Q9NPH3 (IL1AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-1 receptor accessory protein
Short name=IL-1 receptor accessory protein
Short name=IL-1RAcP

Alternative name(s):
Interleukin-1 receptor 3
Short name=IL-1R-3
Short name=IL-1R3

Gene names

Name:	IL1RAP
Synonyms:	C3orf13, IL1R3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Coreceptor with IL1R1. 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. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Ref.1 Ref.3 Ref.13
Subunit structure	The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Associates with IL1R2 to form a non-signaling interleukin-1 receptor complex. Ref.18
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted.
Tissue specificity	Detected in liver, skin, placenta, thymus and lung. Ref.13
Induction	Isoform 1 is down-regulated by phorbol ester treatment. Isoform 2 is induced by phorbol ester treatment. Ref.3 Ref.4
Sequence similarities	Belongs to the interleukin-1 receptor family. Contains 3 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 TIR domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	immune response Traceable author statement PubMed 9065432. Source: ProtInc inflammatory response Traceable author statement PubMed 9065432. Source: ProtInc interleukin-2 biosynthetic process Inferred from electronic annotation. Source: Compara protein complex assembly Traceable author statement PubMed 7775431. Source: ProtInc
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement PubMed 7775431. Source: ProtInc
Molecular_function	interleukin-1 receptor activity Inferred from electronic annotation. Source: Compara signal transducer activity Traceable author statement PubMed 9065432. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NPH3-1)

Also known as: Membrane-bound IL-1RAcP; mIL-1RAcP;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NPH3-2)

Also known as: Soluble IL-1RAcP; sIL-1RAcP;

The sequence of this isoform differs from the canonical sequence as follows:
     351-356: VPAPRY → GNRCGQ
     357-570: Missing.

Isoform 3 (identifier: Q9NPH3-3)

Also known as: Soluble IL-1RAcP-beta; sIL-1RAcP-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     302-570: ISHSRTEDET...GLSYSSLKNV → ASSKIHSGTG...PILPGSFWNR

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: Q9NPH3-5)

Also known as: AcPb; mIL-1RAcP687;

The sequence of this isoform differs from the canonical sequence as follows:
     449-570: IVTDETLSFI...GLSYSSLKNV → NTVEAVFDFI...LSNNNDFYIL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 570

550

Interleukin-1 receptor accessory protein

PRO_0000015450

Regions

Topological domain

21 – 367

347

Extracellular Potential

Transmembrane

368 – 388

21

Helical; Potential

Topological domain

389 – 570

182

Cytoplasmic Potential

Domain

21 – 128

108

Ig-like C2-type 1

Domain

141 – 230

90

Ig-like C2-type 2

Domain

242 – 348

107

Ig-like C2-type 3

Domain

403 – 549

147

TIR

Amino acid modifications

Modified residue

395

1

Phosphothreonine By similarity

Modified residue

398

1

Phosphothreonine By similarity

Modified residue

557

1

Phosphoserine Ref.16

Glycosylation

57

1

N-linked (GlcNAc...) Potential

Glycosylation

107

1

N-linked (GlcNAc...) Ref.18

Glycosylation

111

1

N-linked (GlcNAc...) Ref.18

Glycosylation

118

1

N-linked (GlcNAc...) Ref.18

Glycosylation

196

1

N-linked (GlcNAc...) Potential

Glycosylation

209

1

N-linked (GlcNAc...) Ref.18

Glycosylation

299

1

N-linked (GlcNAc...) Potential

Disulfide bond

24 ↔ 122

Ref.18

Disulfide bond

47 ↔ 114

Ref.18

Disulfide bond

137 ↔ 181

Ref.18

Disulfide bond

160 ↔ 212

Ref.18

Disulfide bond

266 ↔ 332

Ref.18

Natural variations

Alternative sequence

302 – 570

269

ISHSR…SLKNV → ASSKIHSGTGLWFWSHSPAS GDSHCCLPCLLARDGPILPG SFWNR in isoform 3.

VSP_008052

Alternative sequence

351 – 356

6

VPAPRY → GNRCGQ in isoform 2.

VSP_008050

Alternative sequence

357 – 570

214

Missing in isoform 2.

VSP_008051

Alternative sequence

449 – 570

122

IVTDE…SLKNV → NTVEAVFDFIQRSRRMIVVL SPDYVTEKSISMLEFKLGVM CQNSIATKLIVVEYRPLEHP HPGILQLKESVSFVSWKGEK SKHSGSKFWKALRLALPLRS LSASSGWNESCSSQSDISLD HVQRRRSRLKEPPELQSSER AAGSPPAPGTMSKHRGKSSA TCRCCVTYCEGENHLRNKSR AEIHNQPQWETHLCKPVPQE SETQWIQNGTRLEPPAPQIS ALALHHFTDLSNNNDFYIL in isoform 4.

VSP_041256

Natural variant

473

1

V → M.
Corresponds to variant rs34661910 [ dbSNP | Ensembl ].

VAR_053383

Secondary structure

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570

Helix Strand Turn

Details...

Beta strand

25 – 29

5

Beta strand

31 – 33

3

Beta strand

36 – 38

3

Beta strand

43 – 46

4

Helix

49 – 53

5

Beta strand

54 – 56

3

Helix

58 – 63

6

Beta strand

67 – 76

10

Beta strand

80 – 82

3

Helix

88 – 90

3

Beta strand

92 – 95

4

Beta strand

98 – 103

6

Helix

106 – 108

3

Beta strand

110 – 117

8

Beta strand

122 – 132

11

Beta strand

146 – 150

5

Beta strand

154 – 159

6

Beta strand

174 – 179

6

Beta strand

188 – 193

6

Beta strand

196 – 201

6

Helix

204 – 206

3

Beta strand

208 – 218

11

Beta strand

221 – 234

14

Helix

237 – 239

3

Beta strand

244 – 246

3

Beta strand

250 – 252

3

Beta strand

266 – 270

5

Beta strand

279 – 285

7

Beta strand

300 – 303

4

Beta strand

310 – 314

5

Turn

323 – 327

5

Beta strand

331 – 335

5

Beta strand

340 – 344

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Membrane-bound IL-1RAcP) (mIL-1RAcP) [UniParc]. Last modified August 22, 2003. Version 2. Checksum: 5F47F8D0ECA98B8A	FASTA	570	65,418
	10 20 30 40 50 60 MTLLWCVVSL YFYGILQSDA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST 70 80 90 100 110 120 AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT 130 140 150 160 170 180 YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG 190 200 210 220 230 240 CYKIQNFNNV IPEGMNLSFL IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVVGSPKNA 250 260 270 280 290 300 VPPVIHSPND HVVYEKEPGE ELLIPCTVYF SFLMDSRNEV WWTIDGKKPD DITIDVTINE 310 320 330 340 350 360 SISHSRTEDE TRTQILSIKK VTSEDLKRSY VCHARSAKGE VAKAAKVKQK VPAPRYTVEL 370 380 390 400 410 420 ACGFGATVLL VVILIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNAEEEEF 430 440 450 460 470 480 VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL 490 500 510 520 530 540 LELKAGLENM ASRGNINVIL VQYKAVKETK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK 550 560 570 QLQVAMPVKK SPRRSSSDEQ GLSYSSLKNV
	Isoform 2 (Soluble IL-1RAcP) (sIL-1RAcP) [UniParc]. Checksum: 39B72452C458A1C3	FASTA	356	41,019
	10 20 30 40 50 60 MTLLWCVVSL YFYGILQSDA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST 70 80 90 100 110 120 AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT 130 140 150 160 170 180 YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG 190 200 210 220 230 240 CYKIQNFNNV IPEGMNLSFL IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVVGSPKNA 250 260 270 280 290 300 VPPVIHSPND HVVYEKEPGE ELLIPCTVYF SFLMDSRNEV WWTIDGKKPD DITIDVTINE 310 320 330 340 350 SISHSRTEDE TRTQILSIKK VTSEDLKRSY VCHARSAKGE VAKAAKVKQK GNRCGQ
	Isoform 3 (Soluble IL-1RAcP-beta) (sIL-1RAcP-beta) [UniParc]. Checksum: 6F13B34E6763E062	FASTA	346	39,743
	10 20 30 40 50 60 MTLLWCVVSL YFYGILQSDA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST 70 80 90 100 110 120 AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT 130 140 150 160 170 180 YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG 190 200 210 220 230 240 CYKIQNFNNV IPEGMNLSFL IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVVGSPKNA 250 260 270 280 290 300 VPPVIHSPND HVVYEKEPGE ELLIPCTVYF SFLMDSRNEV WWTIDGKKPD DITIDVTINE 310 320 330 340 SASSKIHSGT GLWFWSHSPA SGDSHCCLPC LLARDGPILP GSFWNR
	Isoform 4 (AcPb) (mIL-1RAcP687) [UniParc]. Checksum: 5489237C18503D4C	FASTA	687	78,603
	10 20 30 40 50 60 MTLLWCVVSL YFYGILQSDA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKFNYST 70 80 90 100 110 120 AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT 130 140 150 160 170 180 YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY IEYGIQRITC PNVDGYFPSS VKPTITWYMG 190 200 210 220 230 240 CYKIQNFNNV IPEGMNLSFL IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVVGSPKNA 250 260 270 280 290 300 VPPVIHSPND HVVYEKEPGE ELLIPCTVYF SFLMDSRNEV WWTIDGKKPD DITIDVTINE 310 320 330 340 350 360 SISHSRTEDE TRTQILSIKK VTSEDLKRSY VCHARSAKGE VAKAAKVKQK VPAPRYTVEL 370 380 390 400 410 420 ACGFGATVLL VVILIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNAEEEEF 430 440 450 460 470 480 VLLTLRGVLE NEFGYKLCIF DRDSLPGGNT VEAVFDFIQR SRRMIVVLSP DYVTEKSISM 490 500 510 520 530 540 LEFKLGVMCQ NSIATKLIVV EYRPLEHPHP GILQLKESVS FVSWKGEKSK HSGSKFWKAL 550 560 570 580 590 600 RLALPLRSLS ASSGWNESCS SQSDISLDHV QRRRSRLKEP PELQSSERAA GSPPAPGTMS 610 620 630 640 650 660 KHRGKSSATC RCCVTYCEGE NHLRNKSRAE IHNQPQWETH LCKPVPQESE TQWIQNGTRL 670 680 EPPAPQISAL ALHHFTDLSN NNDFYIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein." Huang J., Gao X., Li S., Cao Z. Proc. Natl. Acad. Sci. U.S.A. 94:12829-12832(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH IL1R1 AND IRAK1. Tissue: Placenta.
[2]	Saito T., Seki N. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"IL-1 signaling cascade in liver cells and the involvement of a soluble form of the IL-1 receptor accessory protein." Jensen L.E., Muzio M., Mantovani A., Whitehead A.S. J. Immunol. 164:5277-5286(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, INDUCTION BY PHORBOL ESTERS. Tissue: Liver.
[4]	"Expression of alternatively spliced interleukin-1 receptor accessory protein mRNAs is differentially regulated during inflammation and apoptosis." Jensen L.E., Whitehead A.S. Cell. Signal. 15:793-802(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), INDUCTION BY PHORBOL ESTERS. Tissue: Liver.
[5]	"A novel alternatively spliced interleukin-1 receptor accessory protein mIL-1RAcP687." Lu H.L., Yang C.Y., Chen H.C., Hung C.S., Chiang Y.C., Ting L.P. Mol. Immunol. 45:1374-1384(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[6]	"A central nervous system-restricted isoform of the interleukin-1 receptor accessory protein modulates neuronal responses to interleukin-1." 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. Immunity 30:817-831(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[7]	"The DNA sequence, annotation and analysis of human chromosome 3." 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. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Skin.
[10]	"The human gene encoding the interleukin-1 receptor accessory protein (IL1RAP) maps to chromosome 3q28 by fluorescence in situ hybridization and radiation hybrid mapping." Dale M., Hammond D.W., Cox A., Nicklin M.J.H. Genomics 47:325-326(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-179.
[11]	"The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: a novel mechanism of regulation of IL-1 responsiveness." Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D., Martin M.U. J. Immunol. 161:6871-6877(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IL1R2.
[12]	"Characterization of a cascade of protein interactions initiated at the IL-1 receptor." Boch J.A., Yoshida Y., Koyama Y., Wara-Aswapati N., Peng H., Unlu S., Auron P.E. Biochem. Biophys. Res. Commun. 303:525-531(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IRAK2.
[13]	"The soluble form of IL-1 receptor accessory protein enhances the ability of soluble type II IL-1 receptor to inhibit IL-1 action." Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M., MacVittie T.J., Virca G.D., Sims J.E. Immunity 18:87-96(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (SECRETED FORMS), TISSUE SPECIFICITY.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"Structural insights into the assembly and activation of IL-1beta with its receptors." Wang D., Zhang S., Li L., Liu X., Mei K., Wang X. Nat. Immunol. 11:905-911(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 21-350 IN COMPLEX WITH IL1R2 AND IL1B, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-107; ASN-111; ASN-118 AND ASN-209.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF029213 mRNA. Translation: AAB84059.1.
AB006537 mRNA. Translation: BAA25421.1.
AF167343 mRNA. Translation: AAF71687.1.
AF167340 , AF167335, AF167336, AF167337, AF167338, AF167339 Genomic DNA. Translation: AAF71688.1.
AF167342 , AF167335, AF167336, AF167337, AF167338, AF167339, AF167340, AF167341 Genomic DNA. Translation: AAF71689.1.
AF538730 mRNA. Translation: AAQ01755.1.
AF538731 mRNA. Translation: AAQ01756.1.
AF538732 mRNA. Translation: AAQ01757.1.
AF538733 mRNA. Translation: AAQ01758.1.
AF538734 mRNA. Translation: AAQ01759.1.
AF487335 mRNA. Translation: AAO49451.1.
EF591790 mRNA. Translation: ABU90811.1.
FJ998418 mRNA. Translation: ACR82488.1.
AC008249 Genomic DNA. No translation available.
AC108747 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78100.1.
CH471052 Genomic DNA. Translation: EAW78102.1.
BC053621 mRNA. Translation: AAH53621.1.
AF016261 Genomic DNA. Translation: AAC39609.1.

IPI

IPI00031789.
IPI00107619.
IPI00337687.
IPI00925621.

RefSeq

NP_001161400.1. NM_001167928.1.
NP_001161401.1. NM_001167929.1.
NP_001161402.1. NM_001167930.1.
NP_001161403.1. NM_001167931.1.
NP_002173.1. NM_002182.3.
NP_608273.1. NM_134470.3.

UniGene

Hs.478673.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3O4O	X-ray	3.30	B	21-350	[»]
4DEP	X-ray	3.10	C/F	21-367	[»]

ProteinModelPortal

Q9NPH3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33487N.

IntAct

Q9NPH3. 9 interactions.

MINT

MINT-1184198.

STRING

9606.ENSP00000072516.

PTM databases

PhosphoSite

Q9NPH3.

Polymorphism databases

DMDM

34222652.

Proteomic databases

PaxDb

Q9NPH3.

PRIDE

Q9NPH3.

Protocols and materials databases

DNASU

3556.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000072516; ENSP00000072516; ENSG00000196083.
ENST00000317757; ENSP00000314807; ENSG00000196083.
ENST00000342550; ENSP00000345829; ENSG00000196083.
ENST00000412504; ENSP00000412053; ENSG00000196083.
ENST00000413869; ENSP00000416296; ENSG00000196083.
ENST00000422485; ENSP00000409352; ENSG00000196083.
ENST00000422940; ENSP00000387371; ENSG00000196083.
ENST00000439062; ENSP00000401132; ENSG00000196083.
ENST00000443369; ENSP00000408893; ENSG00000196083.
ENST00000447382; ENSP00000390541; ENSG00000196083.

GeneID

3556.

KEGG

hsa:3556.

UCSC

uc003fsk.3. human.
uc003fsm.2. human.
uc003fsq.3. human.

Organism-specific databases

CTD

3556.

GeneCards

GC03P190231.

HGNC

HGNC:5995. IL1RAP.

HPA

HPA035293.

MIM

602626. gene.

neXtProt

NX_Q9NPH3.

PharmGKB

PA29811.

GenAtlas

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Phylogenomic databases

eggNOG

NOG145997.

HOGENOM

HOG000092977.

HOVERGEN

HBG104298.

InParanoid

Q9NPH3.

KO

K04723.

OMA

VQKITCP.

OrthoDB

EOG46MBJ6.

PhylomeDB

Q9NPH3.

Enzyme and pathway databases

Pathway_Interaction_DB

il1pathway. IL1-mediated signaling events.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9NPH3.

Bgee

Q9NPH3.

CleanEx

HS_IL1RAP.

Genevestigator

Q9NPH3.

GermOnline

ENSG00000196083. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL1-receptor_fam.
IPR004074. IL1_rcpt_I/II.
IPR000157. TIR_dom.
[Graphical view]

PANTHER

PTHR11890. PTHR11890. 1 hit.

Pfam

PF01582. TIR. 1 hit.
[Graphical view]

PRINTS

PR01536. INTRLKN1R12F.

SMART

SM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view]

SUPFAM

SSF52200. TIR. 1 hit.

PROSITE

PS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9NPH3.

GenomeRNAi

3556.

NextBio

13880.

SOURCE

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Entry information

Entry name

IL1AP_HUMAN

Accession

Primary (citable) accession number: Q9NPH3
Secondary accession number(s): B1NLD0 , D3DNW0, O14915, Q86WJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	August 22, 2003
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.