PTBP2_MOUSE
ID PTBP2_MOUSE Reviewed; 531 AA.
AC Q91Z31; Q7TNW7; Q9CUW2; Q9QYC2; Q9R0V9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Polypyrimidine tract-binding protein 2 {ECO:0000305};
DE AltName: Full=Brain-enriched polypyrimidine tract-binding protein;
DE Short=Brain-enriched PTB;
DE AltName: Full=Neural polypyrimidine tract-binding protein;
DE AltName: Full=RRM-type RNA-binding protein brPTB;
GN Name=Ptbp2 {ECO:0000312|MGI:MGI:1860489}; Synonyms=Brptb, Nptb;
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] (ISOFORM 2), FUNCTION, INTERACTION WITH NOVA1
RP AND NOVA2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain;
RX PubMed=10829067; DOI=10.1073/pnas.110128397;
RA Polydorides A.D., Okano H.J., Yang Y.Y.L., Stefani G., Darnell R.B.;
RT "A brain-enriched polypyrimidine tract-binding protein antagonizes the
RT ability of Nova to regulate neuron-specific alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6350-6355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 421-531 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-361.
RX PubMed=14667811; DOI=10.1016/s0888-7543(03)00207-6;
RA Rahman L., Bliskovski V., Kaye F.J., Zajac-Kaye M.;
RT "Evolutionary conservation of a 2-kb intronic sequence flanking a tissue-
RT specific alternative exon in the PTBP2 gene.";
RL Genomics 83:76-84(2004).
RN [5]
RP FUNCTION.
RX PubMed=11726525; DOI=10.1093/emboj/20.23.6899;
RA Pilipenko E.V., Viktorova E.G., Guest S.T., Agol V.I., Roos R.P.;
RT "Cell-specific proteins regulate viral RNA translation and virus-induced
RT disease.";
RL EMBO J. 20:6899-6908(2001).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11231079; DOI=10.1016/s0925-4773(00)00566-9;
RA Lillevaeli K., Kulla A., Oerd T.;
RT "Comparative expression analysis of the genes encoding polypyrimidine tract
RT binding protein (PTB) and its neural homologue (brPTB) in prenatal and
RT postnatal mouse brain.";
RL Mech. Dev. 101:217-220(2001).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=12213192; DOI=10.1006/geno.2002.6826;
RA Rahman L., Bliskovski V., Reinhold W., Zajac-Kaye M.;
RT "Alternative splicing of brain-specific PTB defines a tissue-specific
RT isoform pattern that predicts distinct functional roles.";
RL Genomics 80:245-249(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [10]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=30638744; DOI=10.1016/j.neuron.2018.12.019;
RA Saito Y., Yuan Y., Zucker-Scharff I., Fak J.J., Jereb S., Tajima Y.,
RA Licatalosi D.D., Darnell R.B.;
RT "Differential NOVA2-Mediated Splicing in Excitatory and Inhibitory Neurons
RT Regulates Cortical Development and Cerebellar Function.";
RL Neuron 101:707-720.e5(2019).
CC -!- FUNCTION: RNA-binding protein which binds to intronic polypyrimidine
CC tracts and mediates negative regulation of exons splicing
CC (PubMed:10829067, PubMed:30638744). May antagonize in a tissue-specific
CC manner the ability of NOVA1 to activate exon selection
CC (PubMed:10829067). In addition to its function in pre-mRNA splicing,
CC also plays a role in the regulation of translation (PubMed:11726525).
CC {ECO:0000269|PubMed:10829067, ECO:0000269|PubMed:11726525,
CC ECO:0000269|PubMed:30638744}.
CC -!- SUBUNIT: Monomer. Identified in a mRNP complex, at least composed of
CC DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2,
CC STAU1, STAU2, SYNCRIP and YBX1. Part of a ternary complex containing
CC KHSRP and HNRPH1 (By similarity). Interacts with NOVA1; the interaction
CC is direct (PubMed:10829067). Interacts with NOVA2; the interaction is
CC direct (PubMed:10829067). {ECO:0000250|UniProtKB:Q9UKA9,
CC ECO:0000269|PubMed:10829067}.
CC -!- INTERACTION:
CC Q91Z31; Q9WVE0: Aicda; NbExp=4; IntAct=EBI-647632, EBI-3835567;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10829067}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91Z31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91Z31-2; Sequence=VSP_018019;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain, including cerebellum,
CC brainstem, spinal cord, and hypothalamus. Also expressed in the
CC peripheral nervous system and neural crest derivatives, including the
CC dorsal root and trigeminal ganglia, the cochlear spiral and intestinal
CC ganglion cells, and the adrenal medulla. Also detected to a lower
CC extent in testis, heart, liver, lung, skeletal muscle and thymus (at
CC protein level). {ECO:0000269|PubMed:10829067,
CC ECO:0000269|PubMed:11231079}.
CC -!- DEVELOPMENTAL STAGE: Expressed in whole brain tissues from 11.5 dpc to
CC adulthood. {ECO:0000269|PubMed:10829067, ECO:0000269|PubMed:11231079}.
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DR EMBL; AF095718; AAF21807.2; -; mRNA.
DR EMBL; AK013734; BAB28977.1; -; mRNA.
DR EMBL; AK137348; BAE23317.1; -; mRNA.
DR EMBL; BC010255; AAH10255.1; -; mRNA.
DR EMBL; AY333752; AAQ01150.1; -; Genomic_DNA.
DR EMBL; BK000527; DAA00061.1; -; mRNA.
DR CCDS; CCDS38616.1; -. [Q91Z31-2]
DR CCDS; CCDS80010.1; -. [Q91Z31-1]
DR RefSeq; NP_001297640.1; NM_001310711.1. [Q91Z31-1]
DR RefSeq; NP_062423.1; NM_019550.2. [Q91Z31-2]
DR AlphaFoldDB; Q91Z31; -.
DR BMRB; Q91Z31; -.
DR SMR; Q91Z31; -.
DR BioGRID; 207834; 16.
DR CORUM; Q91Z31; -.
DR IntAct; Q91Z31; 2.
DR STRING; 10090.ENSMUSP00000029780; -.
DR iPTMnet; Q91Z31; -.
DR PhosphoSitePlus; Q91Z31; -.
DR SwissPalm; Q91Z31; -.
DR EPD; Q91Z31; -.
DR jPOST; Q91Z31; -.
DR MaxQB; Q91Z31; -.
DR PaxDb; Q91Z31; -.
DR PeptideAtlas; Q91Z31; -.
DR PRIDE; Q91Z31; -.
DR ProteomicsDB; 291611; -. [Q91Z31-1]
DR ProteomicsDB; 291612; -. [Q91Z31-2]
DR Antibodypedia; 19957; 230 antibodies from 31 providers.
DR DNASU; 56195; -.
DR Ensembl; ENSMUST00000029780; ENSMUSP00000029780; ENSMUSG00000028134. [Q91Z31-2]
DR Ensembl; ENSMUST00000200097; ENSMUSP00000143510; ENSMUSG00000028134. [Q91Z31-1]
DR GeneID; 56195; -.
DR KEGG; mmu:56195; -.
DR UCSC; uc008rdi.1; mouse. [Q91Z31-1]
DR UCSC; uc008rdk.2; mouse. [Q91Z31-2]
DR CTD; 58155; -.
DR MGI; MGI:1860489; Ptbp2.
DR VEuPathDB; HostDB:ENSMUSG00000028134; -.
DR eggNOG; KOG1190; Eukaryota.
DR GeneTree; ENSGT01050000244924; -.
DR InParanoid; Q91Z31; -.
DR OMA; NLGESHH; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q91Z31; -.
DR TreeFam; TF319824; -.
DR BioGRID-ORCS; 56195; 0 hits in 108 CRISPR screens.
DR ChiTaRS; Ptbp2; mouse.
DR PRO; PR:Q91Z31; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91Z31; protein.
DR Bgee; ENSMUSG00000028134; Expressed in spermatocyte and 271 other tissues.
DR ExpressionAtlas; Q91Z31; baseline and differential.
DR Genevisible; Q91Z31; MM.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:MGI.
DR GO; GO:0033119; P:negative regulation of RNA splicing; ISO:MGI.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR CDD; cd12778; RRM1_PTBP2; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
DR CDD; cd12696; RRM3_PTBP2; 1.
DR CDD; cd12702; RRM4_PTBP2; 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; IPR035002; PTBP2_RRM1.
DR InterPro; IPR034799; PTBP2_RRM3.
DR InterPro; IPR034800; PTBP2_RRM4.
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; Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..531
FT /note="Polypyrimidine tract-binding protein 2"
FT /id="PRO_0000232929"
FT DOMAIN 59..133
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 181..257
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 338..412
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 455..529
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA9"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT VAR_SEQ 489
FT /note="Q -> QR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10829067,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018019"
FT CONFLICT 93
FT /note="G -> E (in Ref. 3; AAH10255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 57489 MW; 3A93CA4E3E1D6AA3 CRC64;
MDGIVTEVAV GVKRGSDELL SGSVLSSPNS NMSGMVVTAN GNDSKKFKGE DKMDGAPSRV
LHIRKLPGEV TETEVIALGL PFGKVTNILM LKGKNQAFLE LATEEAAITM VNYYSAVTPH
LRNQPIYIQY SNHKELKTDN TLNQRAQVVL QAVTAVQTAN TPLSGTTVSE SAVTPAQSPV
LRIIIDNMYY PVTLDVLHQI FSKFGAVLKI ITFTKNNQFQ ALLQYGDPVN AQQAKLALDG
QNIYNACCTL RIDFSKLVNL NVKYNNDKSR DYTRPDLPSG DGQPALDPAI AAAFAKETSL
LAVPGALSPL AIPNAAAAAA AAAAGRVGMP GVSAGGNTVL LVSNLNEEMV TPQSLFTLFG
VYGDVQRVKI LYNKKDSALI QMADGNQSQL AMNHLNGQKM YGKIIRVTLS KHQTVQLPRE
GLDDQGLTKD FGNSPLHRFK KPGSKNFQNI FPPSATLHLS NIPPSVAEED LRTLFANTGG
TVKAFKFFQD HKMALLQMAT VEEAIQALID LHNYNLGENH HLRVSFSKST I
