IRF9_HUMAN - dbPTM
IRF9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IRF9_HUMAN
UniProt AC Q00978
Protein Name Interferon regulatory factor 9
Gene Name IRF9
Organism Homo sapiens (Human).
Sequence Length 393
Subcellular Localization Cytoplasm . Nucleus . Translocated into the nucleus upon activation by IFN-alpha/beta.
Protein Description Transcription factor that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state..
Protein Sequence MASGRARCTRKLRNWVVEQVESGQFPGVCWDDTAKTMFRIPWKHAGKQDFREDQDAAFFKAWAIFKGKYKEGDTGGPAVWKTRLRCALNKSSEFKEVPERGRMDVAEPYKVYQLLPPGIVSGQPGTQKVPSKRQHSSVSSERKEEEDAMQNCTLSPSVLQDSLNNEEEGASGGAVHSDIGSSSSSSSPEPQEVTDTTEAPFQGDQRSLEFLLPPEPDYSLLLTFIYNGRVVGEAQVQSLDCRLVAEPSGSESSMEQVLFPKPGPLEPTQRLLSQLERGILVASNPRGLFVQRLCPIPISWNAPQAPPGPGPHLLPSNECVELFRTAYFCRDLVRYFQGLGPPPKFQVTLNFWEESHGSSHTPQNLITVKMEQAFARYLLEQTPEQQAAILSLV
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
43AcetylationTMFRIPWKHAGKQDF
CCEECCCHHCCCCCC
20.4417923090
47UbiquitinationIPWKHAGKQDFREDQ
CCCHHCCCCCCCHHH
47.6929967540
47AcetylationIPWKHAGKQDFREDQ
CCCHHCCCCCCCHHH
47.6917923090
68AcetylationAWAIFKGKYKEGDTG
HHHHHCCCCCCCCCC
54.4617923090
81UbiquitinationTGGPAVWKTRLRCAL
CCCCHHHHHHHHHHH
19.7129967540
81AcetylationTGGPAVWKTRLRCAL
CCCCHHHHHHHHHHH
19.7117923090
90AcetylationRLRCALNKSSEFKEV
HHHHHHCCCCCCCCC
57.0917923090
110AcetylationMDVAEPYKVYQLLPP
CCCCCCCEEEECCCC
45.2217923090
128AcetylationSGQPGTQKVPSKRQH
CCCCCCCCCCCCCCC
56.8217923090
131PhosphorylationPGTQKVPSKRQHSSV
CCCCCCCCCCCCCCC
43.3827251275
132AcetylationGTQKVPSKRQHSSVS
CCCCCCCCCCCCCCC
50.4317923090
136PhosphorylationVPSKRQHSSVSSERK
CCCCCCCCCCCCCHH
24.8926699800
137PhosphorylationPSKRQHSSVSSERKE
CCCCCCCCCCCCHHH
24.7226699800
139PhosphorylationKRQHSSVSSERKEEE
CCCCCCCCCCHHHHH
28.5626699800
140PhosphorylationRQHSSVSSERKEEED
CCCCCCCCCHHHHHH
38.9926699800
238PhosphorylationVGEAQVQSLDCRLVA
CEEEEECCCEEEEEE
27.5830108239
248PhosphorylationCRLVAEPSGSESSME
EEEEEECCCCCCCCC
46.5928348404
250PhosphorylationLVAEPSGSESSMEQV
EEEECCCCCCCCCCC
38.3528348404
252PhosphorylationAEPSGSESSMEQVLF
EECCCCCCCCCCCCC
36.3624719451
253PhosphorylationEPSGSESSMEQVLFP
ECCCCCCCCCCCCCC
23.4528348404
273PhosphorylationEPTQRLLSQLERGIL
CHHHHHHHHHHHCEE
36.9924247654
361PhosphorylationESHGSSHTPQNLITV
HHCCCCCCCCCEEEE
28.63-

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

Oops, there are no upstream regulatory protein records of IRF9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IRF9_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 IRF9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT1_HUMANSTAT1physical
8943351
STAT2_HUMANSTAT2physical
8943351
STAT2_HUMANSTAT2physical
9242679
ARI3B_HUMANARID3Bphysical
20211142
VENTX_HUMANVENTXphysical
20211142
TLX3_HUMANTLX3physical
20211142
DMRTD_HUMANDMRTC2physical
20211142
DACH2_HUMANDACH2physical
20211142
STAT2_HUMANSTAT2physical
21903422
IRF1_HUMANIRF1physical
12799427
I2BP1_HUMANIRF2BP1physical
12799427
MYO1F_HUMANMYO1Fphysical
21988832
S10AD_HUMANS100A13physical
21988832
STAT2_HUMANSTAT2physical
28514442
RAD18_HUMANRAD18physical
28514442
UB2R2_HUMANUBE2R2physical
28514442
ARI1_HUMANARIH1physical
28514442
FBLN1_HUMANFBLN1physical
28514442
ANKH1_HUMANANKHD1physical
28514442
ANR17_HUMANANKRD17physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IRF9_HUMAN

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Related Literatures of Post-Translational Modification

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