Full text data of IL1R2
IL1R2
(IL1RB)
[Confidence: high (a blood group or CD marker)]
Interleukin-1 receptor type 2; IL-1R-2; IL-1RT-2; IL-1RT2 (CD121 antigen-like family member B; CDw121b; IL-1 type II receptor; Interleukin-1 receptor beta; IL-1R-beta; Interleukin-1 receptor type II; CD121b; Interleukin-1 receptor type 2, membrane form; mIL-1R2; mIL-1RII; Interleukin-1 receptor type 2, soluble form; sIL-1R2; sIL-1RII; Flags: Precursor)
Interleukin-1 receptor type 2; IL-1R-2; IL-1RT-2; IL-1RT2 (CD121 antigen-like family member B; CDw121b; IL-1 type II receptor; Interleukin-1 receptor beta; IL-1R-beta; Interleukin-1 receptor type II; CD121b; Interleukin-1 receptor type 2, membrane form; mIL-1R2; mIL-1RII; Interleukin-1 receptor type 2, soluble form; sIL-1R2; sIL-1RII; Flags: Precursor)
UniProt
P27930
ID IL1R2_HUMAN Reviewed; 398 AA.
AC P27930; D3DVJ5; Q6LCE6; Q9UE68;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Interleukin-1 receptor type 2;
DE Short=IL-1R-2;
DE Short=IL-1RT-2;
DE Short=IL-1RT2;
DE AltName: Full=CD121 antigen-like family member B;
DE AltName: Full=CDw121b;
DE AltName: Full=IL-1 type II receptor;
DE AltName: Full=Interleukin-1 receptor beta;
DE Short=IL-1R-beta;
DE AltName: Full=Interleukin-1 receptor type II;
DE AltName: CD_antigen=CD121b;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, membrane form;
DE Short=mIL-1R2;
DE Short=mIL-1RII;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, soluble form;
DE Short=sIL-1R2;
DE Short=sIL-1RII;
DE Flags: Precursor;
GN Name=IL1R2; Synonyms=IL1RB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=B-cell;
RX PubMed=1833184;
RA McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D.,
RA Brunton L.L., Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I.,
RA Copeland N.G., Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D.,
RA Dower S.K., Spriggs M.K., Sims J.E.;
RT "A novel IL-1 receptor, cloned from B cells by mammalian expression,
RT is expressed in many cell types.";
RL EMBO J. 10:2821-2832(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), IL1B-BINDING, AND
RP SUBCELLULAR LOCATION (ISOFORM SHORT).
RX PubMed=8702856; DOI=10.1074/jbc.271.34.20965;
RA Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.;
RT "Cloning and characterization of an alternatively processed human type
RT II interleukin-1 receptor mRNA.";
RL J. Biol. Chem. 271:20965-20972(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Chou H.-H., Takashiba T., Takigawa M., Maeda H., Asahara Y.,
RA Nishimura F., Arai H., Murayama Y.;
RT "Complete nucleotide sequence and expression of the human interleukin-
RT 1 receptor type II in human gingival fibroblasts.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-181 AND LYS-292.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, PROTEOLYTIC PROCESSING, AND LIGAND-BINDING.
RX PubMed=7989776;
RA Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
RA Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
RT "Elevated levels of shed type II IL-1 receptor in sepsis. Potential
RT role for type II receptor in regulation of IL-1 responses.";
RL J. Immunol. 153:5802-5809(1994).
RN [9]
RP LIGAND-BINDING.
RX PubMed=7878046; DOI=10.1073/pnas.92.5.1714;
RA Symons J.A., Young P.R., Duff G.W.;
RT "Soluble type II interleukin 1 (IL-1) receptor binds and blocks
RT processing of IL-1 beta precursor and loses affinity for IL-1 receptor
RT antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1714-1718(1995).
RN [10]
RP PROTEOLYTIC PROCESSING.
RX PubMed=9395521; DOI=10.1074/jbc.272.50.31764;
RA Orlando S., Sironi M., Bianchi G., Drummond A.H., Boraschi D.,
RA Yabes D., Mantovani A.;
RT "Role of metalloproteases in the release of the IL-1 type II decoy
RT receptor.";
RL J. Biol. Chem. 272:31764-31769(1997).
RN [11]
RP FUNCTION, AND INTERACTION WITH IL1RAP.
RX PubMed=9862719;
RA Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
RA Martin M.U.;
RT "The type II IL-1 receptor interacts with the IL-1 receptor accessory
RT protein: a novel mechanism of regulation of IL-1 responsiveness.";
RL J. Immunol. 161:6871-6877(1998).
RN [12]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=10975853;
RA Neumann D., Kollewe C., Martin M.U., Boraschi D.;
RT "The membrane form of the type II IL-1 receptor accounts for
RT inhibitory function.";
RL J. Immunol. 165:3350-3357(2000).
RN [13]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=12530978; DOI=10.1016/S1074-7613(02)00514-9;
RA Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M.,
RA MacVittie T.J., Virca G.D., Sims J.E.;
RT "The soluble form of IL-1 receptor accessory protein enhances the
RT ability of soluble type II IL-1 receptor to inhibit IL-1 action.";
RL Immunity 18:87-96(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 14-343 IN COMPLEX WITH IL1RAP
RP AND IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-112 AND
RP ASN-219.
RX PubMed=20802483; DOI=10.1038/ni.1925;
RA Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
RT "Structural insights into the assembly and activation of IL-1beta with
RT its receptors.";
RL Nat. Immunol. 11:905-911(2010).
CC -!- FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces
CC IL1B activities. Serves as a decoy receptor by competetive binding
CC to IL1B and preventing its binding to IL1R1. Also modulates
CC cellular response through non-signaling association with IL1RAP
CC after binding to IL1B. IL1R2 (membrane and secreted forms)
CC preferentially binds IL1B and poorly IL1A and IL1RN. The secreted
CC IL1R2 recruits secreted IL1RAP with high affinity; this complex
CC formation may be the dominant mechanism for neutralization of IL1B
CC by secreted/soluble receptors.
CC -!- SUBUNIT: Associates with IL1RAP to form a non-signaling
CC interleukin-1 receptor complex.
CC -!- SUBCELLULAR LOCATION: Isoform Short: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass
CC type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P27930-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P27930-2; Sequence=VSP_042222;
CC -!- PTM: A soluble form (sIL1R2) can also be produced by proteolytic
CC cleavage at the cell surface (shedding) involving a
CC metalloproteinase; hovever, several sIL1R2 forms ranging from 45
CC and 60 kDa are reported.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il1r2/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X59770; CAA42441.1; -; mRNA.
DR EMBL; U64094; AAB05878.1; -; mRNA.
DR EMBL; U74649; AAD00242.1; -; mRNA.
DR EMBL; AY124010; AAM64221.1; -; Genomic_DNA.
DR EMBL; AC007165; AAK52072.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01800.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01801.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01802.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01803.1; -; Genomic_DNA.
DR EMBL; BC039031; AAH39031.1; -; mRNA.
DR PIR; S17428; S17428.
DR RefSeq; NP_001248348.1; NM_001261419.1.
DR RefSeq; NP_004624.1; NM_004633.3.
DR UniGene; Hs.25333; -.
DR PDB; 3O4O; X-ray; 3.30 A; C=14-343.
DR PDBsum; 3O4O; -.
DR ProteinModelPortal; P27930; -.
DR SMR; P27930; 28-343.
DR IntAct; P27930; 3.
DR STRING; 9606.ENSP00000330959; -.
DR DrugBank; DB00026; Anakinra.
DR PhosphoSite; P27930; -.
DR DMDM; 124310; -.
DR PaxDb; P27930; -.
DR PRIDE; P27930; -.
DR DNASU; 7850; -.
DR Ensembl; ENST00000332549; ENSP00000330959; ENSG00000115590.
DR Ensembl; ENST00000393414; ENSP00000377066; ENSG00000115590.
DR Ensembl; ENST00000441002; ENSP00000414611; ENSG00000115590.
DR GeneID; 7850; -.
DR KEGG; hsa:7850; -.
DR UCSC; uc002tbm.3; human.
DR CTD; 7850; -.
DR GeneCards; GC02P102608; -.
DR HGNC; HGNC:5994; IL1R2.
DR HPA; HPA027597; -.
DR HPA; HPA027598; -.
DR MIM; 147811; gene.
DR neXtProt; NX_P27930; -.
DR PharmGKB; PA29810; -.
DR eggNOG; NOG44340; -.
DR HOGENOM; HOG000113036; -.
DR HOVERGEN; HBG052104; -.
DR InParanoid; P27930; -.
DR KO; K04387; -.
DR OMA; RQEYSEN; -.
DR OrthoDB; EOG77HDDW; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; P27930; -.
DR GeneWiki; Interleukin_1_receptor,_type_II; -.
DR GenomeRNAi; 7850; -.
DR NextBio; 30276; -.
DR PRO; PR:P27930; -.
DR ArrayExpress; P27930; -.
DR Bgee; P27930; -.
DR CleanEx; HS_IL1R2; -.
DR Genevestigator; P27930; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004908; F:interleukin-1 receptor activity; TAS:ProtInc.
DR GO; GO:0004910; F:interleukin-1, Type II, blocking receptor activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR004077; IL-1_rcpt_II-typ.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR PRINTS; PR01539; INTRLEUKN1R2.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 13 Potential.
FT CHAIN 14 398 Interleukin-1 receptor type 2, membrane
FT form.
FT /FTId=PRO_0000015439.
FT CHAIN 14 ? Interleukin-1 receptor type 2, soluble
FT form.
FT /FTId=PRO_0000415348.
FT TOPO_DOM 14 343 Extracellular (Potential).
FT TRANSMEM 344 369 Helical; (Potential).
FT TOPO_DOM 370 398 Cytoplasmic (Potential).
FT DOMAIN 18 124 Ig-like C2-type 1.
FT DOMAIN 134 223 Ig-like C2-type 2.
FT DOMAIN 237 349 Ig-like C2-type 3.
FT REGION 329 343 Contains proteolytic cleavage site
FT (Probable).
FT CARBOHYD 66 66 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 112 112 N-linked (GlcNAc...).
FT CARBOHYD 219 219 N-linked (GlcNAc...).
FT CARBOHYD 277 277 N-linked (GlcNAc...) (Potential).
FT DISULFID 28 116
FT DISULFID 50 108
FT DISULFID 152 207
FT DISULFID 258 326
FT VAR_SEQ 297 398 Missing (in isoform Short).
FT /FTId=VSP_042222.
FT VARIANT 181 181 E -> K (in dbSNP:rs28385682).
FT /FTId=VAR_019132.
FT VARIANT 292 292 E -> K (in dbSNP:rs3218976).
FT /FTId=VAR_019133.
FT CONFLICT 123 123 L -> F (in Ref. 2; AAD00242).
FT CONFLICT 171 171 K -> R (in Ref. 2; AAD00242).
FT CONFLICT 199 199 L -> Q (in Ref. 2; AAD00242).
FT STRAND 29 33
FT STRAND 38 41
FT STRAND 47 49
FT STRAND 70 73
FT STRAND 82 84
FT STRAND 86 89
FT STRAND 92 98
FT STRAND 104 107
FT STRAND 110 112
FT STRAND 115 126
FT HELIX 130 132
FT HELIX 133 136
FT STRAND 138 143
FT STRAND 148 151
FT TURN 156 158
FT STRAND 161 163
FT STRAND 170 173
FT STRAND 181 185
FT STRAND 189 196
FT HELIX 199 201
FT STRAND 203 210
FT STRAND 219 229
FT STRAND 260 265
FT STRAND 271 279
FT STRAND 281 285
FT STRAND 287 289
FT STRAND 301 303
FT STRAND 305 308
FT STRAND 325 330
FT STRAND 333 335
SQ SEQUENCE 398 AA; 45421 MW; 2C2A03ADA6F3AC5B CRC64;
MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC PQVPYWLWAS
VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ EDSGTYVCTT RNASYCDKMS
IELRVFENTD AFLPFISYPQ ILTLSTSGVL VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN
EKFLSVRGTT HLLVHDVALE DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII
SPLKTISASL GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE
NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW GIVLAPLSLA
FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK
//
ID IL1R2_HUMAN Reviewed; 398 AA.
AC P27930; D3DVJ5; Q6LCE6; Q9UE68;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Interleukin-1 receptor type 2;
DE Short=IL-1R-2;
DE Short=IL-1RT-2;
DE Short=IL-1RT2;
DE AltName: Full=CD121 antigen-like family member B;
DE AltName: Full=CDw121b;
DE AltName: Full=IL-1 type II receptor;
DE AltName: Full=Interleukin-1 receptor beta;
DE Short=IL-1R-beta;
DE AltName: Full=Interleukin-1 receptor type II;
DE AltName: CD_antigen=CD121b;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, membrane form;
DE Short=mIL-1R2;
DE Short=mIL-1RII;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 2, soluble form;
DE Short=sIL-1R2;
DE Short=sIL-1RII;
DE Flags: Precursor;
GN Name=IL1R2; Synonyms=IL1RB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=B-cell;
RX PubMed=1833184;
RA McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D.,
RA Brunton L.L., Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I.,
RA Copeland N.G., Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D.,
RA Dower S.K., Spriggs M.K., Sims J.E.;
RT "A novel IL-1 receptor, cloned from B cells by mammalian expression,
RT is expressed in many cell types.";
RL EMBO J. 10:2821-2832(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), IL1B-BINDING, AND
RP SUBCELLULAR LOCATION (ISOFORM SHORT).
RX PubMed=8702856; DOI=10.1074/jbc.271.34.20965;
RA Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.;
RT "Cloning and characterization of an alternatively processed human type
RT II interleukin-1 receptor mRNA.";
RL J. Biol. Chem. 271:20965-20972(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Chou H.-H., Takashiba T., Takigawa M., Maeda H., Asahara Y.,
RA Nishimura F., Arai H., Murayama Y.;
RT "Complete nucleotide sequence and expression of the human interleukin-
RT 1 receptor type II in human gingival fibroblasts.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-181 AND LYS-292.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, PROTEOLYTIC PROCESSING, AND LIGAND-BINDING.
RX PubMed=7989776;
RA Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
RA Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
RT "Elevated levels of shed type II IL-1 receptor in sepsis. Potential
RT role for type II receptor in regulation of IL-1 responses.";
RL J. Immunol. 153:5802-5809(1994).
RN [9]
RP LIGAND-BINDING.
RX PubMed=7878046; DOI=10.1073/pnas.92.5.1714;
RA Symons J.A., Young P.R., Duff G.W.;
RT "Soluble type II interleukin 1 (IL-1) receptor binds and blocks
RT processing of IL-1 beta precursor and loses affinity for IL-1 receptor
RT antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1714-1718(1995).
RN [10]
RP PROTEOLYTIC PROCESSING.
RX PubMed=9395521; DOI=10.1074/jbc.272.50.31764;
RA Orlando S., Sironi M., Bianchi G., Drummond A.H., Boraschi D.,
RA Yabes D., Mantovani A.;
RT "Role of metalloproteases in the release of the IL-1 type II decoy
RT receptor.";
RL J. Biol. Chem. 272:31764-31769(1997).
RN [11]
RP FUNCTION, AND INTERACTION WITH IL1RAP.
RX PubMed=9862719;
RA Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
RA Martin M.U.;
RT "The type II IL-1 receptor interacts with the IL-1 receptor accessory
RT protein: a novel mechanism of regulation of IL-1 responsiveness.";
RL J. Immunol. 161:6871-6877(1998).
RN [12]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=10975853;
RA Neumann D., Kollewe C., Martin M.U., Boraschi D.;
RT "The membrane form of the type II IL-1 receptor accounts for
RT inhibitory function.";
RL J. Immunol. 165:3350-3357(2000).
RN [13]
RP FUNCTION AS DECOY RECEPTOR.
RX PubMed=12530978; DOI=10.1016/S1074-7613(02)00514-9;
RA Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M.,
RA MacVittie T.J., Virca G.D., Sims J.E.;
RT "The soluble form of IL-1 receptor accessory protein enhances the
RT ability of soluble type II IL-1 receptor to inhibit IL-1 action.";
RL Immunity 18:87-96(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 14-343 IN COMPLEX WITH IL1RAP
RP AND IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-112 AND
RP ASN-219.
RX PubMed=20802483; DOI=10.1038/ni.1925;
RA Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
RT "Structural insights into the assembly and activation of IL-1beta with
RT its receptors.";
RL Nat. Immunol. 11:905-911(2010).
CC -!- FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces
CC IL1B activities. Serves as a decoy receptor by competetive binding
CC to IL1B and preventing its binding to IL1R1. Also modulates
CC cellular response through non-signaling association with IL1RAP
CC after binding to IL1B. IL1R2 (membrane and secreted forms)
CC preferentially binds IL1B and poorly IL1A and IL1RN. The secreted
CC IL1R2 recruits secreted IL1RAP with high affinity; this complex
CC formation may be the dominant mechanism for neutralization of IL1B
CC by secreted/soluble receptors.
CC -!- SUBUNIT: Associates with IL1RAP to form a non-signaling
CC interleukin-1 receptor complex.
CC -!- SUBCELLULAR LOCATION: Isoform Short: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass
CC type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P27930-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P27930-2; Sequence=VSP_042222;
CC -!- PTM: A soluble form (sIL1R2) can also be produced by proteolytic
CC cleavage at the cell surface (shedding) involving a
CC metalloproteinase; hovever, several sIL1R2 forms ranging from 45
CC and 60 kDa are reported.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il1r2/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X59770; CAA42441.1; -; mRNA.
DR EMBL; U64094; AAB05878.1; -; mRNA.
DR EMBL; U74649; AAD00242.1; -; mRNA.
DR EMBL; AY124010; AAM64221.1; -; Genomic_DNA.
DR EMBL; AC007165; AAK52072.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01800.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01801.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01802.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01803.1; -; Genomic_DNA.
DR EMBL; BC039031; AAH39031.1; -; mRNA.
DR PIR; S17428; S17428.
DR RefSeq; NP_001248348.1; NM_001261419.1.
DR RefSeq; NP_004624.1; NM_004633.3.
DR UniGene; Hs.25333; -.
DR PDB; 3O4O; X-ray; 3.30 A; C=14-343.
DR PDBsum; 3O4O; -.
DR ProteinModelPortal; P27930; -.
DR SMR; P27930; 28-343.
DR IntAct; P27930; 3.
DR STRING; 9606.ENSP00000330959; -.
DR DrugBank; DB00026; Anakinra.
DR PhosphoSite; P27930; -.
DR DMDM; 124310; -.
DR PaxDb; P27930; -.
DR PRIDE; P27930; -.
DR DNASU; 7850; -.
DR Ensembl; ENST00000332549; ENSP00000330959; ENSG00000115590.
DR Ensembl; ENST00000393414; ENSP00000377066; ENSG00000115590.
DR Ensembl; ENST00000441002; ENSP00000414611; ENSG00000115590.
DR GeneID; 7850; -.
DR KEGG; hsa:7850; -.
DR UCSC; uc002tbm.3; human.
DR CTD; 7850; -.
DR GeneCards; GC02P102608; -.
DR HGNC; HGNC:5994; IL1R2.
DR HPA; HPA027597; -.
DR HPA; HPA027598; -.
DR MIM; 147811; gene.
DR neXtProt; NX_P27930; -.
DR PharmGKB; PA29810; -.
DR eggNOG; NOG44340; -.
DR HOGENOM; HOG000113036; -.
DR HOVERGEN; HBG052104; -.
DR InParanoid; P27930; -.
DR KO; K04387; -.
DR OMA; RQEYSEN; -.
DR OrthoDB; EOG77HDDW; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; P27930; -.
DR GeneWiki; Interleukin_1_receptor,_type_II; -.
DR GenomeRNAi; 7850; -.
DR NextBio; 30276; -.
DR PRO; PR:P27930; -.
DR ArrayExpress; P27930; -.
DR Bgee; P27930; -.
DR CleanEx; HS_IL1R2; -.
DR Genevestigator; P27930; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004908; F:interleukin-1 receptor activity; TAS:ProtInc.
DR GO; GO:0004910; F:interleukin-1, Type II, blocking receptor activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR004077; IL-1_rcpt_II-typ.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR PRINTS; PR01539; INTRLEUKN1R2.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 13 Potential.
FT CHAIN 14 398 Interleukin-1 receptor type 2, membrane
FT form.
FT /FTId=PRO_0000015439.
FT CHAIN 14 ? Interleukin-1 receptor type 2, soluble
FT form.
FT /FTId=PRO_0000415348.
FT TOPO_DOM 14 343 Extracellular (Potential).
FT TRANSMEM 344 369 Helical; (Potential).
FT TOPO_DOM 370 398 Cytoplasmic (Potential).
FT DOMAIN 18 124 Ig-like C2-type 1.
FT DOMAIN 134 223 Ig-like C2-type 2.
FT DOMAIN 237 349 Ig-like C2-type 3.
FT REGION 329 343 Contains proteolytic cleavage site
FT (Probable).
FT CARBOHYD 66 66 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 112 112 N-linked (GlcNAc...).
FT CARBOHYD 219 219 N-linked (GlcNAc...).
FT CARBOHYD 277 277 N-linked (GlcNAc...) (Potential).
FT DISULFID 28 116
FT DISULFID 50 108
FT DISULFID 152 207
FT DISULFID 258 326
FT VAR_SEQ 297 398 Missing (in isoform Short).
FT /FTId=VSP_042222.
FT VARIANT 181 181 E -> K (in dbSNP:rs28385682).
FT /FTId=VAR_019132.
FT VARIANT 292 292 E -> K (in dbSNP:rs3218976).
FT /FTId=VAR_019133.
FT CONFLICT 123 123 L -> F (in Ref. 2; AAD00242).
FT CONFLICT 171 171 K -> R (in Ref. 2; AAD00242).
FT CONFLICT 199 199 L -> Q (in Ref. 2; AAD00242).
FT STRAND 29 33
FT STRAND 38 41
FT STRAND 47 49
FT STRAND 70 73
FT STRAND 82 84
FT STRAND 86 89
FT STRAND 92 98
FT STRAND 104 107
FT STRAND 110 112
FT STRAND 115 126
FT HELIX 130 132
FT HELIX 133 136
FT STRAND 138 143
FT STRAND 148 151
FT TURN 156 158
FT STRAND 161 163
FT STRAND 170 173
FT STRAND 181 185
FT STRAND 189 196
FT HELIX 199 201
FT STRAND 203 210
FT STRAND 219 229
FT STRAND 260 265
FT STRAND 271 279
FT STRAND 281 285
FT STRAND 287 289
FT STRAND 301 303
FT STRAND 305 308
FT STRAND 325 330
FT STRAND 333 335
SQ SEQUENCE 398 AA; 45421 MW; 2C2A03ADA6F3AC5B CRC64;
MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC PQVPYWLWAS
VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ EDSGTYVCTT RNASYCDKMS
IELRVFENTD AFLPFISYPQ ILTLSTSGVL VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN
EKFLSVRGTT HLLVHDVALE DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII
SPLKTISASL GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE
NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW GIVLAPLSLA
FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK
//
MIM
147811
*RECORD*
*FIELD* NO
147811
*FIELD* TI
*147811 INTERLEUKIN 1 RECEPTOR, TYPE II; IL1R2
;;INTERLEUKIN 1 RECEPTOR, BETA, TYPE II; IL1RB
read more*FIELD* TX
CLONING
McMahan et al. (1991) used an expression cloning method to isolate human
and murine cDNA clones encoding the type II IL1 receptor. The mature
receptor was found to consist of a ligand-binding portion comprised of 3
immunoglobulin-like domains, a single transmembrane region, and a short
cytoplasmic domain of 29 amino acids. The last contrasts with the 215
amino acid cytoplasmic domain of the type I receptor (IL1RA; 147810) and
suggests that the 2 receptors may interact with different signal
transduction pathways. Both IL1 receptors appear to be well conserved in
evolution and map to the same chromosomal region. The molecular mass of
the type I receptor is about 80,000; that of the type II receptor is
about 60,000.
GENE FUNCTION
Colotta et al. (1993) reported results they interpreted as indicating
that interleukin-1 acts on myelomonocytic cells through the type I
receptor and that the type II receptor inhibits IL1 activity by acting
as a decoy target for IL1.
GENE STRUCTURE
Dale and Nicklin (1999) showed by radiation hybrid mapping that IL1R1
(147810), IL1R2, IL1RL2 (604512), IL1RL1 (601203), and IL18R1 (604494)
map to 2q12 and are transcribed in the same direction, with IL1R2 being
transcribed towards the cluster.
MAPPING
McMahan et al. (1991) mapped the type II IL1 receptor to chromosome
2q12-q22 by study of somatic cell hybrids and in situ hybridization.
IL1A (147760) and IL1B (147720), the human genes for interleukin-1, map
to 2q13-q21. The two IL1R genes map to mouse chromosome 1; in contrast
to the human, the mouse Il1 genes map to a separate chromosome, i.e.,
chromosome 2.
MOLECULAR GENETICS
Hao et al. (2004) conducted a large-scale case-control study exploring
the associations of 426 single-nucleotide polymorphisms (SNPs) with
preterm delivery (PTD) in 300 mothers with PTD and 458 mothers with term
deliveries. Twenty-five candidate genes were included in the final
haplotype analysis. Gene haplotypes at IL1R2 in blacks, NOS2A (1163730)
in whites, and OPRM1 (600018) in Hispanics were only associated with PTD
in these specific ethnic groups.
*FIELD* RF
1. Colotta, F.; Re, F.; Muzio, M.; Bertini, R.; Polentarutti, N.;
Sironi, M.; Giri, J. G.; Dower, S. K.; Sims, J. E.; Mantovani, A.
: Interleukin-1 type II receptor: a decoy target for IL-1 that is
regulated by IL-4. Science 261: 472-475, 1993.
2. Dale, M.; Nicklin, M. J.: Interleukin-1 receptor cluster: gene
organization of IL1R2, IL1R1, IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2),
and IL18R1 (IL-1Rrp) on human chromosome 2q. Genomics 57: 177-179,
1999.
3. Hao, K.; Wang, X.; Niu, T.; Xu, X.; Li, A.; Chang, W.; Wang, L.;
Li, G.; Laird, N.; Xu., X.: A candidate gene association study on
preterm delivery: application of high-throughput genotyping technology
and advanced statistical methods. Hum. Molec. Genet. 13: 683-691,
2004.
4. McMahan, C. J.; Slack, J. L.; Mosley, B.; Cosman, D.; Lupton, S.
D.; Brunton, L. L.; Grubin, C. E.; Wignall, J. M.; Jenkins, N. A.;
Brannan, C. I.; Copeland, N. G.; Huebner, K.; Croce, C. M.; Cannizzaro,
L. A.; Benjamin, D.; Dower, S. K.; Spriggs, M. K.; Sims, J. E.: A
novel IL-1 receptor, cloned from B cells by mammalian expression,
is expressed in many cell types. EMBO J. 10: 2821-2832, 1991.
*FIELD* CN
George E. Tiller - updated: 10/5/2006
Paul J. Converse - updated: 2/4/2000
*FIELD* CD
Victor A. McKusick: 5/14/1993
*FIELD* ED
mgross: 04/03/2012
terry: 3/21/2012
alopez: 10/5/2006
carol: 2/4/2000
carol: 12/22/1998
dkim: 7/2/1998
mark: 7/3/1997
carol: 5/13/1994
carol: 8/25/1993
carol: 5/14/1993
*RECORD*
*FIELD* NO
147811
*FIELD* TI
*147811 INTERLEUKIN 1 RECEPTOR, TYPE II; IL1R2
;;INTERLEUKIN 1 RECEPTOR, BETA, TYPE II; IL1RB
read more*FIELD* TX
CLONING
McMahan et al. (1991) used an expression cloning method to isolate human
and murine cDNA clones encoding the type II IL1 receptor. The mature
receptor was found to consist of a ligand-binding portion comprised of 3
immunoglobulin-like domains, a single transmembrane region, and a short
cytoplasmic domain of 29 amino acids. The last contrasts with the 215
amino acid cytoplasmic domain of the type I receptor (IL1RA; 147810) and
suggests that the 2 receptors may interact with different signal
transduction pathways. Both IL1 receptors appear to be well conserved in
evolution and map to the same chromosomal region. The molecular mass of
the type I receptor is about 80,000; that of the type II receptor is
about 60,000.
GENE FUNCTION
Colotta et al. (1993) reported results they interpreted as indicating
that interleukin-1 acts on myelomonocytic cells through the type I
receptor and that the type II receptor inhibits IL1 activity by acting
as a decoy target for IL1.
GENE STRUCTURE
Dale and Nicklin (1999) showed by radiation hybrid mapping that IL1R1
(147810), IL1R2, IL1RL2 (604512), IL1RL1 (601203), and IL18R1 (604494)
map to 2q12 and are transcribed in the same direction, with IL1R2 being
transcribed towards the cluster.
MAPPING
McMahan et al. (1991) mapped the type II IL1 receptor to chromosome
2q12-q22 by study of somatic cell hybrids and in situ hybridization.
IL1A (147760) and IL1B (147720), the human genes for interleukin-1, map
to 2q13-q21. The two IL1R genes map to mouse chromosome 1; in contrast
to the human, the mouse Il1 genes map to a separate chromosome, i.e.,
chromosome 2.
MOLECULAR GENETICS
Hao et al. (2004) conducted a large-scale case-control study exploring
the associations of 426 single-nucleotide polymorphisms (SNPs) with
preterm delivery (PTD) in 300 mothers with PTD and 458 mothers with term
deliveries. Twenty-five candidate genes were included in the final
haplotype analysis. Gene haplotypes at IL1R2 in blacks, NOS2A (1163730)
in whites, and OPRM1 (600018) in Hispanics were only associated with PTD
in these specific ethnic groups.
*FIELD* RF
1. Colotta, F.; Re, F.; Muzio, M.; Bertini, R.; Polentarutti, N.;
Sironi, M.; Giri, J. G.; Dower, S. K.; Sims, J. E.; Mantovani, A.
: Interleukin-1 type II receptor: a decoy target for IL-1 that is
regulated by IL-4. Science 261: 472-475, 1993.
2. Dale, M.; Nicklin, M. J.: Interleukin-1 receptor cluster: gene
organization of IL1R2, IL1R1, IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2),
and IL18R1 (IL-1Rrp) on human chromosome 2q. Genomics 57: 177-179,
1999.
3. Hao, K.; Wang, X.; Niu, T.; Xu, X.; Li, A.; Chang, W.; Wang, L.;
Li, G.; Laird, N.; Xu., X.: A candidate gene association study on
preterm delivery: application of high-throughput genotyping technology
and advanced statistical methods. Hum. Molec. Genet. 13: 683-691,
2004.
4. McMahan, C. J.; Slack, J. L.; Mosley, B.; Cosman, D.; Lupton, S.
D.; Brunton, L. L.; Grubin, C. E.; Wignall, J. M.; Jenkins, N. A.;
Brannan, C. I.; Copeland, N. G.; Huebner, K.; Croce, C. M.; Cannizzaro,
L. A.; Benjamin, D.; Dower, S. K.; Spriggs, M. K.; Sims, J. E.: A
novel IL-1 receptor, cloned from B cells by mammalian expression,
is expressed in many cell types. EMBO J. 10: 2821-2832, 1991.
*FIELD* CN
George E. Tiller - updated: 10/5/2006
Paul J. Converse - updated: 2/4/2000
*FIELD* CD
Victor A. McKusick: 5/14/1993
*FIELD* ED
mgross: 04/03/2012
terry: 3/21/2012
alopez: 10/5/2006
carol: 2/4/2000
carol: 12/22/1998
dkim: 7/2/1998
mark: 7/3/1997
carol: 5/13/1994
carol: 8/25/1993
carol: 5/14/1993