ATF7_MOUSE - dbPTM
ATF7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATF7_MOUSE
UniProt AC Q8R0S1
Protein Name Cyclic AMP-dependent transcription factor ATF-7
Gene Name Atf7
Organism Mus musculus (Mouse).
Sequence Length 413
Subcellular Localization Nucleus . Nucleus, nucleoplasm. Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear peiphery (By similarity)..
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 (By similarity)..
Protein Sequence MGDDRPFVCSAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKASDDDEKKGAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTTKPVVISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQIGSPTGSLPLVMHLANGQTMPMLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNNSGSISPSGHPMPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQNQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLGK
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 Orthologous
Protein Cluster
42PhosphorylationLKFGPARTDSVIIAD
EEECCCCCCCEEEEC
34.4327087446
44PhosphorylationFGPARTDSVIIADQT
ECCCCCCCEEEECCC
18.0123684622
51PhosphorylationSVIIADQTPTPTRFL
CEEEECCCCCCCHHH
29.6725521595
53PhosphorylationIIADQTPTPTRFLKN
EEECCCCCCCHHHHC
40.4525521595
55PhosphorylationADQTPTPTRFLKNCE
ECCCCCCCHHHHCHH
36.2127087446
72PhosphorylationGLFNELASSFEHEFK
CHHHHHHHHHHHHHH
48.4626643407
73PhosphorylationLFNELASSFEHEFKK
HHHHHHHHHHHHHHH
29.1029514104
82PhosphorylationEHEFKKASDDDEKKG
HHHHHHCCCCCCCCC
50.91-
97PhosphorylationAAGPLDMSLPSTPDI
CCCCCCCCCCCCCCC
36.4727087446
100PhosphorylationPLDMSLPSTPDIKIK
CCCCCCCCCCCCCCC
58.8421082442
101PhosphorylationLDMSLPSTPDIKIKE
CCCCCCCCCCCCCCC
24.0427087446
116PhosphorylationEEPVEVDSSPPDSPA
CCCCCCCCCCCCCCC
50.3426643407
117PhosphorylationEPVEVDSSPPDSPAS
CCCCCCCCCCCCCCC
35.6726643407
121PhosphorylationVDSSPPDSPASSPCS
CCCCCCCCCCCCCCC
28.3026643407
124PhosphorylationSPPDSPASSPCSPPL
CCCCCCCCCCCCCCC
37.8926643407
125PhosphorylationPPDSPASSPCSPPLK
CCCCCCCCCCCCCCC
31.8426643407
128PhosphorylationSPASSPCSPPLKEKE
CCCCCCCCCCCCCCC
32.7026643407
137PhosphorylationPLKEKEVTTKPVVIS
CCCCCCCCCCCEEEE
30.1425367039
138PhosphorylationLKEKEVTTKPVVIST
CCCCCCCCCCEEEEC
38.2325367039
144PhosphorylationTTKPVVISTPTPTIV
CCCCEEEECCCCCEE
19.4125367039
168PhosphorylationGYDPLHPTLPSPTSV
CCCCCCCCCCCCCCE
40.3225367039
171PhosphorylationPLHPTLPSPTSVITQ
CCCCCCCCCCCEEEE
43.8725367039
173PhosphorylationHPTLPSPTSVITQAP
CCCCCCCCCEEEECC
39.7125367039
174PhosphorylationPTLPSPTSVITQAPP
CCCCCCCCEEEECCC
18.2025367039
226PhosphorylationISLARPVSMVPNIPG
HHHCCCCCCCCCCCC
19.4225777480
242PhosphorylationPGPPVNNSGSISPSG
CCCCCCCCCCCCCCC
28.8126643407
244PhosphorylationPPVNNSGSISPSGHP
CCCCCCCCCCCCCCC
21.5126643407
246PhosphorylationVNNSGSISPSGHPMP
CCCCCCCCCCCCCCC
18.0826643407
248PhosphorylationNSGSISPSGHPMPSE
CCCCCCCCCCCCCCH
42.8325777480
254PhosphorylationPSGHPMPSEAKMRLK
CCCCCCCCHHHHHHH
43.8925777480
326PhosphorylationTGGRRRRTVDEDPDE
CCCCCCCCCCCCHHH
30.4225521595
358PhosphorylationQKRKLWVSSLEKKAE
HHHHHHHHHHHHHHH
20.0225338131
359PhosphorylationKRKLWVSSLEKKAEE
HHHHHHHHHHHHHHH
30.8129514104

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
51TPhosphorylationKinaseMAPK11Q9WUI1
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
51TPhosphorylation

29490055
53TPhosphorylation

29490055

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCAF1_MOUSEAtf7ipphysical
10777215

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATF7_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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