SF3B2_HUMAN
ID SF3B2_HUMAN Reviewed; 895 AA.
AC Q13435; A8K485; B4DT19; Q7L4T5; Q7Z627; Q969K1; Q96CM6; Q9BWD2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Splicing factor 3B subunit 2;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 145 kDa subunit;
DE Short=SF3b145;
DE AltName: Full=Spliceosome-associated protein 145;
DE Short=SAP 145;
GN Name=SF3B2; Synonyms=SAP145;
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 [LARGE SCALE MRNA].
RC TISSUE=Lymphoblast, and Peripheral blood;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Kidney, Lung, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-895, AND PROTEIN SEQUENCE OF 174-182 AND
RP 817-840.
RC TISSUE=Cervix carcinoma;
RX PubMed=8566756; DOI=10.1101/gad.10.2.233;
RA Gozani O., Feld R., Reed R.;
RT "Evidence that sequence-independent binding of highly conserved U2 snRNP
RT proteins upstream of the branch site is required for assembly of
RT spliceosomal complex A.";
RL Genes Dev. 10:233-243(1996).
RN [4]
RP CHARACTERIZATION OF THE SPLICEOSOME.
RX PubMed=10882114; DOI=10.1016/s1097-2765(00)80318-4;
RA Das R., Zhou Z., Reed R.;
RT "Functional association of U2 snRNP with the ATP-independent spliceosomal
RT complex E.";
RL Mol. Cell 5:779-787(2000).
RN [5]
RP IDENTIFICATION IN THE SF3B COMPLEX.
RX PubMed=12234937; DOI=10.1093/emboj/cdf480;
RA Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.;
RT "Characterization of novel SF3b and 17S U2 snRNP proteins, including a
RT human Prp5p homologue and an SF3b DEAD-box protein.";
RL EMBO J. 21:4978-4988(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [7]
RP IDENTIFICATION IN THE SF3B COMPLEX, AND ELECTRON MICROSCOPY OF THE SF3B
RP COMPLEX.
RX PubMed=12738865; DOI=10.1126/science.1084155;
RA Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H.;
RT "Molecular architecture of the multiprotein splicing factor SF3b.";
RL Science 300:980-984(2003).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435 AND SER-436, AND
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 [10]
RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=16923959; DOI=10.1128/mcb.01170-06;
RA Terada Y., Yasuda Y.;
RT "Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation
RT by interacting with the splicing factor SAP145.";
RL Mol. Cell. Biol. 26:8149-8158(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-307; SER-309;
RP THR-311 AND THR-780, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435 AND SER-436, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-309; SER-360;
RP SER-362 AND THR-780, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND IDENTIFICATION BY MASS
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-309; SER-431;
RP SER-435; SER-436 AND THR-780, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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-431; SER-435 AND SER-436, AND
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; THR-298; SER-307;
RP SER-309; THR-311; SER-317; SER-431; SER-435; SER-436; THR-780 AND SER-861,
RP AND 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311; SER-431; SER-435 AND
RP SER-436, AND 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 [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-222; ARG-245; ARG-247 AND
RP ARG-515, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-412, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-400, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-400, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-280; LYS-400; LYS-412;
RP LYS-492; LYS-543; LYS-770; LYS-790; LYS-843 AND LYS-857, AND IDENTIFICATION
RP BY MASS 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 [28]
RP STRUCTURE BY NMR OF 24-68.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SAP domain of human splicing factor 3B subunit
RT 2.";
RL Submitted (APR-2007) to the PDB data bank.
RN [29]
RP METHYLATION AT ARG-508 BY PRMT9, MUTAGENESIS OF ARG-471; ARG-495; ARG-502;
RP ARG-508; ARG-515; ARG-530 AND ARG-537, INTERACTION WITH SMN1, AND
RP IDENTIFICATION IN A COMPLEX WITH PRMT9; SF3B2 AND SF3B4.
RX PubMed=25737013; DOI=10.1038/ncomms7428;
RA Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C.,
RA Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.;
RT "PRMT9 is a type II methyltransferase that methylates the splicing factor
RT SAP145.";
RL Nat. Commun. 6:6428-6428(2015).
RN [30]
RP MUTAGENESIS OF PHE-506; LYS-507; ARG-508; LYS-509 AND TYR-510.
RX PubMed=25979344; DOI=10.1074/jbc.m115.659433;
RA Hadjikyriacou A., Yang Y., Espejo A., Bedford M.T., Clarke S.G.;
RT "Unique features of human protein arginine methyltransferase 9 (PRMT9) and
RT its substrate RNA splicing factor SF3B2.";
RL J. Biol. Chem. 290:16723-16743(2015).
RN [31]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [32]
RP FUNCTION, IDENTIFICATION IN THE SF3B COMPLEX, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27720643; DOI=10.1016/j.molcel.2016.08.036;
RA Cretu C., Schmitzova J., Ponce-Salvatierra A., Dybkov O.,
RA De Laurentiis E.I., Sharma K., Will C.L., Urlaub H., Luehrmann R., Pena V.;
RT "Molecular architecture of SF3b and structural consequences of its cancer-
RT related mutations.";
RL Mol. Cell 64:307-319(2016).
RN [33]
RP INTERACTION WITH RBM7.
RX PubMed=27905398; DOI=10.1038/ncomms13573;
RA Falk S., Finogenova K., Melko M., Benda C., Lykke-Andersen S., Jensen T.H.,
RA Conti E.;
RT "Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections
RT to splicing factors.";
RL Nat. Commun. 7:13573-13573(2016).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SF3B COMPLEX,
RP AND SUBCELLULAR LOCATION.
RX PubMed=28541300; DOI=10.1038/ncomms15522;
RA Teng T., Tsai J.H., Puyang X., Seiler M., Peng S., Prajapati S., Aird D.,
RA Buonamici S., Caleb B., Chan B., Corson L., Feala J., Fekkes P., Gerard B.,
RA Karr C., Korpal M., Liu X., Lowe J.T., Mizui Y., Palacino J., Park E.,
RA Smith P.G., Subramanian V., Wu Z.J., Zou J., Yu L., Chicas A., Warmuth M.,
RA Larsen N., Zhu P.;
RT "Splicing modulators act at the branch point adenosine binding pocket
RT defined by the PHF5A-SF3b complex.";
RL Nat. Commun. 8:15522-15522(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A'
CC complex assembly formed by the stable binding of U2 snRNP to the
CC branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of
CC SF3A/SF3B complex upstream of the branch site is essential, it may
CC anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved
CC in the assembly of the 'E' complex (PubMed:10882114). Belongs also to
CC the minor U12-dependent spliceosome, which is involved in the splicing
CC of rare class of nuclear pre-mRNA intron (PubMed:15146077).
CC {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:12234937,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638).
CC Component of the U11/U12 snRNPs that are part of the U12-type
CC spliceosome (PubMed:15146077). Component of splicing factor SF3B which
CC is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4,
CC SF3B5, SF3B6, PHF5A and DDX42 (PubMed:12234937, PubMed:12738865,
CC PubMed:27720643, PubMed:28541300). SF3B associates with the splicing
CC factor SF3A and a 12S RNA unit to form the U2 small nuclear
CC ribonucleoproteins complex (U2 snRNP) (PubMed:12234937). Interacts
CC directly with SF3B4 (PubMed:25737013). The SF3B complex composed of
CC SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2
CC (PubMed:27720643). Found in a complex with PRMT9, SF3B2 and SF3B4
CC (PubMed:25737013). Interacts (Arg-508-methylated form) with SMN1 (via
CC Tudor domain) (PubMed:25737013). Interacts with RBM7 (PubMed:27905398).
CC Interacts with ERCC6 (PubMed:26030138). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:12738865,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:25737013,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:27905398, ECO:0000269|PubMed:28541300}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr.
CC {ECO:0000269|PubMed:16923959}.
CC -!- INTERACTION:
CC Q13435; O60231: DHX16; NbExp=2; IntAct=EBI-749111, EBI-311446;
CC Q13435; P22607: FGFR3; NbExp=3; IntAct=EBI-749111, EBI-348399;
CC Q13435; Q70Z53: FRA10AC1; NbExp=2; IntAct=EBI-749111, EBI-710176;
CC Q13435; P01112: HRAS; NbExp=3; IntAct=EBI-749111, EBI-350145;
CC Q13435; O60341: KDM1A; NbExp=2; IntAct=EBI-749111, EBI-710124;
CC Q13435; Q6P2P2: PRMT9; NbExp=9; IntAct=EBI-749111, EBI-10962083;
CC Q13435; O43395: PRPF3; NbExp=2; IntAct=EBI-749111, EBI-744322;
CC Q13435; Q6P2Q9: PRPF8; NbExp=3; IntAct=EBI-749111, EBI-538479;
CC Q13435; O15541: RNF113A; NbExp=2; IntAct=EBI-749111, EBI-2130294;
CC Q13435; Q15427: SF3B4; NbExp=8; IntAct=EBI-749111, EBI-348469;
CC Q13435; O95391: SLU7; NbExp=2; IntAct=EBI-749111, EBI-750559;
CC Q13435; Q16637: SMN2; NbExp=4; IntAct=EBI-749111, EBI-395421;
CC Q13435; Q01081: U2AF1; NbExp=2; IntAct=EBI-749111, EBI-632461;
CC Q13435; Q9HCS7: XAB2; NbExp=2; IntAct=EBI-749111, EBI-295232;
CC Q13435; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-749111, EBI-3920997;
CC Q13435; Q9Y649; NbExp=3; IntAct=EBI-749111, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300}. Nucleus speckle
CC {ECO:0000269|PubMed:16923959}.
CC -!- PTM: Methylation at Arg-508 by PRMT9 is required for the interaction
CC with SMN1. {ECO:0000269|PubMed:25737013}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97461.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA97461.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH53577.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAG61831.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK290850; BAF83539.1; -; mRNA.
DR EMBL; AK300016; BAG61831.1; ALT_INIT; mRNA.
DR EMBL; BC000401; AAH00401.2; -; mRNA.
DR EMBL; BC007610; AAH07610.1; -; mRNA.
DR EMBL; BC014125; AAH14125.2; -; mRNA.
DR EMBL; BC053577; AAH53577.1; ALT_SEQ; mRNA.
DR EMBL; U41371; AAA97461.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31612.1; -.
DR RefSeq; NP_006833.2; NM_006842.2.
DR PDB; 2DO5; NMR; -; A=24-68.
DR PDB; 5Z56; EM; 5.10 A; 2=1-895.
DR PDB; 5Z57; EM; 6.50 A; 2=1-895.
DR PDB; 5Z58; EM; 4.90 A; 2=1-895.
DR PDB; 6AH0; EM; 5.70 A; 2=1-895.
DR PDB; 6AHD; EM; 3.80 A; 2=1-895.
DR PDB; 6FF4; EM; 16.00 A; 8=1-895.
DR PDB; 6FF7; EM; 4.50 A; 8=1-895.
DR PDB; 6QX9; EM; 3.28 A; B2=1-895.
DR PDB; 6Y50; EM; 4.10 A; 8=1-895.
DR PDB; 6Y53; EM; 7.10 A; 8=1-895.
DR PDB; 6Y5Q; EM; 7.10 A; 8=1-895.
DR PDB; 7ABG; EM; 7.80 A; T=1-895.
DR PDB; 7ABH; EM; 4.50 A; T=1-895.
DR PDB; 7ABI; EM; 8.00 A; T=1-895.
DR PDB; 7DVQ; EM; 2.89 A; 2=1-895.
DR PDB; 7ONB; EM; 3.10 A; I=1-895.
DR PDB; 7Q3L; EM; 2.30 A; B=1-895.
DR PDB; 7Q4O; EM; 2.20 A; B=1-895.
DR PDB; 7Q4P; EM; 2.20 A; B=1-895.
DR PDBsum; 2DO5; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 6Y50; -.
DR PDBsum; 6Y53; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABH; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7ONB; -.
DR PDBsum; 7Q3L; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; Q13435; -.
DR SMR; Q13435; -.
DR BioGRID; 116188; 374.
DR ComplexPortal; CPX-2227; SF3B complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR CORUM; Q13435; -.
DR IntAct; Q13435; 107.
DR MINT; Q13435; -.
DR STRING; 9606.ENSP00000318861; -.
DR ChEMBL; CHEMBL1229011; -.
DR GlyGen; Q13435; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13435; -.
DR MetOSite; Q13435; -.
DR PhosphoSitePlus; Q13435; -.
DR SwissPalm; Q13435; -.
DR BioMuta; SF3B2; -.
DR DMDM; 296452908; -.
DR EPD; Q13435; -.
DR jPOST; Q13435; -.
DR MassIVE; Q13435; -.
DR MaxQB; Q13435; -.
DR PaxDb; Q13435; -.
DR PeptideAtlas; Q13435; -.
DR PRIDE; Q13435; -.
DR ProteomicsDB; 59431; -.
DR TopDownProteomics; Q13435; -.
DR Antibodypedia; 30058; 225 antibodies from 26 providers.
DR DNASU; 10992; -.
DR Ensembl; ENST00000322535.11; ENSP00000318861.6; ENSG00000087365.16.
DR GeneID; 10992; -.
DR KEGG; hsa:10992; -.
DR MANE-Select; ENST00000322535.11; ENSP00000318861.6; NM_006842.3; NP_006833.2.
DR UCSC; uc001ogy.2; human.
DR CTD; 10992; -.
DR DisGeNET; 10992; -.
DR GeneCards; SF3B2; -.
DR HGNC; HGNC:10769; SF3B2.
DR HPA; ENSG00000087365; Low tissue specificity.
DR MIM; 605591; gene.
DR neXtProt; NX_Q13435; -.
DR OpenTargets; ENSG00000087365; -.
DR PharmGKB; PA35687; -.
DR VEuPathDB; HostDB:ENSG00000087365; -.
DR eggNOG; KOG2330; Eukaryota.
DR GeneTree; ENSGT00390000006734; -.
DR InParanoid; Q13435; -.
DR OMA; MYRQFYR; -.
DR OrthoDB; 1275099at2759; -.
DR PhylomeDB; Q13435; -.
DR TreeFam; TF300635; -.
DR PathwayCommons; Q13435; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q13435; -.
DR SIGNOR; Q13435; -.
DR BioGRID-ORCS; 10992; 752 hits in 1086 CRISPR screens.
DR ChiTaRS; SF3B2; human.
DR EvolutionaryTrace; Q13435; -.
DR GeneWiki; SF3B2; -.
DR GenomeRNAi; 10992; -.
DR Pharos; Q13435; Tbio.
DR PRO; PR:Q13435; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13435; protein.
DR Bgee; ENSG00000087365; Expressed in ventricular zone and 199 other tissues.
DR ExpressionAtlas; Q13435; baseline and differential.
DR Genevisible; Q13435; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR InterPro; IPR007180; DUF382.
DR InterPro; IPR006568; PSP_pro-rich.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF04037; DUF382; 1.
DR Pfam; PF04046; PSP; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00581; PSP; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Host-virus interaction; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..895
FT /note="Splicing factor 3B subunit 2"
FT /id="PRO_0000174328"
FT DOMAIN 24..58
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..550
FT /note="Required for interaction with PRMT9"
FT /evidence="ECO:0000269|PubMed:25737013"
FT REGION 691..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..199
FT /evidence="ECO:0000255"
FT COMPBIAS 10..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 222
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 245
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 247
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 508
FT /note="Omega-N-methylarginine; by PRMT9; alternate"
FT /evidence="ECO:0000269|PubMed:25737013"
FT MOD_RES 508
FT /note="Symmetric dimethylarginine; by PRMT9; alternate"
FT /evidence="ECO:0000269|PubMed:25737013"
FT MOD_RES 515
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 780
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 770
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 790
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 843
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 857
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 471
FT /note="R->K: Does not affect methylation by PRMT9."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 495
FT /note="R->K: Does not affect methylation by PRMT9."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 502
FT /note="R->K: Does not affect methylation by PRMT9."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 506
FT /note="F->A: Does not affect methylation by PRMT9; when
FT associated with A-510."
FT /evidence="ECO:0000269|PubMed:25979344"
FT MUTAGEN 507
FT /note="K->A: Moderately diminished formation of omega-N
FT monomethylarginine but greatly reduced formation of
FT symmetrical dimethylarginine; when associated with A-509."
FT /evidence="ECO:0000269|PubMed:25979344"
FT MUTAGEN 507
FT /note="K->R: Moderately diminished formation of omega-N
FT monomethylarginine but greatly reduced formation of
FT symmetrical dimethylarginine; when associated with R-509.
FT Abolishes formation of omega-N monomethylarginine and
FT formation of symmetrical dimethylarginine; when associated
FT with R-508. Abolishes formation of omega-N
FT monomethylarginine and formation of symmetrical
FT dimethylarginine; when associated with K-508 and R-509."
FT /evidence="ECO:0000269|PubMed:25979344"
FT MUTAGEN 508
FT /note="R->K: Abolishes interaction with SMN1; Abolishes
FT methylation by PRMT9. Abolishes formation of omega-N
FT monomethylarginine and formation of symmetrical
FT dimethylarginine; when associated with R-507. Abolishes
FT formation of omega-N monomethylarginine and formation of
FT symmetrical dimethylarginine; when associated with R-507.
FT Abolishes formation of omega-N monomethylarginine and
FT formation of symmetrical dimethylarginine; when associated
FT with R-507 and R-509."
FT /evidence="ECO:0000269|PubMed:25737013,
FT ECO:0000269|PubMed:25979344"
FT MUTAGEN 509
FT /note="K->A: Moderately diminished formation of omega-N
FT monomethylarginine but greatly reduced formation of
FT symmetrical dimethylarginine; when associated with A-507."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 509
FT /note="K->R: Moderately diminished formation of omega-N
FT monomethylarginine but greatly reduced formation of
FT symmetrical dimethylarginine; when associated with R-507.
FT Abolishes formation of omega-N monomethylarginine and
FT formation of symmetrical dimethylarginine; when associated
FT with K-508 and R-507."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 510
FT /note="Y->A: Does not affect methylation by PRMT9; when
FT associated with A-506."
FT /evidence="ECO:0000269|PubMed:25979344"
FT MUTAGEN 515
FT /note="R->K: Does not affect methylation by PRMT9."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 530
FT /note="R->K: Does not affect methylation by PRMT9."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 537
FT /note="R->K: Does not affect methylation by PRMT9."
FT /evidence="ECO:0000269|PubMed:25737013"
FT CONFLICT 602
FT /note="K -> E (in Ref. 1; BAF83539)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="E -> G (in Ref. 1; BAF83539)"
FT /evidence="ECO:0000305"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:2DO5"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:2DO5"
FT HELIX 462..468
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 485..492
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 509..513
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 514..518
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 533..543
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 549..554
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 593..597
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 611..616
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 633..639
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 657..659
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 692..702
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 895 AA; 100228 MW; D372AFA679443AD6 CRC64;
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL VERLQSYTRQ
TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP PLQPPPPPPP PPPGLGLGFP
MAHPPNLGPP PPLRVGEPVA LSEEERLKLA QQQAALLMQQ EERAKQQGDH SLKEHELLEQ
QKRAAVLLEQ ERQQEIAKMG TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG
APVPRPRGPP PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA
RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR EKDSTRSRGS
DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK KEKEKEPEKL DKLENSAAPK
KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS KKKLRRMNRF TVAELKQLVA RPDVVEMHDV
TAQDPKLLVH LKATRNSVPV PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL
QEKEEQKTMK SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR
LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI PGLNSPIPES
CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE EEIDRTPWGE LEPSDEESSE
EEEEEESDED KPDETGFITP ADSGLITPGG FSSVPAGMET PELIELRKKK IEEAMDGSET
PQLFTVLPEK RTATVGGAMM GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM
TQKYEEHVRE QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF
