PCBP2_MOUSE
ID PCBP2_MOUSE Reviewed; 362 AA.
AC Q61990; Q61383; Q62042;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Poly(rC)-binding protein 2;
DE AltName: Full=Alpha-CP2;
DE AltName: Full=CTBP;
DE Short=CBP;
DE AltName: Full=Putative heterogeneous nuclear ribonucleoprotein X;
DE Short=hnRNP X;
GN Name=Pcbp2; Synonyms=Cbp, Hnrnpx, Hnrpx;
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] (ISOFORMS 1 AND 2).
RX PubMed=8367306; DOI=10.1093/nar/21.16.3894;
RA Hahm K.B., Kim G., Turch C., Smale S.T.;
RT "Isolation of a murine gene encoding a nucleic acid-binding protein with
RT homology to hnRNP K.";
RL Nucleic Acids Res. 21:3894-3894(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM 2).
RC STRAIN=C57BL/6 X 129/Ola; TISSUE=Liver;
RX PubMed=8208614; DOI=10.1093/nar/22.10.1885;
RA Goller M., Funke B., Gehe-Becker C., Kroeger B., Lottspeich F., Horak I.;
RT "Murine protein which binds preferentially to oligo-C-rich single-stranded
RT nucleic acids.";
RL Nucleic Acids Res. 22:1885-1889(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA Horak I.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=10936052; DOI=10.1006/geno.2000.6244;
RA Makeyev A.V., Liebhaber S.A.;
RT "Identification of two novel mammalian genes establishes a subfamily of KH-
RT domain RNA-binding proteins.";
RL Genomics 67:301-316(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC preferentially to oligo dC. Major cellular poly(rC)-binding protein.
CC Binds also poly(rU). Negatively regulates cellular antiviral responses
CC mediated by MAVS signaling. It acts as an adapter between MAVS and the
CC E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitinationa and
CC degradation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135 (By
CC similarity). Interacts with MAVS (via C-terminus) and ITCH (via WW
CC domains) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q61990-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61990-2; Sequence=VSP_002820;
CC Name=3;
CC IsoId=Q61990-3; Sequence=VSP_002821;
CC -!- DOMAIN: The KH domains mediates poly(C) binding. {ECO:0000250}.
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DR EMBL; L19661; AAA03705.1; -; mRNA.
DR EMBL; X75947; CAA53546.1; -; mRNA.
DR EMBL; X97982; CAA66619.1; -; mRNA.
DR EMBL; AF236845; AAK14059.1; -; Genomic_DNA.
DR EMBL; AF236842; AAK14059.1; JOINED; Genomic_DNA.
DR EMBL; AF236843; AAK14059.1; JOINED; Genomic_DNA.
DR EMBL; AF236844; AAK14059.1; JOINED; Genomic_DNA.
DR CCDS; CCDS27884.1; -. [Q61990-3]
DR CCDS; CCDS49741.1; -. [Q61990-1]
DR CCDS; CCDS49742.1; -. [Q61990-2]
DR PIR; S78515; S78515.
DR RefSeq; NP_001096635.1; NM_001103165.1. [Q61990-1]
DR RefSeq; NP_001096636.1; NM_001103166.1. [Q61990-2]
DR RefSeq; NP_035172.2; NM_011042.2. [Q61990-3]
DR AlphaFoldDB; Q61990; -.
DR SMR; Q61990; -.
DR BioGRID; 202043; 30.
DR IntAct; Q61990; 19.
DR MINT; Q61990; -.
DR STRING; 10090.ENSMUSP00000076294; -.
DR iPTMnet; Q61990; -.
DR PhosphoSitePlus; Q61990; -.
DR SwissPalm; Q61990; -.
DR REPRODUCTION-2DPAGE; Q61990; -.
DR EPD; Q61990; -.
DR jPOST; Q61990; -.
DR MaxQB; Q61990; -.
DR PaxDb; Q61990; -.
DR PeptideAtlas; Q61990; -.
DR PRIDE; Q61990; -.
DR ProteomicsDB; 294027; -. [Q61990-1]
DR ProteomicsDB; 294028; -. [Q61990-2]
DR ProteomicsDB; 294029; -. [Q61990-3]
DR Antibodypedia; 15218; 279 antibodies from 36 providers.
DR DNASU; 18521; -.
DR Ensembl; ENSMUST00000077037; ENSMUSP00000076294; ENSMUSG00000056851. [Q61990-1]
DR Ensembl; ENSMUST00000078404; ENSMUSP00000077509; ENSMUSG00000056851. [Q61990-1]
DR Ensembl; ENSMUST00000229618; ENSMUSP00000155430; ENSMUSG00000056851. [Q61990-2]
DR Ensembl; ENSMUST00000229854; ENSMUSP00000155038; ENSMUSG00000056851. [Q61990-3]
DR GeneID; 18521; -.
DR KEGG; mmu:18521; -.
DR UCSC; uc007xvy.2; mouse. [Q61990-1]
DR UCSC; uc007xvz.2; mouse. [Q61990-2]
DR UCSC; uc009vat.1; mouse. [Q61990-3]
DR CTD; 5094; -.
DR MGI; MGI:108202; Pcbp2.
DR VEuPathDB; HostDB:ENSMUSG00000056851; -.
DR eggNOG; KOG2190; Eukaryota.
DR GeneTree; ENSGT00940000154129; -.
DR HOGENOM; CLU_022670_0_1_1; -.
DR InParanoid; Q61990; -.
DR OMA; SIAKEPH; -.
DR OrthoDB; 954970at2759; -.
DR PhylomeDB; Q61990; -.
DR TreeFam; TF318292; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 18521; 21 hits in 77 CRISPR screens.
DR ChiTaRS; Pcbp2; mouse.
DR PRO; PR:Q61990; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61990; protein.
DR Bgee; ENSMUSG00000056851; Expressed in retinal neural layer and 256 other tissues.
DR ExpressionAtlas; Q61990; baseline and differential.
DR Genevisible; Q61990; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:1990829; F:C-rich single-stranded DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0039694; P:viral RNA genome replication; ISO:MGI.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Immunity; Innate immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..362
FT /note="Poly(rC)-binding protein 2"
FT /id="PRO_0000050091"
FT DOMAIN 13..75
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 97..162
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 284..348
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15366"
FT VAR_SEQ 194..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8367306"
FT /id="VSP_002820"
FT VAR_SEQ 263..275
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002821"
SQ SEQUENCE 362 AA; 38222 MW; 70C8AF710E3BF3C0 CRC64;
MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT
LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI
KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLESP PKGVTIPYRP
KPSSSPVIFA GGQDRYSTGS DSASFPHTTP SMCLNPDLEG PPLEAYTIQG QYAIPQPDLT
KLHQLAMQQS HFPMTHGNTG FSGIESSSPE VKGYWAGLDA SAQTTSHELT IPNDLIGCII
GRQGAKINEI RQMSGAQIKI ANPVEGSTDR QVTITGSAAS ISLAQYLINV RLSSETGGMG
SS
