ATF6A_HUMAN - dbPTM
ATF6A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATF6A_HUMAN
UniProt AC P18850
Protein Name Cyclic AMP-dependent transcription factor ATF-6 alpha
Gene Name ATF6
Organism Homo sapiens (Human).
Sequence Length 670
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein.
Processed cyclic AMP-dependent transcription factor ATF-6 alpha: Nucleus. Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. THBS4 promotes i
Protein Description Transmembrane glycoprotein of the endoplasmic reticulum that functions as a transcription activator and initiates the unfolded protein response (UPR) during endoplasmic reticulum stress. Cleaved upon ER stress, the N-terminal processed cyclic AMP-dependent transcription factor ATF-6 alpha translocates to the nucleus where it activates transcription of genes involved in the UPR. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. May play a role in foveal development and cone function in the retina..
Protein Sequence MGEPAGVAGTMESPFSPGLFHRLDEDWDSALFAELGYFTDTDELQLEAANETYENNFDNLDFDLDLMPWESDIWDINNQICTVKDIKAEPQPLSPASSSYSVSSPRSVDSYSSTQHVPEELDLSSSSQMSPLSLYGENSNSLSSAEPLKEDKPVTGPRNKTENGLTPKKKIQVNSKPSIQPKPLLLPAAPKTQTNSSVPAKTIIIQTVPTLMPLAKQQPIISLQPAPTKGQTVLLSQPTVVQLQAPGVLPSAQPVLAVAGGVTQLPNHVVNVVPAPSANSPVNGKLSVTKPVLQSTMRNVGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGTLKRQLDEVVSENQRLKVPSPKRRVVCVMIVLAFIILNYGPMSMLEQDSRRMNPSVSPANQRRHLLGFSAKEAQDTSDGIIQKNSYRYDHSVSNDKALMVLTEEPLLYIPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNNQQKTRILQGALEQGSNSQLMAVQYTETTSSISRNSGSELQVYYASPRSYQDFFEAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININENVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDQQRNQTNTFFGSPPAATEATHVVSTIPESLQ
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
10PhosphorylationEPAGVAGTMESPFSP
CCCCCCCCCCCCCCC		14.1829759185
13PhosphorylationGVAGTMESPFSPGLF
CCCCCCCCCCCCCHH		22.0325850435
16PhosphorylationGTMESPFSPGLFHRL
CCCCCCCCCCHHHCC		22.8025850435
87SumoylationICTVKDIKAEPQPLS
EEEHHHCCCCCCCCC		57.75-
87AcetylationICTVKDIKAEPQPLS
EEEHHHCCCCCCCCC		57.7526051181
87SumoylationICTVKDIKAEPQPLS
EEEHHHCCCCCCCCC		57.7528112733
87UbiquitinationICTVKDIKAEPQPLS
EEEHHHCCCCCCCCC		57.7521906983
94PhosphorylationKAEPQPLSPASSSYS
CCCCCCCCCCCCCCC		25.7128355574
97PhosphorylationPQPLSPASSSYSVSS
CCCCCCCCCCCCCCC		24.1727732954
97O-linked_GlycosylationPQPLSPASSSYSVSS
CCCCCCCCCCCCCCC		24.1730379171
98PhosphorylationQPLSPASSSYSVSSP
CCCCCCCCCCCCCCC		35.0927732954
99PhosphorylationPLSPASSSYSVSSPR
CCCCCCCCCCCCCCC		20.9427732954
100PhosphorylationLSPASSSYSVSSPRS
CCCCCCCCCCCCCCC		18.2923312004
101PhosphorylationSPASSSYSVSSPRSV
CCCCCCCCCCCCCCC		19.9227732954
103PhosphorylationASSSYSVSSPRSVDS
CCCCCCCCCCCCCCC		28.7825159151
104PhosphorylationSSSYSVSSPRSVDSY
CCCCCCCCCCCCCCC		23.3728985074
152SumoylationAEPLKEDKPVTGPRN
CCCCCCCCCCCCCCC		42.34-
152SumoylationAEPLKEDKPVTGPRN
CCCCCCCCCCCCCCC		42.34-
161PhosphorylationVTGPRNKTENGLTPK
CCCCCCCCCCCCCCC		37.9322210691
166PhosphorylationNKTENGLTPKKKIQV
CCCCCCCCCCCCEEC		34.1725002506
175PhosphorylationKKKIQVNSKPSIQPK
CCCEECCCCCCCCCC		47.2723532336
176UbiquitinationKKIQVNSKPSIQPKP
CCEECCCCCCCCCCC		37.27-
176SumoylationKKIQVNSKPSIQPKP
CCEECCCCCCCCCCC		37.27-
176AcetylationKKIQVNSKPSIQPKP
CCEECCCCCCCCCCC		37.2723954790
176SumoylationKKIQVNSKPSIQPKP
CCEECCCCCCCCCCC		37.27-
182SumoylationSKPSIQPKPLLLPAA
CCCCCCCCCCEECCC		31.74-
182AcetylationSKPSIQPKPLLLPAA
CCCCCCCCCCEECCC		31.7426051181
182SumoylationSKPSIQPKPLLLPAA
CCCCCCCCCCEECCC		31.74-
191SumoylationLLLPAAPKTQTNSSV
CEECCCCCCCCCCCC		48.84-
191SumoylationLLLPAAPKTQTNSSV
CEECCCCCCCCCCCC		48.84-
201UbiquitinationTNSSVPAKTIIIQTV
CCCCCCCEEEEEEEC		33.9021906983
201AcetylationTNSSVPAKTIIIQTV
CCCCCCCEEEEEEEC		33.9026051181
216UbiquitinationPTLMPLAKQQPIISL
CCCHHHHHCCCEEEE		58.09-
290SumoylationNGKLSVTKPVLQSTM
CCEECCCHHHHHHHH		30.85-
290SumoylationNGKLSVTKPVLQSTM
CCEECCCHHHHHHHH		30.85-
290UbiquitinationNGKLSVTKPVLQSTM
CCEECCCHHHHHHHH		30.85-
296PhosphorylationTKPVLQSTMRNVGSD
CHHHHHHHHHHHCHH		13.74-
302PhosphorylationSTMRNVGSDIAVLRR
HHHHHHCHHHHHHHH		22.8926471730
330PhosphorylationSRKKKKEYMLGLEAR
HHHHHHHHHHHHHHH		13.4022817900
339UbiquitinationLGLEARLKAALSENE
HHHHHHHHHHHHHCH		26.51-
349UbiquitinationLSENEQLKKENGTLK
HHHCHHHHHHCCCHH		58.71-
373PhosphorylationNQRLKVPSPKRRVVC
CCCCCCCCHHHHHHH		46.1423898821
410PhosphorylationRRMNPSVSPANQRRH
HHCCCCCCHHHHHHH		23.7226091039
424UbiquitinationHLLGFSAKEAQDTSD
HHHCCCHHCCCCCCC		53.0021906983
436UbiquitinationTSDGIIQKNSYRYDH
CCCCEEECCCEECCC		37.1421906983
472N-linked_GlycosylationPPCQPLINTTESLRL
CCCCCCCCCHHHHHC		48.9414699159
474O-linked_GlycosylationCQPLINTTESLRLNH
CCCCCCCHHHHHCCH		21.0614699159
474O-linked_GlycosylationCQPLINTTESLRLNH
CCCCCCCHHHHHCCH		21.06-
506UbiquitinationRMTNNQQKTRILQGA
CCCCHHHHHHHHHHH		29.97-
565PhosphorylationAIRRRGDTFYVVSFR
HHHHCCCEEEEEEEC		21.4930622161
567PhosphorylationRRRGDTFYVVSFRRD
HHCCCEEEEEEECCC		11.3130622161
584N-linked_GlycosylationLLPATTHNKTTRPKM
ECEECCCCCCCCCCE		41.0814699159
586O-linked_GlycosylationPATTHNKTTRPKMSI
EECCCCCCCCCCEEE		33.10-
586O-linked_GlycosylationPATTHNKTTRPKMSI
EECCCCCCCCCCEEE		33.1014699159
590UbiquitinationHNKTTRPKMSIVLPA
CCCCCCCCEEEEEEE		41.82-
629UbiquitinationDTRILHIKSSSVPPY
CCEEEEEECCCCCCC		33.27-
632PhosphorylationILHIKSSSVPPYLRD
EEEEECCCCCCCCCH		45.8121659604
643N-linked_GlycosylationYLRDQQRNQTNTFFG
CCCHHHCCCCCCCCC		49.0014699159
645O-linked_GlycosylationRDQQRNQTNTFFGSP
CHHHCCCCCCCCCCC		39.51-
645O-linked_GlycosylationRDQQRNQTNTFFGSP
CHHHCCCCCCCCCCC		39.5114699159
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
166TPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATF6A_HUMAN !!
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 ATF6A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYY1_HUMANYY1physical
10866666
ATF6A_HUMANATF6physical
11158310
ATF6B_HUMANATF6Bphysical
11158310
SRF_HUMANSRFphysical
9271374
TYY1_HUMANYY1physical
15899857
SRBP2_HUMANSREBF2physical
14765107
SP1_HUMANSP1genetic
22354938
A4_HUMANAPPphysical
21832049
ATF6A_HUMANATF6physical
23661758
XBP1_HUMANXBP1physical
23661758
PMGE_HUMANBPGMphysical
21988832
DDC_HUMANDDCphysical
21988832
NNMT_HUMANNNMTphysical
21988832
TNR1A_HUMANTNFRSF1Aphysical
21988832
APOD_HUMANAPODphysical
25609649
S3TC1_HUMANSH3TC1physical
25609649
RFWD2_HUMANRFWD2physical
25609649
STK40_HUMANSTK40physical
25609649
ACLY_HUMANACLYphysical
25609649
PARG_HUMANPARGphysical
25609649
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
DB00852Pseudoephedrine
Regulatory Network of ATF6A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Underglycosylation of ATF6 as a novel sensing mechanism foractivation of the unfolded protein response.";
Hong M., Luo S., Baumeister P., Huang J.M., Gogia R.K., Li M.,Lee A.S.;
J. Biol. Chem. 279:11354-11363(2004).
Cited for: GLYCOSYLATION AT ASN-472; ASN-584 AND ASN-643, AND MUTAGENESIS OFTHR-474; THR-586 AND THR-645.

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