ID DND1_HUMAN Reviewed; 353 AA. AC Q8IYX4; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 29-MAY-2024, entry version 160. DE RecName: Full=Dead end protein homolog 1; DE AltName: Full=RNA-binding motif, single-stranded-interacting protein 4; GN Name=DND1; Synonyms=RBMS4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12932328; DOI=10.1016/s0960-9822(03)00537-2; RA Weidinger G., Stebler J., Slanchev K., Dumstrei K., Wise C., RA Lovell-Badge R., Thisse C., Thisse B., Raz E.; RT "Dead end, a novel vertebrate germ plasm component, is required for RT zebrafish primordial germ cell migration and survival."; RL Curr. Biol. 13:1429-1434(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=18155131; DOI=10.1016/j.cell.2007.11.034; RA Kedde M., Strasser M.J., Boldajipour B., Oude Vrielink J.A., Slanchev K., RA le Sage C., Nagel R., Voorhoeve P.M., van Duijse J., Oerom U.A., Lund A.H., RA Perrakis A., Raz E., Agami R.; RT "RNA-binding protein Dnd1 inhibits microRNA access to target mRNA."; RL Cell 131:1273-1286(2007). CC -!- FUNCTION: RNA-binding factor that positively regulates gene expression CC by prohibiting miRNA-mediated gene suppression. Relieves miRNA CC repression in germline cells (By similarity). Prohibits the function of CC several miRNAs by blocking the accessibility of target mRNAs. Sequence- CC specific RNA-binding factor that binds specifically to U-rich regions CC (URRs) in the 3' untranslated region (3'-UTR) of several mRNAs. Does CC not bind to miRNAs. May play a role during primordial germ cell (PGC) CC survival (By similarity). However, does not seem to be essential for CC PGC migration (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:18155131}. CC -!- SUBUNIT: Interacts with APOBEC3. {ECO:0000250}. CC -!- INTERACTION: CC Q8IYX4; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-12071340, EBI-11987469; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18155131}. Cytoplasm CC {ECO:0000269|PubMed:18155131}. Note=Perinuclear germ granules, also CC called germ plasm or chromatoid body. Colocalizes in perinuclear sites CC with APOBEC3 (By similarity). {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; AY321065; AAQ63635.1; -; mRNA. DR EMBL; BC033496; AAH33496.1; -; mRNA. DR CCDS; CCDS4236.1; -. DR RefSeq; NP_919225.1; NM_194249.2. DR PDB; 6LE1; X-ray; 2.30 A; A=139-217. DR PDB; 7Q4L; NMR; -; A=12-235. DR PDBsum; 6LE1; -. DR PDBsum; 7Q4L; -. DR AlphaFoldDB; Q8IYX4; -. DR SMR; Q8IYX4; -. DR BioGRID; 131887; 19. DR IntAct; Q8IYX4; 8. DR STRING; 9606.ENSP00000445366; -. DR iPTMnet; Q8IYX4; -. DR PhosphoSitePlus; Q8IYX4; -. DR BioMuta; DND1; -. DR DMDM; 60389799; -. DR EPD; Q8IYX4; -. DR MassIVE; Q8IYX4; -. DR PaxDb; 9606-ENSP00000445366; -. DR PeptideAtlas; Q8IYX4; -. DR ProteomicsDB; 71258; -. DR Antibodypedia; 49888; 259 antibodies from 24 providers. DR DNASU; 373863; -. DR Ensembl; ENST00000542735.2; ENSP00000445366.1; ENSG00000256453.2. DR GeneID; 373863; -. DR KEGG; hsa:373863; -. DR MANE-Select; ENST00000542735.2; ENSP00000445366.1; NM_194249.3; NP_919225.1. DR UCSC; uc003lgt.4; human. DR AGR; HGNC:23799; -. DR CTD; 373863; -. DR DisGeNET; 373863; -. DR GeneCards; DND1; -. DR HGNC; HGNC:23799; DND1. DR HPA; ENSG00000256453; Group enriched (brain, testis). DR MIM; 609385; gene. DR neXtProt; NX_Q8IYX4; -. DR OpenTargets; ENSG00000256453; -. DR PharmGKB; PA134931157; -. DR VEuPathDB; HostDB:ENSG00000256453; -. DR eggNOG; KOG0117; Eukaryota. DR GeneTree; ENSGT00940000159225; -. DR HOGENOM; CLU_022960_0_0_1; -. DR InParanoid; Q8IYX4; -. DR OMA; CERVNPV; -. DR OrthoDB; 3184171at2759; -. DR PhylomeDB; Q8IYX4; -. DR TreeFam; TF314932; -. DR PathwayCommons; Q8IYX4; -. DR SignaLink; Q8IYX4; -. DR BioGRID-ORCS; 373863; 40 hits in 1139 CRISPR screens. DR GenomeRNAi; 373863; -. DR Pharos; Q8IYX4; Tbio. DR PRO; PR:Q8IYX4; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q8IYX4; Protein. DR Bgee; ENSG00000256453; Expressed in primordial germ cell in gonad and 84 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:CACAO. DR GO; GO:0007281; P:germ cell development; IEA:Ensembl. DR GO; GO:0048255; P:mRNA stabilization; IBA:GO_Central. DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd20313; DSRM_DND1; 1. DR CDD; cd12487; RRM1_DND1; 1. DR CDD; cd12493; RRM2_DND1; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR044448; DND1_DSRM. DR InterPro; IPR034414; DND1_RRM1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR21245:SF4; DEAD END PROTEIN HOMOLOG 1; 1. DR PANTHER; PTHR21245; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; 1. DR Pfam; PF14709; DND1_DSRM; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Developmental protein; Nucleus; KW Reference proteome; Repeat; RNA-binding. FT CHAIN 1..353 FT /note="Dead end protein homolog 1" FT /id="PRO_0000081568" FT DOMAIN 58..136 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 140..213 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT HELIX 17..29 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:7Q4L" FT HELIX 71..81 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 100..107 FT /evidence="ECO:0007829|PDB:7Q4L" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 139..145 FT /evidence="ECO:0007829|PDB:6LE1" FT HELIX 151..158 FT /evidence="ECO:0007829|PDB:6LE1" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:6LE1" FT STRAND 165..172 FT /evidence="ECO:0007829|PDB:6LE1" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:6LE1" FT STRAND 180..188 FT /evidence="ECO:0007829|PDB:6LE1" FT HELIX 189..205 FT /evidence="ECO:0007829|PDB:6LE1" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:7Q4L" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:7Q4L" FT HELIX 218..232 FT /evidence="ECO:0007829|PDB:7Q4L" SQ SEQUENCE 353 AA; 38687 MW; 15014AA66BFD4F0F CRC64; MQSKRDCELW CERVNPENKA ALEAWVRETG IRLVQVNGQR KYGGPPPGWV GSPPPAGSEV FIGRLPQDVY EHQLIPLFQR VGRLYEFRLM MTFSGLNRGF AYARYSSRRG AQAAIATLHN HPLRPSCPLL VCRSTEKCEL SVDGLPPNLT RSALLLALQP LGPGLQEARL LPSPGPAPGQ IALLKFSSHR AAAMAKKALV EGQSHLCGEQ VAVEWLKPDL KQRLRQQLVG PFLRSPQPEG SQLALARDKL GFQGARATLQ LLCQRMKLGS PVFLTKCLGI GPAGWHRFWY QVVIPGHPVP FSGLIWVVLT LDGRDGHEVA KDAVSVRLLQ ALSESGANLL WSAGAEAGTM VKQ //