ID PI4KB_HUMAN Reviewed; 816 AA. AC Q9UBF8; B4DGI2; O15096; P78405; Q5VWB9; Q5VWC0; Q5VWC1; Q9BWR6; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 199. DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000305}; DE Short=PI4K-beta; DE Short=PI4Kbeta; DE Short=PtdIns 4-kinase beta; DE EC=2.7.1.67 {ECO:0000269|PubMed:11277933, ECO:0000269|PubMed:9405935}; DE AltName: Full=NPIK; DE AltName: Full=PI4K92; DE AltName: Full=PI4KIII {ECO:0000303|PubMed:22124328, ECO:0000303|PubMed:22258260}; GN Name=PI4KB {ECO:0000312|HGNC:HGNC:8984}; Synonyms=PIK4CB; 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 {ECO:0000312|EMBL:AAC51156.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=9405935; DOI=10.1093/dnares/4.4.273; RA Suzuki K., Hirano H., Okutomi K., Suzuki M., Kuga Y., Fujiwara T., RA Kanemoto N., Isono K., Horie M.; RT "Identification and characterization of a novel human phosphatidylinositol RT 4-kinase."; RL DNA Res. 4:273-280(1997). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain {ECO:0000312|EMBL:BAA21661.1}; RX PubMed=9405938; DOI=10.1093/dnares/4.4.301; RA Saito T., Seki N., Ishii H., Ohira M., Hayashi A., Kozuma S., Hori T.-A.; RT "Complementary DNA cloning and chromosomal mapping of a novel RT phosphatidylinositol kinase gene."; RL DNA Res. 4:301-305(1997). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ACTIVITY REGULATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Heart {ECO:0000269|PubMed:9020160}; RX PubMed=9020160; DOI=10.1074/jbc.272.7.4384; RA Meyers R., Cantley L.C.; RT "Cloning and characterization of a wortmannin-sensitive human RT phosphatidylinositol 4-kinase."; RL J. Biol. Chem. 272:4384-4390(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain {ECO:0000312|EMBL:AAH00029.1}, and Testis RC {ECO:0000312|EMBL:AAH40300.1}; 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 [8] RP PROTEIN SEQUENCE OF 2-118; 121-229; 236-303; 319-442; 497-798 AND 804-816 RP (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, RP PHOSPHORYLATION AT SER-294, INTERACTION WITH ACBD3; ARMH3; RAB11B; YWHAB; RP YWHAE; YWHAG; YWHAH; YWHAQ; YWHAZ AND SFN, MUTAGENESIS OF 40-LEU--VAL-42; RP 43-ILE--PRO-45; 46-GLU-VAL-47; 49-GLN-LYS-50; CYS-52; 53-GLN-GLU-54; RP 55-VAL-LEU-56 AND 57-GLU--VAL-59, AND MASS SPECTROMETRY. RX PubMed=23572552; DOI=10.1128/mbio.00098-13; RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.; RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected RT by enteroviral and kobuviral 3A protein binding."; RL MBio 4:E00098-E00098(2013). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=9148941; DOI=10.1074/jbc.272.20.13236; RA Wong K., Meyers R., Cantley L.C.; RT "Subcellular locations of phosphatidylinositol 4-kinase isoforms."; RL J. Biol. Chem. 272:13236-13241(1997). RN [10] RP FUNCTION. RX PubMed=10559940; DOI=10.1038/12993; RA Godi A., Pertile P., Meyers R., Marra P., Di Tullio G., Iurisci C., RA Luini A., Corda D., De Matteis M.A.; RT "ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates RT synthesis of PtdIns(4,5)P2 on the Golgi complex."; RL Nat. Cell Biol. 1:280-287(1999). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY RP REGULATION, COFACTOR, AND PHOSPHORYLATION AT SER-258; THR-263; SER-266; RP SER-277; SER-294; THR-438; SER-511 AND THR-519. RX PubMed=11277933; DOI=10.1046/j.1432-1327.2001.02089.x; RA Suer S., Sickmann A., Meyer H.E., Herberg F.W., Heilmeyer L.M.G. Jr.; RT "Human phosphatidylinositol 4-kinase isoform PI4K92. Expression of the RT recombinant enzyme and determination of multiple phosphorylation sites."; RL Eur. J. Biochem. 268:2099-2106(2001). RN [12] RP FUNCTION. RX PubMed=12749687; DOI=10.1002/tbmb.718540873; RA Heilmeyer L.M.G. Jr., Vereb G. Jr., Vereb G., Kakuk A., Szivak I.; RT "Mammalian phosphatidylinositol 4-kinases."; RL IUBMB Life 55:59-65(2003). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY RP 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 [14] RP INTERACTION WITH ARF1 AND ARF3, AND SUBCELLULAR LOCATION. RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x; RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.; RT "Specificity, promiscuity and localization of ARF protein interactions with RT NCS-1 and phosphatidylinositol-4 kinase-III beta."; RL Traffic 8:1080-1092(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-277; SER-428 AND RP SER-511, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 (ISOFORM 2), AND RP IDENTIFICATION BY 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-266 AND SER-428, AND 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY RP 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 [21] RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, IDENTIFICATION IN A RP COMPLEX AICHI VIRUS PROTEIN 3A/ACBD3/PI4KB (MICROBIAL INFECTION), AND RP INTERACTION WITH ACBD3. RX PubMed=22124328; DOI=10.1038/emboj.2011.429; RA Sasaki J., Ishikawa K., Arita M., Taniguchi K.; RT "ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication RT sites."; RL EMBO J. 31:754-766(2012). RN [22] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=22253445; DOI=10.1074/jbc.m111.312561; RA Yang N., Ma P., Lang J., Zhang Y., Deng J., Ju X., Zhang G., Jiang C.; RT "Phosphatidylinositol 4-kinase IIIbeta is required for severe acute RT respiratory syndrome coronavirus spike-mediated cell entry."; RL J. Biol. Chem. 287:8457-8467(2012). RN [23] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH AICHI VIRUS PROTEIN 3A RP (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX AICHI VIRUS PROTEIN RP 3A/ACBD3/PI4KB (MICROBIAL INFECTION), AND INTERACTION WITH ACBD3. RX PubMed=22258260; DOI=10.1128/jvi.06778-11; RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., Derisi J.L.; RT "The 3A protein from multiple picornaviruses utilizes the golgi adaptor RT protein ACBD3 to recruit PI4KIIIbeta."; RL J. Virol. 86:3605-3616(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-266; SER-277; RP SER-428; SER-511 AND THR-517, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [25] RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION (MICROBIAL INFECTION). RX PubMed=24672044; DOI=10.1128/jvi.00208-14; RA Ishikawa-Sasaki K., Sasaki J., Taniguchi K.; RT "A complex comprising phosphatidylinositol 4-kinase IIIbeta, ACBD3, and RT Aichi virus proteins enhances phosphatidylinositol 4-phosphate synthesis RT and is critical for formation of the viral replication complex."; RL J. Virol. 88:6586-6598(2014). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [27] RP INTERACTION WITH GGA2, AND SUBCELLULAR LOCATION. RX PubMed=28289207; DOI=10.1073/pnas.1615163114; RA Daboussi L., Costaguta G., Ghukasyan R., Payne G.S.; RT "Conserved role for Gga proteins in phosphatidylinositol 4-kinase RT localization to the trans-Golgi network."; RL Proc. Natl. Acad. Sci. U.S.A. 114:3433-3438(2017). RN [28] RP INTERACTION WITH ACBD3, MUTAGENESIS OF ILE-43 AND ASP-44, FUNCTION RP (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX PROTEIN 3A/ACBD3/PI4KB RP (MICROBIAL INFECTION), AND ACTIVITY REGULATION (MICROBIAL INFECTION). RX PubMed=27989622; DOI=10.1016/j.str.2016.11.016; RA McPhail J.A., Ottosen E.H., Jenkins M.L., Burke J.E.; RT "The molecular basis of Aichi virus 3A protein activation of RT phosphatidylinositol 4 kinase IIIbeta, PI4KB, through ACBD3."; RL Structure 25:121-131(2017). RN [29] RP INTERACTION WITH ATG9A. RX PubMed=30917996; DOI=10.1083/jcb.201901115; RA Judith D., Jefferies H.B.J., Boeing S., Frith D., Snijders A.P., RA Tooze S.A.; RT "ATG9A shapes the forming autophagosome through Arfaptin 2 and RT phosphatidylinositol 4-kinase IIIbeta."; RL J. Cell Biol. 218:1634-1652(2019). RN [30] RP INVOLVEMENT IN DFNA87, VARIANTS DFNA87 ARG-121; GLY-449; LYS-682 AND RP ARG-754, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP CHARACTERIZATION OF VARIANTS DFNA87 ARG-121; GLY-449; LYS-682 AND ARG-754. RX PubMed=33358777; DOI=10.1016/j.jgg.2020.07.008; RA Su X., Feng Y., Rahman S.A., Wu S., Li G., Rueschendorf F., Zhao L., RA Cui H., Liang J., Fang L., Hu H., Froehler S., Yu Y., Patone G., Hummel O., RA Chen Q., Raile K., Luft F.C., Baehring S., Hussain K., Chen W., Zhang J., RA Gong M.; RT "Phosphatidylinositol 4-kinase beta mutations cause nonsyndromic RT sensorineural deafness and inner ear malformation."; RL J. Genet. Genomics 47:618-626(2020). RN [31] RP STRUCTURE BY NMR OF 1-68 IN COMPLEX WITH ACBD3, INTERACTION WITH ACBD3, AND RP MUTAGENESIS OF VAL-42; ILE-43; VAL-47; VAL-55 AND LEU-56. RX PubMed=27009356; DOI=10.1038/srep23641; RA Klima M., Toth D.J., Hexnerova R., Baumlova A., Chalupska D., Tykvart J., RA Rezabkova L., Sengupta N., Man P., Dubankova A., Humpolickova J., RA Nencka R., Veverka V., Balla T., Boura E.; RT "Structural insights and in vitro reconstitution of membrane targeting and RT activation of human PI4KB by the ACBD3 protein."; RL Sci. Rep. 6:23641-23641(2016). CC -!- FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first CC committed step in the production of the second messenger CC inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi CC disintegration/reorganization during mitosis, possibly via its CC phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By CC similarity) (PubMed:10559940, PubMed:11277933, PubMed:12749687, CC PubMed:9405935). May play an important role in the inner ear CC development. {ECO:0000250|UniProtKB:O08561, CC ECO:0000269|PubMed:10559940, ECO:0000269|PubMed:11277933, CC ECO:0000269|PubMed:12749687, ECO:0000269|PubMed:33358777, CC ECO:0000269|PubMed:9405935}. CC -!- FUNCTION: (Microbial infection) Plays an essential role in Aichi virus CC RNA replication (PubMed:22124328, PubMed:27989622, PubMed:22258260). CC Recruited by ACBD3 at the viral replication sites (PubMed:22124328, CC PubMed:27989622). {ECO:0000269|PubMed:22124328, CC ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:27989622}. CC -!- FUNCTION: (Microbial infection) Required for cellular spike-mediated CC entry of human coronavirus SARS-CoV. {ECO:0000269|PubMed:22253445}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; CC EC=2.7.1.67; Evidence={ECO:0000269|PubMed:11277933, CC ECO:0000269|PubMed:9405935}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; CC Evidence={ECO:0000305|PubMed:11277933}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11277933}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11277933}; CC -!- ACTIVITY REGULATION: Inhibited by wortmannin and adenosine CC (PubMed:11277933). Increased kinase activity upon interaction with CC NCS1/FREQ (By similarity). {ECO:0000250|UniProtKB:O02810, CC ECO:0000269|PubMed:11277933}. CC -!- ACTIVITY REGULATION: (Microbial infection) Activated by Aichi virus CC protein 3A, this activation is sensitized by ACBD3. CC {ECO:0000269|PubMed:24672044, ECO:0000269|PubMed:27989622}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1 mM for PtdIns {ECO:0000269|PubMed:11277933}; CC KM=1 mM for ATP {ECO:0000269|PubMed:11277933}; CC -!- SUBUNIT: Interacts with ARF1 and ARF3 in the Golgi complex, but not CC with ARF4, ARF5 or ARF6 (PubMed:17555535). Interacts with NCS1/FREQ in CC a calcium-independent manner. Interacts with CALN1/CABP8 and CC CALN2/CABP7; in a calcium-dependent manner; this interaction competes CC with NCS1/FREQ binding (By similarity). Interacts with ACBD3 CC (PubMed:23572552, PubMed:27009356, PubMed:27989622, PubMed:22124328, CC PubMed:22258260). Interacts with ARMH3, YWHAB, YWHAE, YWHAG, YWHAH, CC YWHAQ, YWHAZ and SFN (PubMed:23572552). Interacts with GGA2 (via VHS CC domain); the interaction is important for PI4KB location at the Golgi CC apparatus membrane (PubMed:28289207). Interacts with ATG9A CC (PubMed:30917996). {ECO:0000250|UniProtKB:O08561, CC ECO:0000269|PubMed:17555535, ECO:0000269|PubMed:22124328, CC ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:23572552, CC ECO:0000269|PubMed:27009356, ECO:0000269|PubMed:27989622, CC ECO:0000269|PubMed:28289207, ECO:0000269|PubMed:30917996}. CC -!- SUBUNIT: (Microbial infection) Interacts with Aichi virus protein 3A. CC Part of a complex Aichi virus protein 3A/ACBD3/PI4KB that allows the CC synthesis of PI4P at the viral RNA replication sites. CC {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:22258260, CC ECO:0000269|PubMed:27989622}. CC -!- INTERACTION: CC Q9UBF8; Q9H3P7: ACBD3; NbExp=4; IntAct=EBI-1053214, EBI-1791792; CC Q9UBF8; P27348: YWHAQ; NbExp=3; IntAct=EBI-1053214, EBI-359854; CC Q9UBF8; P03495: NS; Xeno; NbExp=2; IntAct=EBI-1053214, EBI-2548993; CC Q9UBF8; PRO_0000424692 [P03300]; Xeno; NbExp=9; IntAct=EBI-1053214, EBI-21242141; CC Q9UBF8-2; P62491: RAB11A; NbExp=5; IntAct=EBI-16107849, EBI-745098; CC -!- SUBCELLULAR LOCATION: Endomembrane system. Mitochondrion outer CC membrane; Peripheral membrane protein. Rough endoplasmic reticulum CC membrane; Peripheral membrane protein. Golgi apparatus CC {ECO:0000269|PubMed:22124328}. Golgi apparatus membrane CC {ECO:0000269|PubMed:24672044, ECO:0000269|PubMed:27009356, CC ECO:0000269|PubMed:28289207}. Cytoplasm, perinuclear region. Note=Found CC in the outer membrane of mitochondria and membranes of the rough CC endoplasmic reticulum. Recruited to the Golgi complex by the small CC GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5- CC bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi CC apparatus membrane by ACBD3 (PubMed:24672044, PubMed:27009356, CC PubMed:28289207). GGA2 is also involved in the recruitment CC (PubMed:28289207). {ECO:0000269|PubMed:24672044, CC ECO:0000269|PubMed:27009356, ECO:0000269|PubMed:28289207}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1 {ECO:0000269|PubMed:9405935}; Synonyms=NPIK-B CC {ECO:0000269|PubMed:9405935}; CC IsoId=Q9UBF8-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:9405935}; Synonyms=NPIK-C CC {ECO:0000269|PubMed:9405935}; CC IsoId=Q9UBF8-2; Sequence=VSP_050627; CC Name=3; CC IsoId=Q9UBF8-3; Sequence=VSP_037133; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart, CC skeletal muscle, pancreas, testis and ovary. Weakly expressed in liver CC (PubMed:9020160, PubMed:9405935, PubMed:9405938). Expressed in the CC innear ear in the epithelium of the spinal organ of corti. CC {ECO:0000269|PubMed:33358777, ECO:0000269|PubMed:9020160, CC ECO:0000269|PubMed:9405935, ECO:0000269|PubMed:9405938}. CC -!- DEVELOPMENTAL STAGE: Expressed in 11-week old fetal inner ear. CC {ECO:0000269|PubMed:33358777}. CC -!- DISEASE: Deafness, autosomal dominant, 87 (DFNA87) [MIM:620281]: A form CC of non-syndromic, sensorineural hearing loss. Sensorineural hearing CC loss results from damage to the neural receptors of the inner ear, the CC nerve pathways to the brain, or the area of the brain that receives CC sound information. DFNA87 is characterized by prelingual, profound CC sensorineural hearing loss with inner ear anomalies, including cochlear CC maldevelopment, absence of the osseous spiral lamina, and/or an CC enlarged vestibular aqueduct. {ECO:0000269|PubMed:33358777}. Note=The CC disease may be caused by variants affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA21661.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW53450.1; Type=Erroneous gene model prediction; 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; AJ011121; CAA09495.1; -; mRNA. DR EMBL; AJ011122; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AJ011123; CAA09496.1; -; mRNA. DR EMBL; AB005910; BAA21661.1; ALT_INIT; mRNA. DR EMBL; U81802; AAC51156.1; -; mRNA. DR EMBL; AK294606; BAG57793.1; -; mRNA. DR EMBL; AL391069; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53449.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53450.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC000029; AAH00029.1; -; mRNA. DR EMBL; BC040300; AAH40300.1; -; mRNA. DR CCDS; CCDS55637.1; -. [Q9UBF8-3] DR CCDS; CCDS55638.1; -. [Q9UBF8-2] DR CCDS; CCDS81376.1; -. [Q9UBF8-1] DR PIR; JC5706; JC5706. DR RefSeq; NP_001185702.1; NM_001198773.2. [Q9UBF8-2] DR RefSeq; NP_001185703.1; NM_001198774.1. [Q9UBF8-2] DR RefSeq; NP_001185704.1; NM_001198775.2. [Q9UBF8-3] DR RefSeq; NP_001317650.1; NM_001330721.1. [Q9UBF8-1] DR RefSeq; NP_002642.1; NM_002651.3. DR RefSeq; XP_016856979.1; XM_017001490.1. DR RefSeq; XP_016856980.1; XM_017001491.1. DR RefSeq; XP_016856981.1; XM_017001492.1. DR PDB; 2N73; NMR; -; B=1-68. DR PDB; 4D0L; X-ray; 2.94 A; A/C/E=121-799. DR PDB; 4D0M; X-ray; 6.00 A; A/C/G/I/M/O/Q/S/W/Y/c/g=121-799. DR PDB; 4WAE; X-ray; 3.32 A; A=128-799. DR PDB; 4WAG; X-ray; 3.41 A; A=128-799. DR PDB; 5C46; X-ray; 2.65 A; E=121-799. DR PDB; 5C4G; X-ray; 3.20 A; E=121-799. DR PDB; 5EUQ; X-ray; 3.20 A; E=121-248, E=523-799. DR PDB; 5FBL; X-ray; 3.37 A; A=128-799. DR PDB; 5FBQ; X-ray; 3.79 A; A=128-799. DR PDB; 5FBR; X-ray; 3.28 A; A=128-799. DR PDB; 5FBV; X-ray; 3.29 A; A=128-799. DR PDB; 5FBW; X-ray; 3.49 A; A=128-799. DR PDB; 5LX2; X-ray; 2.58 A; B=292-297. DR PDB; 5NAS; X-ray; 2.08 A; C/D=289-297. DR PDB; 6GL3; X-ray; 2.77 A; A/B=317-428, A/B=532-798. DR PDBsum; 2N73; -. DR PDBsum; 4D0L; -. DR PDBsum; 4D0M; -. DR PDBsum; 4WAE; -. DR PDBsum; 4WAG; -. DR PDBsum; 5C46; -. DR PDBsum; 5C4G; -. DR PDBsum; 5EUQ; -. DR PDBsum; 5FBL; -. DR PDBsum; 5FBQ; -. DR PDBsum; 5FBR; -. DR PDBsum; 5FBV; -. DR PDBsum; 5FBW; -. DR PDBsum; 5LX2; -. DR PDBsum; 5NAS; -. DR PDBsum; 6GL3; -. DR AlphaFoldDB; Q9UBF8; -. DR SMR; Q9UBF8; -. DR BioGRID; 111316; 56. DR DIP; DIP-42267N; -. DR IntAct; Q9UBF8; 27. DR MINT; Q9UBF8; -. DR STRING; 9606.ENSP00000357869; -. DR BindingDB; Q9UBF8; -. DR ChEMBL; CHEMBL3268; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q9UBF8; -. DR GuidetoPHARMACOLOGY; 2149; -. DR SwissLipids; SLP:000001947; -. [Q9UBF8-2] DR GlyGen; Q9UBF8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UBF8; -. DR PhosphoSitePlus; Q9UBF8; -. DR BioMuta; PI4KB; -. DR DMDM; 38372507; -. DR CPTAC; CPTAC-2965; -. DR CPTAC; CPTAC-2966; -. DR EPD; Q9UBF8; -. DR jPOST; Q9UBF8; -. DR MassIVE; Q9UBF8; -. DR MaxQB; Q9UBF8; -. DR PaxDb; 9606-ENSP00000357869; -. DR PeptideAtlas; Q9UBF8; -. DR ProteomicsDB; 83959; -. [Q9UBF8-1] DR ProteomicsDB; 83960; -. [Q9UBF8-2] DR ProteomicsDB; 83961; -. [Q9UBF8-3] DR Pumba; Q9UBF8; -. DR Antibodypedia; 1666; 159 antibodies from 30 providers. DR DNASU; 5298; -. DR Ensembl; ENST00000368872.5; ENSP00000357866.1; ENSG00000143393.17. [Q9UBF8-2] DR Ensembl; ENST00000368873.6; ENSP00000357867.1; ENSG00000143393.17. [Q9UBF8-1] DR Ensembl; ENST00000368874.8; ENSP00000357868.4; ENSG00000143393.17. [Q9UBF8-2] DR Ensembl; ENST00000529142.5; ENSP00000433149.1; ENSG00000143393.17. [Q9UBF8-3] DR GeneID; 5298; -. DR KEGG; hsa:5298; -. DR MANE-Select; ENST00000368873.6; ENSP00000357867.1; NM_001369623.2; NP_001356552.1. DR UCSC; uc001ext.4; human. [Q9UBF8-1] DR AGR; HGNC:8984; -. DR CTD; 5298; -. DR DisGeNET; 5298; -. DR GeneCards; PI4KB; -. DR HGNC; HGNC:8984; PI4KB. DR HPA; ENSG00000143393; Low tissue specificity. DR MalaCards; PI4KB; -. DR MIM; 602758; gene. DR MIM; 620281; phenotype. DR neXtProt; NX_Q9UBF8; -. DR OpenTargets; ENSG00000143393; -. DR PharmGKB; PA162399420; -. DR VEuPathDB; HostDB:ENSG00000143393; -. DR eggNOG; KOG0903; Eukaryota. DR GeneTree; ENSGT00550000074892; -. DR InParanoid; Q9UBF8; -. DR OMA; RPYKILC; -. DR OrthoDB; 147843at2759; -. DR PhylomeDB; Q9UBF8; -. DR TreeFam; TF102042; -. DR BioCyc; MetaCyc:HS07046-MONOMER; -. DR BRENDA; 2.7.1.67; 2681. DR PathwayCommons; Q9UBF8; -. DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane. DR SignaLink; Q9UBF8; -. DR SIGNOR; Q9UBF8; -. DR BioGRID-ORCS; 5298; 200 hits in 1169 CRISPR screens. DR ChiTaRS; PI4KB; human. DR GeneWiki; PI4KB; -. DR GenomeRNAi; 5298; -. DR Pharos; Q9UBF8; Tchem. DR PRO; PR:Q9UBF8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UBF8; Protein. DR Bgee; ENSG00000143393; Expressed in right lobe of thyroid gland and 208 other cell types or tissues. DR ExpressionAtlas; Q9UBF8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; TAS:ProtInc. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB. DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0048839; P:inner ear development; IMP:UniProtKB. DR GO; GO:0007040; P:lysosome organization; IDA:MGI. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd22246; PI4KB_NTD; 1. DR CDD; cd05168; PI4Kc_III_beta; 1. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000403; PI3/4_kinase_cat_dom. DR InterPro; IPR036940; PI3/4_kinase_cat_sf. DR InterPro; IPR018936; PI3/4_kinase_CS. DR InterPro; IPR001263; PI3K_accessory_dom. DR InterPro; IPR049160; PI4KB-PIK1_PIK. DR InterPro; IPR015433; PI_Kinase. DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1. DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF21245; PI4KB-PIK1_PIK; 1. DR SMART; SM00146; PI3Kc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00915; PI3_4_KINASE_1; 1. DR PROSITE; PS00916; PI3_4_KINASE_2; 1. DR PROSITE; PS50290; PI3_4_KINASE_3; 1. DR PROSITE; PS51545; PIK_HELICAL; 1. DR Genevisible; Q9UBF8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Deafness; Direct protein sequencing; Disease variant; KW Endoplasmic reticulum; Golgi apparatus; Host-virus interaction; Kinase; KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Non-syndromic deafness; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:23572552" FT CHAIN 2..816 FT /note="Phosphatidylinositol 4-kinase beta" FT /id="PRO_0000088829" FT DOMAIN 29..242 FT /note="PIK helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878" FT DOMAIN 535..801 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 41..67 FT /note="Interaction with ACBD3" FT /evidence="ECO:0000269|PubMed:27009356, FT ECO:0000269|PubMed:27989622, ECO:0000305|PubMed:23572552" FT REGION 101..120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 248..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 541..547 FT /note="G-loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 668..676 FT /note="Catalytic loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 687..711 FT /note="Activation loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT COMPBIAS 277..294 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000269|PubMed:23572552" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11277933, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 263 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:11277933" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11277933, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 275 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BKC8" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11277933, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 284 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BKC8" FT MOD_RES 294 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11277933, FT ECO:0000269|PubMed:23572552" FT MOD_RES 428 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 438 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:11277933" FT MOD_RES 511 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11277933, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 517 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 519 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:11277933" FT VAR_SEQ 1..332 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037133" FT VAR_SEQ 304..318 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9020160, ECO:0000303|PubMed:9405935" FT /id="VSP_050627" FT VARIANT 121 FT /note="Q -> R (in DFNA87; unable to rescue defective inner FT ear phenotype and sound stimuli response in zebrafish FT morphants)" FT /evidence="ECO:0000269|PubMed:33358777" FT /id="VAR_088345" FT VARIANT 449 FT /note="V -> G (in DFNA87; uncertain significance; unable to FT rescue defective inner ear phenotype and sound stimuli FT response in zebrafish morphants)" FT /evidence="ECO:0000269|PubMed:33358777" FT /id="VAR_088346" FT VARIANT 682 FT /note="E -> K (in DFNA87; uncertain significance; unable to FT rescue defective inner ear phenotype and sound stimuli FT response in zebrafish morphants)" FT /evidence="ECO:0000269|PubMed:33358777" FT /id="VAR_088347" FT VARIANT 754 FT /note="M -> R (in DFNA87; uncertain significance; unable to FT rescue defective inner ear phenotype and sound stimuli FT response in zebrafish morphants)" FT /evidence="ECO:0000269|PubMed:33358777" FT /id="VAR_088348" FT MUTAGEN 40..42 FT /note="LSV->AAA: Small decrease in ARMH3-binding. No effect FT on ACBD3-, nor RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 42 FT /note="V->A: No loss of interaction with ACBD3." FT /evidence="ECO:0000269|PubMed:27009356" FT MUTAGEN 43..45 FT /note="IDP->AAA: Drastically decreased ACBD3-binding. No FT effect on ARMH3-, nor RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 43 FT /note="I->A: Loss of interaction with ACBD3." FT /evidence="ECO:0000269|PubMed:27009356, FT ECO:0000269|PubMed:27989622" FT MUTAGEN 44 FT /note="D->A: Loss of interaction with ACBD3." FT /evidence="ECO:0000269|PubMed:27989622" FT MUTAGEN 46..47 FT /note="EV->AA: No effect on ACBD3-, ARMH3-, nor FT RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 47 FT /note="V->A: No loss of interaction with ACBD3." FT /evidence="ECO:0000269|PubMed:27009356" FT MUTAGEN 49..50 FT /note="QK->AA: No effect on ACBD3-, ARMH3-, nor FT RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 52 FT /note="C->A: No effect on ACBD3-, ARMH3-, nor FT RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 53..54 FT /note="QE->AA: Drastically decreased ARMH3- and FT RAB11B-binding. 6-fold increase in ACBD3-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 55..56 FT /note="VL->AA: Drastically decreased ACBD3-binding. No FT effect on ARMH3-, nor RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT MUTAGEN 55 FT /note="V->A: Loss of interaction with ACBD3." FT /evidence="ECO:0000269|PubMed:27009356" FT MUTAGEN 56 FT /note="L->A: Loss of interaction with ACBD3." FT /evidence="ECO:0000269|PubMed:27009356" FT MUTAGEN 57..59 FT /note="EKV->AAA: No effect on ACBD3-, ARMH3-, nor FT RAB11B-binding." FT /evidence="ECO:0000269|PubMed:23572552" FT CONFLICT 216 FT /note="L -> V (in Ref. 3; AAC51156)" FT /evidence="ECO:0000305" FT CONFLICT 339 FT /note="L -> V (in Ref. 3; AAC51156)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="A -> V (in Ref. 3; AAC51156)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="P -> S (in Ref. 3; AAC51156)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="F -> S (in Ref. 4; BAG57793)" FT /evidence="ECO:0000305" FT CONFLICT 754 FT /note="M -> L (in Ref. 4; BAG57793)" FT /evidence="ECO:0000305" FT CONFLICT 796 FT /note="S -> G (in Ref. 4; BAG57793)" FT /evidence="ECO:0000305" FT HELIX 45..63 FT /evidence="ECO:0007829|PDB:2N73" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 141..150 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 154..163 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 169..173 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 188..204 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 206..218 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 234..242 FT /evidence="ECO:0007829|PDB:5C46" FT TURN 319..322 FT /evidence="ECO:0007829|PDB:4WAE" FT HELIX 323..338 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:6GL3" FT HELIX 345..356 FT /evidence="ECO:0007829|PDB:5C46" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 376..380 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:6GL3" FT STRAND 397..405 FT /evidence="ECO:0007829|PDB:5C46" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 537..546 FT /evidence="ECO:0007829|PDB:5C46" FT TURN 549..552 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 556..564 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 570..588 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 600..602 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 608..610 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 614..618 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 619..625 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 630..637 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 644..667 FT /evidence="ECO:0007829|PDB:5C46" FT TURN 674..676 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 677..680 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 712..717 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 721..723 FT /evidence="ECO:0007829|PDB:6GL3" FT HELIX 724..741 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 744..755 FT /evidence="ECO:0007829|PDB:5C46" FT HELIX 761..763 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 765..767 FT /evidence="ECO:0007829|PDB:5FBR" FT HELIX 768..774 FT /evidence="ECO:0007829|PDB:5C46" FT STRAND 778..780 FT /evidence="ECO:0007829|PDB:6GL3" FT HELIX 782..796 FT /evidence="ECO:0007829|PDB:5C46" FT MOD_RES Q9UBF8-2:294 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 816 AA; 91379 MW; CAD8791729BB4308 CRC64; MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK LLHGGVAVSS RGTPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGAAVAS GTAKGARRRR QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM //