ID HNRPD_MOUSE Reviewed; 355 AA. AC Q60668; Q60667; Q80ZJ0; Q91X94; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 04-AUG-2003, sequence version 2. DT 27-MAR-2024, entry version 202. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein D0; DE Short=hnRNP D0; DE AltName: Full=AU-rich element RNA-binding protein 1; GN Name=Hnrnpd; Synonyms=Auf1, Hnrpd; 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] OF 1-228 (ISOFORMS 2/4), AND NUCLEOTIDE SEQUENCE RP [MRNA] OF 25-355 (ISOFORM 3). RC STRAIN=BALB/cJ; TISSUE=Embryo; RX PubMed=7959009; DOI=10.1016/0378-1119(94)90168-6; RA Ehrenman K., Long L., Wagner B.J., Brewer G.; RT "Characterization of cDNAs encoding the murine A+U-rich RNA-binding protein RT AUF1."; RL Gene 149:315-319(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 5-355 (ISOFORM 1). RC TISSUE=Brain, and Salivary 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 184-197, 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-83, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-83; SER-190 AND RP THR-193, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-272; ARG-278; ARG-282 AND RP ARG-345, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-280 AND ARG-282 (ISOFORM RP 3), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-261 AND ARG-263 (ISOFORM 4), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Binds with high affinity to RNA molecules that contain AU- CC rich elements (AREs) found within the 3'-UTR of many proto-oncogenes CC and cytokine mRNAs. Also binds to double- and single-stranded DNA CC sequences in a specific manner and functions a transcription factor. CC Each of the RNA-binding domains specifically can bind solely to a CC single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to CC the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA CC oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the CC telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to CC DNA inhibits the formation of DNA quadruplex structure which may play a CC role in telomere elongation. May be involved in translationally coupled CC mRNA turnover. Implicated with other RNA-binding proteins in the CC cytoplasmic deadenylation/translational and decay interplay of the FOS CC mRNA mediated by the major coding-region determinant of instability CC (mCRD) domain. May play a role in the regulation of the rhythmic CC expression of circadian clock core genes. Directly binds to the 3'UTR CC of CRY1 mRNA and induces CRY1 rhythmic translation. May also be CC involved in the regulation of PER2 translation. CC {ECO:0000250|UniProtKB:Q14103}. CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex CC containing untranslated mRNAs. Part of a complex associated with the CC FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP. CC Interacts with IGF2BP2. Interacts with GTPBP1. Interacts with EIF4G1; CC the interaction requires RNA. Interacts with EIF3B and RPS3. CC {ECO:0000250|UniProtKB:Q14103}. CC -!- INTERACTION: CC Q60668; P06151: Ldha; NbExp=2; IntAct=EBI-299932, EBI-444940; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14103}. Cytoplasm CC {ECO:0000250|UniProtKB:Q14103}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. Component of ribonucleosomes. CC Cytoplasmic localization oscillates diurnally. CC {ECO:0000250|UniProtKB:Q14103}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q60668-1; Sequence=Displayed; CC Name=2; CC IsoId=Q60668-2; Sequence=VSP_007940; CC Name=3; Synonyms=muAUF1-3; CC IsoId=Q60668-3; Sequence=VSP_007941; CC Name=4; CC IsoId=Q60668-4; Sequence=VSP_007940, VSP_007941; CC -!- PTM: Methylated by PRMT1, in an insulin-dependent manner. The PRMT1- CC mediated methylation regulates its phosphorylation (By similarity). CC {ECO:0000250|UniProtKB:Q14103}. CC -!- PTM: Arg-345 is dimethylated, probably to asymmetric dimethylarginine. CC {ECO:0000250|UniProtKB:Q14103}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA64653.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAA64653.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305}; CC Sequence=AAA64654.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAA64654.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305}; 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; U11273; AAA64653.1; ALT_SEQ; mRNA. DR EMBL; U11274; AAA64654.1; ALT_SEQ; mRNA. DR EMBL; BC011172; AAH11172.2; -; mRNA. DR EMBL; BC049098; AAH49098.1; -; mRNA. DR CCDS; CCDS39180.1; -. [Q60668-2] DR CCDS; CCDS39181.1; -. [Q60668-3] DR CCDS; CCDS39182.1; -. [Q60668-1] DR CCDS; CCDS51571.1; -. [Q60668-4] DR PIR; I49069; I49069. DR PIR; I49070; I49070. DR RefSeq; NP_001070733.1; NM_001077265.2. [Q60668-1] DR RefSeq; NP_001070734.1; NM_001077266.2. DR RefSeq; NP_001070735.1; NM_001077267.2. DR RefSeq; NP_031542.2; NM_007516.3. [Q60668-3] DR RefSeq; XP_006534798.1; XM_006534735.3. [Q60668-1] DR AlphaFoldDB; Q60668; -. DR SMR; Q60668; -. DR BioGRID; 198279; 53. DR ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex. DR DIP; DIP-31411N; -. DR IntAct; Q60668; 14. DR MINT; Q60668; -. DR STRING; 10090.ENSMUSP00000132735; -. DR GlyGen; Q60668; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q60668; -. DR PhosphoSitePlus; Q60668; -. DR SwissPalm; Q60668; -. DR EPD; Q60668; -. DR jPOST; Q60668; -. DR MaxQB; Q60668; -. DR PaxDb; 10090-ENSMUSP00000132735; -. DR PeptideAtlas; Q60668; -. DR ProteomicsDB; 269614; -. [Q60668-1] DR ProteomicsDB; 269615; -. [Q60668-2] DR ProteomicsDB; 269616; -. [Q60668-3] DR ProteomicsDB; 269617; -. [Q60668-4] DR Pumba; Q60668; -. DR Antibodypedia; 1448; 510 antibodies from 33 providers. DR DNASU; 11991; -. DR Ensembl; ENSMUST00000019128.15; ENSMUSP00000019128.9; ENSMUSG00000000568.16. [Q60668-3] DR Ensembl; ENSMUST00000172361.8; ENSMUSP00000132735.2; ENSMUSG00000000568.16. [Q60668-1] DR GeneID; 11991; -. DR KEGG; mmu:11991; -. DR UCSC; uc008ygt.2; mouse. [Q60668-1] DR UCSC; uc008ygu.2; mouse. [Q60668-3] DR AGR; MGI:101947; -. DR CTD; 3184; -. DR MGI; MGI:101947; Hnrnpd. DR VEuPathDB; HostDB:ENSMUSG00000000568; -. DR eggNOG; KOG0118; Eukaryota. DR GeneTree; ENSGT00940000158010; -. DR InParanoid; Q60668; -. DR OMA; LQDEHTI; -. DR OrthoDB; 3127428at2759; -. DR PhylomeDB; Q60668; -. DR TreeFam; TF314808; -. DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway. DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA. DR BioGRID-ORCS; 11991; 10 hits in 80 CRISPR screens. DR ChiTaRS; Hnrnpd; mouse. DR PRO; PR:Q60668; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q60668; Protein. DR Bgee; ENSMUSG00000000568; Expressed in embryonic post-anal tail and 267 other cell types or tissues. DR ExpressionAtlas; Q60668; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; ISO:MGI. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI. DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:MGI. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:MGI. DR GO; GO:0003729; F:mRNA binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB. DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB. DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISO:MGI. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl. DR GO; GO:0071732; P:cellular response to nitric oxide; ISO:MGI. DR GO; GO:1904586; P:cellular response to putrescine; ISO:MGI. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0097167; P:circadian regulation of translation; ISS:UniProtKB. DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI. DR GO; GO:1990828; P:hepatocyte dedifferentiation; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0048255; P:mRNA stabilization; ISO:MGI. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI. DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; IMP:BHF-UCL. DR GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0043488; P:regulation of mRNA stability; IMP:MGI. DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL. DR GO; GO:0051592; P:response to calcium ion; ISO:MGI. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:1901355; P:response to rapamycin; ISO:MGI. DR GO; GO:1904383; P:response to sodium phosphate; ISO:MGI. DR CDD; cd12756; RRM1_hnRNPD; 1. DR CDD; cd12583; RRM2_hnRNPD; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR48033:SF3; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0; 1. DR PANTHER; PTHR48033; RNA-BINDING (RRM/RBD/RNP MOTIFS) FAMILY PROTEIN; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. DR Genevisible; Q60668; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Biological rhythms; Cytoplasm; KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT CHAIN 2..355 FT /note="Heterogeneous nuclear ribonucleoprotein D0" FT /id="PRO_0000081850" FT DOMAIN 97..179 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 182..261 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 67..91 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 119 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 127 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 165 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 193 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 243 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 251 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 271 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 272 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 278 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 280 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 282 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 345 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 345 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT MOD_RES 345 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 72 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT CROSSLNK 129 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT CROSSLNK 197 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q14103" FT VAR_SEQ 74..92 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_007940" FT VAR_SEQ 285..334 FT /note="GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN FT -> D (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7959009" FT /id="VSP_007941" FT CONFLICT 22..23 FT /note="SA -> G (in Ref. 1; AAA64653)" FT /evidence="ECO:0000305" FT CONFLICT 35..38 FT /note="AQGP -> RRA (in Ref. 1; AAA64654)" FT /evidence="ECO:0000305" FT CONFLICT 35..37 FT /note="AQG -> RR (in Ref. 1; AAA64653)" FT /evidence="ECO:0000305" FT CONFLICT 50..53 FT /note="GSAA -> LCG (in Ref. 1; AAA64654)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="N -> K (in Ref. 1; AAA64654)" FT /evidence="ECO:0000305" FT CONFLICT 227..228 FT /note="FI -> ID (in Ref. 1; AAA64653)" FT /evidence="ECO:0000305" FT MOD_RES Q60668-3:280 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q60668-3:282 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q60668-4:261 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q60668-4:263 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" SQ SEQUENCE 355 AA; 38354 MW; 5941DFC6F65B88DF CRC64; MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAAAAQGPAA AAGSGSGGGG SAAGGTEGGS AEAEGAKIDA SKNEEDEGHS NSSPRHTEAA AAQREEWKMF IGGLSWDTTK KDLKDYFSKF GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY //