IRAK3_HUMAN - dbPTM
IRAK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IRAK3_HUMAN
UniProt AC Q9Y616
Protein Name Interleukin-1 receptor-associated kinase 3
Gene Name IRAK3 {ECO:0000312|EMBL:AAH57800.1}
Organism Homo sapiens (Human).
Sequence Length 596
Subcellular Localization
Protein Description Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex..
Protein Sequence MAGNCGARGALSAHTLLFDLPPALLGELCAVLDSCDGALGWRGLAERLSSSWLDVRHIEKYVDQGKSGTRELLWSWAQKNKTIGDLLQVLQEMGHRRAIHLITNYGAVLSPSEKSYQEGGFPNILFKETANVTVDNVLIPEHNEKGILLKSSISFQNIIEGTRNFHKDFLIGEGEIFEVYRVEIQNLTYAVKLFKQEKKMQCKKHWKRFLSELEVLLLFHHPNILELAAYFTETEKFCLIYPYMRNGTLFDRLQCVGDTAPLPWHIRIGILIGISKAIHYLHNVQPCSVICGSISSANILLDDQFQPKLTDFAMAHFRSHLEHQSCTINMTSSSSKHLWYMPEEYIRQGKLSIKTDVYSFGIVIMEVLTGCRVVLDDPKHIQLRDLLRELMEKRGLDSCLSFLDKKVPPCPRNFSAKLFCLAGRCAATRAKLRPSMDEVLNTLESTQASLYFAEDPPTSLKSFRCPSPLFLENVPSIPVEDDESQNNNLLPSDEGLRIDRMTQKTPFECSQSEVMFLSLDKKPESKRNEEACNMPSSSCEESWFPKYIVPSQDLRPYKVNIDPSSEAPGHSCRSRPVESSCSSKFSWDEYEQYKKE
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
49 (in isoform 2)Phosphorylation-28.6625278378
51 (in isoform 2)Phosphorylation-28.4325278378
51PhosphorylationLAERLSSSWLDVRHI
HHHHHHCCCEEHHHH		28.4324247654
54 (in isoform 2)Phosphorylation-29.1925278378
55 (in isoform 2)Phosphorylation-4.4925278378
61PhosphorylationDVRHIEKYVDQGKSG
EHHHHHHHHHCCCCC		9.1124719451
67PhosphorylationKYVDQGKSGTRELLW
HHHHCCCCCHHHHHH		52.8224719451
69PhosphorylationVDQGKSGTRELLWSW
HHCCCCCHHHHHHHH		28.2329978859
75PhosphorylationGTRELLWSWAQKNKT
CHHHHHHHHHHHCCC		16.7129978859
110PhosphorylationTNYGAVLSPSEKSYQ
HCCCCEECCCHHHHH		21.5619369195
112PhosphorylationYGAVLSPSEKSYQEG
CCCEECCCHHHHHCC		55.0428450419
115PhosphorylationVLSPSEKSYQEGGFP
EECCCHHHHHCCCCC		28.1824247654
116PhosphorylationLSPSEKSYQEGGFPN
ECCCHHHHHCCCCCC		22.9623532336
131UbiquitinationILFKETANVTVDNVL
CEEEECCCEEECCEE		37.1021890473
131UbiquitinationILFKETANVTVDNVL
CEEEECCCEEECCEE		37.1021890473
154PhosphorylationILLKSSISFQNIIEG
EEEEEEEECCHHHHC		23.8024247654
162PhosphorylationFQNIIEGTRNFHKDF
CCHHHHCCCCCCCCC		15.06-
188PhosphorylationRVEIQNLTYAVKLFK
EEEEEHHHHHHHHHH		19.5819835603
189PhosphorylationVEIQNLTYAVKLFKQ
EEEEHHHHHHHHHHH		16.7419835603
192UbiquitinationQNLTYAVKLFKQEKK
EHHHHHHHHHHHHHH		39.7821890473
199AcetylationKLFKQEKKMQCKKHW
HHHHHHHHHHCHHHH		33.197377661
318UbiquitinationDFAMAHFRSHLEHQS
HHHHHHHHHHHHHCC		17.1921890473
318UbiquitinationDFAMAHFRSHLEHQS
HHHHHHHHHHHHHCC		17.1921890473
325PhosphorylationRSHLEHQSCTINMTS
HHHHHHCCEEEEECC		18.3524247654
327PhosphorylationHLEHQSCTINMTSSS
HHHHCCEEEEECCCC		22.1921082442
331PhosphorylationQSCTINMTSSSSKHL
CCEEEEECCCCCCEE		22.4429759185
332PhosphorylationSCTINMTSSSSKHLW
CEEEEECCCCCCEEE		19.9029759185
333PhosphorylationCTINMTSSSSKHLWY
EEEEECCCCCCEEEE		29.4829759185
334PhosphorylationTINMTSSSSKHLWYM
EEEECCCCCCEEEEC		43.0829759185
379UbiquitinationRVVLDDPKHIQLRDL
EEECCCCCHHCHHHH		61.4022817900
398PhosphorylationMEKRGLDSCLSFLDK
HHHCCHHHHHHHHHC		23.23-
401PhosphorylationRGLDSCLSFLDKKVP
CCHHHHHHHHHCCCC		28.26-
415PhosphorylationPPCPRNFSAKLFCLA
CCCCCCHHHHHHHHH		28.2217192257
467PhosphorylationLKSFRCPSPLFLENV
CHHCCCCCCCCCCCC		37.5519369195
484PhosphorylationIPVEDDESQNNNLLP
CCCCCCCCCCCCCCC		45.2422817900
510PhosphorylationQKTPFECSQSEVMFL
CCCCCCCCCCCEEEE		29.5522817900
512PhosphorylationTPFECSQSEVMFLSL
CCCCCCCCCEEEEEC		18.8322817900
518PhosphorylationQSEVMFLSLDKKPES
CCCEEEEECCCCCCH		24.2128060719
547PhosphorylationEESWFPKYIVPSQDL
HHCCCCCCCCCCCCC		13.8527642862
551O-linked_GlycosylationFPKYIVPSQDLRPYK
CCCCCCCCCCCCCEE		25.9830379171
590PhosphorylationSKFSWDEYEQYKKE-
CCCCHHHHHHHHCC-		13.0827642862
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 IRAK3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IRAK3_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 IRAK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IRAK1_HUMANIRAK1physical
21903422
IRAK2_HUMANIRAK2physical
21903422
IRAK4_HUMANIRAK4physical
21903422
NSA2_HUMANNSA2physical
21988832
NONO_HUMANNONOphysical
21988832
NTRK3_HUMANNTRK3physical
21988832
LDB1_HUMANLDB1physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611064Asthma-related traits 5 (ASRT5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IRAK3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-110; SER-154; SER-415;SER-467; SER-484; SER-510 AND SER-512, AND MASS SPECTROMETRY.

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