ID NS1BP_HUMAN Reviewed; 642 AA. AC Q9Y6Y0; A8K8R6; Q1G4T6; Q1G4T7; Q5TF75; Q6NW38; Q7LCG2; Q9NZX0; Q9Y480; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 3. DT 27-MAR-2024, entry version 175. DE RecName: Full=Influenza virus NS1A-binding protein; DE Short=NS1-BP; DE Short=NS1-binding protein {ECO:0000303|PubMed:9696811}; DE AltName: Full=Aryl hydrocarbon receptor-associated protein 3 {ECO:0000303|PubMed:16582008}; DE AltName: Full=Kelch-like protein 39 {ECO:0000303|PubMed:25619834}; GN Name=IVNS1ABP {ECO:0000312|HGNC:HGNC:16951}; GN Synonyms=ARA3, FLARA3, KIAA0850, KLHL39 {ECO:0000303|PubMed:25619834}, GN NS1, NS1BP; ORFNames=HSPC068; 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 [MRNA], INTERACTION WITH INFLUENZA A VIRUS RP NON-STRUCTURAL PROTEIN 1 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=9696811; DOI=10.1128/jvi.72.9.7170-7180.1998; RA Wolff T., O'Neill R.E., Palese P.; RT "NS1-Binding protein (NS1-BP): a novel human protein that interacts with RT the influenza A virus nonstructural NS1 protein is relocalized in the RT nuclei of infected cells."; RL J. Virol. 72:7170-7180(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, REGION, MUTAGENESIS OF RP VAL-198 AND GLU-288, AND INTERACTION WITH AHR. RX PubMed=16582008; DOI=10.1124/mol.106.024380; RA Dunham E.E., Stevens E.A., Glover E., Bradfield C.A.; RT "The aryl hydrocarbon receptor signaling pathway is modified through RT interactions with a Kelch protein."; RL Mol. Pharmacol. 70:8-15(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Chen B.S., Zhang K.M.; RT "A novel gene from endothelium cells stimulated by human plasma LDL RT -- similar to NS1-binding protein."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [5] RP SEQUENCE REVISION. RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-322, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-338, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP INTERACTION WITH HNRNPK, AND FUNCTION (MICROBIAL INFECTION). RX PubMed=23825951; DOI=10.1371/journal.ppat.1003460; RA Tsai P.L., Chiou N.T., Kuss S., Garcia-Sastre A., Lynch K.W., RA Fontoura B.M.; RT "Cellular RNA binding proteins NS1-BP and hnRNP K regulate influenza A RT virus RNA splicing."; RL PLoS Pathog. 9:E1003460-E1003460(2013). RN [21] RP INTERACTION WITH KLHL20, AND FUNCTION. RX PubMed=25619834; DOI=10.1038/onc.2014.435; RA Chen H.Y., Hu J.Y., Chen T.H., Lin Y.C., Liu X., Lin M.Y., Lang Y.D., RA Yen Y., Chen R.H.; RT "KLHL39 suppresses colon cancer metastasis by blocking KLHL20-mediated PML RT and DAPK ubiquitination."; RL Oncogene 34:5141-5151(2015). RN [22] RP INVOLVEMENT IN IMD70, VARIANTS IMD70 358-ARG--PHE-642 DEL AND RP 633-TRP--PHE-642 DEL, AND CHARACTERIZATION OF VARIANTS IMD70 RP 358-ARG--PHE-642 DEL AND 633-TRP--PHE-642 DEL. RX PubMed=32499645; DOI=10.1038/s41586-020-2265-1; RG Primary Immunodeficiency Consortium for the NIHR Bioresource; RA Thaventhiran J.E.D., Lango Allen H., Burren O.S., Rae W., Greene D., RA Staples E., Zhang Z., Farmery J.H.R., Simeoni I., Rivers E., Maimaris J., RA Penkett C.J., Stephens J., Deevi S.V.V., Sanchis-Juan A., Gleadall N.S., RA Thomas M.J., Sargur R.B., Gordins P., Baxendale H.E., Brown M., RA Tuijnenburg P., Worth A., Hanson S., Linger R.J., Buckland M.S., RA Rayner-Matthews P.J., Gilmour K.C., Samarghitean C., Seneviratne S.L., RA Sansom D.M., Lynch A.G., Megy K., Ellinghaus E., Ellinghaus D., RA Jorgensen S.F., Karlsen T.H., Stirrups K.E., Cutler A.J., Kumararatne D.S., RA Chandra A., Edgar J.D.M., Herwadkar A., Cooper N., Grigoriadou S., RA Huissoon A.P., Goddard S., Jolles S., Schuetz C., Boschann F., Lyons P.A., RA Hurles M.E., Savic S., Burns S.O., Kuijpers T.W., Turro E., Ouwehand W.H., RA Thrasher A.J., Smith K.G.C.; RT "Whole-genome sequencing of a sporadic primary immunodeficiency cohort."; RL Nature 583:90-95(2020). RN [23] {ECO:0007744|PDB:5YY8} RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 330-642. RX PubMed=29497022; DOI=10.1107/s2053230x18001577; RA Guo L., Liu Y.; RT "Crystal structure of the Kelch domain of human NS1-binding protein at RT 1.98A resolution."; RL Acta Crystallogr. F 74:174-178(2018). CC -!- FUNCTION: Involved in many cell functions, including pre-mRNA splicing, CC the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and CC protein ubiquitination. Plays a role in the dynamic organization of the CC actin skeleton as a stabilizer of actin filaments by association with CC F-actin through Kelch repeats (By similarity). Protects cells from cell CC death induced by actin destabilization (By similarity). Functions as CC modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the CC concentration of AHR available to activate transcription CC (PubMed:16582008). In addition, functions as a negative regulator of CC BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated CC proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834). CC Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811). CC {ECO:0000250|UniProtKB:Q920Q8, ECO:0000269|PubMed:16582008, CC ECO:0000269|PubMed:25619834, ECO:0000269|PubMed:9696811}. CC -!- FUNCTION: (Microbial infection) Involved in the alternative splicing of CC influenza A virus M1 mRNA through interaction with HNRNPK, thereby CC facilitating the generation of viral M2 protein. CC {ECO:0000269|PubMed:23825951, ECO:0000269|PubMed:9696811}. CC -!- SUBUNIT: Homodimer; through the BTB domain (By similarity). Interacts CC with AHR/Aryl hydrocarbon receptor (PubMed:16582008). Interacts with CC HNRNPK (PubMed:23825951). Interacts (via kelch repeats) with KLHL20 CC (via kelch repeats); this interaction blocks the assembly of Cul3- CC KLHL20 complex (PubMed:25619834). {ECO:0000250|UniProtKB:Q920Q8, CC ECO:0000269|PubMed:16582008, ECO:0000269|PubMed:23825951, CC ECO:0000269|PubMed:25619834}. CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus non- CC structural protein 1/NS (PubMed:9696811). {ECO:0000269|PubMed:9696811}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9696811}. CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9696811}. Nucleus, CC nucleoplasm {ECO:0000269|PubMed:9696811}. Note=Associated with actin CC filaments (By similarity). Localization related to speckle domains CC which correspond to interchromatin granules and are enriched in factors CC involved in pre-mRNA splicing (PubMed:9696811). Following influenza A CC virus infection, redistribution from speckles to a more diffuse CC distribution in the nucleoplasm (PubMed:9696811). CC {ECO:0000250|UniProtKB:Q920Q8, ECO:0000269|PubMed:9696811}. CC -!- DOMAIN: When the BTB domain is lacking, AHR signaling induction CC promoted by IVNS1ABP is massively increased; Thus, the BTB domain CC inhibits AHR signaling induced by IVNS1ABP. CC {ECO:0000269|PubMed:16582008}. CC -!- DISEASE: Immunodeficiency 70 (IMD70) [MIM:618969]: A primary CC immunodeficiency clinically characterized by human papillomavirus- CC associated warts on the hands, feet and face, recurrent bacterial CC infections, and autoinflammatory features, such as colitis, celiac CC disease, and retinal vasculitis. Immunologic workup shows decreased CC CD4+ T cells, decreased CD19+ B cells, and hypogammaglobulinemia. IMD70 CC inheritance is autosomal dominant with incomplete penetrance. CC {ECO:0000269|PubMed:32499645}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAF29040.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA74873.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA10029.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ012449; CAA10029.1; ALT_FRAME; mRNA. DR EMBL; DQ443528; ABE03889.1; -; mRNA. DR EMBL; DQ443529; ABE03890.1; -; mRNA. DR EMBL; AF205218; AAG43485.1; -; mRNA. DR EMBL; AB020657; BAA74873.2; ALT_INIT; mRNA. DR EMBL; AF161553; AAF29040.1; ALT_FRAME; mRNA. DR EMBL; AL078644; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK292431; BAF85120.1; -; mRNA. DR EMBL; CH471067; EAW91194.1; -; Genomic_DNA. DR EMBL; BC067739; AAH67739.1; -; mRNA. DR CCDS; CCDS1368.1; -. DR RefSeq; NP_006460.2; NM_006469.4. DR PDB; 5YY8; X-ray; 1.98 A; A=330-642. DR PDB; 6N34; X-ray; 2.80 A; A/B=1-137. DR PDB; 6N3H; X-ray; 2.60 A; A/B=321-642. DR PDBsum; 5YY8; -. DR PDBsum; 6N34; -. DR PDBsum; 6N3H; -. DR AlphaFoldDB; Q9Y6Y0; -. DR SMR; Q9Y6Y0; -. DR BioGRID; 115869; 162. DR IntAct; Q9Y6Y0; 59. DR STRING; 9606.ENSP00000356468; -. DR GlyGen; Q9Y6Y0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y6Y0; -. DR PhosphoSitePlus; Q9Y6Y0; -. DR BioMuta; IVNS1ABP; -. DR DMDM; 146325015; -. DR EPD; Q9Y6Y0; -. DR jPOST; Q9Y6Y0; -. DR MassIVE; Q9Y6Y0; -. DR MaxQB; Q9Y6Y0; -. DR PaxDb; 9606-ENSP00000356468; -. DR PeptideAtlas; Q9Y6Y0; -. DR ProteomicsDB; 86824; -. DR Pumba; Q9Y6Y0; -. DR Antibodypedia; 1274; 137 antibodies from 26 providers. DR DNASU; 10625; -. DR Ensembl; ENST00000367498.8; ENSP00000356468.3; ENSG00000116679.16. DR GeneID; 10625; -. DR KEGG; hsa:10625; -. DR MANE-Select; ENST00000367498.8; ENSP00000356468.3; NM_006469.5; NP_006460.2. DR UCSC; uc001grl.4; human. DR AGR; HGNC:16951; -. DR CTD; 10625; -. DR DisGeNET; 10625; -. DR GeneCards; IVNS1ABP; -. DR HGNC; HGNC:16951; IVNS1ABP. DR HPA; ENSG00000116679; Tissue enriched (bone). DR MalaCards; IVNS1ABP; -. DR MIM; 609209; gene. DR MIM; 618969; phenotype. DR neXtProt; NX_Q9Y6Y0; -. DR OpenTargets; ENSG00000116679; -. DR PharmGKB; PA134875300; -. DR VEuPathDB; HostDB:ENSG00000116679; -. DR eggNOG; KOG4441; Eukaryota. DR GeneTree; ENSGT00940000155635; -. DR HOGENOM; CLU_004253_14_2_1; -. DR InParanoid; Q9Y6Y0; -. DR OMA; TEIVQDY; -. DR OrthoDB; 5472491at2759; -. DR PhylomeDB; Q9Y6Y0; -. DR TreeFam; TF329218; -. DR PathwayCommons; Q9Y6Y0; -. DR SignaLink; Q9Y6Y0; -. DR BioGRID-ORCS; 10625; 16 hits in 1203 CRISPR screens. DR ChiTaRS; IVNS1ABP; human. DR GeneWiki; IVNS1ABP; -. DR GenomeRNAi; 10625; -. DR Pharos; Q9Y6Y0; Tbio. DR PRO; PR:Q9Y6Y0; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y6Y0; Protein. DR Bgee; ENSG00000116679; Expressed in ganglionic eminence and 208 other cell types or tissues. DR ExpressionAtlas; Q9Y6Y0; baseline and differential. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005681; C:spliceosomal complex; TAS:ProtInc. DR GO; GO:0005667; C:transcription regulator complex; TAS:ProtInc. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB. DR GO; GO:0009615; P:response to virus; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB. DR GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc. DR CDD; cd18502; BACK_NS1BP_IVNS1ABP; 1. DR CDD; cd18306; BTB_POZ_NS1BP; 1. DR Gene3D; 1.25.40.420; -; 1. DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2. DR InterPro; IPR011705; BACK. DR InterPro; IPR017096; BTB-kelch_protein. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR015915; Kelch-typ_b-propeller. DR InterPro; IPR006652; Kelch_1. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR PANTHER; PTHR24412:SF396; INFLUENZA VIRUS NS1A-BINDING PROTEIN; 1. DR PANTHER; PTHR24412; KELCH PROTEIN; 1. DR Pfam; PF07707; BACK; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF01344; Kelch_1; 6. DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1. DR PRINTS; PR00501; KELCHREPEAT. DR SMART; SM00875; BACK; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00612; Kelch; 6. DR SUPFAM; SSF117281; Kelch motif; 2. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR Genevisible; Q9Y6Y0; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Cytoskeleton; Host-virus interaction; KW Kelch repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..642 FT /note="Influenza virus NS1A-binding protein" FT /id="PRO_0000285077" FT DOMAIN 32..99 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT DOMAIN 134..233 FT /note="BACK" FT REPEAT 369..415 FT /note="Kelch 1" FT REPEAT 416..463 FT /note="Kelch 2" FT REPEAT 465..512 FT /note="Kelch 3" FT REPEAT 513..559 FT /note="Kelch 4" FT REPEAT 560..606 FT /note="Kelch 5" FT REPEAT 608..642 FT /note="Kelch 6" FT REGION 164..368 FT /note="Sufficient for AHR interaction and signaling" FT REGION 257..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 264..281 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 338 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT VARIANT 358..642 FT /note="Missing (in IMD70; uncertain significance; strong FT decrease in protein expression)" FT /evidence="ECO:0000269|PubMed:32499645" FT /id="VAR_084531" FT VARIANT 633..642 FT /note="Missing (in IMD70; uncertain significance; strong FT decrease in protein expression)" FT /evidence="ECO:0000269|PubMed:32499645" FT /id="VAR_084532" FT MUTAGEN 198 FT /note="V->M: Significant inhibition of interaction with FT AHR; partial decrease of AHR signaling induced by FT IVNS1ABP." FT /evidence="ECO:0000269|PubMed:16582008" FT MUTAGEN 288 FT /note="E->K: Significant inhibition of interaction with FT AHR; partial decrease of AHR signaling induced by FT IVNS1ABP." FT /evidence="ECO:0000269|PubMed:16582008" FT CONFLICT 111 FT /note="K -> E (in Ref. 1; CAA10029)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="R -> H (in Ref. 1; CAA10029)" FT /evidence="ECO:0000305" FT CONFLICT 218 FT /note="E -> G (in Ref. 10; AAH67739)" FT /evidence="ECO:0000305" FT CONFLICT 579 FT /note="Y -> H (in Ref. 2; ABE03889/ABE03890)" FT /evidence="ECO:0000305" FT CONFLICT 591 FT /note="N -> H (in Ref. 1; CAA10029)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="V -> A (in Ref. 1; CAA10029)" FT /evidence="ECO:0000305" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 12..27 FT /evidence="ECO:0007829|PDB:6N34" FT STRAND 34..38 FT /evidence="ECO:0007829|PDB:6N34" FT STRAND 41..45 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 47..51 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 55..60 FT /evidence="ECO:0007829|PDB:6N34" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:6N34" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 80..92 FT /evidence="ECO:0007829|PDB:6N34" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 102..111 FT /evidence="ECO:0007829|PDB:6N34" FT HELIX 115..126 FT /evidence="ECO:0007829|PDB:6N34" FT STRAND 362..366 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 369..373 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 385..388 FT /evidence="ECO:0007829|PDB:5YY8" FT TURN 390..392 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 409..413 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 416..421 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:6N3H" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 433..437 FT /evidence="ECO:0007829|PDB:5YY8" FT TURN 438..441 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 442..446 FT /evidence="ECO:0007829|PDB:5YY8" FT HELIX 447..449 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 457..461 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 464..468 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 482..486 FT /evidence="ECO:0007829|PDB:5YY8" FT TURN 487..490 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 491..494 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 513..533 FT /evidence="ECO:0007829|PDB:5YY8" FT TURN 534..537 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 538..541 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 553..557 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 560..564 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 569..572 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 576..580 FT /evidence="ECO:0007829|PDB:5YY8" FT TURN 581..584 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 585..588 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 600..604 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 607..611 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 616..619 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 623..627 FT /evidence="ECO:0007829|PDB:5YY8" FT TURN 628..631 FT /evidence="ECO:0007829|PDB:5YY8" FT STRAND 632..636 FT /evidence="ECO:0007829|PDB:5YY8" SQ SEQUENCE 642 AA; 71729 MW; 456E30DC4E351CCD CRC64; MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL ACCSPYLFEI FNSDSDPHGI SHVKFDDLNP EAVEVLLNYA YTAQLKADKE LVKDVYSAAK KLKMDRVKQV CGDYLLSRMD VTSCISYRNF ASCMGDSRLL NKVDAYIQEH LLQISEEEEF LKLPRLKLEV MLEDNVCLPS NGKLYTKVIN WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNLLDGQ AEVFGSDDDH IQFVQKKPPR ENGHKQISSS STGCLSSPNA TVQSPKHEWK IVASEKTSNN TYLCLAVLDG IFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQQDELIEKP MSPMQYARSG LGTAEMNGKL IAAGGYNREE CLRTVECYNP HTDHWSFLAP MRTPRARFQM AVLMGQLYVV GGSNGHSDDL SCGEMYDSNI DDWIPVPELR TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK NCDVFDPVTK LWTSCAPLNI RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT LIAPMNVARR GAGVAVLNGK LFVCGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG IATVGNTIYA VGGFDGNEFL NTVEVYNLES NEWSPYTKIF QF //