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Q9NPH3

- IL1AP_HUMAN

UniProt

Q9NPH3 - IL1AP_HUMAN

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Protein

Interleukin-1 receptor accessory protein

Gene

IL1RAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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.By similarity3 Publications

GO - Molecular functioni

  1. interleukin-1 receptor activity Source: Ensembl
  2. signal transducer activity Source: ProtInc

GO - Biological processi

  1. immune response Source: ProtInc
  2. inflammatory response Source: ProtInc
  3. interleukin-2 biosynthetic process Source: Ensembl
  4. protein complex assembly Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_22442. Interleukin-1 signaling.
SignaLinkiQ9NPH3.

Names & Taxonomyi

Protein namesi
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 namesi
Name:IL1RAP
Synonyms:C3orf13, IL1R3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:5995. IL1RAP.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 367347ExtracellularSequence AnalysisAdd
BLAST
Transmembranei368 – 38821HelicalSequence AnalysisAdd
BLAST
Topological domaini389 – 570182CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of plasma membrane Source: ProtInc
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 570550Interleukin-1 receptor accessory proteinPRO_0000015450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1221 PublicationPROSITE-ProRule annotation
Disulfide bondi47 ↔ 1141 PublicationPROSITE-ProRule annotation
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi107 – 1071N-linked (GlcNAc...)1 Publication
Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication
Glycosylationi118 – 1181N-linked (GlcNAc...)1 Publication
Disulfide bondi137 ↔ 1811 PublicationPROSITE-ProRule annotation
Disulfide bondi160 ↔ 2121 PublicationPROSITE-ProRule annotation
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)1 Publication
Disulfide bondi266 ↔ 3321 PublicationPROSITE-ProRule annotation
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
Modified residuei557 – 5571Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NPH3.
PaxDbiQ9NPH3.
PRIDEiQ9NPH3.

PTM databases

PhosphoSiteiQ9NPH3.

Expressioni

Tissue specificityi

Detected in liver, skin, placenta, thymus and lung.1 Publication

Inductioni

Isoform 1 is down-regulated by phorbol ester treatment. Isoform 2 is induced by phorbol ester treatment.2 Publications

Gene expression databases

BgeeiQ9NPH3.
CleanExiHS_IL1RAP.
ExpressionAtlasiQ9NPH3. baseline and differential.
GenevestigatoriQ9NPH3.

Organism-specific databases

HPAiHPA035293.

Interactioni

Subunit structurei

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.By similarity3 Publications

Protein-protein interaction databases

BioGridi109771. 17 interactions.
DIPiDIP-33487N.
IntActiQ9NPH3. 10 interactions.
MINTiMINT-1184198.
STRINGi9606.ENSP00000072516.

Structurei

Secondary structure

1
570
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 295Combined sources
Beta strandi31 – 333Combined sources
Beta strandi36 – 383Combined sources
Beta strandi43 – 464Combined sources
Helixi49 – 535Combined sources
Beta strandi54 – 563Combined sources
Helixi58 – 636Combined sources
Beta strandi67 – 7610Combined sources
Beta strandi80 – 823Combined sources
Helixi88 – 903Combined sources
Beta strandi92 – 954Combined sources
Beta strandi98 – 1036Combined sources
Helixi106 – 1083Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi122 – 13211Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi154 – 1596Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi196 – 2016Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 21811Combined sources
Beta strandi221 – 23414Combined sources
Helixi237 – 2393Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi300 – 3034Combined sources
Beta strandi310 – 3145Combined sources
Turni323 – 3275Combined sources
Beta strandi331 – 3355Combined sources
Beta strandi340 – 3445Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4OX-ray3.30B21-350[»]
4DEPX-ray3.10C/F21-367[»]
ProteinModelPortaliQ9NPH3.
SMRiQ9NPH3. Positions 24-346, 403-547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPH3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 128108Ig-like C2-type 1Add
BLAST
Domaini141 – 23090Ig-like C2-type 2Add
BLAST
Domaini242 – 348107Ig-like C2-type 3Add
BLAST
Domaini403 – 549147TIRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the interleukin-1 receptor family.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG145997.
GeneTreeiENSGT00760000119071.
HOGENOMiHOG000092977.
HOVERGENiHBG104298.
InParanoidiQ9NPH3.
KOiK04723.
OMAiRCDDWGV.
OrthoDBiEOG7CVPXJ.
PhylomeDBiQ9NPH3.
TreeFamiTF325519.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.40.50.10140. 1 hit.
InterProiIPR007110. 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]
PANTHERiPTHR11890. PTHR11890. 1 hit.
PfamiPF01582. TIR. 1 hit.
[Graphical view]
PRINTSiPR01536. INTRLKN1R12F.
SMARTiSM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NPH3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTLLWCVVSL YFYGILQSDA SERCDDWGLD TMRQIQVFED EPARIKCPLF
60 70 80 90 100
EHFLKFNYST AHSAGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW
110 120 130 140 150
FRPTLLNDTG NYTCMLRNTT YCSKVAFPLE VVQKDSCFNS PMKLPVHKLY
160 170 180 190 200
IEYGIQRITC PNVDGYFPSS VKPTITWYMG CYKIQNFNNV IPEGMNLSFL
210 220 230 240 250
IALISNNGNY TCVVTYPENG RTFHLTRTLT VKVVGSPKNA VPPVIHSPND
260 270 280 290 300
HVVYEKEPGE ELLIPCTVYF SFLMDSRNEV WWTIDGKKPD DITIDVTINE
310 320 330 340 350
SISHSRTEDE TRTQILSIKK VTSEDLKRSY VCHARSAKGE VAKAAKVKQK
360 370 380 390 400
VPAPRYTVEL ACGFGATVLL VVILIVVYHV YWLEMVLFYR AHFGTDETIL
410 420 430 440 450
DGKEYDIYVS YARNAEEEEF VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV
460 470 480 490 500
TDETLSFIQK SRRLLVVLSP NYVLQGTQAL LELKAGLENM ASRGNINVIL
510 520 530 540 550
VQYKAVKETK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK QLQVAMPVKK
560 570
SPRRSSSDEQ GLSYSSLKNV
Length:570
Mass (Da):65,418
Last modified:August 22, 2003 - v2
Checksum:i5F47F8D0ECA98B8A
GO
Isoform 2 (identifier: Q9NPH3-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:356
Mass (Da):41,019
Checksum:i39B72452C458A1C3
GO
Isoform 3 (identifier: Q9NPH3-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:346
Mass (Da):39,743
Checksum:i6F13B34E6763E062
GO
Isoform 4 (identifier: Q9NPH3-5) [UniParc]FASTAAdd to Basket

Also known as: AcPb, mIL-1RAcP687

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

Show »
Length:687
Mass (Da):78,603
Checksum:i5489237C18503D4C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti473 – 4731V → M.
Corresponds to variant rs34661910 [ dbSNP | Ensembl ].
VAR_053383

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei302 – 570269ISHSR…SLKNV → ASSKIHSGTGLWFWSHSPAS GDSHCCLPCLLARDGPILPG SFWNR in isoform 3. 1 PublicationVSP_008052Add
BLAST
Alternative sequencei351 – 3566VPAPRY → GNRCGQ in isoform 2. 3 PublicationsVSP_008050
Alternative sequencei357 – 570214Missing in isoform 2. 3 PublicationsVSP_008051Add
BLAST
Alternative sequencei449 – 570122IVTDE…SLKNV → NTVEAVFDFIQRSRRMIVVL SPDYVTEKSISMLEFKLGVM CQNSIATKLIVVEYRPLEHP HPGILQLKESVSFVSWKGEK SKHSGSKFWKALRLALPLRS LSASSGWNESCSSQSDISLD HVQRRRSRLKEPPELQSSER AAGSPPAPGTMSKHRGKSSA TCRCCVTYCEGENHLRNKSR AEIHNQPQWETHLCKPVPQE SETQWIQNGTRLEPPAPQIS ALALHHFTDLSNNNDFYIL in isoform 4. 2 PublicationsVSP_041256Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3298.1. [Q9NPH3-1]
CCDS46982.1. [Q9NPH3-2]
CCDS54696.1. [Q9NPH3-5]
RefSeqiNP_001161400.1. NM_001167928.1. [Q9NPH3-1]
NP_001161401.1. NM_001167929.1. [Q9NPH3-1]
NP_001161402.1. NM_001167930.1. [Q9NPH3-2]
NP_001161403.1. NM_001167931.1. [Q9NPH3-5]
NP_002173.1. NM_002182.3. [Q9NPH3-1]
NP_608273.1. NM_134470.3. [Q9NPH3-2]
XP_005247490.1. XM_005247433.1. [Q9NPH3-5]
UniGeneiHs.478673.

Genome annotation databases

EnsembliENST00000072516; 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]
GeneIDi3556.
KEGGihsa:3556.
UCSCiuc003fsk.3. human. [Q9NPH3-2]
uc003fsm.2. human. [Q9NPH3-1]
uc003fsq.3. human. [Q9NPH3-5]

Polymorphism databases

DMDMi34222652.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS3298.1. [Q9NPH3-1 ]
CCDS46982.1. [Q9NPH3-2 ]
CCDS54696.1. [Q9NPH3-5 ]
RefSeqi NP_001161400.1. NM_001167928.1. [Q9NPH3-1 ]
NP_001161401.1. NM_001167929.1. [Q9NPH3-1 ]
NP_001161402.1. NM_001167930.1. [Q9NPH3-2 ]
NP_001161403.1. NM_001167931.1. [Q9NPH3-5 ]
NP_002173.1. NM_002182.3. [Q9NPH3-1 ]
NP_608273.1. NM_134470.3. [Q9NPH3-2 ]
XP_005247490.1. XM_005247433.1. [Q9NPH3-5 ]
UniGenei Hs.478673.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O4O X-ray 3.30 B 21-350 [» ]
4DEP X-ray 3.10 C/F 21-367 [» ]
ProteinModelPortali Q9NPH3.
SMRi Q9NPH3. Positions 24-346, 403-547.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109771. 17 interactions.
DIPi DIP-33487N.
IntActi Q9NPH3. 10 interactions.
MINTi MINT-1184198.
STRINGi 9606.ENSP00000072516.

PTM databases

PhosphoSitei Q9NPH3.

Polymorphism databases

DMDMi 34222652.

Proteomic databases

MaxQBi Q9NPH3.
PaxDbi Q9NPH3.
PRIDEi Q9NPH3.

Protocols and materials databases

DNASUi 3556.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000072516 ; 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 ]
GeneIDi 3556.
KEGGi hsa:3556.
UCSCi uc003fsk.3. human. [Q9NPH3-2 ]
uc003fsm.2. human. [Q9NPH3-1 ]
uc003fsq.3. human. [Q9NPH3-5 ]

Organism-specific databases

CTDi 3556.
GeneCardsi GC03P190231.
HGNCi HGNC:5995. IL1RAP.
HPAi HPA035293.
MIMi 602626. gene.
neXtProti NX_Q9NPH3.
PharmGKBi PA29811.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145997.
GeneTreei ENSGT00760000119071.
HOGENOMi HOG000092977.
HOVERGENi HBG104298.
InParanoidi Q9NPH3.
KOi K04723.
OMAi RCDDWGV.
OrthoDBi EOG7CVPXJ.
PhylomeDBi Q9NPH3.
TreeFami TF325519.

Enzyme and pathway databases

Reactomei REACT_22442. Interleukin-1 signaling.
SignaLinki Q9NPH3.

Miscellaneous databases

EvolutionaryTracei Q9NPH3.
GeneWikii IL1RAP.
GenomeRNAii 3556.
NextBioi 13880.
PROi Q9NPH3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NPH3.
CleanExi HS_IL1RAP.
ExpressionAtlasi Q9NPH3. baseline and differential.
Genevestigatori Q9NPH3.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
3.40.50.10140. 1 hit.
InterProi IPR007110. 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 ]
PANTHERi PTHR11890. PTHR11890. 1 hit.
Pfami PF01582. TIR. 1 hit.
[Graphical view ]
PRINTSi PR01536. INTRLKN1R12F.
SMARTi SM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view ]
SUPFAMi SSF52200. SSF52200. 1 hit.
PROSITEi PS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. 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.

Entry informationi

Entry nameiIL1AP_HUMAN
AccessioniPrimary (citable) accession number: Q9NPH3
Secondary accession number(s): B1NLD0
, D3DNW0, O14915, Q86WJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: November 26, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3