SF3B6_HUMAN
ID SF3B6_HUMAN Reviewed; 125 AA.
AC Q9Y3B4; Q53TM1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Splicing factor 3B subunit 6;
DE AltName: Full=Pre-mRNA branch site protein p14;
DE AltName: Full=SF3b 14 kDa subunit;
DE Short=SF3B14a;
DE AltName: Full=Spliceosome-associated protein, 14-kDa;
DE AltName: Full=Splicing factor 3b, subunit 6, 14kDa;
GN Name=SF3B6; Synonyms=SAP14, SF3B14, SF3B14A;
GN ORFNames=CGI-110, HSPC175, HT006;
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], AND PROTEIN SEQUENCE OF 29-39 AND 41-58.
RX PubMed=11500380; DOI=10.1093/emboj/20.16.4536;
RA Will C.L., Schneider C., MacMillan A.M., Katopodis N.F., Neubauer G.,
RA Wilm M., Luehrmann R., Query C.C.;
RT "A novel U2 and U11/U12 snRNP protein that associates with the pre-mRNA
RT branch site.";
RL EMBO J. 20:4536-4546(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Testis;
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [9]
RP IDENTIFICATION IN THE SF3B COMPLEX, AND SUBCELLULAR LOCATION.
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 [10]
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29 AND LYS-41, AND IDENTIFICATION
RP 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 [13]
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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
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 [17]
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).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, 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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SF3B1, SUBUNIT,
RP RNA-BINDING, FUNCTION, AND REGION.
RX PubMed=16432215; DOI=10.1073/pnas.0508048103;
RA Schellenberg M.J., Edwards R.A., Ritchie D.B., Kent O.A., Golas M.M.,
RA Stark H., Luhrmann R., Glover J.N., MacMillan A.M.;
RT "Crystal structure of a core spliceosomal protein interface.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1266-1271(2006).
RN [20]
RP STRUCTURE BY NMR OF 8-93 IN COMPLEX WITH SF3B1.
RG RIKEN structural genomics initiative (RSGI);
RT "NMR solution structure of the human spliceosomal protein complex p14-
RT SF3B155.";
RL Submitted (JAN-2007) to the PDB data bank.
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 11-125 IN COMPLEX WITH SF3B1, AND
RP SUBUNIT.
RX PubMed=21062891; DOI=10.1261/rna.2224411;
RA Schellenberg M.J., Dul E.L., MacMillan A.M.;
RT "Structural model of the p14/SF3b155 - branch duplex complex.";
RL RNA 17:155-165(2011).
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 (PubMed:12234937). Directly
CC contacts the pre-mRNA branch site adenosine for the first catalytic
CC step of splicing (PubMed:16432215). Enters the spliceosome and
CC associates with the pre-mRNA branch site as part of the 17S U2 or, in
CC the case of the minor spliceosome, as part of the 18S U11/U12 snRNP
CC complex, and thus may facilitate the interaction of these snRNP with
CC the branch sites of U2 and U12 respectively (PubMed:16432215).
CC {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:16432215,
CC ECO:0000269|PubMed:27720643}.
CC -!- SUBUNIT: Component of splicing factor SF3B complex which is composed of
CC at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6,
CC PHF5A and DDX42 (PubMed:12234937, PubMed:12738865, PubMed:16432215,
CC PubMed:27720643, PubMed:28541300). Within the SF3B complex interacts
CC directly with SF3B1 (PubMed:21062891, PubMed:16432215, Ref.20). The
CC SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and
CC PHF5A interacts with U2AF2 (PubMed:27720643). Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome (PubMed:15146077).
CC {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:12738865,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:16432215,
CC ECO:0000269|PubMed:21062891, ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300, ECO:0000269|Ref.20}.
CC -!- INTERACTION:
CC Q9Y3B4; O75533-1: SF3B1; NbExp=3; IntAct=EBI-1046261, EBI-15565798;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300}.
CC -!- SIMILARITY: Belongs to the SF3B6 family. {ECO:0000305}.
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DR EMBL; AF401310; AAK94041.1; -; mRNA.
DR EMBL; AF151868; AAD34105.1; -; mRNA.
DR EMBL; AF161523; AAF29138.1; -; mRNA.
DR EMBL; AF184213; AAG09698.1; -; mRNA.
DR EMBL; AK311908; BAG34849.1; -; mRNA.
DR EMBL; AC008073; AAY14664.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00767.1; -; Genomic_DNA.
DR EMBL; BC015463; AAH15463.1; -; mRNA.
DR CCDS; CCDS1707.1; -.
DR RefSeq; NP_057131.1; NM_016047.3.
DR PDB; 2F9D; X-ray; 2.50 A; A/B=1-125.
DR PDB; 2F9J; X-ray; 3.00 A; A/B=1-125.
DR PDB; 2FHO; NMR; -; B=8-93.
DR PDB; 3LQV; X-ray; 2.38 A; A/B=11-125.
DR PDB; 5Z56; EM; 5.10 A; 5=1-125.
DR PDB; 5Z57; EM; 6.50 A; 5=1-125.
DR PDB; 5Z58; EM; 4.90 A; 5=1-125.
DR PDB; 6AH0; EM; 5.70 A; 5=1-125.
DR PDB; 6AHD; EM; 3.80 A; 5=1-125.
DR PDB; 6FF4; EM; 16.00 A; z=1-125.
DR PDB; 6FF7; EM; 4.50 A; N/z=1-125.
DR PDB; 6Y53; EM; 7.10 A; z=1-125.
DR PDB; 6Y5Q; EM; 7.10 A; z=1-125.
DR PDB; 7ABG; EM; 7.80 A; z=1-125.
DR PDB; 7ABH; EM; 4.50 A; z=1-125.
DR PDB; 7ABI; EM; 8.00 A; z=1-125.
DR PDB; 7DVQ; EM; 2.89 A; 5=1-125.
DR PDB; 7Q4O; EM; 2.20 A; F=1-125.
DR PDBsum; 2F9D; -.
DR PDBsum; 2F9J; -.
DR PDBsum; 2FHO; -.
DR PDBsum; 3LQV; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6Y53; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABH; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7Q4O; -.
DR AlphaFoldDB; Q9Y3B4; -.
DR BMRB; Q9Y3B4; -.
DR SMR; Q9Y3B4; -.
DR BioGRID; 119651; 133.
DR ComplexPortal; CPX-2227; SF3B complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR CORUM; Q9Y3B4; -.
DR DIP; DIP-44132N; -.
DR IntAct; Q9Y3B4; 46.
DR MINT; Q9Y3B4; -.
DR STRING; 9606.ENSP00000233468; -.
DR GlyGen; Q9Y3B4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3B4; -.
DR PhosphoSitePlus; Q9Y3B4; -.
DR SwissPalm; Q9Y3B4; -.
DR BioMuta; SF3B6; -.
DR DMDM; 12585536; -.
DR EPD; Q9Y3B4; -.
DR jPOST; Q9Y3B4; -.
DR MassIVE; Q9Y3B4; -.
DR MaxQB; Q9Y3B4; -.
DR PaxDb; Q9Y3B4; -.
DR PeptideAtlas; Q9Y3B4; -.
DR PRIDE; Q9Y3B4; -.
DR ProteomicsDB; 86002; -.
DR TopDownProteomics; Q9Y3B4; -.
DR Antibodypedia; 27422; 171 antibodies from 23 providers.
DR DNASU; 51639; -.
DR Ensembl; ENST00000233468.5; ENSP00000233468.4; ENSG00000115128.7.
DR GeneID; 51639; -.
DR KEGG; hsa:51639; -.
DR MANE-Select; ENST00000233468.5; ENSP00000233468.4; NM_016047.4; NP_057131.1.
DR UCSC; uc002rev.4; human.
DR CTD; 51639; -.
DR DisGeNET; 51639; -.
DR GeneCards; SF3B6; -.
DR HGNC; HGNC:30096; SF3B6.
DR HPA; ENSG00000115128; Low tissue specificity.
DR MIM; 607835; gene.
DR neXtProt; NX_Q9Y3B4; -.
DR OpenTargets; ENSG00000115128; -.
DR VEuPathDB; HostDB:ENSG00000115128; -.
DR eggNOG; KOG0114; Eukaryota.
DR GeneTree; ENSGT00390000005908; -.
DR HOGENOM; CLU_012062_25_2_1; -.
DR InParanoid; Q9Y3B4; -.
DR OMA; GYNFMDR; -.
DR OrthoDB; 1603846at2759; -.
DR PhylomeDB; Q9Y3B4; -.
DR PathwayCommons; Q9Y3B4; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q9Y3B4; -.
DR SIGNOR; Q9Y3B4; -.
DR BioGRID-ORCS; 51639; 702 hits in 1008 CRISPR screens.
DR ChiTaRS; SF3B6; human.
DR EvolutionaryTrace; Q9Y3B4; -.
DR GeneWiki; SF3B14; -.
DR GenomeRNAi; 51639; -.
DR Pharos; Q9Y3B4; Tbio.
DR PRO; PR:Q9Y3B4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y3B4; protein.
DR Bgee; ENSG00000115128; Expressed in upper arm skin and 183 other tissues.
DR Genevisible; Q9Y3B4; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IC:ComplexPortal.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR CDD; cd12241; RRM_SF3B14; 1.
DR DisProt; DP01458; -.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00229; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034150; SF3B6_RRM.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..125
FT /note="Splicing factor 3B subunit 6"
FT /id="PRO_0000081725"
FT DOMAIN 19..94
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 16..29
FT /note="Interaction with pre-mRNA branch site"
FT MOD_RES 29
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3LQV"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:3LQV"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3LQV"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:3LQV"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3LQV"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:3LQV"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3LQV"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3LQV"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:3LQV"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3LQV"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:3LQV"
SQ SEQUENCE 125 AA; 14585 MW; A1439DACB78A3208 CRC64;
MAMQAAKRAN IRLPPEVNRI LYIRNLPYKI TAEEMYDIFG KYGPIRQIRV GNTPETRGTA
YVVYEDIFDA KNACDHLSGF NVCNRYLVVL YYNANRAFQK MDTKKKEEQL KLLKEKYGIN
TDPPK
