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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.
27-SEP-2017, entry version 134.
RecName: Full=Influenza virus NS1A-binding protein;
Short=NS1-BP;
Short=NS1-binding protein;
AltName: Full=Aryl hydrocarbon receptor-associated protein 3;
Name=IVNS1ABP; Synonyms=ARA3, FLARA3, KIAA0850, 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 NS, 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).
-!- FUNCTION: Plays a role in cell division and in the dynamic
organization of the actin skeleton as a stabilizer of actin
filaments by association with F-actin through Kelch repeats.
Protects cells from cell death induced by actin destabilization;
Protects neurons from dendritic spines and actin filaments damage
induced by the actin-destabilizing cytochalasin B when
overexpressed. Activates Erk signaling pathway when overexpressed
in cultured cell lines (By similarity). May be a component of the
cellular splicing machinery with a role in pre-mRNA splicing; may
mediate the inhibition of splicing by NS/influenza virus NS1A
protein. Functions as modifier of the AHR/Aryl hydrocarbon
receptor pathway increasing the concentration of AHR available to
activate transcription. {ECO:0000250,
ECO:0000269|PubMed:16582008}.
-!- SUBUNIT: Homodimer; through the BTB domain (By similarity).
Interacts with NS/Influenza virus NS1A protein and with AHR/Aryl
hydrocarbon receptor. {ECO:0000250, ECO:0000269|PubMed:16582008,
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. Following
influenza A virus infection, redistribution from speckles to a
more diffuse distribution in the nucleoplasm. {ECO:0000250}.
-!- 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};
Sequence=CAI17867.1; Type=Erroneous gene model prediction; 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; CAB72329.1; -; Genomic_DNA.
EMBL; AL356273; CAB72329.1; JOINED; Genomic_DNA.
EMBL; AK292431; BAF85120.1; -; mRNA.
EMBL; AL078644; CAI17867.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356273; CAI22094.1; -; Genomic_DNA.
EMBL; AL078644; CAI22094.1; JOINED; Genomic_DNA.
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; -.
ProteinModelPortal; Q9Y6Y0; -.
SMR; Q9Y6Y0; -.
BioGrid; 115869; 73.
IntAct; Q9Y6Y0; 36.
MINT; MINT-1371090; -.
STRING; 9606.ENSP00000356468; -.
iPTMnet; Q9Y6Y0; -.
PhosphoSitePlus; Q9Y6Y0; -.
BioMuta; IVNS1ABP; -.
DMDM; 146325015; -.
EPD; Q9Y6Y0; -.
MaxQB; Q9Y6Y0; -.
PaxDb; Q9Y6Y0; -.
PeptideAtlas; Q9Y6Y0; -.
PRIDE; Q9Y6Y0; -.
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; ENSGT00760000119153; -.
HOVERGEN; HBG082407; -.
InParanoid; Q9Y6Y0; -.
KO; K15046; -.
OMA; PNIDDWI; -.
OrthoDB; EOG091G024F; -.
PhylomeDB; Q9Y6Y0; -.
TreeFam; TF329218; -.
ChiTaRS; IVNS1ABP; human.
GeneWiki; IVNS1ABP; -.
GenomeRNAi; 10625; -.
PRO; PR:Q9Y6Y0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116679; -.
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:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0006383; P:transcription from RNA polymerase III promoter; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.120.10.80; -; 1.
Gene3D; 2.130.10.80; -; 1.
InterPro; IPR011705; BACK.
InterPro; IPR017096; BTB-kelch_protein.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR015916; Gal_Oxidase_b-propeller.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR006652; Kelch_1.
InterPro; IPR029849; NS1BP.
InterPro; IPR011333; SKP1/BTB/POZ.
PANTHER; PTHR24411:SF46; PTHR24411:SF46; 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; SSF54695; SSF54695; 1.
PROSITE; PS50097; BTB; 1.
1: Evidence at protein level;
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}.
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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