ID PTBP1_HUMAN Reviewed; 557 AA. AC P26599; Q9BUQ0; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 12-OCT-2022, sequence version 2. DT 27-MAR-2024, entry version 247. DE RecName: Full=Polypyrimidine tract-binding protein 1; DE Short=PTB; DE AltName: Full=57 kDa RNA-binding protein PPTB-1; DE AltName: Full=Heterogeneous nuclear ribonucleoprotein I; DE Short=hnRNP I; GN Name=PTBP1; Synonyms=PTB; 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] (ISOFORM 2), AND PROTEIN SEQUENCE OF 123-130 AND RP 219-238. RC TISSUE=Placenta; RX PubMed=1906035; DOI=10.1101/gad.5.7.1224; RA Gil A., Sharp P.A., Jamison S.F., Garcia-Blanco M.A.; RT "Characterization of cDNAs encoding the polypyrimidine tract-binding RT protein."; RL Genes Dev. 5:1224-1236(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). RX PubMed=1906036; DOI=10.1101/gad.5.7.1237; RA Patton J.G., Mayer S.A., Tempst P., Nadal-Ginard B.; RT "Characterization and molecular cloning of polypyrimidine tract-binding RT protein: a component of a complex necessary for pre-mRNA splicing."; RL Genes Dev. 5:1237-1251(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=1641332; DOI=10.1093/nar/20.14.3671; RA Ghetti A., Pinol-Roma S., Michael W., Morandi C., Dreyfuss G.; RT "hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear RT localization and association with hnRNAs."; RL Nucleic Acids Res. 20:3671-3678(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, Ovary, and Skin; 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 [8] RP PROTEIN SEQUENCE OF 1-13; 65-92; 123-134; 219-238; 352-374; 437-444; RP 455-463 AND 498-508, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Colon carcinoma, Hepatoma, and Mammary carcinoma; RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Matallanas D., RA Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 123-129; 425-431; 437-452 AND 455-463. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein RT database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [10] RP INTERACTION WITH SFPQ. RX PubMed=10653975; RX DOI=10.1002/(sici)1097-4644(20000315)76:4<559::aid-jcb4>3.3.co;2-l; RA Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.; RT "Differential nuclear localization and nuclear matrix association of the RT splicing factors PSF and PTB."; RL J. Cell. Biochem. 76:559-566(2000). RN [11] RP FUNCTION, AND INTERACTION WITH HNRPH1; PTBP2 AND KHSRP. RX PubMed=11003644; DOI=10.1128/mcb.20.20.7463-7479.2000; RA Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., RA Black D.L.; RT "Cooperative assembly of an hnRNP complex induced by a tissue-specific RT homolog of polypyrimidine tract binding protein."; RL Mol. Cell. Biol. 20:7463-7479(2000). RN [12] RP FUNCTION. RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x; RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.; RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is RT regulated by an intricate interplay of cis elements and trans factors."; RL J. Neurochem. 88:1078-1090(2004). RN [13] RP FUNCTION. RX PubMed=14966131; DOI=10.1074/jbc.m313439200; RA Zuccato E., Buratti E., Stuani C., Baralle F.E., Pagani F.; RT "An intronic polypyrimidine-rich element downstream of the donor site RT modulates cystic fibrosis transmembrane conductance regulator exon 9 RT alternative splicing."; RL J. Biol. Chem. 279:16980-16988(2004). RN [14] RP FUNCTION, AND RNA-BINDING. RX PubMed=16260624; DOI=10.1128/mcb.25.22.10111-10121.2005; RA Lin J.C., Tarn W.Y.; RT "Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic RT action of RBM4 and PTB."; RL Mol. Cell. Biol. 25:10111-10121(2005). RN [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-141, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [19] RP FUNCTION. RX PubMed=20010808; DOI=10.1038/nature08697; RA David C.J., Chen M., Assanah M., Canoll P., Manley J.L.; RT "HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA RT splicing in cancer."; RL Nature 463:364-368(2010). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-141, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [21] 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 [22] RP FUNCTION. RX PubMed=21518792; DOI=10.1083/jcb.201007131; RA Lin J.C., Tarn W.Y.; RT "RBM4 down-regulates PTB and antagonizes its activity in muscle cell- RT specific alternative splicing."; RL J. Cell Biol. 193:509-520(2011). RN [23] RP FUNCTION. RX PubMed=21518806; DOI=10.1261/rna.2549411; RA Kafasla P., Lin H., Curry S., Jackson R.J.; RT "Activation of picornaviral IRESs by PTB shows differential dependence on RT each PTB RNA-binding domain."; RL RNA 17:1120-1131(2011). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-459, 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 [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; TYR-127; SER-141 AND RP SER-459, 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 [28] RP 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 [29] 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 [30] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65 AND LYS-218, AND RP IDENTIFICATION 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 [31] RP STRUCTURE BY NMR OF 361-557, AND RNA-BINDING. RX PubMed=10856256; DOI=10.1093/emboj/19.12.3132; RA Conte M.R., Gruene T., Ghuman J., Kelly G., Ladas A., Matthews S., RA Curry S.; RT "Structure of tandem RNA recognition motifs from polypyrimidine tract RT binding protein reveals novel features of the RRM fold."; RL EMBO J. 19:3132-3141(2000). RN [32] RP STRUCTURE BY NMR OF 55-327, SUBUNIT, AND RNA-BINDING. RX PubMed=15341728; DOI=10.1016/j.str.2004.07.008; RA Simpson P.J., Monie T.P., Szendroei A., Davydova N., Tyzack J.K., RA Conte M.R., Read C.M., Cary P.D., Svergun D.I., Konarev P.V., Curry S., RA Matthews S.; RT "Structure and RNA interactions of the N-terminal RRM domains of PTB."; RL Structure 12:1631-1643(2004). RN [33] RP STRUCTURE BY NMR OF 49-557 IN COMPLEXES WITH RNA, AND FUNCTION. RX PubMed=16179478; DOI=10.1126/science.1114066; RA Oberstrass F.C., Auweter S.D., Erat M., Hargous Y., Henning A., Wenter P., RA Reymond L., Amir-Ahmady B., Pitsch S., Black D.L., Allain F.H.; RT "Structure of PTB bound to RNA: specific binding and implications for RT splicing regulation."; RL Science 309:2054-2057(2005). RN [34] RP STRUCTURE BY NMR OF 350-557. RX PubMed=16362043; DOI=10.1038/sj.emboj.7600911; RA Vitali F., Henning A., Oberstrass F.C., Hargous Y., Auweter S.D., Erat M., RA Allain F.H.; RT "Structure of the two most C-terminal RNA recognition motifs of PTB using RT segmental isotope labeling."; RL EMBO J. 25:150-162(2006). CC -!- FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of CC alternative splicing events. Activates exon skipping of its own pre- CC mRNA during muscle cell differentiation. Binds to the polypyrimidine CC tract of introns. May promote RNA looping when bound to two separate CC polypyrimidine tracts in the same pre-mRNA. May promote the binding of CC U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching CC between mutually exclusive exons during maturation of the TPM1 pre- CC mRNA. Represses the splicing of MAPT/Tau exon 10 (PubMed:15009664). CC Binds to polypyrimidine-rich controlling element (PCE) of CFTR and CC promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and CC its role in exon inclusion of CFTR exon 9 (PubMed:14966131). Plays a CC role in the splicing of pyruvate kinase PKM by binding repressively to CC a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion CC and resulting in exon 10 inclusion and production of the PKM M2 isoform CC (PubMed:20010808). In case of infection by picornaviruses, binds to the CC viral internal ribosome entry site (IRES) and stimulates the IRES- CC mediated translation (PubMed:21518806). {ECO:0000269|PubMed:11003644, CC ECO:0000269|PubMed:14966131, ECO:0000269|PubMed:15009664, CC ECO:0000269|PubMed:16179478, ECO:0000269|PubMed:16260624, CC ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:21518792, CC ECO:0000269|PubMed:21518806}. CC -!- SUBUNIT: Monomer. Part of a ternary complex containing KHSRP, PTBP1, CC PTBP2 and HNRPH1. Interacts with RAVER1 and SFPQ. CC {ECO:0000269|PubMed:10653975, ECO:0000269|PubMed:11003644, CC ECO:0000269|PubMed:15341728}. CC -!- INTERACTION: CC P26599; Q15365: PCBP1; NbExp=2; IntAct=EBI-350540, EBI-946095; CC P26599; Q96PU8: QKI; NbExp=3; IntAct=EBI-350540, EBI-945792; CC P26599; P98175: RBM10; NbExp=4; IntAct=EBI-350540, EBI-721525; CC P26599; P23246: SFPQ; NbExp=2; IntAct=EBI-350540, EBI-355453; CC P26599; P09012: SNRPA; NbExp=7; IntAct=EBI-350540, EBI-607085; CC P26599; Q7ZYE9: hnrnpab.L; Xeno; NbExp=4; IntAct=EBI-350540, EBI-1086317; CC P26599; PRO_0000037940 [P29991]; Xeno; NbExp=5; IntAct=EBI-350540, EBI-8826689; CC P26599; PRO_0000308465 [P29991]; Xeno; NbExp=3; IntAct=EBI-350540, EBI-8826747; CC P26599-3; P98175: RBM10; NbExp=3; IntAct=EBI-16437588, EBI-721525; CC P26599-3; Q13148: TARDBP; NbExp=3; IntAct=EBI-16437588, EBI-372899; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P26599-3; Sequence=Displayed; CC Name=2; CC IsoId=P26599-1; Sequence=VSP_061652; CC Name=3; Synonyms=PTB2; CC IsoId=P26599-2; Sequence=VSP_061653; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/46504/PTBP1"; 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; X60648; CAA43056.1; -; mRNA. DR EMBL; X62006; CAA43973.1; -; mRNA. DR EMBL; X65371; CAA46443.1; -; mRNA. DR EMBL; X65372; CAA46444.1; -; mRNA. DR EMBL; X66975; CAA47386.1; -; mRNA. DR EMBL; BT006819; AAP35465.1; -; mRNA. DR EMBL; AC006273; AAC99798.1; -; Genomic_DNA. DR EMBL; CH471242; EAW61154.1; -; Genomic_DNA. DR EMBL; BC002397; AAH02397.1; -; mRNA. DR EMBL; BC004383; AAH04383.1; -; mRNA. DR EMBL; BC013694; AAH13694.1; -; mRNA. DR CCDS; CCDS32859.1; -. [P26599-1] DR CCDS; CCDS42456.1; -. [P26599-3] DR CCDS; CCDS45892.1; -. [P26599-2] DR PIR; S23016; S23016. DR RefSeq; NP_002810.1; NM_002819.4. [P26599-3] DR RefSeq; NP_114367.1; NM_031990.3. [P26599-2] DR RefSeq; NP_114368.1; NM_031991.3. [P26599-1] DR PDB; 1QM9; NMR; -; A=361-557. DR PDB; 1SJQ; NMR; -; A=55-147. DR PDB; 1SJR; NMR; -; A=147-327. DR PDB; 2AD9; NMR; -; A=49-146. DR PDB; 2ADB; NMR; -; A=172-298. DR PDB; 2ADC; NMR; -; A=350-557. DR PDB; 2EVZ; NMR; -; A=350-557. DR PDB; 2N3O; NMR; -; A=41-163. DR PDB; 3ZZY; X-ray; 1.40 A; A/B=156-285. DR PDB; 3ZZZ; X-ray; 1.55 A; A/B=156-285. DR PDB; 8BGF; NMR; -; A=41-163. DR PDB; 8BWF; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=57-140. DR PDBsum; 1QM9; -. DR PDBsum; 1SJQ; -. DR PDBsum; 1SJR; -. DR PDBsum; 2AD9; -. DR PDBsum; 2ADB; -. DR PDBsum; 2ADC; -. DR PDBsum; 2EVZ; -. DR PDBsum; 2N3O; -. DR PDBsum; 3ZZY; -. DR PDBsum; 3ZZZ; -. DR PDBsum; 8BGF; -. DR PDBsum; 8BWF; -. DR AlphaFoldDB; P26599; -. DR BMRB; P26599; -. DR SASBDB; P26599; -. DR SMR; P26599; -. DR BioGRID; 111697; 426. DR CORUM; P26599; -. DR ELM; P26599; -. DR IntAct; P26599; 88. DR MINT; P26599; -. DR STRING; 9606.ENSP00000349428; -. DR ChEMBL; CHEMBL1293230; -. DR GlyCosmos; P26599; 6 sites, 1 glycan. DR GlyGen; P26599; 9 sites, 2 O-linked glycans (9 sites). DR iPTMnet; P26599; -. DR MetOSite; P26599; -. DR PhosphoSitePlus; P26599; -. DR SwissPalm; P26599; -. DR BioMuta; PTBP1; -. DR DMDM; 131528; -. DR EPD; P26599; -. DR jPOST; P26599; -. DR MassIVE; P26599; -. DR MaxQB; P26599; -. DR PaxDb; 9606-ENSP00000349428; -. DR PeptideAtlas; P26599; -. DR PRIDE; P26599; -. DR ProteomicsDB; 54354; -. [P26599-1] DR ProteomicsDB; 54355; -. [P26599-2] DR ProteomicsDB; 54356; -. [P26599-3] DR Pumba; P26599; -. DR TopDownProteomics; P26599-1; -. [P26599-1] DR TopDownProteomics; P26599-2; -. [P26599-2] DR Antibodypedia; 4613; 510 antibodies from 37 providers. DR DNASU; 5725; -. DR Ensembl; ENST00000349038.8; ENSP00000014112.5; ENSG00000011304.22. [P26599-1] DR Ensembl; ENST00000356948.11; ENSP00000349428.4; ENSG00000011304.22. [P26599-3] DR Ensembl; ENST00000394601.8; ENSP00000408096.1; ENSG00000011304.22. [P26599-2] DR GeneID; 5725; -. DR KEGG; hsa:5725; -. DR MANE-Select; ENST00000356948.11; ENSP00000349428.4; NM_002819.5; NP_002810.1. DR UCSC; uc002lpp.3; human. [P26599-3] DR AGR; HGNC:9583; -. DR CTD; 5725; -. DR DisGeNET; 5725; -. DR GeneCards; PTBP1; -. DR HGNC; HGNC:9583; PTBP1. DR HPA; ENSG00000011304; Low tissue specificity. DR MIM; 600693; gene. DR neXtProt; NX_P26599; -. DR OpenTargets; ENSG00000011304; -. DR PharmGKB; PA33934; -. DR VEuPathDB; HostDB:ENSG00000011304; -. DR eggNOG; KOG1190; Eukaryota. DR GeneTree; ENSGT01050000244924; -. DR HOGENOM; CLU_015171_7_1_1; -. DR InParanoid; P26599; -. DR OMA; AANNNAC; -. DR OrthoDB; 4825346at2759; -. DR PhylomeDB; P26599; -. DR TreeFam; TF319824; -. DR PathwayCommons; P26599; -. DR Reactome; R-HSA-6803529; FGFR2 alternative splicing. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR SignaLink; P26599; -. DR SIGNOR; P26599; -. DR BioGRID-ORCS; 5725; 422 hits in 1180 CRISPR screens. DR ChiTaRS; PTBP1; human. DR EvolutionaryTrace; P26599; -. DR GeneWiki; PTBP1; -. DR GenomeRNAi; 5725; -. DR Pharos; P26599; Tbio. DR PRO; PR:P26599; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P26599; Protein. DR Bgee; ENSG00000011304; Expressed in thymus and 212 other cell types or tissues. DR ExpressionAtlas; P26599; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; EXP:DisProt. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0008187; F:poly-pyrimidine tract binding; TAS:ProtInc. DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:FlyBase. DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IDA:UniProtKB. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB. DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl. DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL. DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central. DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR CDD; cd12777; RRM1_PTBP1; 1. DR CDD; cd12782; RRM2_PTBP1; 1. DR CDD; cd12695; RRM3_PTBP1; 1. DR CDD; cd12701; RRM4_PTBP1; 1. DR DisProt; DP01601; -. DR Gene3D; 3.30.70.330; -; 4. DR InterPro; IPR006536; HnRNP-L/PTB. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR021790; PTBP1-like_RRM2. DR InterPro; IPR035000; PTBP1_RRM1. DR InterPro; IPR035001; PTBP1_RRM3. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR NCBIfam; TIGR01649; hnRNP-L_PTB; 1. DR PANTHER; PTHR15592; MATRIN 3/NUCLEAR PROTEIN 220-RELATED; 1. DR PANTHER; PTHR15592:SF19; POLYPYRIMIDINE TRACT-BINDING PROTEIN 1; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF13893; RRM_5; 2. DR Pfam; PF11835; RRM_8; 1. DR SMART; SM00360; RRM; 4. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 4. DR PROSITE; PS50102; RRM; 4. DR SWISS-2DPAGE; P26599; -. DR Genevisible; P26599; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; KW RNA-binding; Ubl conjugation. FT CHAIN 1..557 FT /note="Polypyrimidine tract-binding protein 1" FT /id="PRO_0000081737" FT DOMAIN 59..143 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 184..260 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 363..437 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 480..555 FT /note="RRM 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 127 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 138 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT CROSSLNK 65 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 218 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 298..323 FT /note="Missing (in isoform 2)" FT /id="VSP_061652" FT VAR_SEQ 298..305 FT /note="GAPGIISA -> A (in isoform 3)" FT /id="VSP_061653" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:2N3O" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:8BWF" FT HELIX 72..79 FT /evidence="ECO:0007829|PDB:8BWF" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:8BWF" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:8BWF" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:8BWF" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:8BWF" FT HELIX 104..116 FT /evidence="ECO:0007829|PDB:8BWF" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:8BWF" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:1SJQ" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:2AD9" FT STRAND 182..190 FT /evidence="ECO:0007829|PDB:3ZZY" FT HELIX 197..204 FT /evidence="ECO:0007829|PDB:3ZZY" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:3ZZZ" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:3ZZY" FT STRAND 221..229 FT /evidence="ECO:0007829|PDB:3ZZY" FT HELIX 231..241 FT /evidence="ECO:0007829|PDB:3ZZY" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:3ZZY" FT STRAND 250..257 FT /evidence="ECO:0007829|PDB:3ZZY" FT STRAND 259..262 FT /evidence="ECO:0007829|PDB:1SJR" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:3ZZY" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:2ADB" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:2ADB" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:2ADC" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:1QM9" FT HELIX 377..385 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 391..394 FT /evidence="ECO:0007829|PDB:1QM9" FT TURN 397..399 FT /evidence="ECO:0007829|PDB:2EVZ" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:1QM9" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:1QM9" FT HELIX 411..420 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 426..429 FT /evidence="ECO:0007829|PDB:2ADC" FT STRAND 431..434 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 443..451 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 453..457 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 463..466 FT /evidence="ECO:0007829|PDB:1QM9" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:2ADC" FT STRAND 481..484 FT /evidence="ECO:0007829|PDB:1QM9" FT HELIX 493..502 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 509..514 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 520..523 FT /evidence="ECO:0007829|PDB:1QM9" FT HELIX 527..537 FT /evidence="ECO:0007829|PDB:1QM9" FT STRAND 541..545 FT /evidence="ECO:0007829|PDB:2ADC" FT STRAND 550..553 FT /evidence="ECO:0007829|PDB:1QM9" SQ SEQUENCE 557 AA; 59633 MW; DAFE52BAC0E4BE5C CRC64; MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGAP GIISASPYAG AGFPPTFAIP QAAGLSVPNV HGALAPLAIP SAAAAAAAAG RIAIPGLAGA GNSVLLVSNL NPERVTPQSL FILFGVYGDV QRVKILFNKK ENALVQMADG NQAQLAMSHL NGHKLHGKPI RITLSKHQNV QLPREGQEDQ GLTKDYGNSP LHRFKKPGSK NFQNIFPPSA TLHLSNIPPS VSEEDLKVLF SSNGGVVKGF KFFQKDRKMA LIQMGSVEEA VQALIDLHNH DLGENHHLRV SFSKSTI //