PTBP1_HUMAN
ID PTBP1_HUMAN Reviewed; 531 AA.
AC P26599; Q9BUQ0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 238.
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], AND PROTEIN SEQUENCE OF 123-130 AND 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].
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].
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 3).
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 3).
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; 326-348; 411-418;
RP 429-437 AND 472-482, 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; 399-405; 411-426 AND 429-437.
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>3.0.co;2-u;
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-433, 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-433, 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-433, 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 335-531, 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 55-301, 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 49-531 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 324-531.
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=P26599-1; Sequence=Displayed;
CC Name=2; Synonyms=PTB2;
CC IsoId=P26599-2; Sequence=VSP_005802;
CC Name=3;
CC IsoId=P26599-3; Sequence=VSP_043649;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTBP1ID46504ch19p13.html";
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DR EMBL; X62006; CAA43973.1; -; mRNA.
DR EMBL; X65371; CAA46443.1; -; mRNA.
DR EMBL; X65372; CAA46444.1; -; mRNA.
DR EMBL; X60648; CAA43056.1; -; 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=335-531.
DR PDB; 1SJQ; NMR; -; A=55-147.
DR PDB; 1SJR; NMR; -; A=147-301.
DR PDB; 2AD9; NMR; -; A=49-146.
DR PDB; 2ADB; NMR; -; A=172-298.
DR PDB; 2ADC; NMR; -; A=324-531.
DR PDB; 2EVZ; NMR; -; A=324-531.
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 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 AlphaFoldDB; P26599; -.
DR BMRB; P26599; -.
DR SASBDB; P26599; -.
DR SMR; P26599; -.
DR BioGRID; 111697; 355.
DR CORUM; P26599; -.
DR ELM; P26599; -.
DR IntAct; P26599; 86.
DR MINT; P26599; -.
DR STRING; 9606.ENSP00000349428; -.
DR ChEMBL; CHEMBL1293230; -.
DR GlyGen; P26599; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; P26599; -.
DR MetOSite; P26599; -.
DR PhosphoSitePlus; P26599; -.
DR SwissPalm; P26599; -.
DR BioMuta; PTBP1; -.
DR DMDM; 131528; -.
DR SWISS-2DPAGE; P26599; -.
DR EPD; P26599; -.
DR jPOST; P26599; -.
DR MassIVE; P26599; -.
DR MaxQB; P26599; -.
DR PaxDb; P26599; -.
DR PeptideAtlas; P26599; -.
DR PRIDE; P26599; -.
DR ProteomicsDB; 54354; -. [P26599-1]
DR ProteomicsDB; 54355; -. [P26599-2]
DR ProteomicsDB; 54356; -. [P26599-3]
DR TopDownProteomics; P26599-1; -. [P26599-1]
DR TopDownProteomics; P26599-2; -. [P26599-2]
DR Antibodypedia; 4613; 447 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. [P26599-3]
DR UCSC; uc002lpp.3; human. [P26599-1]
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; WHDRVIR; -.
DR OrthoDB; 1545178at2759; -.
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; 395 hits in 1100 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 210 other tissues.
DR ExpressionAtlas; P26599; baseline and differential.
DR Genevisible; P26599; HS.
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: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:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
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: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; cd12693; RRM2_PTBP1_like; 1.
DR CDD; cd12695; RRM3_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; IPR034798; PTBP1/2/3_RRM2.
DR InterPro; IPR035000; PTBP1_RRM1.
DR InterPro; IPR035001; PTBP1_RRM3.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 4.
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..531
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 337..411
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 454..529
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 433
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 297
FT /note="F -> FASPYAGAGFPPTFAIPQAA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005802"
FT VAR_SEQ 297
FT /note="F -> FGAPGIISASPYAGAGFPPTFAIPQAA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_043649"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2N3O"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1SJQ"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:1SJQ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1SJQ"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:1SJQ"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1SJQ"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1SJQ"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2AD9"
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 329..332
FT /evidence="ECO:0007829|PDB:2ADC"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1QM9"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1QM9"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:2EVZ"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1QM9"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1QM9"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:2ADC"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 417..425
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:1QM9"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:2ADC"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1QM9"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:1QM9"
FT HELIX 501..511
FT /evidence="ECO:0007829|PDB:1QM9"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:2ADC"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:1QM9"
SQ SEQUENCE 531 AA; 57221 MW; BE12D5EA21537BED 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 QTMAAAFGLS
VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT PQSLFILFGV
YGDVQRVKIL FNKKENALVQ MADGNQAQLA MSHLNGHKLH GKPIRITLSK HQNVQLPREG
QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF PPSATLHLSN IPPSVSEEDL KVLFSSNGGV
VKGFKFFQKD RKMALIQMGS VEEAVQALID LHNHDLGENH HLRVSFSKST I
