SF3B5_HUMAN
ID SF3B5_HUMAN Reviewed; 86 AA.
AC Q9BWJ5; B2R568; Q7RTV1;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Splicing factor 3B subunit 5;
DE Short=SF3b5;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 10 kDa subunit;
GN Name=SF3B5; Synonyms=SF3B10;
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=Tongue;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP IDENTIFICATION, AND 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 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, 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 [11]
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SF3B1; SF3B3 AND
RP PHF5A, FUNCTION, INTERACTION WITH SF3B1 AND SF3B3, IDENTIFICATION IN THE
RP SF3B COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, AND RNA-BINDING.
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 [14] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex, a constituent of the spliceosome (PubMed:27720643,
CC PubMed:28781166). SF3B complex is required for 'A' complex assembly
CC formed by the stable binding of U2 snRNP to the branchpoint sequence
CC (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex
CC upstream of the branch site is essential, it may anchor U2 snRNP to the
CC pre-mRNA (PubMed:12234937). {ECO:0000269|PubMed:12234937,
CC ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Component of the spliceosome B complex (PubMed:28781166).
CC Component of splicing factor SF3B complex which is composed of at least
CC eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and
CC DDX42 (PubMed:12234937, PubMed:12738865, PubMed:28541300,
CC PubMed:27720643). SF3B associates with the splicing factor SF3A and a
CC 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex
CC (U2 snRNP) (PubMed:12234937). Within the SF3B complex interacts
CC directly with SF3B1 (via HEAT domain) and SF3B3 (PubMed:27720643). 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:27720643,
CC ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC Q9BWJ5; Q96FJ0: STAMBPL1; NbExp=3; IntAct=EBI-2555428, EBI-745021;
CC Q9BWJ5; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-2555428, EBI-8451480;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:28781166}.
CC -!- SIMILARITY: Belongs to the SF3B5 family. {ECO:0000305}.
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DR EMBL; AK312079; BAG35015.1; -; mRNA.
DR EMBL; AL031390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47851.1; -; Genomic_DNA.
DR EMBL; BC000198; AAH00198.1; -; mRNA.
DR EMBL; BK000562; DAA00073.1; -; Genomic_DNA.
DR CCDS; CCDS5204.1; -.
DR RefSeq; NP_112577.1; NM_031287.2.
DR PDB; 5IFE; X-ray; 3.10 A; B=1-86.
DR PDB; 5O9Z; EM; 4.50 A; x=1-86.
DR PDB; 5Z56; EM; 5.10 A; 7=1-86.
DR PDB; 5Z57; EM; 6.50 A; 7=1-86.
DR PDB; 5Z58; EM; 4.90 A; 7=1-86.
DR PDB; 5ZYA; EM; 3.95 A; B=1-86.
DR PDB; 6AH0; EM; 5.70 A; 7=1-86.
DR PDB; 6EN4; X-ray; 3.08 A; B=2-86.
DR PDB; 6FF4; EM; 16.00 A; x=1-86.
DR PDB; 6FF7; EM; 4.50 A; x=1-86.
DR PDB; 6QX9; EM; 3.28 A; B5=1-86.
DR PDB; 6Y50; EM; 4.10 A; x=1-86.
DR PDB; 6Y5Q; EM; 7.10 A; x=1-86.
DR PDB; 7ABG; EM; 7.80 A; x=1-86.
DR PDB; 7ABH; EM; 4.50 A; x=1-86.
DR PDB; 7ABI; EM; 8.00 A; x=1-86.
DR PDB; 7B0I; X-ray; 3.00 A; B=1-86.
DR PDB; 7B91; X-ray; 3.00 A; B=1-86.
DR PDB; 7B92; X-ray; 3.00 A; B=1-86.
DR PDB; 7B9C; X-ray; 2.40 A; B=1-86.
DR PDB; 7DVQ; EM; 2.89 A; 7=1-86.
DR PDB; 7KTS; EM; 19.09 A; T=1-86.
DR PDB; 7OMF; X-ray; 3.00 A; B=1-86.
DR PDB; 7ONB; EM; 3.10 A; B=1-86.
DR PDB; 7OPI; X-ray; 3.10 A; B=1-86.
DR PDB; 7Q3L; EM; 2.30 A; E=1-86.
DR PDB; 7Q4O; EM; 2.20 A; E=1-86.
DR PDB; 7Q4P; EM; 2.20 A; E=1-86.
DR PDBsum; 5IFE; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 5ZYA; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6EN4; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 6Y50; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABH; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7B0I; -.
DR PDBsum; 7B91; -.
DR PDBsum; 7B92; -.
DR PDBsum; 7B9C; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7KTS; -.
DR PDBsum; 7OMF; -.
DR PDBsum; 7ONB; -.
DR PDBsum; 7OPI; -.
DR PDBsum; 7Q3L; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; Q9BWJ5; -.
DR SMR; Q9BWJ5; -.
DR BioGRID; 123645; 87.
DR ComplexPortal; CPX-2227; SF3B complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR CORUM; Q9BWJ5; -.
DR IntAct; Q9BWJ5; 30.
DR MINT; Q9BWJ5; -.
DR STRING; 9606.ENSP00000356541; -.
DR GlyGen; Q9BWJ5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWJ5; -.
DR MetOSite; Q9BWJ5; -.
DR PhosphoSitePlus; Q9BWJ5; -.
DR BioMuta; SF3B5; -.
DR DMDM; 20140757; -.
DR EPD; Q9BWJ5; -.
DR jPOST; Q9BWJ5; -.
DR MassIVE; Q9BWJ5; -.
DR MaxQB; Q9BWJ5; -.
DR PaxDb; Q9BWJ5; -.
DR PeptideAtlas; Q9BWJ5; -.
DR PRIDE; Q9BWJ5; -.
DR ProteomicsDB; 79283; -.
DR TopDownProteomics; Q9BWJ5; -.
DR Antibodypedia; 46681; 44 antibodies from 18 providers.
DR DNASU; 83443; -.
DR Ensembl; ENST00000367569.4; ENSP00000356541.2; ENSG00000169976.7.
DR GeneID; 83443; -.
DR KEGG; hsa:83443; -.
DR MANE-Select; ENST00000367569.4; ENSP00000356541.2; NM_031287.3; NP_112577.1.
DR UCSC; uc003qkr.2; human.
DR CTD; 83443; -.
DR GeneCards; SF3B5; -.
DR HGNC; HGNC:21083; SF3B5.
DR HPA; ENSG00000169976; Low tissue specificity.
DR MIM; 617847; gene.
DR neXtProt; NX_Q9BWJ5; -.
DR OpenTargets; ENSG00000169976; -.
DR PharmGKB; PA134951632; -.
DR VEuPathDB; HostDB:ENSG00000169976; -.
DR eggNOG; KOG3485; Eukaryota.
DR GeneTree; ENSGT00390000013215; -.
DR HOGENOM; CLU_138804_3_1_1; -.
DR InParanoid; Q9BWJ5; -.
DR OMA; PMLSYMA; -.
DR OrthoDB; 1632322at2759; -.
DR PhylomeDB; Q9BWJ5; -.
DR TreeFam; TF300117; -.
DR PathwayCommons; Q9BWJ5; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q9BWJ5; -.
DR SIGNOR; Q9BWJ5; -.
DR BioGRID-ORCS; 83443; 803 hits in 1091 CRISPR screens.
DR ChiTaRS; SF3B5; human.
DR GeneWiki; SF3B5; -.
DR GenomeRNAi; 83443; -.
DR Pharos; Q9BWJ5; Tdark.
DR PRO; PR:Q9BWJ5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BWJ5; protein.
DR Bgee; ENSG00000169976; Expressed in adenohypophysis and 203 other tissues.
DR Genevisible; Q9BWJ5; HS.
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:0000124; C:SAGA complex; IC:ComplexPortal.
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: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; IDA:UniProtKB.
DR GO; GO:1990935; F:splicing factor binding; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IC:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR InterPro; IPR009846; SF3b5/RDS3-10.
DR InterPro; IPR017089; Splicing_factor_3B_subunit_5.
DR PANTHER; PTHR20978; PTHR20978; 1.
DR Pfam; PF07189; SF3b10; 1.
DR PIRSF; PIRSF037010; Splicing_factor_3B_subunit_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..86
FT /note="Splicing factor 3B subunit 5"
FT /id="PRO_0000220757"
FT REGION 15..76
FT /note="Interaction with SF3B1 and SF3B3"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 5
FT /note="Interaction with RNA"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 20
FT /note="Interaction with RNA"
FT /evidence="ECO:0000269|PubMed:27720643"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 28..45
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:7B0I"
SQ SEQUENCE 86 AA; 10135 MW; B8A209EA9F548E8E CRC64;
MTDRYTIHSQ LEHLQSKYIG TGHADTTKWE WLVNQHRDSY CSYMGHFDLL NYFAIAENES
KARVRFNLME KMLQPCGPPA DKPEEN
