NCBP1_HUMAN
ID NCBP1_HUMAN Reviewed; 790 AA.
AC Q09161; B2R718; Q59G76; Q5T1V0; Q5T7X2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Nuclear cap-binding protein subunit 1;
DE AltName: Full=80 kDa nuclear cap-binding protein;
DE Short=CBP80;
DE Short=NCBP 80 kDa subunit;
GN Name=NCBP1; Synonyms=CBP80, NCBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 119-128; 513-522 AND
RP 687-693, AND FUNCTION IN MRNA SPLICING.
RX PubMed=8069914; DOI=10.1016/0092-8674(94)90530-4;
RA Izaurralde E., Lewis J., McGuigan C., Jankowska E., Darzynkiewicz E.,
RA Mattaj I.W.;
RT "A nuclear cap binding protein complex involved in pre-mRNA splicing.";
RL Cell 78:657-668(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7937105; DOI=10.1093/nar/22.19.3861;
RA Kataoka N., Ohno M., Kangawa K., Tokoro Y., Shimura Y.;
RT "Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap
RT binding protein.";
RL Nucleic Acids Res. 22:3861-3865(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP FUNCTION.
RX PubMed=7651522; DOI=10.1038/376709a0;
RA Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C.,
RA Mattaj A.W.;
RT "A cap-binding protein complex mediating U snRNA export.";
RL Nature 376:709-712(1995).
RN [8]
RP INTERACTION WITH HNRNPF AND HNRNPH1.
RX PubMed=9111328; DOI=10.1128/mcb.17.5.2587;
RA Gamberi C., Izaurralde E., Beisel C., Mattaj I.W.;
RT "Interaction between the human nuclear cap-binding protein complex and
RT hnRNP F.";
RL Mol. Cell. Biol. 17:2587-2597(1997).
RN [9]
RP PHOSPHORYLATION AT SER-7; THR-21 AND SER-22, AND MUTAGENESIS OF SER-7;
RP 17-LYS-ARG-18 AND 21-THR-SER-22.
RX PubMed=10973943; DOI=10.1074/jbc.c000482200;
RA Wilson K.F., Wu W.J., Cerione R.A.;
RT "Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase
RT target, the nuclear cap-binding complex.";
RL J. Biol. Chem. 275:37307-37310(2000).
RN [10]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
RX PubMed=11551508; DOI=10.1016/s0092-8674(01)00475-5;
RA Ishigaki Y., Li X., Serin G., Maquat L.E.;
RT "Evidence for a pioneer round of mRNA translation: mRNAs subject to
RT nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20.";
RL Cell 106:607-617(2001).
RN [11]
RP INTERACTION WITH EIF4G1.
RX PubMed=11340157; DOI=10.1128/mcb.21.11.3632-3641.2001;
RA McKendrick L., Thompson E., Ferreira J., Morley S.J., Lewis J.D.;
RT "Interaction of eukaryotic translation initiation factor 4G with the
RT nuclear cap-binding complex provides a link between nuclear and cytoplasmic
RT functions of the m(7) guanosine cap.";
RL Mol. Cell. Biol. 21:3632-3641(2001).
RN [12]
RP FUNCTION.
RX PubMed=12093754; DOI=10.1093/emboj/cdf345;
RA Lejeune F., Ishigaki Y., Li X., Maquat L.E.;
RT "The exon junction complex is detected on CBP80-bound but not eIF4E-bound
RT mRNA in mammalian cells: dynamics of mRNP remodeling.";
RL EMBO J. 21:3536-3545(2002).
RN [13]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH EIF4G1.
RX PubMed=15059963; DOI=10.1101/gad.1170204;
RA Chiu S.-Y., Lejeune F., Ranganathan A.C., Maquat L.E.;
RT "The pioneer translation initiation complex is functionally distinct from
RT but structurally overlaps with the steady-state translation initiation
RT complex.";
RL Genes Dev. 18:745-754(2004).
RN [14]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH EIF4G1
RP AND EIF4G2.
RX PubMed=15361857; DOI=10.1038/nsmb824;
RA Lejeune F., Ranganathan A.C., Maquat L.E.;
RT "eIF4G is required for the pioneer round of translation in mammalian
RT cells.";
RL Nat. Struct. Mol. Biol. 11:992-1000(2004).
RN [15]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND INTERACTION WITH UPF1.
RX PubMed=16186820; DOI=10.1038/nsmb995;
RA Hosoda N., Kim Y.K., Lejeune F., Maquat L.E.;
RT "CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA
RT decay in mammalian cells.";
RL Nat. Struct. Mol. Biol. 12:893-901(2005).
RN [16]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL Cell 127:1389-1400(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP FUNCTION IN MRNA DEADENYLATION, AND INTERACTION WITH PARN.
RX PubMed=16317009; DOI=10.1074/jbc.m508590200;
RA Balatsos N.A.A., Nilsson P., Mazza C., Cusack S., Virtanen A.;
RT "Inhibition of mRNA deadenylation by the nuclear cap binding complex
RT (CBC).";
RL J. Biol. Chem. 281:4517-4522(2006).
RN [19]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [20]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=17873884; DOI=10.1038/nsmb1297;
RA Matsuda D., Hosoda N., Kim Y.K., Maquat L.E.;
RT "Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-
RT bound mRNA.";
RL Nat. Struct. Mol. Biol. 14:974-979(2007).
RN [21]
RP INTERACTION WITH POLDIP3.
RX PubMed=18423201; DOI=10.1016/j.cell.2008.02.031;
RA Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.;
RT "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation
RT efficiency of spliced mRNAs.";
RL Cell 133:303-313(2008).
RN [22]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=18369367; DOI=10.1038/embor.2008.36;
RA Woeller C.F., Gaspari M., Isken O., Maquat L.E.;
RT "NMD resulting from encephalomyocarditis virus IRES-directed translation
RT initiation seems to be restricted to CBP80/20-bound mRNA.";
RL EMBO Rep. 9:446-451(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, 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 [25]
RP FUNCTION IN MIRNAS BIOGENESIS.
RX PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA Dreyfuss G., Thompson C.B.;
RT "Ars2 links the nuclear cap-binding complex to RNA interference and cell
RT proliferation.";
RL Cell 138:328-339(2009).
RN [26]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH KIAA0427,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19648179; DOI=10.1101/gad.1823409;
RA Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K.,
RA Kim Y.K.;
RT "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding
RT protein CBP80/20-dependent translation.";
RL Genes Dev. 23:2033-2045(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, 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 [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
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 [30]
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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [33]
RP INTERACTION WITH DHX34.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [34]
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 [35]
RP FUNCTION, INTERACTION WITH NCBP3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
RN [36]
RP INTERACTION WITH METTL3.
RX PubMed=27117702; DOI=10.1016/j.molcel.2016.03.021;
RA Lin S., Choe J., Du P., Triboulet R., Gregory R.I.;
RT "The m(6)A methyltransferase METTL3 promotes translation in human cancer
RT cells.";
RL Mol. Cell 62:335-345(2016).
RN [37]
RP INTERACTION WITH ZFC3H1.
RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
RA Jensen T.H.;
RT "Identification of a nuclear exosome decay pathway for processed
RT transcripts.";
RL Mol. Cell 64:520-533(2016).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-684, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [39]
RP INTERACTION WITH MTREX.
RX PubMed=30842217; DOI=10.1101/gad.322602.118;
RA Wang J., Chen J., Wu G., Zhang H., Du X., Chen S., Zhang L., Wang K.,
RA Fan J., Gao S., Wu X., Zhang S., Kuai B., Zhao P., Chi B., Wang L., Li G.,
RA Wong C.C.L., Zhou Y., Li J., Yun C., Cheng H.;
RT "NRDE2 negatively regulates exosome functions by inhibiting MTR4
RT recruitment and exosome interaction.";
RL Genes Dev. 33:536-549(2019).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP2.
RX PubMed=11545740; DOI=10.1016/s1097-2765(01)00299-4;
RA Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S.;
RT "Crystal structure of the human nuclear cap binding complex.";
RL Mol. Cell 8:383-396(2001).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP2.
RX PubMed=12374755; DOI=10.1093/emboj/cdf538;
RA Mazza C., Segref A., Mattaj I.W., Cusack S.;
RT "Large-scale induced fit recognition of an m(7)GpppG cap analogue by the
RT human nuclear cap-binding complex.";
RL EMBO J. 21:5548-5557(2002).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP2.
RX PubMed=12434151; DOI=10.1038/nsb874;
RA Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C.,
RA Cerione R.A.;
RT "Structural basis of m7GpppG binding to the nuclear cap-binding protein
RT complex.";
RL Nat. Struct. Biol. 9:912-917(2002).
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in
CC various processes such as pre-mRNA splicing, translation regulation,
CC nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by
CC microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA
CC export from the nucleus via its interaction with ALYREF/THOC4/ALY,
CC leading to the recruitment of the mRNA export machinery to the 5'-end
CC of mRNA and to mRNA export in a 5' to 3' direction through the nuclear
CC pore. The CBC complex is also involved in mediating U snRNA and
CC intronless mRNAs export from the nucleus. The CBC complex is essential
CC for a pioneer round of mRNA translation, before steady state
CC translation when the CBC complex is replaced by cytoplasmic cap-binding
CC protein eIF4E. The pioneer round of mRNA translation mediated by the
CC CBC complex plays a central role in nonsense-mediated mRNA decay (NMD),
CC NMD only taking place in mRNAs bound to the CBC complex, but not on
CC eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at
CC least one exon-junction complex (EJC) via its interaction with UPF1,
CC promoting the interaction between UPF1 and UPF2. The CBC complex is
CC also involved in 'failsafe' NMD, which is independent of the EJC
CC complex, while it does not participate in Staufen-mediated mRNA decay
CC (SMD). During cell proliferation, the CBC complex is also involved in
CC microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is
CC required for miRNA-mediated RNA interference. The CBC complex also acts
CC as a negative regulator of PARN, thereby acting as an inhibitor of mRNA
CC deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly
CC capped RNAs (m7GpppG-capped RNA) but is required to stabilize the
CC movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a
CC high affinity cap-binding state with the cap structure. Associates with
CC NCBP3 to form an alternative cap-binding complex (CBC) which plays a
CC key role in mRNA export and is particularly important in cellular
CC stress situations such as virus infections. The conventional CBC with
CC NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is
CC involved in their export from the nucleus whereas the alternative CBC
CC with NCBP3 does not bind snRNA and associates only with mRNA thereby
CC playing a role only in mRNA export. NCBP1/CBP80 is required for cell
CC growth and viability (PubMed:26382858). {ECO:0000269|PubMed:11551508,
CC ECO:0000269|PubMed:12093754, ECO:0000269|PubMed:15059963,
CC ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:16186820,
CC ECO:0000269|PubMed:16317009, ECO:0000269|PubMed:17190602,
CC ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367,
CC ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:19648179,
CC ECO:0000269|PubMed:26382858, ECO:0000269|PubMed:7651522,
CC ECO:0000269|PubMed:8069914}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with
CC m7GpppG-capped RNA. Found in a U snRNA export complex containing
CC PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA.
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs. Interacts with PHAX/RNUXA, SRRT/ARS2, EIF4G2,
CC IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and
CC ALYREF/THOC4. May interact with EIF4G1; the interaction is however
CC controversial since it is reported by PubMed:11340157, PubMed:15059963
CC and PubMed:15361857, but is not observed by PubMed:19648179. The large
CC PER complex involved in the repression of transcriptional termination
CC is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1/CBP80 and POLR2A.
CC Component of an alternative nuclear cap-binding complex (CBC) composed
CC of NCBP1/CBP80 and NCBP3 (PubMed:26382858). Interacts with METTL3
CC (PubMed:27117702). Interacts with ZFC3H1 in a RNase-insensitive manner
CC (PubMed:27871484). Interacts with MTREX (PubMed:30842217). Interacts
CC with TASOR (By similarity). Interacts with DHX34; the interaction is
CC RNA-dependent (PubMed:25220460). {ECO:0000250|UniProtKB:Q3UYV9,
CC ECO:0000269|PubMed:11340157, ECO:0000269|PubMed:11545740,
CC ECO:0000269|PubMed:12374755, ECO:0000269|PubMed:12434151,
CC ECO:0000269|PubMed:15059963, ECO:0000269|PubMed:15361857,
CC ECO:0000269|PubMed:16186820, ECO:0000269|PubMed:16317009,
CC ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:18423201, ECO:0000269|PubMed:19648179,
CC ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:26382858,
CC ECO:0000269|PubMed:27871484, ECO:0000269|PubMed:30842217,
CC ECO:0000269|PubMed:9111328}.
CC -!- INTERACTION:
CC Q09161; P52298: NCBP2; NbExp=50; IntAct=EBI-464743, EBI-464729;
CC Q09161; P52298-1: NCBP2; NbExp=8; IntAct=EBI-464743, EBI-15798444;
CC Q09161; Q53F19: NCBP3; NbExp=11; IntAct=EBI-464743, EBI-6657994;
CC Q09161; P11940: PABPC1; NbExp=9; IntAct=EBI-464743, EBI-81531;
CC Q09161; O95453: PARN; NbExp=2; IntAct=EBI-464743, EBI-372832;
CC Q09161; Q9BY77: POLDIP3; NbExp=3; IntAct=EBI-464743, EBI-1776152;
CC Q09161; O43586: PSTPIP1; NbExp=3; IntAct=EBI-464743, EBI-1050964;
CC Q09161; Q5VTR2: RNF20; NbExp=3; IntAct=EBI-464743, EBI-2372238;
CC Q09161; O75150: RNF40; NbExp=4; IntAct=EBI-464743, EBI-744408;
CC Q09161; P62753: RPS6; NbExp=3; IntAct=EBI-464743, EBI-356625;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19648179}. Cytoplasm
CC {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92470.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X80030; CAA56334.1; -; mRNA.
DR EMBL; D32002; BAA06769.1; -; mRNA.
DR EMBL; AK312807; BAG35665.1; -; mRNA.
DR EMBL; AB209233; BAD92470.1; ALT_INIT; mRNA.
DR EMBL; AL162385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001450; AAH01450.1; -; mRNA.
DR CCDS; CCDS6728.1; -.
DR PIR; S50082; S50082.
DR RefSeq; NP_002477.1; NM_002486.4.
DR PDB; 1H2T; X-ray; 2.10 A; C=20-652, C=702-790.
DR PDB; 1H2U; X-ray; 2.40 A; A/B=20-652, A/B=702-790.
DR PDB; 1H2V; X-ray; 2.00 A; C=20-790.
DR PDB; 1H6K; X-ray; 2.00 A; A/B/C=20-790.
DR PDB; 1N52; X-ray; 2.11 A; A=1-790.
DR PDB; 1N54; X-ray; 2.72 A; A=1-790.
DR PDB; 3FEX; X-ray; 3.55 A; A=1-790.
DR PDB; 3FEY; X-ray; 2.20 A; A=1-790.
DR PDB; 5OO6; X-ray; 2.80 A; A/D/G/J/M/P/S/V=20-790.
DR PDB; 5OOB; X-ray; 2.79 A; A/C/F/I=20-790.
DR PDB; 6D0Y; X-ray; 2.68 A; C=24-790.
DR PDB; 7ABG; EM; 7.80 A; A5=1-790.
DR PDBsum; 1H2T; -.
DR PDBsum; 1H2U; -.
DR PDBsum; 1H2V; -.
DR PDBsum; 1H6K; -.
DR PDBsum; 1N52; -.
DR PDBsum; 1N54; -.
DR PDBsum; 3FEX; -.
DR PDBsum; 3FEY; -.
DR PDBsum; 5OO6; -.
DR PDBsum; 5OOB; -.
DR PDBsum; 6D0Y; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; Q09161; -.
DR SMR; Q09161; -.
DR BioGRID; 110766; 233.
DR ComplexPortal; CPX-1427; Nuclear cap-binding complex.
DR ComplexPortal; CPX-3624; Alternative nuclear cap-binding complex.
DR CORUM; Q09161; -.
DR DIP; DIP-33244N; -.
DR IntAct; Q09161; 304.
DR MINT; Q09161; -.
DR STRING; 9606.ENSP00000364289; -.
DR ChEMBL; CHEMBL4665589; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR GlyGen; Q09161; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q09161; -.
DR MetOSite; Q09161; -.
DR PhosphoSitePlus; Q09161; -.
DR SwissPalm; Q09161; -.
DR BioMuta; NCBP1; -.
DR DMDM; 1705654; -.
DR EPD; Q09161; -.
DR jPOST; Q09161; -.
DR MassIVE; Q09161; -.
DR MaxQB; Q09161; -.
DR PaxDb; Q09161; -.
DR PeptideAtlas; Q09161; -.
DR PRIDE; Q09161; -.
DR ProteomicsDB; 58717; -.
DR Antibodypedia; 28868; 241 antibodies from 33 providers.
DR DNASU; 4686; -.
DR Ensembl; ENST00000375147.8; ENSP00000364289.3; ENSG00000136937.13.
DR GeneID; 4686; -.
DR KEGG; hsa:4686; -.
DR MANE-Select; ENST00000375147.8; ENSP00000364289.3; NM_002486.5; NP_002477.1.
DR UCSC; uc004axq.4; human.
DR CTD; 4686; -.
DR DisGeNET; 4686; -.
DR GeneCards; NCBP1; -.
DR HGNC; HGNC:7658; NCBP1.
DR HPA; ENSG00000136937; Low tissue specificity.
DR MIM; 600469; gene.
DR neXtProt; NX_Q09161; -.
DR OpenTargets; ENSG00000136937; -.
DR PharmGKB; PA31461; -.
DR VEuPathDB; HostDB:ENSG00000136937; -.
DR eggNOG; KOG1104; Eukaryota.
DR GeneTree; ENSGT00390000001733; -.
DR HOGENOM; CLU_013207_0_0_1; -.
DR InParanoid; Q09161; -.
DR OMA; QPFKIPF; -.
DR OrthoDB; 270650at2759; -.
DR PhylomeDB; Q09161; -.
DR TreeFam; TF313400; -.
DR PathwayCommons; Q09161; -.
DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q09161; -.
DR SIGNOR; Q09161; -.
DR BioGRID-ORCS; 4686; 796 hits in 1088 CRISPR screens.
DR ChiTaRS; NCBP1; human.
DR EvolutionaryTrace; Q09161; -.
DR GenomeRNAi; 4686; -.
DR Pharos; Q09161; Tbio.
DR PRO; PR:Q09161; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q09161; protein.
DR Bgee; ENSG00000136937; Expressed in sural nerve and 164 other tissues.
DR ExpressionAtlas; Q09161; baseline and differential.
DR Genevisible; Q09161; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0005846; C:nuclear cap binding complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0034518; C:RNA cap binding complex; IMP:CAFA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0002191; P:cap-dependent translational initiation; IC:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IMP:ComplexPortal.
DR GO; GO:0008334; P:histone mRNA metabolic process; IMP:ComplexPortal.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IC:ComplexPortal.
DR GO; GO:0031124; P:mRNA 3'-end processing; IC:ComplexPortal.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; EXP:ComplexPortal.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:CAFA.
DR GO; GO:1901409; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain; IC:ComplexPortal.
DR GO; GO:1905216; P:positive regulation of RNA binding; IMP:CAFA.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IMP:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; IC:ComplexPortal.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0006408; P:snRNA export from nucleus; IMP:ComplexPortal.
DR GO; GO:0000245; P:spliceosomal complex assembly; IMP:CAFA.
DR DisProt; DP00392; -.
DR IDEAL; IID00167; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027159; CBP80.
DR InterPro; IPR015172; MIF4G-like_typ-1.
DR InterPro; IPR015174; MIF4G-like_typ-2.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR12412; PTHR12412; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF09088; MIF4G_like; 1.
DR Pfam; PF09090; MIF4G_like_2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; mRNA capping; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-mediated gene silencing;
KW Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..790
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000089364"
FT DOMAIN 28..240
FT /note="MIF4G"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..713
FT /evidence="ECO:0000255"
FT MOTIF 3..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:10973943"
FT MOD_RES 21
FT /note="Phosphothreonine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:10973943,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 22
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:10973943,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 698
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 7
FT /note="S->A: Reduced phosphorylation by RPS6KB1. Abolishes
FT phosphorylation by RPS6KB1; when associated with 21-A-A-
FT 22."
FT /evidence="ECO:0000269|PubMed:10973943"
FT MUTAGEN 17..18
FT /note="KR->AA: Abolishes nuclear localization and
FT phosphorylation by RPS6KB1."
FT /evidence="ECO:0000269|PubMed:10973943"
FT MUTAGEN 21..22
FT /note="TS->A: Reduced phosphorylation by RPS6KB1. Abolishes
FT phosphorylation by RPS6KB1; when associated with A-7."
FT /evidence="ECO:0000269|PubMed:10973943"
FT CONFLICT 80
FT /note="P -> S (in Ref. 3; BAG35665)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="E -> D (in Ref. 4; BAD92470)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="S -> G (in Ref. 3; BAG35665)"
FT /evidence="ECO:0000305"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 98..117
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 121..136
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1N52"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6D0Y"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 177..204
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1H2T"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1H2U"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1N54"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1N52"
FT HELIX 309..325
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 387..400
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 422..426
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 444..458
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 462..468
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:1H2T"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1H2T"
FT HELIX 498..509
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 541..554
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:1H6K"
FT HELIX 559..568
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 570..576
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 580..594
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 598..610
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 616..623
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 629..633
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 635..661
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 693..731
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 738..753
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 755..758
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 759..761
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 762..768
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 776..787
FT /evidence="ECO:0007829|PDB:1H2V"
SQ SEQUENCE 790 AA; 91839 MW; F10DE7B9D16FDA0B CRC64;
MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD
LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN
YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV
GKELYEKKDA EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK
KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF
QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMNTTCV DRFINWFSHH
LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN
PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN
PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE
EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI
LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA
VFQQFCALQA
