PHF5A_HUMAN
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 03-AUG-2022, entry version 161.
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 -!- INTERACTION:
CC Q7RTV0; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2555365, EBI-10976677;
CC Q7RTV0; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2555365, EBI-10975473;
CC Q7RTV0; P60891: PRPS1; NbExp=3; IntAct=EBI-2555365, EBI-749195;
CC Q7RTV0; Q15428: SF3A2; NbExp=2; IntAct=EBI-2555365, EBI-2462271;
CC Q7RTV0; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2555365, EBI-5235340;
CC Q7RTV0; O76024: WFS1; NbExp=3; IntAct=EBI-2555365, EBI-720609;
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}.
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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; 6AHD; EM; 3.80 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 PDB; 6Y50; EM; 4.10 A; y=1-110.
DR PDB; 6Y5Q; EM; 7.10 A; y=1-110.
DR PDB; 7ABG; EM; 7.80 A; y=1-110.
DR PDB; 7ABH; EM; 4.50 A; y=1-110.
DR PDB; 7ABI; EM; 8.00 A; y=1-110.
DR PDB; 7B0I; X-ray; 3.00 A; D=1-98.
DR PDB; 7B91; X-ray; 3.00 A; D=1-98.
DR PDB; 7B92; X-ray; 3.00 A; D=1-98.
DR PDB; 7B9C; X-ray; 2.40 A; D=1-98.
DR PDB; 7DVQ; EM; 2.89 A; 6=1-110.
DR PDB; 7OMF; X-ray; 3.00 A; D=1-98.
DR PDB; 7ONB; EM; 3.10 A; D=1-110.
DR PDB; 7OPI; X-ray; 3.10 A; D=1-98.
DR PDB; 7Q3L; EM; 2.30 A; G=1-110.
DR PDB; 7Q4O; EM; 2.20 A; G=1-110.
DR PDB; 7Q4P; EM; 2.20 A; G=1-110.
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; 6AHD; -.
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; 7OMF; -.
DR PDBsum; 7ONB; -.
DR PDBsum; 7OPI; -.
DR PDBsum; 7Q3L; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; Q7RTV0; -.
DR SMR; Q7RTV0; -.
DR BioGRID; 124296; 122.
DR ComplexPortal; CPX-2227; SF3B complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR CORUM; Q7RTV0; -.
DR IntAct; Q7RTV0; 49.
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; 196 antibodies from 23 providers.
DR DNASU; 84844; -.
DR Ensembl; ENST00000216252.4; ENSP00000216252.3; ENSG00000100410.8.
DR GeneID; 84844; -.
DR KEGG; hsa:84844; -.
DR MANE-Select; ENST00000216252.4; ENSP00000216252.3; NM_032758.4; NP_116147.1.
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 VEuPathDB; HostDB:ENSG00000100410; -.
DR eggNOG; KOG1705; Eukaryota.
DR GeneTree; ENSGT00390000018518; -.
DR HOGENOM; CLU_110369_2_0_1; -.
DR InParanoid; Q7RTV0; -.
DR OMA; AYYCWEC; -.
DR OrthoDB; 1477492at2759; -.
DR PhylomeDB; Q7RTV0; -.
DR TreeFam; TF105627; -.
DR PathwayCommons; Q7RTV0; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q7RTV0; -.
DR SIGNOR; Q7RTV0; -.
DR BioGRID-ORCS; 84844; 744 hits in 1045 CRISPR screens.
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 182 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:0005681; C:spliceosomal complex; IC:ComplexPortal.
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:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
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 BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28541300,
FT ECO:0007744|PDB:5IFE, ECO:0007744|PDB:5SYB"
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:0007744|PubMed:19608861"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:5SYB"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5SYB"
FT TURN 24..28
FT /evidence="ECO:0007829|PDB:5SYB"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5SYB"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5SYB"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5SYB"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:5SYB"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5SYB"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5SYB"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:5SYB"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:5SYB"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5SYB"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 110 AA; 12405 MW; 90F7469DE7292BF7 CRC64;
MAKHHPDLIF CRKQAGVAIG RLCEKCDGKC VICDSYVRPC TLVRICDECN YGSYQGRCVI
CGGPGVSDAY YCKECTIQEK DRDGCPKIVN LGSSKTDLFY ERKKYGFKKR
