IKBP1_HUMAN
ID IKBP1_HUMAN Reviewed; 260 AA.
AC Q5VVH5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Interleukin-1 receptor-associated kinase 1-binding protein 1;
DE Short=IRAK1-binding protein 1;
GN Name=IRAK1BP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 IDENTIFICATION.
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).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with IRAK1 and RELA. Interacts with HSPA8 and HSPA1
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5VVH5; Q8IVT2: MISP; NbExp=3; IntAct=EBI-9658404, EBI-2555085;
CC Q5VVH5; O43189: PHF1; NbExp=3; IntAct=EBI-9658404, EBI-530034;
CC Q5VVH5; O43741: PRKAB2; NbExp=3; IntAct=EBI-9658404, EBI-1053424;
CC Q5VVH5; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-9658404, EBI-10226430;
CC Q5VVH5; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-9658404, EBI-748391;
CC Q5VVH5; Q12800: TFCP2; NbExp=3; IntAct=EBI-9658404, EBI-717422;
CC Q5VVH5; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-9658404, EBI-14096082;
CC Q5VVH5; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-9658404, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The disordered region interacts with HSPA1 and HSPA8.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-56 and/or Ser-62 is required for full
CC activity. Phosphorylated on at least one of Ser-235, Thr-237, Ser-242
CC and Thr-247 upon TNF-alpha activation, which favors nuclear
CC translocation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IRAK1BP1 family. {ECO:0000305}.
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DR EMBL; AL450327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48721.1; -; Genomic_DNA.
DR EMBL; BC112253; AAI12254.1; -; mRNA.
DR EMBL; BC112255; AAI12256.1; -; mRNA.
DR CCDS; CCDS34488.1; -.
DR RefSeq; NP_001010844.1; NM_001010844.3.
DR AlphaFoldDB; Q5VVH5; -.
DR SMR; Q5VVH5; -.
DR BioGRID; 126412; 16.
DR IntAct; Q5VVH5; 10.
DR STRING; 9606.ENSP00000358956; -.
DR iPTMnet; Q5VVH5; -.
DR PhosphoSitePlus; Q5VVH5; -.
DR BioMuta; IRAK1BP1; -.
DR DMDM; 74747244; -.
DR EPD; Q5VVH5; -.
DR MassIVE; Q5VVH5; -.
DR PaxDb; Q5VVH5; -.
DR PeptideAtlas; Q5VVH5; -.
DR PRIDE; Q5VVH5; -.
DR ProteomicsDB; 65465; -.
DR Antibodypedia; 31572; 97 antibodies from 19 providers.
DR DNASU; 134728; -.
DR Ensembl; ENST00000369940.7; ENSP00000358956.1; ENSG00000146243.14.
DR GeneID; 134728; -.
DR KEGG; hsa:134728; -.
DR MANE-Select; ENST00000369940.7; ENSP00000358956.1; NM_001010844.4; NP_001010844.1.
DR UCSC; uc003pim.6; human.
DR CTD; 134728; -.
DR DisGeNET; 134728; -.
DR GeneCards; IRAK1BP1; -.
DR HGNC; HGNC:17368; IRAK1BP1.
DR HPA; ENSG00000146243; Low tissue specificity.
DR MalaCards; IRAK1BP1; -.
DR MIM; 615375; gene.
DR neXtProt; NX_Q5VVH5; -.
DR OpenTargets; ENSG00000146243; -.
DR PharmGKB; PA134919096; -.
DR VEuPathDB; HostDB:ENSG00000146243; -.
DR eggNOG; ENOG502QVHT; Eukaryota.
DR GeneTree; ENSGT00390000012588; -.
DR HOGENOM; CLU_066454_0_0_1; -.
DR InParanoid; Q5VVH5; -.
DR OMA; TQTATRE; -.
DR OrthoDB; 1445231at2759; -.
DR PhylomeDB; Q5VVH5; -.
DR TreeFam; TF328455; -.
DR PathwayCommons; Q5VVH5; -.
DR SignaLink; Q5VVH5; -.
DR BioGRID-ORCS; 134728; 6 hits in 1027 CRISPR screens.
DR ChiTaRS; IRAK1BP1; human.
DR GenomeRNAi; 134728; -.
DR Pharos; Q5VVH5; Tbio.
DR PRO; PR:Q5VVH5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VVH5; protein.
DR Bgee; ENSG00000146243; Expressed in oocyte and 152 other tissues.
DR ExpressionAtlas; Q5VVH5; baseline and differential.
DR Genevisible; Q5VVH5; HS.
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; ISS:UniProtKB.
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..260
FT /note="Interleukin-1 receptor-associated kinase 1-binding
FT protein 1"
FT /id="PRO_0000313733"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..260
FT /note="Required for nuclear localization (NLS)"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ7"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ7"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ7"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ7"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ7"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ7"
SQ SEQUENCE 260 AA; 29106 MW; F8576A4ED9C40352 CRC64;
MSLQKTPPTR VFVELVPWAD RSRENNLASG RETLPGLRHP LSSTQAQTAT REVQVSGTSE
VSAGPDRAQV VVRVSSTKEA AAEAKKSVCR RLDYITQSLQ QQGVQAENIT VTKDFRRVEN
AYHMEAEVCI TFTEFGKMQN ICNFLVEKLD SSVVISPPQF YHTPGSVENL RRQACLVAVE
NAWRKAQEVC NLVGQTLGKP LLIKEEETKE WEGQIDDHQS SRLSSSLTVQ QKIKSATIHA
ASKVFITFEV KGKEKRKKHL
