IRF5_HUMAN - dbPTM
IRF5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IRF5_HUMAN
UniProt AC Q13568
Protein Name Interferon regulatory factor 5
Gene Name IRF5
Organism Homo sapiens (Human).
Sequence Length 498
Subcellular Localization Cytoplasm. Nucleus. Shuttles between the nucleus and the cytoplasm.
Protein Description Transcription factor involved in the induction of interferons IFNA and INFB and inflammatory cytokines upon virus infection. Activated by TLR7 or TLR8 signaling..
Protein Sequence MNQSIPVAPTPPRRVRLKPWLVAQVNSCQYPGLQWVNGEKKLFCIPWRHATRHGPSQDGDNTIFKAWAKETGKYTEGVDEADPAKWKANLRCALNKSRDFRLIYDGPRDMPPQPYKIYEVCSNGPAPTDSQPPEDYSFGAGEEEEEEEELQRMLPSLSLTEDVKWPPTLQPPTLRPPTLQPPTLQPPVVLGPPAPDPSPLAPPPGNPAGFRELLSEVLEPGPLPASLPPAGEQLLPDLLISPHMLPLTDLEIKFQYRGRPPRALTISNPHGCRLFYSQLEATQEQVELFGPISLEQVRFPSPEDIPSDKQRFYTNQLLDVLDRGLILQLQGQDLYAIRLCQCKVFWSGPCASAHDSCPNPIQREVKTKLFSLEHFLNELILFQKGQTNTPPPFEIFFCFGEEWPDRKPREKKLITVQVVPVAARLLLEMFSGELSWSADSIRLQISNPDLKDRMVEQFKELHHIWQSQQRLQPVAQAPPGAGLGVGQGPWPMHPAGMQ
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
10PhosphorylationQSIPVAPTPPRRVRL
CCCCCCCCCCCEECC		35.8722412986
74PhosphorylationWAKETGKYTEGVDEA
HHHHHCCCCCCCCCC		16.0326074081
75PhosphorylationAKETGKYTEGVDEAD
HHHHCCCCCCCCCCC		29.7426074081
136PhosphorylationDSQPPEDYSFGAGEE
CCCCCCCCCCCCCCC		12.30-
156PhosphorylationELQRMLPSLSLTEDV
HHHHHHHHCCCCCCC		26.9927794612
158PhosphorylationQRMLPSLSLTEDVKW
HHHHHHCCCCCCCCC		37.2722412986
160PhosphorylationMLPSLSLTEDVKWPP
HHHHCCCCCCCCCCC		27.1127794612
293PhosphorylationVELFGPISLEQVRFP
HHHHCCCCHHHCCCC		29.0522412986
301PhosphorylationLEQVRFPSPEDIPSD
HHHCCCCCHHHCCCH		37.9022412986
309UbiquitinationPEDIPSDKQRFYTNQ
HHHCCCHHHHHHHHH		47.94-
313PhosphorylationPSDKQRFYTNQLLDV
CCHHHHHHHHHHHHH		13.63-
335PhosphorylationQLQGQDLYAIRLCQC
EECCCCEEEEEECCC		14.31-
411UbiquitinationPDRKPREKKLITVQV
CCCCCCCCCCEEEEH		54.9118824541
412UbiquitinationDRKPREKKLITVQVV
CCCCCCCCCEEEEHH		40.1318824541
430 (in isoform 4)O-linked_Glycosylation-6.5732494619
431PhosphorylationRLLLEMFSGELSWSA
HHHHHHHCCCCCCCC		30.01-
435PhosphorylationEMFSGELSWSADSIR
HHHCCCCCCCCCEEE		18.0622412986
437PhosphorylationFSGELSWSADSIRLQ
HCCCCCCCCCEEEEE		20.8718836453
440PhosphorylationELSWSADSIRLQISN
CCCCCCCEEEEEECC		14.8818836453
446PhosphorylationDSIRLQISNPDLKDR
CEEEEEECCCCHHHH		29.3711303025
462PhosphorylationVEQFKELHHIWQSQQ
HHHHHHHHHHHHCHH		16.1027251275
467PhosphorylationELHHIWQSQQRLQPV
HHHHHHHCHHHCCCC		17.1824247654
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
158SPhosphorylationKinaseTBK1Q9UHD2
Uniprot
293SPhosphorylationKinaseTBK1Q9UHD2
Uniprot
313YPhosphorylationKinaseLYNP07948
PSP
335YPhosphorylationKinaseLYNP07948
PSP
446SPhosphorylationKinaseIKBKBO14920
GPS
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:18824541
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IRF5_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 IRF5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI15_HUMANTRIM15physical
20211142
SIN3A_HUMANSIN3Aphysical
20935208
NCOR2_HUMANNCOR2physical
20935208
HDAC1_HUMANHDAC1physical
20935208
EP300_HUMANEP300physical
20935208
CBP_HUMANCREBBPphysical
20935208
PPBI_HUMANALPIphysical
19786094
IRF5_HUMANIRF5physical
19786094
CE152_HUMANCEP152physical
21903422
CSN1_HUMANGPS1physical
21903422
GRB2_HUMANGRB2physical
21903422
GTPB1_HUMANGTPBP1physical
21903422
GTPB2_HUMANGTPBP2physical
21903422
ZEP1_HUMANHIVEP1physical
21903422
MAVS_HUMANMAVSphysical
21903422
PPM1G_HUMANPPM1Gphysical
21903422
RGS3_HUMANRGS3physical
21903422
CSN7B_HUMANCOPS7Bphysical
23275442
CSN1_HUMANGPS1physical
23275442
CSN2_HUMANCOPS2physical
23275442
CSN3_HUMANCOPS3physical
23275442
CSN4_HUMANCOPS4physical
23275442
CSN5_HUMANCOPS5physical
23275442
CSN6_HUMANCOPS6physical
23275442
CSN8_HUMANCOPS8physical
23275442
IRF5_HUMANIRF5physical
18836453
SGTA_HUMANSGTAphysical
21988832
BIRC3_HUMANBIRC3physical
25565375
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612245Inflammatory bowel disease 14 (IBD14)
612251Systemic lupus erythematosus 10 (SLEB10)
180300Rheumatoid arthritis (RA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IRF5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Insights into interferon regulatory factor activation from thecrystal structure of dimeric IRF5.";
Chen W., Lam S.S., Srinath H., Jiang Z., Correia J.J., Schiffer C.A.,Fitzgerald K.A., Lin K., Royer W.E. Jr.;
Nat. Struct. Mol. Biol. 15:1213-1220(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 232-477 OF MUTANT ASP-440,SUBUNIT, AND PHOSPHORYLATION AT SER-435; SER-437; SER-440 AND SER-446.
"Activation of interferon regulatory factor 5 by site specificphosphorylation.";
Chang Foreman H.C., Van Scoy S., Cheng T.F., Reich N.C.;
PLoS ONE 7:E33098-E33098(2012).
Cited for: PHOSPHORYLATION AT THR-10; SER-158; SER-293; SER-301; SER-435 ANDSER-446, AND SUBCELLULAR LOCATION.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Functional regulation of MyD88-activated interferon regulatory factor5 by K63-linked polyubiquitination.";
Balkhi M.Y., Fitzgerald K.A., Pitha P.M.;
Mol. Cell. Biol. 28:7296-7308(2008).
Cited for: UBIQUITINATION AT LYS-411 AND LYS-412 BY TRAF6.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory