ID PHF5A_HUMAN Reviewed; 110 AA. AC Q7RTV0; Q9UH06; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 22-APR-2020, entry version 150. DE RecName: Full=PHD finger-like domain-containing protein 5A; DE Short=PHD finger-like domain protein 5A; DE AltName: Full=Splicing factor 3B-associated 14 kDa protein; DE Short=SF3b14b; GN Name=PHF5A; 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]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Duodenum, and Lymph; 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 [4] RP FUNCTION, 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 [5] 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 [6] 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 [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, 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 [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [10] 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 [11] RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SF3B1; SF3B3 AND RP SF3B5, 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 [12] RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF MUTANT SER-40 IN COMPLEX WITH RP ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE RP SF3B COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-36. 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 with the PAF1 complex (PAF1C) in transcriptional CC elongation by RNA polymerase II, and in regulation of development and CC maintenance of embryonic stem cell (ESC) pluripotency. Required for CC maintenance of ESCs self-renewal and cellular reprogramming of stem CC cells. Maintains pluripotency by recruiting and stabilizing PAF1C on CC pluripotency genes loci, and by regulating the expression of the CC pluripotency genes. Regulates the deposition of elongation-associated CC histone modifications, including dimethylated histone H3 'Lys-79' CC (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C CC targets, self-renewal and pluripotency genes. Regulates RNA polymerase CC II promoter-proximal pause release of the PAF1C targets and self- CC renewal genes, and the levels of elongating ('Ser-2' phosphorylated) CC RNA polymerase II in their gene bodies. Regulates muscle specification CC in adult stem cells by stabilizing PAF1C in chromatin to promote CC myogenic differentiation (By similarity). Involved in pre-mRNA splicing CC as a component of the splicing factor SF3B complex (PubMed:27720643, CC PubMed:28541300). 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). Acts as a transcriptional regulator by CC binding to the GJA1/Cx43 promoter and enhancing its up-regulation by CC ESR1/ER-alpha (By similarity). {ECO:0000250|UniProtKB:P83870, CC ECO:0000250|UniProtKB:P83871, ECO:0000269|PubMed:12234937, CC ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300}. CC -!- SUBUNIT: Interacts (via N-terminus) with U2AF1 and SRSF5; acts to CC bridge the two. Interacts (via C-terminus) with EP400 and DDX1; acts to CC bridge the two (By similarity). Component of splicing factor SF3B CC complex which is composed of at least eight subunits; SF3B1, SF3B2, CC SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42 (PubMed:12234937, CC PubMed:12738865, PubMed:27720643, PubMed:28541300). Within the SF3B CC complex interacts directly with SF3B1 and SF3B3 (PubMed:27720643). The CC SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and CC PHF5A interacts with U2AF2 (PubMed:27720643). SF3B associates with the CC splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear CC ribonucleoproteins complex (U2 snRNP) (PubMed:12234937). Component of CC the U11/U12 snRNPs that are part of the U12-type spliceosome CC (PubMed:15146077). Interacts with the PAF1 complex (PAF1C) composed of CC CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Within the PAF1C interacts CC directly with CDC73 and WDR61. Interacts with RNA polymerase II (By CC similarity). {ECO:0000250|UniProtKB:P83870, CC ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:12738865, CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643, CC ECO:0000269|PubMed:28541300}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643, CC ECO:0000269|PubMed:28541300}. Nucleus speckle CC {ECO:0000250|UniProtKB:P83870}. CC -!- SIMILARITY: Belongs to the PHF5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR456398; CAG30284.1; -; mRNA. DR EMBL; AL008582; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007321; AAH07321.1; -; mRNA. DR EMBL; BC075808; AAH75808.1; -; mRNA. DR EMBL; BK000563; DAA00074.1; -; mRNA. DR CCDS; CCDS14016.1; -. DR RefSeq; NP_116147.1; NM_032758.3. DR PDB; 5IFE; X-ray; 3.10 A; D=1-110. DR PDB; 5O9Z; EM; 4.50 A; y=1-110. DR PDB; 5SYB; X-ray; 1.82 A; A/B=1-110. DR PDB; 5Z56; EM; 5.10 A; 6=1-110. DR PDB; 5Z57; EM; 6.50 A; 6=1-110. DR PDB; 5Z58; EM; 4.90 A; 6=1-110. DR PDB; 5ZYA; EM; 3.95 A; D=7-91. DR PDB; 6AH0; EM; 5.70 A; 6=1-110. DR PDB; 6EN4; X-ray; 3.08 A; D=1-98. DR PDB; 6FF4; EM; 16.00 A; y=1-110. DR PDB; 6FF7; EM; 4.50 A; y=1-110. DR PDB; 6QX9; EM; 3.28 A; BP=1-104. DR PDBsum; 5IFE; -. DR PDBsum; 5O9Z; -. DR PDBsum; 5SYB; -. 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 SMR; Q7RTV0; -. DR BioGrid; 124296; 55. DR CORUM; Q7RTV0; -. DR IntAct; Q7RTV0; 19. DR MINT; Q7RTV0; -. DR STRING; 9606.ENSP00000216252; -. DR iPTMnet; Q7RTV0; -. DR PhosphoSitePlus; Q7RTV0; -. DR SwissPalm; Q7RTV0; -. DR BioMuta; PHF5A; -. DR DMDM; 46577625; -. DR EPD; Q7RTV0; -. DR jPOST; Q7RTV0; -. DR MassIVE; Q7RTV0; -. DR MaxQB; Q7RTV0; -. DR PaxDb; Q7RTV0; -. DR PeptideAtlas; Q7RTV0; -. DR PRIDE; Q7RTV0; -. DR ProteomicsDB; 68911; -. DR TopDownProteomics; Q7RTV0; -. DR Antibodypedia; 26931; 186 antibodies. DR DNASU; 84844; -. DR Ensembl; ENST00000216252; ENSP00000216252; ENSG00000100410. DR GeneID; 84844; -. DR KEGG; hsa:84844; -. DR UCSC; uc003bab.4; human. DR CTD; 84844; -. DR DisGeNET; 84844; -. DR GeneCards; PHF5A; -. DR HGNC; HGNC:18000; PHF5A. DR HPA; ENSG00000100410; Low tissue specificity. DR MIM; 617846; gene. DR neXtProt; NX_Q7RTV0; -. DR OpenTargets; ENSG00000100410; -. DR PharmGKB; PA134876104; -. DR eggNOG; KOG1705; Eukaryota. DR eggNOG; ENOG4111JIM; LUCA. DR GeneTree; ENSGT00390000018518; -. DR HOGENOM; CLU_110369_2_0_1; -. DR InParanoid; Q7RTV0; -. DR KO; K12834; -. DR OMA; CIICGAP; -. DR OrthoDB; 1477492at2759; -. DR PhylomeDB; Q7RTV0; -. DR TreeFam; TF105627; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR ChiTaRS; PHF5A; human. DR GenomeRNAi; 84844; -. DR Pharos; Q7RTV0; Tbio. DR PRO; PR:Q7RTV0; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q7RTV0; protein. DR Bgee; ENSG00000100410; Expressed in oocyte and 195 other tissues. DR ExpressionAtlas; Q7RTV0; baseline and differential. DR Genevisible; Q7RTV0; HS. DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. 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:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005686; C:U2 snRNP; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl. DR InterPro; IPR005345; PHF5. DR PANTHER; PTHR13120; PTHR13120; 1. DR Pfam; PF03660; PHF5; 1. DR PIRSF; PIRSF016468; PHF5; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; DNA-binding; Metal-binding; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; RNA-binding; Spliceosome; Transcription; KW Transcription regulation; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P83870" FT CHAIN 2..110 FT /note="PHD finger-like domain-containing protein 5A" FT /id="PRO_0000218716" FT REGION 35..51 FT /note="Interaction with SF3B1 AND SF3B3" FT /evidence="ECO:0000269|PubMed:27720643" FT REGION 79..82 FT /note="Interaction with SF3B3" FT /evidence="ECO:0000269|PubMed:27720643" FT METAL 11 FT /note="Zinc 1" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 23 FT /note="Zinc 2" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 26 FT /note="Zinc 2" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 30 FT /note="Zinc 3" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 33 FT /note="Zinc 3" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 46 FT /note="Zinc 1" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 49 FT /note="Zinc 1" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 58 FT /note="Zinc 2" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 61 FT /note="Zinc 2" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 72 FT /note="Zinc 3" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 75 FT /note="Zinc 3" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT METAL 85 FT /note="Zinc 1" FT /evidence="ECO:0000244|PDB:5IFE, ECO:0000244|PDB:5SYB, FT ECO:0000269|PubMed:28541300" FT SITE 17 FT /note="Interaction with SF3B3" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 100 FT /note="Interaction with RNA" FT /evidence="ECO:0000269|PubMed:27720643" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P83870" FT MOD_RES 3 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 94 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MUTAGEN 36 FT /note="Y->C: No apparent effect on cell growth, FT localization of SF3B1 protein or formation of nuclear FT speckles. Alters the structure of the presumed branchpoint FT (BP) adenosine binding pocket within the splicing factor FT SF3B complex which may lead to decreased binding affinity FT and thus affect pre-mRNA splicing." FT /evidence="ECO:0000269|PubMed:28541300" FT MUTAGEN 36 FT /note="Y->E,S,A: Alters the structure of the presumed FT branchpoint (BP) adenosine binding pocket within the FT splicing factor SF3B complex which may lead to decreased FT binding affinity and thus affect pre-mRNA splicing." FT /evidence="ECO:0000269|PubMed:28541300" FT STRAND 5..10 FT /evidence="ECO:0000244|PDB:5SYB" FT STRAND 17..19 FT /evidence="ECO:0000244|PDB:5SYB" FT TURN 24..28 FT /evidence="ECO:0000244|PDB:5SYB" FT TURN 31..33 FT /evidence="ECO:0000244|PDB:5SYB" FT STRAND 39..42 FT /evidence="ECO:0000244|PDB:5SYB" FT HELIX 47..50 FT /evidence="ECO:0000244|PDB:5SYB" FT TURN 53..56 FT /evidence="ECO:0000244|PDB:5SYB" FT TURN 59..61 FT /evidence="ECO:0000244|PDB:5SYB" FT STRAND 63..68 FT /evidence="ECO:0000244|PDB:6FF4" FT STRAND 70..72 FT /evidence="ECO:0000244|PDB:5SYB" FT HELIX 73..77 FT /evidence="ECO:0000244|PDB:5SYB" FT HELIX 80..83 FT /evidence="ECO:0000244|PDB:5SYB" FT STRAND 88..90 FT /evidence="ECO:0000244|PDB:5SYB" FT STRAND 93..96 FT /evidence="ECO:0000244|PDB:6FF4" FT TURN 97..99 FT /evidence="ECO:0000244|PDB:6FF4" SQ SEQUENCE 110 AA; 12405 MW; 90F7469DE7292BF7 CRC64; MAKHHPDLIF CRKQAGVAIG RLCEKCDGKC VICDSYVRPC TLVRICDECN YGSYQGRCVI CGGPGVSDAY YCKECTIQEK DRDGCPKIVN LGSSKTDLFY ERKKYGFKKR //