dbPTM

ATF7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATF7_HUMAN
UniProt AC	P17544
Protein Name	Cyclic AMP-dependent transcription factor ATF-7
Gene Name	ATF7
Organism	Homo sapiens (Human).
Sequence Length	494
Subcellular Localization	Nucleus . Nucleus, nucleoplasm . Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear periphery. Isoform 5: Cytoplasm .
Protein Description	Plays important functions in early cell signaling. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters. Activator of the NF-ELAM1/delta-A site of the E-selectin promoter. Has no intrinsic transcriptional activity, but activates transcription on formation of JUN or FOS heterodimers. Also can bind TRE promoter sequences when heterodimerized with members of the JUN family.; Isoform 4 acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter.; Isoform 5 acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation..
Protein Sequence	MGDDRPFVCNAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKAADEDEKKARSRTVAKKLVAAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTPKPVLISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQMGSPTGSLPLVMHLANGQTMPVLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNSSGSISPSGHPIPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQSQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLESPKESSEPTGSPAPVIQHSSATAPSNGLSVRSAAEAVATSVLTQMASQRTELSMPIQSHVIMTPQSQSAGR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	HKHKHEMTLKFGPAR EECCCEEEEEECCCC	24.66	22304920
42	Phosphorylation	LKFGPARTDSVIIAD EEECCCCCCCEEEEC	34.43	28176443
44	Phosphorylation	FGPARTDSVIIADQT ECCCCCCCEEEECCC	18.01	23401153
51	Phosphorylation	SVIIADQTPTPTRFL CEEEECCCCCCCHHH	29.67	29255136
53	Phosphorylation	IIADQTPTPTRFLKN EEECCCCCCCHHHHC	40.45	29255136
55	Phosphorylation	ADQTPTPTRFLKNCE ECCCCCCCHHHHCHH	36.21	29255136
59	Ubiquitination	PTPTRFLKNCEEVGL CCCCHHHHCHHHCCH	57.76	29967540
72	Phosphorylation	GLFNELASSFEHEFK CHHHHHHHHHHHHHH	48.46	25849741
73	Phosphorylation	LFNELASSFEHEFKK HHHHHHHHHHHHHHH	29.10	25849741
79	Ubiquitination	SSFEHEFKKAADEDE HHHHHHHHHHCCHHH	38.22	29967540
91	Phosphorylation	EDEKKARSRTVAKKL HHHHHHHHHHHHHHH	36.84	24702127
93	Phosphorylation	EKKARSRTVAKKLVA HHHHHHHHHHHHHHH	26.51	24702127
100 (in isoform 2)	Phosphorylation	-	11.30	29507054
101	Phosphorylation	VAKKLVAAAGPLDMS HHHHHHHHHCCCCCC	12.89	18950637
101 (in isoform 2)	Phosphorylation	-	12.89	29743597
108	Phosphorylation	AAGPLDMSLPSTPDI HHCCCCCCCCCCCCC	36.47	29255136
111	Phosphorylation	PLDMSLPSTPDIKIK CCCCCCCCCCCCCCC	58.84	30266825
112	Phosphorylation	LDMSLPSTPDIKIKE CCCCCCCCCCCCCCC	24.04	29255136
118	Sumoylation	STPDIKIKEEEPVEV CCCCCCCCCCCCCCC	54.81	17264123
118	Sumoylation	STPDIKIKEEEPVEV CCCCCCCCCCCCCCC	54.81	-
121 (in isoform 4)	Phosphorylation	-	56.59	29116813
124 (in isoform 4)	Phosphorylation	-	51.85	29116813
125 (in isoform 4)	Phosphorylation	-	9.84	29116813
127	Phosphorylation	EEPVEVDSSPPDSPA CCCCCCCCCCCCCCC	50.34	25159151
128	Phosphorylation	EPVEVDSSPPDSPAS CCCCCCCCCCCCCCC	35.67	25159151
132	Phosphorylation	VDSSPPDSPASSPCS CCCCCCCCCCCCCCC	28.30	25159151
135	Phosphorylation	SPPDSPASSPCSPPL CCCCCCCCCCCCCCC	37.89	25159151
136	Phosphorylation	PPDSPASSPCSPPLK CCCCCCCCCCCCCCC	31.84	25159151
139	Phosphorylation	SPASSPCSPPLKEKE CCCCCCCCCCCCCCC	32.70	25022875
148	Phosphorylation	PLKEKEVTPKPVLIS CCCCCCCCCCCEEEE	27.04	20068231
155	Phosphorylation	TPKPVLISTPTPTIV CCCCEEEECCCCCEE	24.95	29978859
156	Phosphorylation	PKPVLISTPTPTIVR CCCEEEECCCCCEEC	24.96	22496350
158	Phosphorylation	PVLISTPTPTIVRPG CEEEECCCCCEECCC	32.90	20068231
160	Phosphorylation	LISTPTPTIVRPGSL EEECCCCCEECCCCC	34.28	20068231
166	Phosphorylation	PTIVRPGSLPLHLGY CCEECCCCCCCCCCC	29.51	28464451
173	Phosphorylation	SLPLHLGYDPLHPTL CCCCCCCCCCCCCCC	22.28	28122231
179	Phosphorylation	GYDPLHPTLPSPTSV CCCCCCCCCCCCCCE	40.32	28464451
182	Phosphorylation	PLHPTLPSPTSVITQ CCCCCCCCCCCEEEE	43.87	25849741
184	Phosphorylation	HPTLPSPTSVITQAP CCCCCCCCCEEEECC	39.71	25850435
185	Phosphorylation	PTLPSPTSVITQAPP CCCCCCCCEEEECCC	18.20	28464451
188	Phosphorylation	PSPTSVITQAPPSNR CCCCCEEEECCCCCC	19.27	25850435
193	Phosphorylation	VITQAPPSNRQMGSP EEEECCCCCCCCCCC	43.52	25850435
199	Phosphorylation	PSNRQMGSPTGSLPL CCCCCCCCCCCCCCE	17.59	28348404
201	Phosphorylation	NRQMGSPTGSLPLVM CCCCCCCCCCCCEEE	40.89	28348404
203	Phosphorylation	QMGSPTGSLPLVMHL CCCCCCCCCCEEEEE	29.32	28348404
213 (in isoform 4)	Ubiquitination	-	20.80	21890473
227	Phosphorylation	PGPPVQMPSVISLAR CCCCCCCCCCHHCCC	14.35	32142685
237	Phosphorylation	ISLARPVSMVPNIPG HHCCCCCCCCCCCCC	19.42	26074081
248	Phosphorylation	NIPGIPGPPVNSSGS CCCCCCCCCCCCCCC	25.06	32142685
252	Phosphorylation	IPGPPVNSSGSISPS CCCCCCCCCCCCCCC	35.99	26657352
253	Phosphorylation	PGPPVNSSGSISPSG CCCCCCCCCCCCCCC	31.21	29255136
255	Phosphorylation	PPVNSSGSISPSGHP CCCCCCCCCCCCCCC	23.11	26657352
257	Phosphorylation	VNSSGSISPSGHPIP CCCCCCCCCCCCCCC	18.08	29255136
259	Phosphorylation	SSGSISPSGHPIPSE CCCCCCCCCCCCCCH	42.83	29255136
265	Phosphorylation	PSGHPIPSEAKMRLK CCCCCCCCHHHHHHH	51.40	29255136
304	Phosphorylation	VTARPEQSQILIQHP EEECHHHCCEEEECC	19.95	29255136
315	Phosphorylation	IQHPDAPSPAQPQVS EECCCCCCCCCCCCC	34.29	29255136
322	Phosphorylation	SPAQPQVSPAQPTPS CCCCCCCCCCCCCCC	14.85	29255136
327	Phosphorylation	QVSPAQPTPSTGGRR CCCCCCCCCCCCCCC	20.14	25850435
330	Phosphorylation	PAQPTPSTGGRRRRT CCCCCCCCCCCCCCC	44.87	-
334	Ubiquitination	TPSTGGRRRRTVDED CCCCCCCCCCCCCCC	35.39	32015554
337	Phosphorylation	TGGRRRRTVDEDPDE CCCCCCCCCCCCHHH	30.42	29255136
342	Ubiquitination	RRTVDEDPDERRQRF CCCCCCCHHHHHHHH	43.23	29967540
358	Phosphorylation	ERNRAAASRCRQKRK HHHHHHHHHHHHHHH	27.47	22817900
363	Ubiquitination	AASRCRQKRKLWVSS HHHHHHHHHHHHHHH	31.95	29967540
368	Ubiquitination	RQKRKLWVSSLEKKA HHHHHHHHHHHHHHH	3.95	21890473
368 (in isoform 2)	Ubiquitination	-	3.95	21890473
368	Phosphorylation	RQKRKLWVSSLEKKA HHHHHHHHHHHHHHH	3.95	32142685
379 (in isoform 3)	Ubiquitination	-	31.39	21890473
389	Ubiquitination	NIQLSNEVTLLRNEV CCCCHHHHHHHHHHH	5.52	21890473
389	Ubiquitination	NIQLSNEVTLLRNEV CCCCHHHHHHHHHHH	5.52	21890473
400 (in isoform 1)	Ubiquitination	-	27.16	21890473
400	Ubiquitination	RNEVAQLKQLLLAHK HHHHHHHHHHHHHCC	27.16	32015554
402	Phosphorylation	EVAQLKQLLLAHKDC HHHHHHHHHHHCCCC	3.96	32142685
413	Phosphorylation	HKDCPVTALQKKTQG CCCCCCHHHHHHHCC	14.29	24275569
418	Phosphorylation	VTALQKKTQGYLESP CHHHHHHHCCCCCCC	33.97	18669648
421	Phosphorylation	LQKKTQGYLESPKES HHHHHCCCCCCCCCC	9.47	30576142
423	Phosphorylation	KKTQGYLESPKESSE HHHCCCCCCCCCCCC	57.41	23186163
424	Phosphorylation	KTQGYLESPKESSEP HHCCCCCCCCCCCCC	38.38	25159151
428	Phosphorylation	YLESPKESSEPTGSP CCCCCCCCCCCCCCC	46.24	30266825
429	Phosphorylation	LESPKESSEPTGSPA CCCCCCCCCCCCCCC	49.00	30266825
432	Phosphorylation	PKESSEPTGSPAPVI CCCCCCCCCCCCCEE	46.36	23401153
434	Phosphorylation	ESSEPTGSPAPVIQH CCCCCCCCCCCEEEC	21.99	29255136
442	Phosphorylation	PAPVIQHSSATAPSN CCCEEECCCCCCCCC	12.80	23403867
442 (in isoform 1)	O-linked_Glycosylation	-	12.80	30059200
443	Phosphorylation	APVIQHSSATAPSNG CCEEECCCCCCCCCC	27.75	23403867
445	Phosphorylation	VIQHSSATAPSNGLS EEECCCCCCCCCCCC	40.84	23403867
448	Phosphorylation	HSSATAPSNGLSVRS CCCCCCCCCCCCHHH	40.86	17081983
452	Phosphorylation	TAPSNGLSVRSAAEA CCCCCCCCHHHHHHH	19.51	17081983
455 (in isoform 1)	O-linked_Glycosylation	-	29.67	30059200
455	O-linked_Glycosylation	SNGLSVRSAAEAVAT CCCCCHHHHHHHHHH	29.67	30059200
462	O-linked_Glycosylation	SAAEAVATSVLTQMA HHHHHHHHHHHHHHH	16.87	30059200
463 (in isoform 1)	O-linked_Glycosylation	-	12.85	30059200
470	Phosphorylation	SVLTQMASQRTELSM HHHHHHHHCCCCCCC	18.17	26714015
473	Phosphorylation	TQMASQRTELSMPIQ HHHHHCCCCCCCCCC	33.37	27251275
476	Phosphorylation	ASQRTELSMPIQSHV HHCCCCCCCCCCCEE	19.11	27251275
481	Phosphorylation	ELSMPIQSHVIMTPQ CCCCCCCCEEEECCC	22.05	27251275
486	Phosphorylation	IQSHVIMTPQSQSAG CCCEEEECCCHHCCC	13.67	25159151
489	Phosphorylation	HVIMTPQSQSAGR-- EEEECCCHHCCCC--	27.57	27251275
491	Phosphorylation	IMTPQSQSAGR---- EECCCHHCCCC----	37.63	27251275

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
51	T	Phosphorylation	Kinase	P38B	Q15759	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
51	T	Phosphorylation	10376527
On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51.
53	T	Phosphorylation	10376527
On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51.

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 ATF7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAF12_HUMAN	TAF12	physical	15735663
TAF4_HUMAN	TAF4	physical	15735663
CREB1_HUMAN	CREB1	physical	22939629
MK08_HUMAN	MAPK8	physical	11566021
OCAD1_HUMAN	OCIAD1	physical	20195357
RMP_HUMAN	URI1	physical	20195357
TAOK3_HUMAN	TAOK3	physical	20195357
MITD1_HUMAN	MITD1	physical	20195357
KASH5_HUMAN	CCDC155	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
TM239_HUMAN	TMEM239	physical	25416956
MBD3_HUMAN	MBD3	physical	21516116

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 ATF7_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-42; THR-51; THR-53;SER-108 AND THR-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-51; THR-53; THR-55 ANDSER-424, 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-51; THR-53; SER-108 ANDTHR-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-108 AND THR-112, ANDMASS SPECTROMETRY.	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-51; THR-53; SER-111;THR-112; SER-127; SER-128; SER-132; SER-135; SER-136 AND SER-139, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"p38beta2-mediated phosphorylation and sumoylation of ATF7 aremutually exclusive."; Camuzeaux B., Diring J., Hamard P.J., Oulad-Abdelghani M., Donzeau M.,Vigneron M., Kedinger C., Chatton B.; J. Mol. Biol. 384:980-991(2008). Cited for: PHOSPHORYLATION AT THR-51; THR-53 AND THR-112, SUMOYLATION AT LYS-118,FUNCTION, AND MUTAGENESIS OF THR-51; THR-53; THR-112 AND LYS-118.	18950637 [Abstract]

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