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 02-JUN-2021, entry version 36. 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; Saccharomycetes; OC 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., Netto O.V.C., RA Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F., RA Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H., RA Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D., RA 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 of CC transcripts in the cell. RNA localization is a widespread mechanism for CC achieving localized protein synthesis. Required for the asymmetric CC localization to the daughter cell nucleus of the ASH1 transcript, CC coding for a specific repressor of transcription. Overexpression CC inhibits translation of the ASH1 transcript. Involved in the stability CC of transcripts, like the MTL1 mRNA. Involved in structural and CC functional organization of telomeric chromatin and regulates silencing CC at the HMR locus (By 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 YCK1. CC Phosphorylation at its C-terminus reduces its RNA-binding capacity (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HEK2 family. {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; ACFL01000072; EEU07706.1; -; Genomic_DNA. DR SMR; C7GND0; -. DR Proteomes; UP000008073; Unassembled WGS sequence. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; 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 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 3: Inferred from homology; KW Chromatin regulator; Chromosome; Cytoplasm; mRNA transport; Nucleus; KW Phosphoprotein; Repeat; RNA-binding; Telomere; Translation regulation; KW Transport. FT CHAIN 1..381 FT /note="Heterogeneous nuclear rnp K-like protein 2" FT /id="PRO_0000408193" FT DOMAIN 43..107 FT /note="KH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 156..221 FT /note="KH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 258..326 FT /note="KH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 344..381 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..26 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 360..381 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 358 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38199" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38199" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38199" 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 //