ID HEK2_YEAS2 Reviewed; 381 AA. AC C7GND0; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 13-OCT-2009, sequence version 1. DT 07-JAN-2015, entry version 18. DE RecName: Full=Heterogeneous nuclear rnp K-like protein 2; DE AltName: Full=KH domain-containing protein 1; GN Name=HEK2; Synonyms=KHD1; ORFNames=C1Q_01761; OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=574961; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAY291; RX PubMed=19812109; DOI=10.1101/gr.091777.109; RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., RA Netto O.V.C., Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., RA Noronha M.F., Dominska M., Andrietta M.G.S., Andrietta S.R., RA Cunha A.F., Gomes L.H., Tavares F.C.A., Alcarde A.R., Dietrich F.S., RA McCusker J.H., Petes T.D., Pereira G.A.G.; RT "Genome structure of a Saccharomyces cerevisiae strain widely used in RT bioethanol production."; RL Genome Res. 19:2258-2270(2009). CC -!- FUNCTION: RNA-binding protein involved in the correct localization CC of transcripts in the cell. RNA localization is a widespread CC mechanism for achieving localized protein synthesis. Required for CC the asymmetric localization to the daughter cell nucleus of the CC ASH1 transcript, coding for a specific repressor of transcription. CC Overexpression inhibits translation of the ASH1 transcript. CC Involved in the stability of transcripts, like the MTL1 mRNA. CC Involved in structural and functional organization of telomeric CC chromatin and regulates silencing at the HMR locus (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Binds RNA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, P-body CC {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, telomere CC {ECO:0000250}. CC -!- PTM: Phosphorylated by the plasma membrane-Anchored casein kinase CC YCK1. Phosphorylation at its C-terminus reduces its RNA-binding CC capacity (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HEK2 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 3 KH domains. {ECO:0000255|PROSITE- CC ProRule:PRU00117}. 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; ACFL01000072; EEU07706.1; -; Genomic_DNA. DR OrthoDB; EOG77HDRG; -. DR Proteomes; UP000008073; Unassembled WGS sequence. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR Gene3D; 3.30.1370.10; -; 3. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR Pfam; PF00013; KH_1; 3. DR SMART; SM00322; KH; 3. DR SUPFAM; SSF54791; SSF54791; 3. DR PROSITE; PS50084; KH_TYPE_1; 3. PE 3: Inferred from homology; KW Chromatin regulator; Chromosome; Complete proteome; Cytoplasm; KW mRNA transport; Nucleus; Phosphoprotein; Repeat; RNA-binding; KW Telomere; Translation regulation; Transport. FT CHAIN 1 381 Heterogeneous nuclear rnp K-like protein FT 2. FT /FTId=PRO_0000408193. FT DOMAIN 43 107 KH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT DOMAIN 156 221 KH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT DOMAIN 258 326 KH 3. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT MOD_RES 358 358 Phosphoserine. {ECO:0000250}. FT MOD_RES 360 360 Phosphoserine. {ECO:0000250}. FT MOD_RES 362 362 Phosphoserine. {ECO:0000250}. SQ SEQUENCE 381 AA; 41698 MW; CAEAEEFBE6D77A5C CRC64; MSQFFEAATP VAIPTNNTNG GSSDAGSAAT GGAPVVGTTA QPTINHRLLL SLKEAAKIIG TKGSTISRIR AANSVKIGIS EKVPGCSDRI LSCAGNVINV ANAIGDIVDV LNKRNPENED AAEGEAEEHY YFHFLNHILP APSKDEIRDL QQLEDIGYVR LIVANSHISS IIGKAGATIK SLINKHGVKI VASKDFLPAS DERIIEIQGF PGSITNVLIE ISEIILSDVD VRFSTERSYF PHLKKSSGEP TSPSTSSNTR IELKIPELYV GAIIGRGMNR IKNLKTFTKT NIVVERKDDD DKDENFRKFI ITSKFPKNVK LAESMLLKNL NTEIEKRENY KRKLEAAEGD ATVVTERSDS ASFLEEKEEP QKNHDNKEEQ S //