phosphorylation	RSKIEEPSVVETTHQ HHCCCCCCCEEECCC	41.91	26657352
131	Phosphorylation	EEPSVVETTHQDSPL CCCCCEEECCCCCCC	20.26	28450419
132	Phosphorylation	EPSVVETTHQDSPLP CCCCEEECCCCCCCC	12.20	25159151
136	O-linked_Glycosylation	VETTHQDSPLPHPES EEECCCCCCCCCCCC	23.05	30059200
136	Phosphorylation	VETTHQDSPLPHPES EEECCCCCCCCCCCC	23.05	30266825
143	Phosphorylation	SPLPHPESTTSDEKE CCCCCCCCCCCCCCC	41.24	29978859
144	Phosphorylation	PLPHPESTTSDEKEV CCCCCCCCCCCCCCC	28.76	29978859
145	Phosphorylation	LPHPESTTSDEKEVP CCCCCCCCCCCCCCC	43.38	29978859
146	Phosphorylation	PHPESTTSDEKEVPL CCCCCCCCCCCCCCC	43.81	29978859
226	O-linked_Glycosylation	LHLPNGQTMPVAIPA EECCCCCCCCEEEEC	25.49	30059200
234	O-linked_Glycosylation	MPVAIPASITSSNVH CCEEEECCCCCCCCC	22.50	30059200
236	O-linked_Glycosylation	VAIPASITSSNVHVP EEEECCCCCCCCCCC	24.49	30059200
238	O-linked_Glycosylation	IPASITSSNVHVPAA EECCCCCCCCCCCCE	33.93	30059200
253	Phosphorylation	VPLVRPVTMVPSVPG ECEEEECEECCCCCC	18.35	26074081
257	Phosphorylation	RPVTMVPSVPGIPGP EECEECCCCCCCCCC	29.54	26074081
265	Phosphorylation	VPGIPGPSSPQPVQS CCCCCCCCCCCCCCC	61.64	29255136
266	Phosphorylation	PGIPGPSSPQPVQSE CCCCCCCCCCCCCCH	30.59	26657352
272	Phosphorylation	SSPQPVQSEAKMRLK CCCCCCCCHHHHHHH	39.49	29255136
283	O-linked_Glycosylation	MRLKAALTQQHPPVT HHHHHHHHCCCCCCC	22.81	30059200
283	Phosphorylation	MRLKAALTQQHPPVT HHHHHHHHCCCCCCC	22.81	-
290	O-linked_Glycosylation	TQQHPPVTNGDTVKG HCCCCCCCCCCCCCC	38.98	30059200
290	Phosphorylation	TQQHPPVTNGDTVKG HCCCCCCCCCCCCCC	38.98	-
294	O-linked_Glycosylation	PPVTNGDTVKGHGSG CCCCCCCCCCCCCCC	26.05	30059200
305	Phosphorylation	HGSGLVRTQSEESRP CCCCCCCCCCCCCCC	29.03	23927012
307	Phosphorylation	SGLVRTQSEESRPQS CCCCCCCCCCCCCCC	42.59	23927012
310	Phosphorylation	VRTQSEESRPQSLQQ CCCCCCCCCCCCCCC	45.25	23927012
314	Phosphorylation	SEESRPQSLQQPATS CCCCCCCCCCCCCCC	30.72	23927012
320	Phosphorylation	QSLQQPATSTTETPA CCCCCCCCCCCCCCC	33.03	23927012
321	Phosphorylation	SLQQPATSTTETPAS CCCCCCCCCCCCCCC	35.12	23927012
322	Phosphorylation	LQQPATSTTETPASP CCCCCCCCCCCCCCC	25.05	23927012
323	Phosphorylation	QQPATSTTETPASPA CCCCCCCCCCCCCCC	37.31	23927012
325	Phosphorylation	PATSTTETPASPAHT CCCCCCCCCCCCCCC	23.28	23927012
328	Phosphorylation	STTETPASPAHTTPQ CCCCCCCCCCCCCCC	24.67	23927012
332	Phosphorylation	TPASPAHTTPQTQST CCCCCCCCCCCCCCC	42.13	30278072
333	Phosphorylation	PASPAHTTPQTQSTS CCCCCCCCCCCCCCC	11.97	30278072
336	Phosphorylation	PAHTTPQTQSTSGRR CCCCCCCCCCCCCCC	26.20	23927012
338	Phosphorylation	HTTPQTQSTSGRRRR CCCCCCCCCCCCCHH	28.11	23927012
339	Phosphorylation	TTPQTQSTSGRRRRA CCCCCCCCCCCCHHH	25.94	23927012
340	Phosphorylation	TPQTQSTSGRRRRAA CCCCCCCCCCCHHHH	35.23	23927012
349	Phosphorylation	RRRRAANEDPDEKRR CCHHHHCCCCHHHHH	67.22	1661585
357	Acetylation	DPDEKRRKFLERNRA CCHHHHHHHHHHHHH	59.33	17590016
367	Phosphorylation	ERNRAAASRCRQKRK HHHHHHHHHHHHHHH	27.47	1661585
374	Acetylation	SRCRQKRKVWVQSLE HHHHHHHHHHHHHHH	47.70	17590016
386 (in isoform 2)	Ubiquitination	-	57.63	21890473
386	Ubiquitination	SLEKKAEDLSSLNGQ HHHHHHHHHHHCCHH	57.63	21890473
409	Ubiquitination	RNEVAQLKQLLLAHK HHHHHHHHHHHHHCC	27.16	21890473
409	Ubiquitination	RNEVAQLKQLLLAHK HHHHHHHHHHHHHCC	27.16	21890473
409	Ubiquitination	RNEVAQLKQLLLAHK HHHHHHHHHHHHHCC	27.16	21890473
409 (in isoform 1)	Ubiquitination	-	27.16	21890473
416	Acetylation	KQLLLAHKDCPVTAM HHHHHHCCCCCCEEE	56.25	26051181
427	Phosphorylation	VTAMQKKSGYHTADK CEEEHHHCCCCCCCC	52.17	24275569
429	Phosphorylation	AMQKKSGYHTADKDD EEHHHCCCCCCCCCC	11.77	24275569
431	Phosphorylation	QKKSGYHTADKDDSS HHHCCCCCCCCCCCC	28.24	24247654
437	Phosphorylation	HTADKDDSSEDISVP CCCCCCCCCCCCCCC	45.84	24275569
438	Phosphorylation	TADKDDSSEDISVPS CCCCCCCCCCCCCCC	46.40	23898821
442	Phosphorylation	DDSSEDISVPSSPHT CCCCCCCCCCCCCCC	40.05	24275569
445	Phosphorylation	SEDISVPSSPHTEAI CCCCCCCCCCCCHHC	55.11	25159151
446	Phosphorylation	EDISVPSSPHTEAIQ CCCCCCCCCCCHHCC	18.03	25159151
449	Phosphorylation	SVPSSPHTEAIQHSS CCCCCCCCHHCCCCC	30.42	28348404
455	Phosphorylation	HTEAIQHSSVSTSNG CCHHCCCCCCCCCCC	18.96	28348404
456	Phosphorylation	TEAIQHSSVSTSNGV CHHCCCCCCCCCCCC	20.26	28348404
458	Phosphorylation	AIQHSSVSTSNGVSS HCCCCCCCCCCCCCC	28.24	28348404
459	Phosphorylation	IQHSSVSTSNGVSST CCCCCCCCCCCCCCC	24.85	29449344
460	Phosphorylation	QHSSVSTSNGVSSTS CCCCCCCCCCCCCCH	24.87	29449344
464	Phosphorylation	VSTSNGVSSTSKAEA CCCCCCCCCCHHHHH	29.33	29449344
465	Phosphorylation	STSNGVSSTSKAEAV CCCCCCCCCHHHHHH	34.00	29449344
466	Phosphorylation	TSNGVSSTSKAEAVA CCCCCCCCHHHHHHH	27.09	29449344
467	Phosphorylation	SNGVSSTSKAEAVAT CCCCCCCHHHHHHHH	31.64	29449344
472	Phosphorylation	STSKAEAVATSVLTQ CCHHHHHHHHHHHHH	4.49	15916964
480	Phosphorylation	ATSVLTQMADQSTEP HHHHHHHHHCCCCCC	3.60	15916964
484	Phosphorylation	LTQMADQSTEPALSQ HHHHHCCCCCCHHHH	34.97	30177828
485	Phosphorylation	TQMADQSTEPALSQI HHHHCCCCCCHHHHH	40.11	30177828
490	Phosphorylation	QSTEPALSQIVMAPS CCCCCHHHHHEECCC	21.70	22817900
497	Phosphorylation	SQIVMAPSSQSQPSG HHHEECCCCCCCCCC	31.32	30177828
498	Phosphorylation	QIVMAPSSQSQPSGS HHEECCCCCCCCCCC	32.56	22817900
500	Phosphorylation	VMAPSSQSQPSGS-- EECCCCCCCCCCC--	46.11	30177828
503	Phosphorylation	PSSQSQPSGS----- CCCCCCCCCC-----	43.99	30177828
505	Phosphorylation	SQSQPSGS------- CCCCCCCC-------	41.19	30177828

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
44	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
52	T	Phosphorylation	Kinase	PRKCH	P24723	Uniprot
52	T	Phosphorylation	Kinase	PRKCE	Q02156	GPS
53	T	Phosphorylation	Kinase	MK14	Q16539	PhosphoELM
53	T	Phosphorylation	Kinase	MK08	P45983	PhosphoELM
55	T	Phosphorylation	Kinase	VRK1	Q99986	PhosphoELM
62	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
62	S	Phosphorylation	Kinase	VRK1	Q99986	Uniprot
62	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
69	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
69	T	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
69	T	Phosphorylation	Kinase	MAPK14	P47811	GPS
69	T	Phosphorylation	Kinase	P38A	Q16539	PSP
69	T	Phosphorylation	Kinase	P38B	Q15759	PSP
69	T	Phosphorylation	Kinase	MAPK9	P45984	GPS
69	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
71	T	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
71	T	Phosphorylation	Kinase	PLK3	Q9H4B4	Uniprot
71	T	Phosphorylation	Kinase	MAPK14	P47811	GPS
71	T	Phosphorylation	Kinase	P38A	Q16539	PSP
71	T	Phosphorylation	Kinase	P38G	P53778	PSP
71	T	Phosphorylation	Kinase	P38B	Q15759	PSP
71	T	Phosphorylation	Kinase	MAPK9	P45984	GPS
71	T	Phosphorylation	Kinase	JNK1	P45983	PSP
71	T	Phosphorylation	Kinase	ERK1	P27361	PSP
71	T	Phosphorylation	Kinase	ERK2	P28482	PSP
73	T	Phosphorylation	Kinase	VRK1	Q99986	Uniprot
90	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
90	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
90	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
116	T	Phosphorylation	Kinase	CDK2	P24941	PSP
121	S	Phosphorylation	Kinase	PKCB	P05771	PSP
121	S	Phosphorylation	Kinase	PKCA	P17252	PSP
121	S	Phosphorylation	Kinase	PKCB ISO2	P05771-2	PSP
322	S	Phosphorylation	Kinase	KPCB	P05771	PhosphoELM
322	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
340	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
340	S	Phosphorylation	Kinase	PRKCB	P68403	GPS
340	S	Phosphorylation	Kinase	PRKCA	P17252	Uniprot
340	S	Phosphorylation	Kinase	PRKCB	P05771	Uniprot
349	S	Phosphorylation	Kinase	KPCB	P05771	PhosphoELM
349	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
367	S	Phosphorylation	Kinase	PRKCA	P17252	Uniprot
367	S	Phosphorylation	Kinase	PRKCB	P05771	Uniprot
367	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
367	S	Phosphorylation	Kinase	PRKCB	P68403	GPS
472	S	Phosphorylation	Kinase	ATM	Q13315	PhosphoELM
480	S	Phosphorylation	Kinase	ATM	Q13315	PhosphoELM
490	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
498	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
62	S	Phosphorylation	15105425
Phosphorylation at Ser-62, Thr-73 and Ser-121 activates its transcriptional activity.
69	T	Acetylation	10821277
Phosphorylation at Thr-69 or Thr-71 enhances acetylation of histones H2B and H4.
69	T	Phosphorylation	10821277
Phosphorylation at Thr-69 or Thr-71 enhances acetylation of histones H2B and H4.
69	T	Phosphorylation	9430721
Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity.
71	T	Acetylation	10821277
Phosphorylation at Thr-69 or Thr-71 enhances acetylation of histones H2B and H4.
71	T	Phosphorylation	10821277
Phosphorylation at Thr-69 or Thr-71 enhances acetylation of histones H2B and H4.
71	T	Phosphorylation	9430721
Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity.
73	T	Phosphorylation	15105425
Phosphorylation at Ser-62, Thr-73 and Ser-121 activates its transcriptional activity.
121	S	Phosphorylation	15105425
Phosphorylation at Ser-62, Thr-73 and Ser-121 activates its transcriptional activity.
490	S	Phosphorylation	15916964
ATM-mediated phosphorylation at Ser-490 and Ser-498 stimulates its function in DNA damage response.
498	S	Phosphorylation	15916964
ATM-mediated phosphorylation at Ser-490 and Ser-498 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD3_HUMAN	SMAD3	physical	10085140
SMAD4_HUMAN	SMAD4	physical	10085140
CEBPA_HUMAN	CEBPA	physical	14734562
ATF2_HUMAN	ATF2	physical	8027667
JUN_HUMAN	JUN	physical	8027667
NCOA6_HUMAN	NCOA6	physical	14734562
RUVB2_HUMAN	RUVBL2	physical	11713276
CSK21_HUMAN	CSNK2A1	physical	9685505
CBP_HUMAN	CREBBP	physical	9786917
JUN_HUMAN	JUN	physical	2320002
MK08_HUMAN	MAPK8	physical	7535770
MK14_HUMAN	MAPK14	physical	7535770
UBC9_HUMAN	UBE2I	physical	9488727
UTF1_HUMAN	UTF1	physical	9524124
JUN_HUMAN	JUN	physical	1827203
FOS_HUMAN	FOS	physical	1827203
I2BP1_HUMAN	IRF2BP1	physical	18671972
JDP2_HUMAN	JDP2	physical	18307971
HDAC4_HUMAN	HDAC4	physical	20116378
TYY1_HUMAN	YY1	physical	20211142
CEBPB_HUMAN	CEBPB	physical	16303757
MRE11_HUMAN	MRE11A	physical	15916964
JUN_HUMAN	JUN	physical	10207054
KAT5_HUMAN	KAT5	physical	18397884
RUVB2_HUMAN	RUVBL2	physical	18397884
ATM_HUMAN	ATM	physical	18397884
H2AX_HUMAN	H2AFX	physical	18397884
CCND1_HUMAN	CCND1	physical	10066798
A4_HUMAN	APP	physical	21832049
SRA1_HUMAN	SRA1	physical	20398657
HXK1_HUMAN	HK1	physical	22304920
VDAC1_HUMAN	VDAC1	physical	22304920
SSXT_HUMAN	SS18	physical	22439931
TLE1_HUMAN	TLE1	physical	22439931
SSX2_HUMAN	SSX2	physical	22439931
RPN1_HUMAN	RPN1	physical	22304920
VDAC2_HUMAN	VDAC2	physical	22304920
HS90A_HUMAN	HSP90AA1	physical	22304920
VDAC3_HUMAN	VDAC3	physical	22304920
CH60_HUMAN	HSPD1	physical	22304920
PDIA1_HUMAN	P4HB	physical	22304920
ENPL_HUMAN	HSP90B1	physical	22304920
PDIA3_HUMAN	PDIA3	physical	22304920
4F2_HUMAN	SLC3A2	physical	22304920
ANXA1_HUMAN	ANXA1	physical	22304920
AT1A1_HUMAN	ATP1A1	physical	22304920
KPYM_HUMAN	PKM	physical	22304920
ATPB_HUMAN	ATP5B	physical	22304920
CALR_HUMAN	CALR	physical	22304920
MDHM_HUMAN	MDH2	physical	22304920
GANAB_HUMAN	GANAB	physical	22304920
G3P_HUMAN	GAPDH	physical	22304920
ALDOA_HUMAN	ALDOA	physical	22304920
PHB_HUMAN	PHB	physical	22304920
ITB1_HUMAN	ITGB1	physical	22304920
AHNK_HUMAN	AHNAK	physical	22304920
PROF1_HUMAN	PFN1	physical	22304920
TPIS_HUMAN	TPI1	physical	22304920
FSCN1_HUMAN	FSCN1	physical	22304920
CD44_HUMAN	CD44	physical	22304920
LDHA_HUMAN	LDHA	physical	22304920
LDHB_HUMAN	LDHB	physical	22304920
ECHA_HUMAN	HADHA	physical	22304920
CISY_HUMAN	CS	physical	22304920
VIME_HUMAN	VIM	physical	22304920
1433B_HUMAN	YWHAB	physical	22304920
PDIA4_HUMAN	PDIA4	physical	22304920
DHE4_HUMAN	GLUD2	physical	22304920
RAB7A_HUMAN	RAB7A	physical	22304920
GLYM_HUMAN	SHMT2	physical	22304920
1433S_HUMAN	SFN	physical	22304920
ACADV_HUMAN	ACADVL	physical	22304920
OAT_HUMAN	OAT	physical	22304920
ITA2_HUMAN	ITGA2	physical	22304920
CAP1_HUMAN	CAP1	physical	22304920
TCPG_HUMAN	CCT3	physical	22304920
BASP1_HUMAN	BASP1	physical	22304920
ENOA_HUMAN	ENO1	physical	22304920
ITB4_HUMAN	ITGB4	physical	22304920
PHB2_HUMAN	PHB2	physical	22304920
GSTP1_HUMAN	GSTP1	physical	22304920
PCNA_HUMAN	PCNA	physical	22304920
TBB5_HUMAN	TUBB	physical	22304920
ANXA5_HUMAN	ANXA5	physical	22304920
ACTN1_HUMAN	ACTN1	physical	22304920
K1C18_HUMAN	KRT18	physical	22304920
RHOC_HUMAN	RHOC	physical	22304920
SERPH_HUMAN	SERPINH1	physical	22304920
TCPA_HUMAN	TCP1	physical	22304920
S10AB_HUMAN	S100A11	physical	22304920
TAGL2_HUMAN	TAGLN2	physical	22304920
STIP1_HUMAN	STIP1	physical	22304920
QCR2_HUMAN	UQCRC2	physical	22304920
OST48_HUMAN	DDOST	physical	22304920
K2C8_HUMAN	KRT8	physical	22304920
HS105_HUMAN	HSPH1	physical	22304920
COF1_HUMAN	CFL1	physical	22304920
TPM4_HUMAN	TPM4	physical	22304920
TPM1_HUMAN	TPM1	physical	22304920
BAP31_HUMAN	BCAP31	physical	22304920
ERO1A_HUMAN	ERO1L	physical	22304920
AT2A2_HUMAN	ATP2A2	physical	22304920
RAB2B_HUMAN	RAB2B	physical	22304920
TFR1_HUMAN	TFRC	physical	22304920
QCR1_HUMAN	UQCRC1	physical	22304920
SQOR_HUMAN	SQRDL	physical	22304920
TCPB_HUMAN	CCT2	physical	22304920
SAHH_HUMAN	AHCY	physical	22304920
K2C7_HUMAN	KRT7	physical	22304920
DLDH_HUMAN	DLD	physical	22304920
ATF2_HUMAN	ATF2	physical	22304920
TCPD_HUMAN	CCT4	physical	22304920
CALX_HUMAN	CANX	physical	22304920
HSPB1_HUMAN	HSPB1	physical	22304920
HNRH1_HUMAN	HNRNPH1	physical	22304920
SFXN1_HUMAN	SFXN1	physical	22304920
VAPA_HUMAN	VAPA	physical	22304920
RAB2A_HUMAN	RAB2A	physical	22304920
SRC8_HUMAN	CTTN	physical	22304920
RB11A_HUMAN	RAB11A	physical	22304920
MARCS_HUMAN	MARCKS	physical	22304920
BASI_HUMAN	BSG	physical	22304920
CMC2_HUMAN	SLC25A13	physical	22304920
FETUA_HUMAN	AHSG	physical	22304920
ATPO_HUMAN	ATP5O	physical	22304920
CALU_HUMAN	CALU	physical	22304920
IF5A1_HUMAN	EIF5A	physical	22304920
MIC60_HUMAN	IMMT	physical	22304920
FUMH_HUMAN	FH	physical	22304920
TCPE_HUMAN	CCT5	physical	22304920
ECHB_HUMAN	HADHB	physical	22304920
ERP29_HUMAN	ERP29	physical	22304920
GBB2_HUMAN	GNB2	physical	22304920
CTND1_HUMAN	CTNND1	physical	22304920
GTR1_HUMAN	SLC2A1	physical	22304920
CH10_HUMAN	HSPE1	physical	22304920
APMAP_HUMAN	APMAP	physical	22304920
CLIC1_HUMAN	CLIC1	physical	22304920
DX39B_HUMAN	DDX39B	physical	22304920
AT2A3_HUMAN	ATP2A3	physical	22304920
TACD2_HUMAN	TACSTD2	physical	22304920
ARF1_HUMAN	ARF1	physical	22304920
ANXA3_HUMAN	ANXA3	physical	22304920
PCBP1_HUMAN	PCBP1	physical	22304920
FUBP1_HUMAN	FUBP1	physical	22304920
CMC1_HUMAN	SLC25A12	physical	22304920
GRPE1_HUMAN	GRPEL1	physical	22304920
CTNB1_HUMAN	CTNNB1	physical	22304920
RTN4_HUMAN	RTN4	physical	22304920
S10AA_HUMAN	S100A10	physical	22304920
NACAM_HUMAN	NACA	physical	22304920
NACA_HUMAN	NACA	physical	22304920
ARF4_HUMAN	ARF4	physical	22304920
CY1_HUMAN	CYC1	physical	22304920
EF2_HUMAN	EEF2	physical	22304920
GLSK_HUMAN	GLS	physical	22304920
PRDX5_HUMAN	PRDX5	physical	22304920
TIM9_HUMAN	TIMM9	physical	22304920
PPIF_HUMAN	PPIF	physical	22304920
1433G_HUMAN	YWHAG	physical	22304920
GT251_HUMAN	COLGALT1	physical	22304920
S10A2_HUMAN	S100A2	physical	22304920
RAB14_HUMAN	RAB14	physical	22304920
TMX1_HUMAN	TMX1	physical	22304920
TMEDA_HUMAN	TMED10	physical	22304920
PTN1_HUMAN	PTPN1	physical	22304920
MYDGF_HUMAN	C19orf10	physical	22304920
MK14_HUMAN	MAPK14	physical	11566021
MK08_HUMAN	MAPK8	physical	11566021
RB_HUMAN	RB1	physical	11566021
H2AY_HUMAN	H2AFY	physical	17036053
BACH1_HUMAN	BACH1	physical	23661758
BATF_HUMAN	BATF	physical	23661758
ATF3_HUMAN	ATF3	physical	23661758
ATF4_HUMAN	ATF4	physical	23661758
FOSL1_HUMAN	FOSL1	physical	23661758
FOS_HUMAN	FOS	physical	23661758
JUN_HUMAN	JUN	physical	23661758
ATF2_HUMAN	ATF2	physical	23661758
MLH1_HUMAN	MLH1	physical	21988832
FOS_HUMAN	FOS	physical	25416956
KIFC3_HUMAN	KIFC3	physical	25416956
MK09_HUMAN	MAPK9	physical	25416956
SUMO1_HUMAN	SUMO1	physical	25416956
EXOS8_HUMAN	EXOSC8	physical	25416956
ATF1_HUMAN	ATF1	physical	26344197
CREB1_HUMAN	CREB1	physical	26344197
ATF7_HUMAN	ATF7	physical	28514442
JUN_HUMAN	JUN	physical	28514442
JUND_HUMAN	JUND	physical	28514442
ARI1_HUMAN	ARIH1	physical	28514442
RAD18_HUMAN	RAD18	physical	28514442
DPP8_HUMAN	DPP8	physical	28514442
CR025_HUMAN	C18orf25	physical	28514442

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
DB00852	Pseudoephedrine

Regulatory Network of ATF2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-69; THR-71 AND SER-112,AND MASS SPECTROMETRY.	19690332 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-90 ANDSER-112, AND MASS SPECTROMETRY.	19413330 [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 THR-69; THR-71 AND SER-112,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASSSPECTROMETRY.	18220336 [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 THR-69; THR-71 AND SER-112,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase3 in human corneal epithelial cells."; Wang L., Payton R., Dai W., Lu L.; J. Biol. Chem. 286:1951-1958(2011). Cited for: PHOSPHORYLATION AT THR-71, SUBCELLULAR LOCATION, AND MUTAGENESIS OFTHR-71.	21098032 [Abstract]
"Growth factors can activate ATF2 via a two-step mechanism:phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69through RalGDS-Src-p38."; Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P.,Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A.,van Dam H.; EMBO J. 21:3782-3793(2002). Cited for: PHOSPHORYLATION AT THR-69 AND THR-71.	12110590 [Abstract]
"Selective activation of p38 mitogen-activated protein (MAP) kinaseisoforms by the MAP kinase kinases MKK3 and MKK6."; Enslen H., Raingeaud J., Davis R.J.; J. Biol. Chem. 273:1741-1748(1998). Cited for: PHOSPHORYLATION AT THR-69 AND THR-71.	9430721 [Abstract]

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