PTBP2_RAT
ID PTBP2_RAT Reviewed; 531 AA.
AC Q66H20; Q78ZE9; Q7TNW8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Polypyrimidine tract-binding protein 2 {ECO:0000305};
DE AltName: Full=Neural polypyrimidine tract-binding protein;
DE AltName: Full=PTB-like protein;
GN Name=Ptbp2 {ECO:0000312|RGD:1359267}; Synonyms=Nptb, Ptblp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RX PubMed=11694331; DOI=10.1016/s0165-5728(01)00427-1;
RA Tateiwa H., Gotoh N., Ichikawa M., Kikuchi T., Yoshimura N.;
RT "Molecular cloning and characterization of human PTB-like protein: a
RT possible retinal autoantigen of cancer-associated retinopathy.";
RL J. Neuroimmunol. 120:161-169(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Brown Norway; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-361.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA-binding protein which binds to intronic polypyrimidine
CC tracts and mediates negative regulation of exons splicing. May
CC antagonize in a tissue-specific manner the ability of NOVA1 to activate
CC exon selection. In addition to its function in pre-mRNA splicing, plays
CC also a role in the regulation of translation.
CC {ECO:0000250|UniProtKB:Q91Z31, ECO:0000250|UniProtKB:Q9UKA9}.
CC -!- SUBUNIT: Monomer. Interacts with NOVA1; the interaction is direct.
CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Part of a ternary complex containing KHSRP and HNRPH1 (By
CC similarity). Interacts with NOVA2; the interaction is direct (By
CC similarity). {ECO:0000250|UniProtKB:Q91Z31,
CC ECO:0000250|UniProtKB:Q9UKA9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91Z31}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66H20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66H20-2; Sequence=VSP_018020;
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DR EMBL; AJ010585; CAB54073.1; -; mRNA.
DR EMBL; BC082076; AAH82076.1; -; mRNA.
DR EMBL; AY333750; AAQ01148.1; -; Genomic_DNA.
DR RefSeq; NP_001005555.1; NM_001005555.1. [Q66H20-1]
DR RefSeq; XP_006233300.1; XM_006233238.3. [Q66H20-2]
DR AlphaFoldDB; Q66H20; -.
DR BMRB; Q66H20; -.
DR SMR; Q66H20; -.
DR STRING; 10116.ENSRNOP00000015036; -.
DR iPTMnet; Q66H20; -.
DR PhosphoSitePlus; Q66H20; -.
DR jPOST; Q66H20; -.
DR PaxDb; Q66H20; -.
DR PRIDE; Q66H20; -.
DR Ensembl; ENSRNOT00000104266; ENSRNOP00000091829; ENSRNOG00000010827. [Q66H20-2]
DR GeneID; 310820; -.
DR KEGG; rno:310820; -.
DR UCSC; RGD:1359267; rat. [Q66H20-1]
DR CTD; 58155; -.
DR RGD; 1359267; Ptbp2.
DR VEuPathDB; HostDB:ENSRNOG00000010827; -.
DR eggNOG; KOG1190; Eukaryota.
DR GeneTree; ENSGT01050000244924; -.
DR HOGENOM; CLU_015171_7_0_1; -.
DR InParanoid; Q66H20; -.
DR OMA; NLGESHH; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q66H20; -.
DR TreeFam; TF319824; -.
DR PRO; PR:Q66H20; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010827; Expressed in cerebellum and 19 other tissues.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0006376; P:mRNA splice site selection; ISO:RGD.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IMP:RGD.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
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_0000232930"
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:0000250|UniProtKB:Q91Z31"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z31"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 489
FT /note="Q -> QR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11694331"
FT /id="VSP_018020"
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
