IKBP1_MOUSE
ID IKBP1_MOUSE Reviewed; 259 AA.
AC Q9ESJ7; Q8BT82; Q8C645; Q9CRM0; Q9CV21; Q9CX27; Q9JK12;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Interleukin-1 receptor-associated kinase 1-binding protein 1;
DE Short=IRAK1-binding protein 1;
DE AltName: Full=ActA-binding protein 70;
DE AltName: Full=PLK-interacting protein;
DE AltName: Full=Signaling molecule that associates with the mouse pelle-like kinase;
DE Short=SIMPL;
GN Name=Irak1bp1; Synonyms=Aip70, Simpl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IRAK1, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11096118; DOI=10.1074/jbc.m010399200;
RA Vig E., Green M., Liu Y., Yu K.-Y., Kwon H.-J., Tian J., Goebl M.G.,
RA Harrington M.A.;
RT "SIMPL is a tumor necrosis factor-specific regulator of nuclear factor-
RT kappaB activity.";
RL J. Biol. Chem. 276:7859-7866(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Embryo, Testis, Tongue, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-259, AND POSSIBLE INTERACTION WITH
RP LISTERIA MONOCYTOGENES ACTA.
RC STRAIN=CD-1;
RX PubMed=11207567; DOI=10.1046/j.1462-5822.2000.00034.x;
RA Pfeuffer T., Goebel W., Laubinger J., Bachmann M., Kuhn M.;
RT "LaXp180, a mammalian ActA-binding protein, identified with the yeast two-
RT hybrid system co-localizes with intracellular Listeria monocytogenes.";
RL Cell. Microbiol. 2:101-114(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND
RP INTERACTION WITH RELA.
RX PubMed=15485901; DOI=10.1128/mcb.24.21.9317-9326.2004;
RA Kwon H.-J., Breese E.H., Vig-Varga E., Luo Y., Lee Y., Goebl M.G.,
RA Harrington M.A.;
RT "Tumor necrosis factor alpha induction of NF-kappaB requires the novel
RT coactivator SIMPL.";
RL Mol. Cell. Biol. 24:9317-9326(2004).
RN [6]
RP INTERACTION WITH HSPA8 AND HSPA1.
RX PubMed=17233114; DOI=10.1089/dna.2006.25.704;
RA Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
RT "The disordered amino-terminus of SIMPL interacts with members of the 70-
RT kDa heat-shock protein family.";
RL DNA Cell Biol. 25:704-714(2006).
RN [7]
RP PHOSPHORYLATION AT SER-55; SER-61; SER-63; SER-234; THR-236; SER-241 AND
RP THR-246.
RX PubMed=17079333; DOI=10.1152/ajpcell.00456.2006;
RA Luo Y., Kwon H.-J., Montano S., Georgiadis M., Goebl M.G., Harrington M.A.;
RT "Phosphorylation of SIMPL modulates RelA-associated NF-kappaB-dependent
RT transcription.";
RL Am. J. Physiol. 292:C1013-C1023(2007).
CC -!- FUNCTION: Component of the IRAK1-dependent TNFRSF1A signaling pathway
CC that leads to NF-kappa-B activation and is required for cell survival.
CC Acts by enhancing RELA transcriptional activity.
CC {ECO:0000269|PubMed:11096118, ECO:0000269|PubMed:15485901}.
CC -!- SUBUNIT: Interacts with IRAK1 and RELA. Interacts with HSPA8 and HSPA1.
CC May interact with Listeria monocytogenes actA.
CC {ECO:0000269|PubMed:11096118, ECO:0000269|PubMed:15485901,
CC ECO:0000269|PubMed:17233114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15485901}. Nucleus
CC {ECO:0000269|PubMed:15485901}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, brain, kidney, liver and
CC heart. {ECO:0000269|PubMed:11096118}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks at 10 dpc.
CC {ECO:0000269|PubMed:11096118}.
CC -!- DOMAIN: The disordered region interacts with HSPA1 and HSPA8.
CC -!- PTM: Phosphorylation at Ser-55, Ser-61 and/or Ser-63 is required for
CC full activity. Phosphorylated on at least one of Ser-234, Thr-236, Ser-
CC 241 and Thr-246 upon TNF-alpha activation, which favors nuclear
CC translocation. {ECO:0000269|PubMed:17079333}.
CC -!- SIMILARITY: Belongs to the IRAK1BP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB32019.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF093135; AAG16774.1; -; mRNA.
DR EMBL; AK009948; BAB26602.1; -; mRNA.
DR EMBL; AK020170; BAB32019.1; ALT_INIT; mRNA.
DR EMBL; AK020448; BAB32106.2; -; mRNA.
DR EMBL; AK013036; BAC25386.1; -; mRNA.
DR EMBL; AK045436; BAC32366.1; -; mRNA.
DR EMBL; AK076594; BAC36407.1; -; mRNA.
DR EMBL; BC061099; AAH61099.1; -; mRNA.
DR EMBL; AJ242722; CAB92240.1; -; mRNA.
DR CCDS; CCDS23372.1; -.
DR RefSeq; NP_001161712.1; NM_001168240.1.
DR RefSeq; NP_075362.3; NM_022986.4.
DR AlphaFoldDB; Q9ESJ7; -.
DR SMR; Q9ESJ7; -.
DR STRING; 10090.ENSMUSP00000108871; -.
DR iPTMnet; Q9ESJ7; -.
DR PhosphoSitePlus; Q9ESJ7; -.
DR EPD; Q9ESJ7; -.
DR MaxQB; Q9ESJ7; -.
DR PaxDb; Q9ESJ7; -.
DR PRIDE; Q9ESJ7; -.
DR ProteomicsDB; 267222; -.
DR Antibodypedia; 31572; 97 antibodies from 19 providers.
DR DNASU; 65099; -.
DR Ensembl; ENSMUST00000113245; ENSMUSP00000108871; ENSMUSG00000032251.
DR GeneID; 65099; -.
DR KEGG; mmu:65099; -.
DR UCSC; uc009qvs.2; mouse.
DR CTD; 134728; -.
DR MGI; MGI:1929475; Irak1bp1.
DR VEuPathDB; HostDB:ENSMUSG00000032251; -.
DR eggNOG; ENOG502QVHT; Eukaryota.
DR GeneTree; ENSGT00390000012588; -.
DR HOGENOM; CLU_066454_0_0_1; -.
DR InParanoid; Q9ESJ7; -.
DR OMA; TQTATRE; -.
DR OrthoDB; 1445231at2759; -.
DR PhylomeDB; Q9ESJ7; -.
DR TreeFam; TF328455; -.
DR BioGRID-ORCS; 65099; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9ESJ7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ESJ7; protein.
DR Bgee; ENSMUSG00000032251; Expressed in spermatocyte and 233 other tissues.
DR ExpressionAtlas; Q9ESJ7; baseline and differential.
DR Genevisible; Q9ESJ7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR InterPro; IPR007497; DUF541.
DR InterPro; IPR030312; IRAK1BP1.
DR PANTHER; PTHR18842; PTHR18842; 1.
DR Pfam; PF04402; SIMPL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..259
FT /note="Interleukin-1 receptor-associated kinase 1-binding
FT protein 1"
FT /id="PRO_0000313734"
FT REGION 239..259
FT /note="Required for nuclear localization (NLS)"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17079333"
FT CONFLICT 2
FT /note="S -> W (in Ref. 2; BAB32106)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..36
FT /note="QPI -> HAL (in Ref. 2; BAC36407)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..36
FT /note="QPI -> HGF (in Ref. 2; BAC25386)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> N (in Ref. 2; BAB32106)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="H -> R (in Ref. 4; CAB92240)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> T (in Ref. 2; BAB32019)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="K -> E (in Ref. 2; BAB26602)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="A -> S (in Ref. 4; CAB92240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28861 MW; ED57FAD25EF349BB CRC64;
MSLQPAPASR VFMELVPWAD RGRENHPISA AEAQPIGRRP HVAEAHPGAR EVHVSGAAEV
SASPDRALVT VRVSSTKEVS AEAKKSVCRR LDYITQSLQQ QGFQAENVTV TKNIRRVENA
YHMEAEVCIT FTEFGKMQNI CNFLVEKLDS SVVISPPEFY HTPGSVENLR RQACLVAVEN
AWRKAQEVCD LVGQTLGKPL LIKEEETKDW EGQTDDHQLS RLPGTLTVQQ KIKSATIHAA
SKVFITFEVK GKEKKKKHL
