PI4KB_HUMAN
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 03-AUG-2022, entry version 190.
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
RC Testis {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 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 inositol-
CC 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). {ECO:0000250|UniProtKB:O08561,
CC ECO:0000269|PubMed:10559940, ECO:0000269|PubMed:11277933,
CC ECO:0000269|PubMed:12749687, 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=1.0 mM for PtdIns {ECO:0000269|PubMed:11277933};
CC KM=1.0 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; 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 {ECO:0000269|PubMed:9020160, ECO:0000269|PubMed:9405935,
CC ECO:0000269|PubMed:9405938}.
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};
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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; 45.
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 EPD; Q9UBF8; -.
DR jPOST; Q9UBF8; -.
DR MassIVE; Q9UBF8; -.
DR MaxQB; Q9UBF8; -.
DR PaxDb; Q9UBF8; -.
DR PeptideAtlas; Q9UBF8; -.
DR PRIDE; Q9UBF8; -.
DR ProteomicsDB; 83959; -. [Q9UBF8-1]
DR ProteomicsDB; 83960; -. [Q9UBF8-2]
DR ProteomicsDB; 83961; -. [Q9UBF8-3]
DR Antibodypedia; 1666; 141 antibodies from 29 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 CTD; 5298; -.
DR DisGeNET; 5298; -.
DR GeneCards; PI4KB; -.
DR HGNC; HGNC:8984; PI4KB.
DR HPA; ENSG00000143393; Low tissue specificity.
DR MIM; 602758; gene.
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; GNKMFSF; -.
DR OrthoDB; 1147978at2759; -.
DR PhylomeDB; Q9UBF8; -.
DR TreeFam; TF102042; -.
DR BioCyc; MetaCyc:HS07046-MON; -.
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; 179 hits in 1083 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 206 other tissues.
DR ExpressionAtlas; Q9UBF8; baseline and differential.
DR Genevisible; Q9UBF8; HS.
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:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
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 Gene3D; 1.10.1070.11; -; 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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW Host-virus interaction; Kinase; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; 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 MUTAGEN 40..42
FT /note="LSV->AAA: Small decrease in C10ORF76-binding. No
FT effect 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 C10ORF76-, 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-, C10ORF76-, nor RAB11B-
FT 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-, C10ORF76-, nor RAB11B-
FT binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 52
FT /note="C->A: No effect on ACBD3-, C10ORF76-, nor RAB11B-
FT binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 53..54
FT /note="QE->AA: Drastically decreased C10ORF76- and RAB11B-
FT 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 C10ORF76-, 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-, C10ORF76-, 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
