Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)

 IL1AP_HUMAN             Reviewed;         570 AA.
Q9NPH3; B1NLD0; D3DNW0; O14915; Q86WJ7;
22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 2.
10-OCT-2018, entry version 158.
RecName: Full=Interleukin-1 receptor accessory protein;
Short=IL-1 receptor accessory protein;
Short=IL-1RAcP;
AltName: Full=Interleukin-1 receptor 3;
Short=IL-1R-3;
Short=IL-1R3;
Flags: Precursor;
Name=IL1RAP; Synonyms=C3orf13, IL1R3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
IL1R1 AND IRAK1.
TISSUE=Placenta;
PubMed=9371760; DOI=10.1073/pnas.94.24.12829;
Huang J., Gao X., Li S., Cao Z.;
"Recruitment of IRAK to the interleukin 1 receptor complex requires
interleukin 1 receptor accessory protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:12829-12832(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Saito T., Seki N.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
AND INDUCTION BY PHORBOL ESTERS.
TISSUE=Liver;
PubMed=10799889; DOI=10.4049/jimmunol.164.10.5277;
Jensen L.E., Muzio M., Mantovani A., Whitehead A.S.;
"IL-1 signaling cascade in liver cells and the involvement of a
soluble form of the IL-1 receptor accessory protein.";
J. Immunol. 164:5277-5286(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND INDUCTION BY
PHORBOL ESTERS.
TISSUE=Liver;
PubMed=12781872; DOI=10.1016/S0898-6568(03)00039-1;
Jensen L.E., Whitehead A.S.;
"Expression of alternatively spliced interleukin-1 receptor accessory
protein mRNAs is differentially regulated during inflammation and
apoptosis.";
Cell. Signal. 15:793-802(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=17949817; DOI=10.1016/j.molimm.2007.09.002;
Lu H.L., Yang C.Y., Chen H.C., Hung C.S., Chiang Y.C., Ting L.P.;
"A novel alternatively spliced interleukin-1 receptor accessory
protein mIL-1RAcP687.";
Mol. Immunol. 45:1374-1384(2008).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (ISOFORM 4), TISSUE
SPECIFICITY (ISOFORM 4), AND INTERACTION WITH IL1R1.
PubMed=19481478; DOI=10.1016/j.immuni.2009.03.020;
Smith D.E., Lipsky B.P., Russell C., Ketchem R.R., Kirchner J.,
Hensley K., Huang Y., Friedman W.J., Boissonneault V., Plante M.M.,
Rivest S., Sims J.E.;
"A central nervous system-restricted isoform of the interleukin-1
receptor accessory protein modulates neuronal responses to
interleukin-1.";
Immunity 30:817-831(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-179.
PubMed=9479509; DOI=10.1006/geno.1997.5113;
Dale M., Hammond D.W., Cox A., Nicklin M.J.H.;
"The human gene encoding the interleukin-1 receptor accessory protein
(IL1RAP) maps to chromosome 3q28 by fluorescence in situ hybridization
and radiation hybrid mapping.";
Genomics 47:325-326(1998).
[11]
INTERACTION WITH IL1R2.
PubMed=9862719;
Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
Martin M.U.;
"The type II IL-1 receptor interacts with the IL-1 receptor accessory
protein: a novel mechanism of regulation of IL-1 responsiveness.";
J. Immunol. 161:6871-6877(1998).
[12]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=10653850;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K.,
Hada T., Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[13]
INTERACTION WITH IRAK2.
PubMed=12659850; DOI=10.1016/S0006-291X(03)00385-1;
Boch J.A., Yoshida Y., Koyama Y., Wara-Aswapati N., Peng H., Unlu S.,
Auron P.E.;
"Characterization of a cascade of protein interactions initiated at
the IL-1 receptor.";
Biochem. Biophys. Res. Commun. 303:525-531(2003).
[14]
FUNCTION (SECRETED FORMS), AND TISSUE SPECIFICITY.
PubMed=12530978; DOI=10.1016/S1074-7613(02)00514-9;
Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M.,
MacVittie T.J., Virca G.D., Sims J.E.;
"The soluble form of IL-1 receptor accessory protein enhances the
ability of soluble type II IL-1 receptor to inhibit IL-1 action.";
Immunity 18:87-96(2003).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
FUNCTION, AND MODEL OF THE IL-33 SIGNALING COMPLEX.
PubMed=19836339; DOI=10.1016/j.str.2009.08.009;
Lingel A., Weiss T.M., Niebuhr M., Pan B., Appleton B.A., Wiesmann C.,
Bazan J.F., Fairbrother W.J.;
"Structure of IL-33 and its interaction with the ST2 and IL-1RAcP
receptors--insight into heterotrimeric IL-1 signaling complexes.";
Structure 17:1398-1410(2009).
[19]
TISSUE SPECIFICITY.
PubMed=20805474; DOI=10.1073/pnas.1004408107;
Jaeraas M., Johnels P., Hansen N., Agerstam H., Tsapogas P.,
Rissler M., Lassen C., Olofsson T., Bjerrum O.W., Richter J.,
Fioretos T.;
"Isolation and killing of candidate chronic myeloid leukemia stem
cells by antibody targeting of IL-1 receptor accessory protein.";
Proc. Natl. Acad. Sci. U.S.A. 107:16280-16285(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
TISSUE SPECIFICITY.
PubMed=22723552; DOI=10.1182/blood-2012-01-404699;
Barreyro L., Will B., Bartholdy B., Zhou L., Todorova T.I.,
Stanley R.F., Ben-Neriah S., Montagna C., Parekh S., Pellagatti A.,
Boultwood J., Paietta E., Ketterling R.P., Cripe L., Fernandez H.F.,
Greenberg P.L., Tallman M.S., Steidl C., Mitsiades C.S., Verma A.,
Steidl U.;
"Overexpression of IL-1 receptor accessory protein in stem and
progenitor cells and outcome correlation in AML and MDS.";
Blood 120:1290-1298(2012).
[22]
TISSUE SPECIFICITY.
PubMed=23479569; DOI=10.1182/blood-2012-09-458935;
Askmyr M., Aagerstam H., Hansen N., Gordon S., Arvanitakis A.,
Rissler M., Juliusson G., Richter J., Jaeraas M., Fioretos T.;
"Selective killing of candidate AML stem cells by antibody targeting
of IL1RAP.";
Blood 121:3709-3713(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
TISSUE SPECIFICITY.
PubMed=25595648; DOI=10.1152/ajplung.00305.2014;
Xia J., Zhao J., Shang J., Li M., Zeng Z., Zhao J., Wang J., Xu Y.,
Xie J.;
"Increased IL-33 expression in chronic obstructive pulmonary
disease.";
Am. J. Physiol. 308:L27-L27(2015).
[25]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 21-350 IN COMPLEX WITH IL1R2
AND IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-107;
ASN-111; ASN-118 AND ASN-209.
PubMed=20802483; DOI=10.1038/ni.1925;
Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
"Structural insights into the assembly and activation of IL-1beta with
its receptors.";
Nat. Immunol. 11:905-911(2010).
-!- FUNCTION: Coreceptor for IL1RL2 in the IL-36 signaling system (By
similarity). Coreceptor with IL1R1 in the IL-1 signaling system.
Associates with IL1R1 bound to IL1B to form the high affinity
interleukin-1 receptor complex which mediates interleukin-1-
dependent activation of NF-kappa-B and other pathways. Signaling
involves the recruitment of adapter molecules such as TOLLIP,
MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the
receptor/coreceptor subunits. Recruits TOLLIP to the signaling
complex. Does not bind to interleukin-1 alone; binding of IL1RN to
IL1R1, prevents its association with IL1R1 to form a signaling
complex. The cellular response is modulated through a non-
signaling association with the membrane IL1R2 decoy receptor.
Coreceptor for IL1RL1 in the IL-33 signaling system. Can
bidirectionally induce pre- and postsynaptic differentiation of
neurons by trans-synaptically binding to PTPRD (By similarity).
May play a role in IL1B-mediated costimulation of IFNG production
from T-helper 1 (Th1) cells (Probable).
{ECO:0000250|UniProtKB:Q61730, ECO:0000269|PubMed:10799889,
ECO:0000269|PubMed:9371760, ECO:0000305|PubMed:10653850,
ECO:0000305|PubMed:19836339}.
-!- FUNCTION: Isoform 2: Associates with secreted ligand-bound IL1R2
and increases the affinity of secreted IL1R2 for IL1B; this
complex formation may be the dominant mechanism for neutralization
of IL1B by secreted/soluble receptors (PubMed:12530978). Enhances
the ability of secreted IL1R1 to inhibit IL-33 signaling (By
similarity). {ECO:0000250|UniProtKB:Q61730,
ECO:0000269|PubMed:12530978}.
-!- FUNCTION: Isoform 4: Unable to mediate canonical IL-1 signaling
(PubMed:19481478). Required for Src phosphorylation by IL1B. May
be involved in IL1B-potentiated NMDA-induced calcium influx in
neurons (By similarity). {ECO:0000250|UniProtKB:Q61730,
ECO:0000269|PubMed:19481478}.
-!- SUBUNIT: The interleukin-36 receptor complex is a heterodimer of
IL1RL2 and IL1RAP; the association is inhibited by IL36RN (By
similarity). The interleukin-1 receptor complex is a heterodimer
of IL1R1 and IL1RAP. Associates with IL1R2 to form a non-signaling
interleukin-1 receptor complex. Isoform 4 interacts with IL1R1 in
a interleukin-1-dependent manner. Interacts with IL-33-bound
IL1RL1 to form the minimal interleukin-33 signaling complex with a
1:1:1 stoichiometry. Interacts with KIT (independently of
stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-
induced interleukin-33 signaling complex contains IL1RL1, IL1RAP,
KIT and MYD88 (By similarity). Interacts (via the first
immunoglobilin domain) with PTPRD (via the third immunoglobilin
domain); induces pre- and postsynaptic differentiation of neurons
(By similarity). {ECO:0000250|UniProtKB:Q61730,
ECO:0000269|PubMed:19481478, ECO:0000269|PubMed:20802483,
ECO:0000269|PubMed:9371760, ECO:0000269|PubMed:9862719,
ECO:0000305|PubMed:19836339}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Membrane-bound IL-1RAcP, mIL-1RAcP;
IsoId=Q9NPH3-1; Sequence=Displayed;
Name=2; Synonyms=Soluble IL-1RAcP, sIL-1RAcP;
IsoId=Q9NPH3-2; Sequence=VSP_008050, VSP_008051;
Name=3; Synonyms=Soluble IL-1RAcP-beta, sIL-1RAcP-beta;
IsoId=Q9NPH3-3; Sequence=VSP_008052;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4; Synonyms=AcPb, mIL-1RAcP687;
IsoId=Q9NPH3-5; Sequence=VSP_041256;
-!- TISSUE SPECIFICITY: Detected in liver, skin, placenta, thymus and
lung. Isoform 4 is predominantly expressed in brain. Overexpressed
on candidate chronic myeloid leukemia (CML) stem cells,
hematopoietic stem cells and mononuclear cells of patients with
acute myeloid leukemia (AML). Overexpressed in patients with
chronic obstructive pulmonary disease (COPD). Expressed in T-
helper 1 (Th1) and T-helper 2 (Th2) cell subsets
(PubMed:10653850). {ECO:0000269|PubMed:10653850,
ECO:0000269|PubMed:12530978, ECO:0000269|PubMed:19481478,
ECO:0000269|PubMed:20805474, ECO:0000269|PubMed:22723552,
ECO:0000269|PubMed:23479569, ECO:0000269|PubMed:25595648}.
-!- INDUCTION: Isoform 1 is down-regulated by phorbol ester treatment.
Isoform 2 is induced by phorbol ester treatment.
{ECO:0000269|PubMed:10799889, ECO:0000269|PubMed:12781872}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF029213; AAB84059.1; -; mRNA.
EMBL; AB006537; BAA25421.1; -; mRNA.
EMBL; AF167343; AAF71687.1; -; mRNA.
EMBL; AF167340; AAF71688.1; -; Genomic_DNA.
EMBL; AF167335; AAF71688.1; JOINED; Genomic_DNA.
EMBL; AF167336; AAF71688.1; JOINED; Genomic_DNA.
EMBL; AF167337; AAF71688.1; JOINED; Genomic_DNA.
EMBL; AF167338; AAF71688.1; JOINED; Genomic_DNA.
EMBL; AF167339; AAF71688.1; JOINED; Genomic_DNA.
EMBL; AF167342; AAF71689.1; -; Genomic_DNA.
EMBL; AF167335; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF167336; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF167337; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF167338; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF167339; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF167340; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF167341; AAF71689.1; JOINED; Genomic_DNA.
EMBL; AF538730; AAQ01755.1; -; mRNA.
EMBL; AF538731; AAQ01756.1; -; mRNA.
EMBL; AF538732; AAQ01757.1; -; mRNA.
EMBL; AF538733; AAQ01758.1; -; mRNA.
EMBL; AF538734; AAQ01759.1; -; mRNA.
EMBL; AF487335; AAO49451.1; -; mRNA.
EMBL; EF591790; ABU90811.1; -; mRNA.
EMBL; FJ998418; ACR82488.1; -; mRNA.
EMBL; AC008249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78100.1; -; Genomic_DNA.
EMBL; CH471052; EAW78102.1; -; Genomic_DNA.
EMBL; BC053621; AAH53621.1; -; mRNA.
EMBL; AF016261; AAC39609.1; -; Genomic_DNA.
CCDS; CCDS3298.1; -. [Q9NPH3-1]
CCDS; CCDS46982.1; -. [Q9NPH3-2]
CCDS; CCDS54696.1; -. [Q9NPH3-5]
RefSeq; NP_001161400.1; NM_001167928.1. [Q9NPH3-1]
RefSeq; NP_001161401.1; NM_001167929.1. [Q9NPH3-1]
RefSeq; NP_001161402.1; NM_001167930.1. [Q9NPH3-2]
RefSeq; NP_001161403.1; NM_001167931.1. [Q9NPH3-5]
RefSeq; NP_002173.1; NM_002182.3. [Q9NPH3-1]
RefSeq; NP_608273.1; NM_134470.3. [Q9NPH3-2]
UniGene; Hs.478673; -.
PDB; 3O4O; X-ray; 3.30 A; B=21-350.
PDB; 4DEP; X-ray; 3.10 A; C/F=21-367.
PDBsum; 3O4O; -.
PDBsum; 4DEP; -.
ProteinModelPortal; Q9NPH3; -.
SMR; Q9NPH3; -.
BioGrid; 109771; 20.
DIP; DIP-33487N; -.
IntAct; Q9NPH3; 12.
MINT; Q9NPH3; -.
GuidetoPHARMACOLOGY; 1897; -.
GlyConnect; 1425; -.
iPTMnet; Q9NPH3; -.
PhosphoSitePlus; Q9NPH3; -.
BioMuta; IL1RAP; -.
DMDM; 34222652; -.
EPD; Q9NPH3; -.
MaxQB; Q9NPH3; -.
PeptideAtlas; Q9NPH3; -.
PRIDE; Q9NPH3; -.
ProteomicsDB; 81999; -.
ProteomicsDB; 82000; -. [Q9NPH3-2]
ProteomicsDB; 82001; -. [Q9NPH3-3]
ProteomicsDB; 82002; -. [Q9NPH3-5]
DNASU; 3556; -.
Ensembl; ENST00000072516; ENSP00000072516; ENSG00000196083. [Q9NPH3-1]
Ensembl; ENST00000317757; ENSP00000314807; ENSG00000196083. [Q9NPH3-5]
Ensembl; ENST00000342550; ENSP00000345829; ENSG00000196083. [Q9NPH3-3]
Ensembl; ENST00000412504; ENSP00000412053; ENSG00000196083. [Q9NPH3-1]
Ensembl; ENST00000413869; ENSP00000416296; ENSG00000196083. [Q9NPH3-3]
Ensembl; ENST00000422485; ENSP00000409352; ENSG00000196083. [Q9NPH3-2]
Ensembl; ENST00000422940; ENSP00000387371; ENSG00000196083. [Q9NPH3-2]
Ensembl; ENST00000439062; ENSP00000401132; ENSG00000196083. [Q9NPH3-1]
Ensembl; ENST00000443369; ENSP00000408893; ENSG00000196083. [Q9NPH3-5]
Ensembl; ENST00000447382; ENSP00000390541; ENSG00000196083. [Q9NPH3-1]
GeneID; 3556; -.
KEGG; hsa:3556; -.
UCSC; uc003fsk.4; human. [Q9NPH3-1]
CTD; 3556; -.
DisGeNET; 3556; -.
EuPathDB; HostDB:ENSG00000196083.9; -.
GeneCards; IL1RAP; -.
HGNC; HGNC:5995; IL1RAP.
HPA; HPA035293; -.
MIM; 602626; gene.
neXtProt; NX_Q9NPH3; -.
OpenTargets; ENSG00000196083; -.
PharmGKB; PA29811; -.
GeneTree; ENSGT00760000119071; -.
HOGENOM; HOG000092977; -.
HOVERGEN; HBG104298; -.
InParanoid; Q9NPH3; -.
KO; K04723; -.
OMA; PERCDDW; -.
OrthoDB; EOG091G0GXW; -.
PhylomeDB; Q9NPH3; -.
TreeFam; TF325519; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-9014826; Interleukin-36 pathway.
Reactome; R-HSA-9014843; Interleukin-33 signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SignaLink; Q9NPH3; -.
SIGNOR; Q9NPH3; -.
ChiTaRS; IL1RAP; human.
EvolutionaryTrace; Q9NPH3; -.
GeneWiki; IL1RAP; -.
GenomeRNAi; 3556; -.
PRO; PR:Q9NPH3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000196083; Expressed in 175 organ(s), highest expression level in liver.
CleanEx; HS_IL1RAP; -.
ExpressionAtlas; Q9NPH3; baseline and differential.
Genevisible; Q9NPH3; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004908; F:interleukin-1 receptor activity; IEA:Ensembl.
GO; GO:0002114; F:interleukin-33 receptor activity; IEA:Ensembl.
GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0042094; P:interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0038172; P:interleukin-33-mediated signaling pathway; TAS:Reactome.
GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl.
GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
Inflammatory response; Innate immunity; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 570 Interleukin-1 receptor accessory protein.
/FTId=PRO_0000015450.
TOPO_DOM 21 367 Extracellular. {ECO:0000255}.
TRANSMEM 368 388 Helical. {ECO:0000255}.
TOPO_DOM 389 570 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 128 Ig-like C2-type 1.
DOMAIN 141 230 Ig-like C2-type 2.
DOMAIN 242 348 Ig-like C2-type 3.
DOMAIN 403 549 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 69 85 Essential for interaction with PTPRD.
{ECO:0000250|UniProtKB:Q61730}.
MOD_RES 557 557 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20802483}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20802483}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20802483}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20802483}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 24 122 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 47 114 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 137 181 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 160 212 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 266 332 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
VAR_SEQ 302 570 ISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVA
KAAKVKQKVPAPRYTVELACGFGATVLLVVILIVVYHVYWL
EMVLFYRAHFGTDETILDGKEYDIYVSYARNAEEEEFVLLT
LRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLL
VVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAV
KETKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMP
VKKSPRRSSSDEQGLSYSSLKNV -> ASSKIHSGTGLWFW
SHSPASGDSHCCLPCLLARDGPILPGSFWNR (in
isoform 3).
{ECO:0000303|PubMed:12781872}.
/FTId=VSP_008052.
VAR_SEQ 351 356 VPAPRY -> GNRCGQ (in isoform 2).
{ECO:0000303|PubMed:10799889,
ECO:0000303|PubMed:12781872,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008050.
VAR_SEQ 357 570 Missing (in isoform 2).
{ECO:0000303|PubMed:10799889,
ECO:0000303|PubMed:12781872,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008051.
VAR_SEQ 449 570 IVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLEN
MASRGNINVILVQYKAVKETKVKELKRAKTVLTVIKWKGEK
SKYPQGRFWKQLQVAMPVKKSPRRSSSDEQGLSYSSLKNV
-> NTVEAVFDFIQRSRRMIVVLSPDYVTEKSISMLEFKLG
VMCQNSIATKLIVVEYRPLEHPHPGILQLKESVSFVSWKGE
KSKHSGSKFWKALRLALPLRSLSASSGWNESCSSQSDISLD
HVQRRRSRLKEPPELQSSERAAGSPPAPGTMSKHRGKSSAT
CRCCVTYCEGENHLRNKSRAEIHNQPQWETHLCKPVPQESE
TQWIQNGTRLEPPAPQISALALHHFTDLSNNNDFYIL (in
isoform 4). {ECO:0000303|PubMed:17949817,
ECO:0000303|PubMed:19481478}.
/FTId=VSP_041256.
VARIANT 473 473 V -> M (in dbSNP:rs34661910).
/FTId=VAR_053383.
STRAND 25 29 {ECO:0000244|PDB:4DEP}.
STRAND 31 33 {ECO:0000244|PDB:3O4O}.
STRAND 36 38 {ECO:0000244|PDB:4DEP}.
STRAND 43 46 {ECO:0000244|PDB:4DEP}.
HELIX 49 53 {ECO:0000244|PDB:4DEP}.
STRAND 54 56 {ECO:0000244|PDB:4DEP}.
HELIX 58 63 {ECO:0000244|PDB:4DEP}.
STRAND 67 76 {ECO:0000244|PDB:4DEP}.
STRAND 80 82 {ECO:0000244|PDB:4DEP}.
HELIX 88 90 {ECO:0000244|PDB:4DEP}.
STRAND 92 95 {ECO:0000244|PDB:4DEP}.
STRAND 98 103 {ECO:0000244|PDB:4DEP}.
HELIX 106 108 {ECO:0000244|PDB:4DEP}.
STRAND 110 117 {ECO:0000244|PDB:4DEP}.
STRAND 122 132 {ECO:0000244|PDB:4DEP}.
STRAND 146 150 {ECO:0000244|PDB:4DEP}.
STRAND 154 159 {ECO:0000244|PDB:4DEP}.
STRAND 174 179 {ECO:0000244|PDB:4DEP}.
STRAND 188 193 {ECO:0000244|PDB:4DEP}.
STRAND 196 201 {ECO:0000244|PDB:4DEP}.
HELIX 204 206 {ECO:0000244|PDB:4DEP}.
STRAND 208 218 {ECO:0000244|PDB:4DEP}.
STRAND 221 234 {ECO:0000244|PDB:4DEP}.
HELIX 237 239 {ECO:0000244|PDB:4DEP}.
STRAND 244 248 {ECO:0000244|PDB:4DEP}.
STRAND 250 252 {ECO:0000244|PDB:3O4O}.
STRAND 266 270 {ECO:0000244|PDB:4DEP}.
STRAND 279 285 {ECO:0000244|PDB:4DEP}.
STRAND 300 303 {ECO:0000244|PDB:4DEP}.
STRAND 310 314 {ECO:0000244|PDB:4DEP}.
TURN 323 327 {ECO:0000244|PDB:3O4O}.
STRAND 331 335 {ECO:0000244|PDB:4DEP}.
STRAND 340 344 {ECO:0000244|PDB:4DEP}.
SEQUENCE 570 AA; 65418 MW; 5F47F8D0ECA98B8A CRC64;
MTLLWCVVSL YFYGILQSDA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST
AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT
YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG
CYKIQNFNNV IPEGMNLSFL IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVVGSPKNA
VPPVIHSPND HVVYEKEPGE ELLIPCTVYF SFLMDSRNEV WWTIDGKKPD DITIDVTINE
SISHSRTEDE TRTQILSIKK VTSEDLKRSY VCHARSAKGE VAKAAKVKQK VPAPRYTVEL
ACGFGATVLL VVILIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNAEEEEF
VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL
LELKAGLENM ASRGNINVIL VQYKAVKETK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK
QLQVAMPVKK SPRRSSSDEQ GLSYSSLKNV


Related products :

Catalog number Product name Quantity
26-207 IL1RAPL2 is a member of the interleukin 1 receptor family. This protein is similar to the interleukin 1 accessory proteins, and is most closely related to interleukin 1 receptor accessory protein-like 0.05 mg
C477 Interleukin-1 Receptor Accessory Protein IL-1RAcP lmg
C477 Interleukin-1 Receptor Accessory Protein IL-1RAcP 500
C033 Human Interleukin-1 Receptor Accessory Protein IL-1RAcP l0
CC08 Human Interleukin-1 Receptor Accessory Protein IL-1RAcP 50
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP 1 mg
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP 50 ug
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP 10 ug
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP 500 ug
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP, Source: HEK293 3x10μg
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP, Source: HEK293 50μg
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP, Source: HEK293 1mg
C477 Recombinant Human Interleukin-1 Receptor Accessory Protein_IL-1RAcP, Source: HEK293 500ug
CB73 Interleukin-18 receptor accessory protein IL18RAP (C-His tag) 500
E9331h Human Interleukin 18 Receptor Accessory Protein EL 96T
CC35 Interleukin-18 receptor accessory protein IL18RAP (C-Fc-His tag) 500
CB73 Interleukin-18 receptor accessory protein IL18RAP (C-His tag) lmg
CC35 Interleukin-18 receptor accessory protein IL18RAP (C-Fc-His tag) lmg
IRPL1_RAT Rat ELISA Kit FOR Interleukin-1 receptor accessory protein-like 1 96T
E97819Mu ELISA Kit for Interleukin 1 Receptor Accessory Protein (IL1RAP) 96T/Kit
E91655Hu ELISA Kit for Interleukin 18 Receptor Accessory Protein (IL18RAP) 96T/Kit
CSB-EL011624RA Rat Interleukin-1 receptor accessory protein-like 1(IL1RAPL1) ELISA kit 96T
E97819Hu ELISA Kit for Interleukin 1 Receptor Accessory Protein (IL1RAP) 96T/Kit
CSB-EL011623RA Rat Interleukin-1 receptor accessory protein(IL1RAP) ELISA kit 96T
IL1RL2 IL1RAPL2 Gene interleukin 1 receptor accessory protein-like 2


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur