IRF4_HUMAN - dbPTM
IRF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IRF4_HUMAN
UniProt AC Q15306
Protein Name Interferon regulatory factor 4
Gene Name IRF4
Organism Homo sapiens (Human).
Sequence Length 451
Subcellular Localization Nucleus.
Protein Description Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes (By similarity)..
Protein Sequence MNLEGGGRGGEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSIFRIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCALNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLEDPQMSMSHPYTMTTPYPSLPAQQVHNYMMPPLDRSWRDYVPDQPHPEIPYQCPMTFGPRGHHWQGPACENGCQVTGTFYACAPPESQAPGVPTEPSIRSAEALAFSDCRLHICLYYREILVKELTTSSPEGCRISHGHTYDASNLDQVLFPYPEDNGQRKNIEKLLSHLERGVVLWMAPDGLYAKRLCQSRIYWDGPLALCNDRPNKLERDQTCKLFDTQQFLSELQAFAHHGRSLPRFQVTLCFGEEFPDPQRQRKLITAHVEPLLARQLYYFAQQNSGHFLRGYDLPEHISNPEDYHRSIRHSSIQE
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
36UbiquitinationIDQIDSGKYPGLVWE
HHHHHCCCCCCCEEE		52.83-
37PhosphorylationDQIDSGKYPGLVWEN
HHHHCCCCCCCEEEC		13.1720090780
48PhosphorylationVWENEEKSIFRIPWK
EEECCCCEEEECCCC		30.18-
59UbiquitinationIPWKHAGKQDYNREE
CCCCCCCCCCCCHHH		40.56-
62PhosphorylationKHAGKQDYNREEDAA
CCCCCCCCCHHHHHH		17.39-
78MalonylationFKAWALFKGKFREGI
HHHHHHHCCCCCCCC		63.1426320211
103UbiquitinationRLRCALNKSNDFEEL
HHHHHHHCCCCHHHH		52.0322817900
103 (in isoform 1)Ubiquitination-52.0321906983
103 (in isoform 2)Ubiquitination-52.0321906983
103AcetylationRLRCALNKSNDFEEL
HHHHHHHCCCCHHHH		52.0312431469
104PhosphorylationLRCALNKSNDFEELV
HHHHHHCCCCHHHHH		40.3330108239
114PhosphorylationFEELVERSQLDISDP
HHHHHHHHCCCCCCC		22.9130177828
119PhosphorylationERSQLDISDPYKVYR
HHHCCCCCCCCCEEE		32.0030108239
122PhosphorylationQLDISDPYKVYRIVP
CCCCCCCCCEEEECC		20.3420090780
123UbiquitinationLDISDPYKVYRIVPE
CCCCCCCCEEEECCC		37.8722817900
123 (in isoform 2)Ubiquitination-37.8721906983
123 (in isoform 1)Ubiquitination-37.8721906983
125PhosphorylationISDPYKVYRIVPEGA
CCCCCCEEEECCCHH		7.1720090780
140PhosphorylationKKGAKQLTLEDPQMS
HHCCCCCCCCCCCCC		26.1322210691
160PhosphorylationTMTTPYPSLPAQQVH
CCCCCCCCCCHHHHH		40.9322210691
177PhosphorylationMMPPLDRSWRDYVPD
CCCCCCCCHHHCCCC		26.57-
181PhosphorylationLDRSWRDYVPDQPHP
CCCCHHHCCCCCCCC		12.81-
192PhosphorylationQPHPEIPYQCPMTFG
CCCCCCCCCCCCCCC		28.5422817900
201MethylationCPMTFGPRGHHWQGP
CCCCCCCCCCCCCCC		58.41115386575
257PhosphorylationCRLHICLYYREILVK
CEEHHHHHHHHHHHH		8.9629083192
258PhosphorylationRLHICLYYREILVKE
EEHHHHHHHHHHHHH		6.7129083192
263 (in isoform 2)Ubiquitination-5.7821906983
264UbiquitinationYYREILVKELTTSSP
HHHHHHHHHHCCCCC		43.4921906983
264 (in isoform 1)Ubiquitination-43.4921906983
267PhosphorylationEILVKELTTSSPEGC
HHHHHHHCCCCCCCC		26.2329083192
268PhosphorylationILVKELTTSSPEGCR
HHHHHHCCCCCCCCE		39.5729083192
269PhosphorylationLVKELTTSSPEGCRI
HHHHHCCCCCCCCEE		38.3629083192
270PhosphorylationVKELTTSSPEGCRIS
HHHHCCCCCCCCEEC		25.5229083192
306UbiquitinationGQRKNIEKLLSHLER
CCCCCHHHHHHHHHH		51.43-
309O-linked_GlycosylationKNIEKLLSHLERGVV
CCHHHHHHHHHHCEE		36.1430379171
325PhosphorylationWMAPDGLYAKRLCQS
EECCCCHHHHHHHCC		18.66-
326 (in isoform 2)Ubiquitination-8.7821906983
327 (in isoform 1)Ubiquitination-32.1421906983
327UbiquitinationAPDGLYAKRLCQSRI
CCCCHHHHHHHCCCE		32.1421906983
349UbiquitinationLCNDRPNKLERDQTC
ECCCCCCCCCCCCHH		55.17-
356 (in isoform 2)Ubiquitination-2.7521906983
357 (in isoform 1)Ubiquitination-56.4221906983
357UbiquitinationLERDQTCKLFDTQQF
CCCCCHHHCCCHHHH		56.422190698
363UbiquitinationCKLFDTQQFLSELQA
HHCCCHHHHHHHHHH		43.2525015289
398UbiquitinationFPDPQRQRKLITAHV
CCCHHHHHHHHHHCH		37.6325015289
399UbiquitinationPDPQRQRKLITAHVE
CCHHHHHHHHHHCHH		35.5825015289
428PhosphorylationSGHFLRGYDLPEHIS
CCCCCCCCCCCHHHC		14.1020090780
435PhosphorylationYDLPEHISNPEDYHR
CCCCHHHCCHHHHHH		48.5230108239
440PhosphorylationHISNPEDYHRSIRHS
HHCCHHHHHHHHHHH		9.4720090780
443PhosphorylationNPEDYHRSIRHSSIQ
CHHHHHHHHHHHHCC		15.6327080861
447PhosphorylationYHRSIRHSSIQE---
HHHHHHHHHCCC---		21.2030108239
448PhosphorylationHRSIRHSSIQE----
HHHHHHHHCCC----		23.3630108239
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
447SPhosphorylationKinaseROCK2O75116
Uniprot
448SPhosphorylationKinaseROCK2O75116
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IRF4_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 IRF4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
16189514
STAT6_HUMANSTAT6physical
10601358
BCL6_HUMANBCL6physical
10601358
NFAC2_HUMANNFATC2physical
11956291
SPI1_HUMANSPI1physical
10022840
SPI1_HUMANSPI1physical
12372320
PRDM1_MOUSEPrdm1physical
11342629
PROX1_HUMANPROX1physical
20211142
HXB13_HUMANHOXB13physical
20211142
BATF_HUMANBATFphysical
20211142
ETV7_HUMANETV7physical
20211142
PRC2B_HUMANPRRC2Bphysical
21903422
CARM1_HUMANCARM1physical
21903422
ELP1_HUMANIKBKAPphysical
21903422
IRAK1_HUMANIRAK1physical
21903422
PEG10_HUMANPEG10physical
21903422
TLK2_HUMANTLK2physical
21903422
VPS35_HUMANVPS35physical
21903422
YTDC2_HUMANYTHDC2physical
21903422
BCL6_HUMANBCL6physical
11342629
STAT6_HUMANSTAT6physical
11342629
RIPK2_HUMANRIPK2physical
24670424
MYD88_HUMANMYD88physical
24670424
TRAF6_HUMANTRAF6physical
24670424
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
254500Multiple myeloma (MM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IRF4_HUMAN

loading...

Related Literatures of Post-Translational Modification

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