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Influenza virus NS1A-binding protein (NS1-BP) (NS1-binding protein) (Aryl hydrocarbon receptor-associated protein 3)

 NS1BP_HUMAN             Reviewed;         642 AA.
Q9Y6Y0; A8K8R6; Q1G4T6; Q1G4T7; Q5TF75; Q6NW38; Q7LCG2; Q9NZX0;
Q9Y480;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
07-NOV-2018, entry version 144.
RecName: Full=Influenza virus NS1A-binding protein;
Short=NS1-BP;
Short=NS1-binding protein {ECO:0000303|PubMed:9696811};
AltName: Full=Aryl hydrocarbon receptor-associated protein 3 {ECO:0000303|PubMed:16582008};
AltName: Full=Kelch-like protein 39 {ECO:0000303|PubMed:25619834};
Name=IVNS1ABP {ECO:0000312|HGNC:HGNC:16951};
Synonyms=ARA3, FLARA3, KIAA0850, KLHL39 {ECO:0000303|PubMed:25619834},
NS1, NS1BP; ORFNames=HSPC068;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH INFLUENZA A VIRUS
NON-STRUCTURAL PROTEIN 1 (MICROBIAL INFECTION), AND SUBCELLULAR
LOCATION.
PubMed=9696811;
Wolff T., O'Neill R.E., Palese P.;
"NS1-Binding protein (NS1-BP): a novel human protein that interacts
with the influenza A virus nonstructural NS1 protein is relocalized in
the nuclei of infected cells.";
J. Virol. 72:7170-7180(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, REGION, MUTAGENESIS OF
VAL-198 AND GLU-288, AND INTERACTION WITH AHR.
PubMed=16582008; DOI=10.1124/mol.106.024380;
Dunham E.E., Stevens E.A., Glover E., Bradfield C.A.;
"The aryl hydrocarbon receptor signaling pathway is modified through
interactions with a Kelch protein.";
Mol. Pharmacol. 70:8-15(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Chen B.S., Zhang K.M.;
"A novel gene from endothelium cells stimulated by human plasma LDL
-- similar to NS1-binding protein.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[5]
SEQUENCE REVISION.
Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-322, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-338, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INTERACTION WITH HNRNPK, AND FUNCTION (MICROBIAL INFECTION).
PubMed=23825951; DOI=10.1371/journal.ppat.1003460;
Tsai P.L., Chiou N.T., Kuss S., Garcia-Sastre A., Lynch K.W.,
Fontoura B.M.;
"Cellular RNA binding proteins NS1-BP and hnRNP K regulate influenza A
virus RNA splicing.";
PLoS Pathog. 9:E1003460-E1003460(2013).
[21]
INTERACTION WITH KLHL20, AND FUNCTION.
PubMed=25619834; DOI=10.1038/onc.2014.435;
Chen H.Y., Hu J.Y., Chen T.H., Lin Y.C., Liu X., Lin M.Y., Lang Y.D.,
Yen Y., Chen R.H.;
"KLHL39 suppresses colon cancer metastasis by blocking KLHL20-mediated
PML and DAPK ubiquitination.";
Oncogene 34:5141-5151(2015).
[22] {ECO:0000244|PDB:5YY8}
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 330-642.
PubMed=29497022; DOI=10.1107/S2053230X18001577;
Guo L., Liu Y.;
"Crystal structure of the Kelch domain of human NS1-binding protein at
1.98A resolution.";
Acta Crystallogr. F 74:174-178(2018).
-!- FUNCTION: Involved in many cell functions, including pre-mRNA
splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin
organization and protein ubiquitination. Plays a role in the
dynamic organization of the actin skeleton as a stabilizer of
actin filaments by association with F-actin through Kelch repeats
(By similarity). Protects cells from cell death induced by actin
destabilization (By similarity). Functions as modifier of the
AHR/Aryl hydrocarbon receptor pathway increasing the concentration
of AHR available to activate transcription (PubMed:16582008). In
addition, functions as a negative regulator of BCR(KLHL20) E3
ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis
of PML and DAPK1, two tumor suppressors (PubMed:25619834).
Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811).
{ECO:0000250|UniProtKB:Q920Q8, ECO:0000269|PubMed:16582008,
ECO:0000269|PubMed:25619834, ECO:0000269|PubMed:9696811}.
-!- FUNCTION: (Microbial infection) Involved in the alternative
splicing of influenza A virus M1 mRNA through interaction with
HNRNPK, thereby facilitating the generation of viral M2 protein.
{ECO:0000269|PubMed:23825951, ECO:0000269|PubMed:9696811}.
-!- SUBUNIT: Homodimer; through the BTB domain (By similarity).
Interacts with AHR/Aryl hydrocarbon receptor (PubMed:16582008).
Interacts with HNRNPK (PubMed:23825951). Interacts (via kelch
repeats) with KLHL20 (via kelch repeats); this interaction blocks
the assembly of Cul3-KLHL20 complex (PubMed:25619834).
{ECO:0000250|UniProtKB:Q920Q8, ECO:0000269|PubMed:16582008,
ECO:0000269|PubMed:23825951, ECO:0000269|PubMed:25619834}.
-!- SUBUNIT: (Microbial infection) Interacts with influenza A virus
non-structural protein 1/NS (PubMed:9696811).
{ECO:0000269|PubMed:9696811}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9696811}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9696811}. Nucleus,
nucleoplasm {ECO:0000269|PubMed:9696811}. Note=Associated with
actin filaments (By similarity). Localization related to speckle
domains which correspond to interchromatin granules and are
enriched in factors involved in pre-mRNA splicing
(PubMed:9696811). Following influenza A virus infection,
redistribution from speckles to a more diffuse distribution in the
nucleoplasm (PubMed:9696811). {ECO:0000250|UniProtKB:Q920Q8,
ECO:0000269|PubMed:9696811}.
-!- DOMAIN: When the BTB domain is lacking, AHR signaling induction
promoted by IVNS1ABP is massively increased; Thus, the BTB domain
inhibits AHR signaling induced by IVNS1ABP.
{ECO:0000269|PubMed:16582008}.
-!- SEQUENCE CAUTION:
Sequence=AAF29040.1; Type=Frameshift; Positions=100, 102; Evidence={ECO:0000305};
Sequence=BAA74873.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA10029.1; Type=Frameshift; Positions=612; Evidence={ECO:0000305};
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EMBL; AJ012449; CAA10029.1; ALT_FRAME; mRNA.
EMBL; DQ443528; ABE03889.1; -; mRNA.
EMBL; DQ443529; ABE03890.1; -; mRNA.
EMBL; AF205218; AAG43485.1; -; mRNA.
EMBL; AB020657; BAA74873.2; ALT_INIT; mRNA.
EMBL; AF161553; AAF29040.1; ALT_FRAME; mRNA.
EMBL; AL078644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK292431; BAF85120.1; -; mRNA.
EMBL; CH471067; EAW91194.1; -; Genomic_DNA.
EMBL; BC067739; AAH67739.1; -; mRNA.
CCDS; CCDS1368.1; -.
RefSeq; NP_006460.2; NM_006469.4.
UniGene; Hs.497183; -.
UniGene; Hs.662668; -.
PDB; 5YY8; X-ray; 1.98 A; A=330-642.
PDBsum; 5YY8; -.
ProteinModelPortal; Q9Y6Y0; -.
SMR; Q9Y6Y0; -.
BioGrid; 115869; 89.
IntAct; Q9Y6Y0; 22.
STRING; 9606.ENSP00000356468; -.
iPTMnet; Q9Y6Y0; -.
PhosphoSitePlus; Q9Y6Y0; -.
BioMuta; IVNS1ABP; -.
DMDM; 146325015; -.
EPD; Q9Y6Y0; -.
MaxQB; Q9Y6Y0; -.
PaxDb; Q9Y6Y0; -.
PeptideAtlas; Q9Y6Y0; -.
PRIDE; Q9Y6Y0; -.
ProteomicsDB; 86824; -.
Ensembl; ENST00000367498; ENSP00000356468; ENSG00000116679.
GeneID; 10625; -.
KEGG; hsa:10625; -.
UCSC; uc001grl.4; human.
CTD; 10625; -.
DisGeNET; 10625; -.
EuPathDB; HostDB:ENSG00000116679.15; -.
GeneCards; IVNS1ABP; -.
HGNC; HGNC:16951; IVNS1ABP.
HPA; HPA003405; -.
MIM; 609209; gene.
neXtProt; NX_Q9Y6Y0; -.
OpenTargets; ENSG00000116679; -.
PharmGKB; PA134875300; -.
eggNOG; KOG4441; Eukaryota.
eggNOG; ENOG410XNX8; LUCA.
GeneTree; ENSGT00760000118825; -.
HOVERGEN; HBG082407; -.
InParanoid; Q9Y6Y0; -.
KO; K15046; -.
OMA; PESNEWS; -.
OrthoDB; EOG091G024F; -.
PhylomeDB; Q9Y6Y0; -.
TreeFam; TF329218; -.
ChiTaRS; IVNS1ABP; human.
GeneWiki; IVNS1ABP; -.
GenomeRNAi; 10625; -.
PRO; PR:Q9Y6Y0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116679; Expressed in 236 organ(s), highest expression level in adult mammalian kidney.
CleanEx; HS_IVNS1ABP; -.
ExpressionAtlas; Q9Y6Y0; baseline and differential.
Genevisible; Q9Y6Y0; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005681; C:spliceosomal complex; TAS:ProtInc.
GO; GO:0005667; C:transcription factor complex; TAS:ProtInc.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.120.10.80; -; 2.
InterPro; IPR011705; BACK.
InterPro; IPR017096; BTB-kelch_protein.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR006652; Kelch_1.
InterPro; IPR029849; NS1BP.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
PANTHER; PTHR24411:SF7; PTHR24411:SF7; 1.
Pfam; PF07707; BACK; 1.
Pfam; PF00651; BTB; 1.
Pfam; PF01344; Kelch_1; 6.
PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
SMART; SM00875; BACK; 1.
SMART; SM00225; BTB; 1.
SMART; SM00612; Kelch; 6.
SUPFAM; SSF117281; SSF117281; 2.
SUPFAM; SSF54695; SSF54695; 1.
PROSITE; PS50097; BTB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoskeleton;
Host-virus interaction; Kelch repeat; Nucleus; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 642 Influenza virus NS1A-binding protein.
/FTId=PRO_0000285077.
DOMAIN 32 99 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
DOMAIN 134 233 BACK.
REPEAT 369 415 Kelch 1.
REPEAT 416 463 Kelch 2.
REPEAT 465 512 Kelch 3.
REPEAT 513 559 Kelch 4.
REPEAT 560 606 Kelch 5.
REPEAT 608 642 Kelch 6.
REGION 164 368 Sufficient for AHR interaction and
signaling.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MUTAGEN 198 198 V->M: Significant inhibition of
interaction with AHR; partial decrease of
AHR signaling induced by IVNS1ABP.
{ECO:0000269|PubMed:16582008}.
MUTAGEN 288 288 E->K: Significant inhibition of
interaction with AHR; partial decrease of
AHR signaling induced by IVNS1ABP.
{ECO:0000269|PubMed:16582008}.
CONFLICT 111 111 K -> E (in Ref. 1; CAA10029).
{ECO:0000305}.
CONFLICT 148 148 R -> H (in Ref. 1; CAA10029).
{ECO:0000305}.
CONFLICT 218 218 E -> G (in Ref. 10; AAH67739).
{ECO:0000305}.
CONFLICT 579 579 Y -> H (in Ref. 2; ABE03889/ABE03890).
{ECO:0000305}.
CONFLICT 591 591 N -> H (in Ref. 1; CAA10029).
{ECO:0000305}.
CONFLICT 623 623 V -> A (in Ref. 1; CAA10029).
{ECO:0000305}.
STRAND 362 366 {ECO:0000244|PDB:5YY8}.
STRAND 369 373 {ECO:0000244|PDB:5YY8}.
STRAND 385 388 {ECO:0000244|PDB:5YY8}.
TURN 390 392 {ECO:0000244|PDB:5YY8}.
STRAND 395 398 {ECO:0000244|PDB:5YY8}.
STRAND 409 413 {ECO:0000244|PDB:5YY8}.
STRAND 416 421 {ECO:0000244|PDB:5YY8}.
STRAND 428 431 {ECO:0000244|PDB:5YY8}.
STRAND 433 437 {ECO:0000244|PDB:5YY8}.
TURN 438 441 {ECO:0000244|PDB:5YY8}.
STRAND 442 446 {ECO:0000244|PDB:5YY8}.
HELIX 447 449 {ECO:0000244|PDB:5YY8}.
STRAND 457 461 {ECO:0000244|PDB:5YY8}.
STRAND 464 468 {ECO:0000244|PDB:5YY8}.
STRAND 482 486 {ECO:0000244|PDB:5YY8}.
TURN 487 490 {ECO:0000244|PDB:5YY8}.
STRAND 491 494 {ECO:0000244|PDB:5YY8}.
STRAND 502 504 {ECO:0000244|PDB:5YY8}.
STRAND 506 510 {ECO:0000244|PDB:5YY8}.
STRAND 513 533 {ECO:0000244|PDB:5YY8}.
TURN 534 537 {ECO:0000244|PDB:5YY8}.
STRAND 538 541 {ECO:0000244|PDB:5YY8}.
STRAND 553 557 {ECO:0000244|PDB:5YY8}.
STRAND 560 564 {ECO:0000244|PDB:5YY8}.
STRAND 569 572 {ECO:0000244|PDB:5YY8}.
STRAND 576 580 {ECO:0000244|PDB:5YY8}.
TURN 581 584 {ECO:0000244|PDB:5YY8}.
STRAND 585 588 {ECO:0000244|PDB:5YY8}.
STRAND 600 604 {ECO:0000244|PDB:5YY8}.
STRAND 607 611 {ECO:0000244|PDB:5YY8}.
STRAND 616 619 {ECO:0000244|PDB:5YY8}.
STRAND 623 627 {ECO:0000244|PDB:5YY8}.
TURN 628 631 {ECO:0000244|PDB:5YY8}.
STRAND 632 636 {ECO:0000244|PDB:5YY8}.
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


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