IRF2_HUMAN - dbPTM
IRF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IRF2_HUMAN
UniProt AC P14316
Protein Name Interferon regulatory factor 2
Gene Name IRF2
Organism Homo sapiens (Human).
Sequence Length 349
Subcellular Localization Nucleus.
Protein Description Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation..
Protein Sequence MPVERMRMRPWLEEQINSNTIPGLKWLNKEKKIFQIPWMHAARHGWDVEKDAPLFRNWAIHTGKHQPGVDKPDPKTWKANFRCAMNSLPDIEEVKDKSIKKGNNAFRVYRMLPLSERPSKKGKKPKTEKEDKVKHIKQEPVESSLGLSNGVSDLSPEYAVLTSTIKNEVDSTVNIIVVGQSHLDSNIENQEIVTNPPDICQVVEVTTESDEQPVSMSELYPLQISPVSSYAESETTDSVPSDEESAEGRPHWRKRNIEGKQYLSNMGTRGSYLLPGMASFVTSNKPDLQVTIKEESNPVPYNSSWPPFQDLPLSSSMTPASSSSRPDRETRASVIKKTSDITQARVKSC
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
18PhosphorylationWLEEQINSNTIPGLK
HHHHHHHCCCCCCCH		36.6625022875
29AcetylationPGLKWLNKEKKIFQI
CCCHHHCCCCEEEEC		69.6012738767
31AcetylationLKWLNKEKKIFQIPW
CHHHCCCCEEEECCH		53.4212738767
32AcetylationKWLNKEKKIFQIPWM
HHHCCCCEEEECCHH		50.2512738767
75AcetylationGVDKPDPKTWKANFR
CCCCCCHHHHHHHHH		74.5212738767
78SumoylationKPDPKTWKANFRCAM
CCCHHHHHHHHHHHH		38.39-
78UbiquitinationKPDPKTWKANFRCAM
CCCHHHHHHHHHHHH		38.3912738767
78SumoylationKPDPKTWKANFRCAM
CCCHHHHHHHHHHHH		38.3912738767
78AcetylationKPDPKTWKANFRCAM
CCCHHHHHHHHHHHH		38.3912738767
98PhosphorylationIEEVKDKSIKKGNNA
HHHHHHHCCCCCCCC		50.1828509920
115PhosphorylationVYRMLPLSERPSKKG
EEEECCCCCCCCCCC		29.6228348404
119PhosphorylationLPLSERPSKKGKKPK
CCCCCCCCCCCCCCC		53.9023186163
137SumoylationEDKVKHIKQEPVESS
HHHHHHHHHCCCCHH		48.61-
137SumoylationEDKVKHIKQEPVESS
HHHHHHHHHCCCCHH		48.6128112733
143PhosphorylationIKQEPVESSLGLSNG
HHHCCCCHHHCCCCC		30.9730108239
144PhosphorylationKQEPVESSLGLSNGV
HHCCCCHHHCCCCCC		16.9830108239
148PhosphorylationVESSLGLSNGVSDLS
CCHHHCCCCCCCCCC		29.7326657352
152PhosphorylationLGLSNGVSDLSPEYA
HCCCCCCCCCCHHHH		33.9430108239
155PhosphorylationSNGVSDLSPEYAVLT
CCCCCCCCHHHHHHH		22.2229523821
158PhosphorylationVSDLSPEYAVLTSTI
CCCCCHHHHHHHHHH		12.8529523821
162PhosphorylationSPEYAVLTSTIKNEV
CHHHHHHHHHHHHCC		19.7529523821
163PhosphorylationPEYAVLTSTIKNEVD
HHHHHHHHHHHHCCC		24.7919413330
164PhosphorylationEYAVLTSTIKNEVDS
HHHHHHHHHHHCCCC		30.6419413330
166SumoylationAVLTSTIKNEVDSTV
HHHHHHHHHCCCCCE		47.33-
166SumoylationAVLTSTIKNEVDSTV
HHHHHHHHHCCCCCE		47.3328112733
225PhosphorylationELYPLQISPVSSYAE
HCCCEEECCCCHHCC		13.2928112733
228PhosphorylationPLQISPVSSYAESET
CEEECCCCHHCCCCC		22.4826074081
229PhosphorylationLQISPVSSYAESETT
EEECCCCHHCCCCCC		28.7026074081
230PhosphorylationQISPVSSYAESETTD
EECCCCHHCCCCCCC		13.5926074081
241PhosphorylationETTDSVPSDEESAEG
CCCCCCCCCHHHCCC		56.3424275569
245PhosphorylationSVPSDEESAEGRPHW
CCCCCHHHCCCCCCH		29.5824275569
260SumoylationRKRNIEGKQYLSNMG
HHCCCCCHHHHHHCC		23.99-
260SumoylationRKRNIEGKQYLSNMG
HHCCCCCHHHHHHCC		23.99-
271PhosphorylationSNMGTRGSYLLPGMA
HHCCCCCCCCCCCHH		14.8727067055
272PhosphorylationNMGTRGSYLLPGMAS
HCCCCCCCCCCCHHH		18.3227067055
293SumoylationPDLQVTIKEESNPVP
CCCEEEEEECCCCCC		46.17-
293SumoylationPDLQVTIKEESNPVP
CCCEEEEEECCCCCC		46.17-
333PhosphorylationPDRETRASVIKKTSD
CCHHHHHHHHHHHHH		22.5328348404
338PhosphorylationRASVIKKTSDITQAR
HHHHHHHHHHCHHHH		26.9923401153
339PhosphorylationASVIKKTSDITQARV
HHHHHHHHHCHHHHH		35.5827732954
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
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:19032150
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
75KAcetylation

12738767
137KSumoylation

18514056
293KSumoylation

18514056
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 IRF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAT2B_HUMANKAT2Bphysical
11304541
EP300_HUMANEP300physical
11304541
KAT2B_HUMANKAT2Bphysical
10022868
KAT2A_HUMANKAT2Aphysical
10022868
BRD7_HUMANBRD7physical
11025449
ATG7_HUMANATG7physical
21903422
I2BPL_HUMANIRF2BPLphysical
21903422
FOXK1_HUMANFOXK1physical
21903422
FOXK2_HUMANFOXK2physical
21903422
HCFC1_HUMANHCFC1physical
21903422
HCFC2_HUMANHCFC2physical
21903422
I2BP1_HUMANIRF2BP1physical
21903422
I2BP2_HUMANIRF2BP2physical
21903422
AP5Z1_HUMANAP5Z1physical
21903422
PP2BA_HUMANPPP3CAphysical
21903422
PP2BB_HUMANPPP3CBphysical
21903422
MDM2_HUMANMDM2physical
19032150
I2BP1_HUMANIRF2BP1physical
12799427
I2BP2_HUMANIRF2BP2physical
12799427
A4_HUMANAPPphysical
21832049
NUCL_HUMANNCLphysical
16582966
I2BPL_HUMANIRF2BPLphysical
28514442
F208B_HUMANFAM208Bphysical
28514442
CATS_HUMANCTSSphysical
28514442
I2BP2_HUMANIRF2BP2physical
28514442
I2BP1_HUMANIRF2BP1physical
28514442
FOXK2_HUMANFOXK2physical
28514442
FOXK1_HUMANFOXK1physical
28514442
HCFC2_HUMANHCFC2physical
28514442
PRDM1_HUMANPRDM1genetic
28494239
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
There are no disease associations of PTM sites.
Regulatory Network of IRF2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Interferon regulatory factor-2 regulates cell growth through itsacetylation.";
Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.;
J. Biol. Chem. 278:25401-25407(2003).
Cited for: ACETYLATION AT LYS-75 AND LYS-78, INTERACTION WITH CREBBP, FUNCTION,MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-75 AND LYS-78.
Sumoylation
ReferencePubMed
"Regulation of IRF2 transcriptional activity by its sumoylation.";
Han K.-J., Jiang L., Shu H.-B.;
Biochem. Biophys. Res. Commun. 372:772-778(2008).
Cited for: SUMOYLATION AT LYS-137; LYS-166 AND LYS-293, FUNCTION, AND MUTAGENESISOF LYS-137; LYS-166 AND LYS-293.

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