NS1BP_HUMAN
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 03-AUG-2022, entry version 166.
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}, NS1,
GN 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};
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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; 140.
DR IntAct; Q9Y6Y0; 51.
DR STRING; 9606.ENSP00000356468; -.
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; Q9Y6Y0; -.
DR PeptideAtlas; Q9Y6Y0; -.
DR PRIDE; Q9Y6Y0; -.
DR ProteomicsDB; 86824; -.
DR Antibodypedia; 1274; 121 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 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; TWTFIAP; -.
DR OrthoDB; 251780at2759; -.
DR PhylomeDB; Q9Y6Y0; -.
DR TreeFam; TF329218; -.
DR PathwayCommons; Q9Y6Y0; -.
DR SignaLink; Q9Y6Y0; -.
DR BioGRID-ORCS; 10625; 16 hits in 1123 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 206 other tissues.
DR ExpressionAtlas; Q9Y6Y0; baseline and differential.
DR Genevisible; Q9Y6Y0; HS.
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 Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 3.30.710.10; -; 1.
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 Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
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 pathological
FT significance; strong decrease in protein expression)"
FT /evidence="ECO:0000269|PubMed:32499645"
FT /id="VAR_084531"
FT VARIANT 633..642
FT /note="Missing (in IMD70; uncertain pathological
FT significance; strong 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
