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Q9NPH3 (IL1AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 570550Interleukin-1 receptor accessory protein
PRO_0000015450

Regions

Topological domain21 – 367347Extracellular Potential
Transmembrane368 – 38821Helical; Potential
Topological domain389 – 570182Cytoplasmic Potential
Domain21 – 128108Ig-like C2-type 1
Domain141 – 23090Ig-like C2-type 2
Domain242 – 348107Ig-like C2-type 3
Domain403 – 549147TIR

Amino acid modifications

Modified residue5571Phosphoserine Ref.16
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Ref.18
Glycosylation1111N-linked (GlcNAc...) Ref.18
Glycosylation1181N-linked (GlcNAc...) Ref.18
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Ref.18
Glycosylation2991N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 122 Ref.18
Disulfide bond47 ↔ 114 Ref.18
Disulfide bond137 ↔ 181 Ref.18
Disulfide bond160 ↔ 212 Ref.18
Disulfide bond266 ↔ 332 Ref.18

Natural variations

Alternative sequence302 – 570269ISHSR…SLKNV → ASSKIHSGTGLWFWSHSPAS GDSHCCLPCLLARDGPILPG SFWNR in isoform 3.
VSP_008052
Alternative sequence351 – 3566VPAPRY → GNRCGQ in isoform 2.
VSP_008050
Alternative sequence357 – 570214Missing in isoform 2.
VSP_008051
Alternative sequence449 – 570122IVTDE…SLKNV → NTVEAVFDFIQRSRRMIVVL SPDYVTEKSISMLEFKLGVM CQNSIATKLIVVEYRPLEHP HPGILQLKESVSFVSWKGEK SKHSGSKFWKALRLALPLRS LSASSGWNESCSSQSDISLD HVQRRRSRLKEPPELQSSER AAGSPPAPGTMSKHRGKSSA TCRCCVTYCEGENHLRNKSR AEIHNQPQWETHLCKPVPQE SETQWIQNGTRLEPPAPQIS ALALHHFTDLSNNNDFYIL in isoform 4.
VSP_041256
Natural variant4731V → M.
Corresponds to variant rs34661910 [ dbSNP | Ensembl ].
VAR_053383

Secondary structure

.................................................................. 570
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Membrane-bound IL-1RAcP) (mIL-1RAcP) [UniParc].

Last modified August 22, 2003. Version 2.
Checksum: 5F47F8D0ECA98B8A

FASTA57065,418
        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 

« Hide

Isoform 2 (Soluble IL-1RAcP) (sIL-1RAcP) [UniParc].

Checksum: 39B72452C458A1C3
Show »

FASTA35641,019
Isoform 3 (Soluble IL-1RAcP-beta) (sIL-1RAcP-beta) [UniParc].

Checksum: 6F13B34E6763E062
Show »

FASTA34639,743
Isoform 4 (AcPb) (mIL-1RAcP687) [UniParc].

Checksum: 5489237C18503D4C
Show »

FASTA68778,603

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 expand/collapse EMBL AC list , AF167335, AF167336, AF167337, AF167338, AF167339 Genomic DNA. Translation: AAF71688.1.
AF167342 expand/collapse EMBL AC list , 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.
RefSeqNP_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.
XP_005247490.1. XM_005247433.1.
UniGeneHs.478673.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4OX-ray3.30B21-350[»]
4DEPX-ray3.10C/F21-367[»]
ProteinModelPortalQ9NPH3.
SMRQ9NPH3. Positions 24-346, 403-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109771. 17 interactions.
DIPDIP-33487N.
IntActQ9NPH3. 10 interactions.
MINTMINT-1184198.
STRING9606.ENSP00000072516.

PTM databases

PhosphoSiteQ9NPH3.

Polymorphism databases

DMDM34222652.

Proteomic databases

PaxDbQ9NPH3.
PRIDEQ9NPH3.

Protocols and materials databases

DNASU3556.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000072516; ENSP00000072516; ENSG00000196083. [Q9NPH3-1]
ENST00000317757; ENSP00000314807; ENSG00000196083. [Q9NPH3-5]
ENST00000342550; ENSP00000345829; ENSG00000196083. [Q9NPH3-3]
ENST00000412504; ENSP00000412053; ENSG00000196083. [Q9NPH3-1]
ENST00000413869; ENSP00000416296; ENSG00000196083. [Q9NPH3-3]
ENST00000422485; ENSP00000409352; ENSG00000196083. [Q9NPH3-2]
ENST00000422940; ENSP00000387371; ENSG00000196083. [Q9NPH3-2]
ENST00000439062; ENSP00000401132; ENSG00000196083. [Q9NPH3-1]
ENST00000443369; ENSP00000408893; ENSG00000196083. [Q9NPH3-5]
ENST00000447382; ENSP00000390541; ENSG00000196083. [Q9NPH3-1]
GeneID3556.
KEGGhsa:3556.
UCSCuc003fsk.3. human. [Q9NPH3-2]
uc003fsm.2. human. [Q9NPH3-1]
uc003fsq.3. human. [Q9NPH3-5]

Organism-specific databases

CTD3556.
GeneCardsGC03P190231.
HGNCHGNC:5995. IL1RAP.
HPAHPA035293.
MIM602626. gene.
neXtProtNX_Q9NPH3.
PharmGKBPA29811.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145997.
HOGENOMHOG000092977.
HOVERGENHBG104298.
InParanoidQ9NPH3.
KOK04723.
OMAMPVKKSS.
OrthoDBEOG7CVPXJ.
PhylomeDBQ9NPH3.
TreeFamTF325519.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ9NPH3.

Gene expression databases

ArrayExpressQ9NPH3.
BgeeQ9NPH3.
CleanExHS_IL1RAP.
GenevestigatorQ9NPH3.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
3.40.50.10140. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL-1_rcpt_fam.
IPR004074. IL-1_rcpt_I/II-typ.
IPR000157. TIR_dom.
[Graphical view]
PANTHERPTHR11890. PTHR11890. 1 hit.
PfamPF01582. TIR. 1 hit.
[Graphical view]
PRINTSPR01536. INTRLKN1R12F.
SMARTSM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NPH3.
GeneWikiIL1RAP.
GenomeRNAi3556.
NextBio13880.
PROQ9NPH3.
SOURCESearch...

Entry information

Entry nameIL1AP_HUMAN
AccessionPrimary (citable) accession number: Q9NPH3
Secondary accession number(s): B1NLD0 expand/collapse secondary AC list , D3DNW0, O14915, Q86WJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM