PTBP1_MOUSE
ID PTBP1_MOUSE Reviewed; 527 AA.
AC P17225;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Polypyrimidine tract-binding protein 1;
DE Short=PTB;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein I;
DE Short=hnRNP I;
GN Name=Ptbp1; Synonyms=Ptb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 312-341.
RX PubMed=1722210; DOI=10.1016/s0021-9258(18)54280-0;
RA Bothwell A.L.M., Ballard D.W., Philbrick W.M., Lindwall G., Maher S.E.,
RA Bridgett M.M., Jamison S.F., Garcia-Blanco M.A.;
RT "Murine polypyrimidine tract binding protein. Purification, cloning, and
RT mapping of the RNA binding domain.";
RL J. Biol. Chem. 266:24657-24663(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-14 AND 84-91, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [3]
RP INTERACTION WITH RAVER1.
RX PubMed=11724819; DOI=10.1083/jcb.200105044;
RA Huettelmaier S., Illenberger S., Grosheva I., Ruediger M., Singer R.H.,
RA Jockusch B.M.;
RT "Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and
RT microfilament attachment proteins.";
RL J. Cell Biol. 155:775-786(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
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).
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. Binds to
CC polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon
CC skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon
CC inclusion of CFTR exon 9. Plays a role in the splicing of pyruvate
CC kinase PKM by binding repressively to a polypyrimidine tract flanking
CC PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10
CC inclusion and production of the PKM M2 isoform.
CC {ECO:0000250|UniProtKB:P26599}.
CC -!- SUBUNIT: Monomer. Part of a ternary complex containing KHSRP, PTBP1,
CC PTBP2 and HNRPH1. Interacts with SFPQ (By similarity). Interacts with
CC RAVER1. {ECO:0000250, ECO:0000269|PubMed:11724819}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in myoblast; expression gradually
CC decreases during muscle cell differentiation (at protein level).
CC {ECO:0000269|PubMed:21518792}.
CC -!- DOMAIN: The C-terminal 195 amino acids of PTB are sufficient for
CC specific RNA binding.
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DR EMBL; X52101; CAA36321.1; -; mRNA.
DR AlphaFoldDB; P17225; -.
DR BMRB; P17225; -.
DR SMR; P17225; -.
DR CORUM; P17225; -.
DR IntAct; P17225; 4.
DR MINT; P17225; -.
DR STRING; 10090.ENSMUSP00000126192; -.
DR iPTMnet; P17225; -.
DR PhosphoSitePlus; P17225; -.
DR SwissPalm; P17225; -.
DR EPD; P17225; -.
DR jPOST; P17225; -.
DR MaxQB; P17225; -.
DR PeptideAtlas; P17225; -.
DR PRIDE; P17225; -.
DR ProteomicsDB; 291581; -.
DR TopDownProteomics; P17225; -.
DR MGI; MGI:97791; Ptbp1.
DR eggNOG; KOG1190; Eukaryota.
DR InParanoid; P17225; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR ChiTaRS; Ptbp1; mouse.
DR PRO; PR:P17225; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P17225; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0001069; F:regulatory region RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IPI:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:ARUK-UCL.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:ARUK-UCL.
DR GO; GO:0033119; P:negative regulation of RNA splicing; ISO:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS: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; IEA:UniProtKB-KW.
DR CDD; cd12777; RRM1_PTBP1; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
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; 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 Acetylation; Activator; Direct protein sequencing; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Ubl conjugation.
FT CHAIN 1..527
FT /note="Polypyrimidine tract-binding protein 1"
FT /id="PRO_0000081738"
FT DOMAIN 58..142
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 183..259
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 335..386
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 450..525
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
SQ SEQUENCE 527 AA; 56478 MW; F18FDF376010D76A CRC64;
MDGIVPDIAV GTKRGSDELF STCVSNGPFI MSSSASAANG NDSKKFKGDN RSAGVPSRVI
HVRKLPSDVT EGEVISLGLP FGKVTNLLML KGKNQAFIEM NTEEAANTMV NYYTSVAPVL
RGQPIYIQFS NHKELKTDSS PNQVRAQAAL QAVNSVQSGN LALAASAAAV DAGMAMAGQS
PVLRIIVENL FYPVTLDVLH QIFSKFGTVL KIITFTKNNQ FQALLQYADP VSAQHAKLSL
DGQNIYNACC TLRIDFSKLT SLNVKYNNDK SRDYTRPDLP SGDSQPSLDQ TMAAAFGLSV
PNVHGALAPL AIPSAAAAAA ASRIAIPGLA GAGNSVLLVS NLNPERVTPQ SLFILFGVYG
DVQRVKILFN KKENALVQMA DGSQAQLGEP PERAQAAREV SAHYTVQASE CAAAREGQED
QGLTKDYGSS PLRFKKPGSK NFQNIFPPSA TLHLSNIPPS VSEDDLKSLF SSNGGVVKGF
KFFQKDRKMA LIQMGSVEEA VQALIELHNH DLGENHHLRV SFSKSTI
