PCBP1_MOUSE
ID PCBP1_MOUSE Reviewed; 356 AA.
AC P60335;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Poly(rC)-binding protein 1;
DE AltName: Full=Alpha-CP1;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein E1;
DE Short=hnRNP E1;
GN Name=Pcbp1;
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 [GENOMIC DNA / MRNA].
RX PubMed=10455157; DOI=10.1074/jbc.274.35.24849;
RA Makeyev A.V., Chkheidze A.N., Liebhaber S.A.;
RT "A set of highly conserved RNA-binding proteins, alphaCP-1 and alphaCP-2,
RT implicated in mRNA stabilization, are coexpressed from an intronless gene
RT and its intron-containing paralog.";
RL J. Biol. Chem. 274:24849-24857(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 326-346, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-189 AND SER-190, AND
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. {ECO:0000250}.
CC -!- INTERACTION:
CC P60335; Q99N13: Hdac9; NbExp=6; IntAct=EBI-309059, EBI-645361;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF139894; AAD51920.1; -; mRNA.
DR EMBL; AF139895; AAD51921.1; -; Genomic_DNA.
DR EMBL; BC069915; AAH69915.1; -; mRNA.
DR EMBL; BC004793; AAH04793.1; -; mRNA.
DR CCDS; CCDS20314.1; -.
DR RefSeq; NP_035995.1; NM_011865.3.
DR AlphaFoldDB; P60335; -.
DR SMR; P60335; -.
DR BioGRID; 204835; 94.
DR IntAct; P60335; 17.
DR MINT; P60335; -.
DR STRING; 10090.ENSMUSP00000054863; -.
DR iPTMnet; P60335; -.
DR PhosphoSitePlus; P60335; -.
DR SwissPalm; P60335; -.
DR REPRODUCTION-2DPAGE; IPI00128904; -.
DR REPRODUCTION-2DPAGE; P60335; -.
DR EPD; P60335; -.
DR jPOST; P60335; -.
DR MaxQB; P60335; -.
DR PaxDb; P60335; -.
DR PeptideAtlas; P60335; -.
DR PRIDE; P60335; -.
DR ProteomicsDB; 294026; -.
DR Antibodypedia; 16295; 449 antibodies from 37 providers.
DR DNASU; 23983; -.
DR Ensembl; ENSMUST00000053015; ENSMUSP00000054863; ENSMUSG00000051695.
DR GeneID; 23983; -.
DR KEGG; mmu:23983; -.
DR UCSC; uc009csc.1; mouse.
DR CTD; 5093; -.
DR MGI; MGI:1345635; Pcbp1.
DR VEuPathDB; HostDB:ENSMUSG00000051695; -.
DR eggNOG; KOG2190; Eukaryota.
DR GeneTree; ENSGT00940000161582; -.
DR HOGENOM; CLU_022670_0_1_1; -.
DR InParanoid; P60335; -.
DR OMA; GQDRCGD; -.
DR OrthoDB; 954970at2759; -.
DR PhylomeDB; P60335; -.
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; 23983; 20 hits in 59 CRISPR screens.
DR ChiTaRS; Pcbp1; mouse.
DR PRO; PR:P60335; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P60335; protein.
DR Bgee; ENSMUSG00000051695; Expressed in metanephric ureteric bud and 255 other tissues.
DR Genevisible; P60335; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0098847; F:sequence-specific single stranded DNA binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0008494; F:translation activator activity; TAS:MGI.
DR GO; GO:0006397; P:mRNA processing; TAS:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
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 Acetylation; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..356
FT /note="Poly(rC)-binding protein 1"
FT /id="PRO_0000050088"
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 279..343
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15365"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15365"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15365"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15365"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15365"
SQ SEQUENCE 356 AA; 37498 MW; 6D1A261276CA206D CRC64;
MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS EGNCPERIIT
LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL RLVVPATQCG SLIGKGGCKI
KEIRESTGAQ VQVAGDMLPN STERAITIAG VPQSVTECVK QICLVMLETL SQSPQGRVMT
IPYQPMPASS PVICAGGQDR CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ
VARQQSHFAM MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA
NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE KGMGCS
