SIGIR_HUMAN - dbPTM
SIGIR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIGIR_HUMAN
UniProt AC Q6IA17
Protein Name Single Ig IL-1-related receptor
Gene Name SIGIRR
Organism Homo sapiens (Human).
Sequence Length 410
Subcellular Localization Membrane
Single-pass type III membrane protein .
Protein Description Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP..
Protein Sequence MPGVCDRAPDFLSPSEDQVLRPALGSSVALNCTAWVVSGPHCSLPSVQWLKDGLPLGIGGHYSLHEYSWVKANLSEVLVSSVLGVNVTSTEVYGAFTCSIQNISFSSFTLQRAGPTSHVAAVLASLLVLLALLLAALLYVKCRLNVLLWYQDAYGEVEINDGKLYDAYVSYSDCPEDRKFVNFILKPQLERRRGYKLFLDDRDLLPRAEPSADLLVNLSRCRRLIVVLSDAFLSRAWCSHSFREGLCRLLELTRRPIFITFEGQRRDPAHPALRLLRQHRHLVTLLLWRPGSVTPSSDFWKEVQLALPRKVQYRPVEGDPQTQLQDDKDPMLILRGRVPEGRALDSEVDPDPEGDLGVRGPVFGEPSAPPHTSGVSLGESRSSEVDVSDLGSRNYSARTDFYCLVSKDDM
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
31N-linked_GlycosylationLGSSVALNCTAWVVS
CCCCEECCCEEEEEE
16.03UniProtKB CARBOHYD
67PhosphorylationGHYSLHEYSWVKANL
CCCCHHHCCCHHCCH
9.3322468782
73N-linked_GlycosylationEYSWVKANLSEVLVS
HCCCHHCCHHHHHHH
38.08UniProtKB CARBOHYD
75PhosphorylationSWVKANLSEVLVSSV
CCHHCCHHHHHHHHH
26.0122468782
86N-linked_GlycosylationVSSVLGVNVTSTEVY
HHHHHCCCCCCCEEE
29.56UniProtKB CARBOHYD
102N-linked_GlycosylationAFTCSIQNISFSSFT
EEEEEEEEEEEEEEE
30.15UniProtKB CARBOHYD
165PhosphorylationEINDGKLYDAYVSYS
EECCCEEEEEEEECC
11.3023401153
168PhosphorylationDGKLYDAYVSYSDCP
CCEEEEEEEECCCCC
6.2423401153
170PhosphorylationKLYDAYVSYSDCPED
EEEEEEEECCCCCCC
13.2723401153
171PhosphorylationLYDAYVSYSDCPEDR
EEEEEEECCCCCCCC
9.8523401153
172PhosphorylationYDAYVSYSDCPEDRK
EEEEEECCCCCCCCC
25.8223401153
179UbiquitinationSDCPEDRKFVNFILK
CCCCCCCCHHHHHHH
67.02-
186UbiquitinationKFVNFILKPQLERRR
CHHHHHHHHHHHHHC
26.38-
196 (in isoform 2)Ubiquitination-35.2721890473
196 (in isoform 1)Ubiquitination-35.2721890473
196UbiquitinationLERRRGYKLFLDDRD
HHHHCCCEEEECCHH
35.272189047
211PhosphorylationLLPRAEPSADLLVNL
CCCCCCCCHHHHHHH
26.39-
219PhosphorylationADLLVNLSRCRRLIV
HHHHHHHHHHHHHHH
24.91-
239PhosphorylationFLSRAWCSHSFREGL
HHHHHHCCCHHHHHH
16.0926552605
241PhosphorylationSRAWCSHSFREGLCR
HHHHCCCHHHHHHHH
15.0926552605
253PhosphorylationLCRLLELTRRPIFIT
HHHHHHHHCCCEEEE
18.4327542207
328UbiquitinationQTQLQDDKDPMLILR
CCCCCCCCCCEEEEE
72.52-
346 (in isoform 2)Phosphorylation-40.1328111955
346PhosphorylationPEGRALDSEVDPDPE
CCCCCCCCCCCCCCC
40.1328188228
364 (in isoform 2)Phosphorylation-46.2525849741
366 (in isoform 2)Phosphorylation-35.8528450419
367PhosphorylationGPVFGEPSAPPHTSG
CCCCCCCCCCCCCCC
49.4523312004
372PhosphorylationEPSAPPHTSGVSLGE
CCCCCCCCCCCCCCC
32.7126074081
373PhosphorylationPSAPPHTSGVSLGES
CCCCCCCCCCCCCCC
33.8826074081
376PhosphorylationPPHTSGVSLGESRSS
CCCCCCCCCCCCCCC
33.8926074081
380PhosphorylationSGVSLGESRSSEVDV
CCCCCCCCCCCCCCH
35.3530576142
382PhosphorylationVSLGESRSSEVDVSD
CCCCCCCCCCCCHHH
39.8825849741
383PhosphorylationSLGESRSSEVDVSDL
CCCCCCCCCCCHHHC
40.2923911959
388PhosphorylationRSSEVDVSDLGSRNY
CCCCCCHHHCCCCCC
23.7428060719
392PhosphorylationVDVSDLGSRNYSART
CCHHHCCCCCCCCCC
25.3428060719
395PhosphorylationSDLGSRNYSARTDFY
HHCCCCCCCCCCCEE
11.5523312004
396PhosphorylationDLGSRNYSARTDFYC
HCCCCCCCCCCCEEE
18.1523312004
399PhosphorylationSRNYSARTDFYCLVS
CCCCCCCCCEEEEEE
30.1226552605
402PhosphorylationYSARTDFYCLVSKDD
CCCCCCEEEEEECCC
6.4128796482
406PhosphorylationTDFYCLVSKDDM---
CCEEEEEECCCC---
19.8828985074
464 (in isoform 2)Phosphorylation-23663014
465 (in isoform 2)Phosphorylation-23663014
466 (in isoform 2)Phosphorylation-23663014

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 SIGIR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIGIR_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 SIGIR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIGIR_HUMANSIGIRRphysical
12925853
IRAK1_HUMANIRAK1physical
12925853
TRAF6_HUMANTRAF6physical
12925853
A4_HUMANAPPphysical
21832049

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 SIGIR_HUMAN

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Related Literatures of Post-Translational Modification

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