ID   HEK2_YEAST              Reviewed;         381 AA.
AC   P38199; D6VPW7; E9P8X5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Heterogeneous nuclear rnp K-like protein 2;
DE   AltName: Full=KH domain-containing protein 1;
GN   Name=HEK2; Synonyms=KHD1; OrderedLocusNames=YBL032W; ORFNames=YBL0418;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7725803; DOI=10.1002/yea.320101217;
RA   van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A.;
RT   "Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the
RT   ribosomal protein L19 as well as proteins with homologies to components of
RT   the hnRNP and snRNP complexes and to the human proliferation-associated
RT   p120 antigen.";
RL   Yeast 10:1663-1673(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   DOMAIN.
RX   PubMed=10331606;
RX   DOI=10.1002/(sici)1096-8628(19990528)84:3<272::aid-ajmg21>3.3.co;2-4;
RA   Currie J.R., Brown W.T.;
RT   "KH domain-containing proteins of yeast: absence of a fragile X gene
RT   homologue.";
RL   Am. J. Med. Genet. 84:272-276(1999).
RN   [6]
RP   RNA-BINDING, AND FUNCTION.
RX   PubMed=11867544; DOI=10.1093/emboj/21.5.1158;
RA   Irie K., Tadauchi T., Takizawa P.A., Vale R.D., Matsumoto K.,
RA   Herskowitz I.;
RT   "The Khd1 protein, which has three KH RNA-binding motifs, is required for
RT   proper localization of ASH1 mRNA in yeast.";
RL   EMBO J. 21:1158-1167(2002).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11739741; DOI=10.1128/mcb.22.1.286-297.2002;
RA   Denisenko O., Bomsztyk K.;
RT   "Yeast hnRNP K-like genes are involved in regulation of the telomeric
RT   position effect and telomere length.";
RL   Mol. Cell. Biol. 22:286-297(2002).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   RNA-BINDING.
RX   PubMed=16010288;
RA   Paziewska A., Wyrwicz L.S., Ostrowski J.;
RT   "The binding activity of yeast RNAs to yeast Hek2p and mammalian hnRNP K
RT   proteins, determined using the three-hybrid system.";
RL   Cell. Mol. Biol. Lett. 10:227-235(2005).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [12]
RP   FUNCTION, RNA-BINDING, AND PHOSPHORYLATION.
RX   PubMed=17588515; DOI=10.1016/j.molcel.2007.05.016;
RA   Paquin N., Menade M., Poirier G., Donato D., Drouet E., Chartrand P.;
RT   "Local activation of yeast ASH1 mRNA translation through phosphorylation of
RT   Khd1p by the casein kinase Yck1p.";
RL   Mol. Cell 26:795-809(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [14]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18067921; DOI=10.1016/j.jmb.2007.11.001;
RA   Denisenko O., Bomsztyk K.;
RT   "Epistatic interaction between the K-homology domain protein HEK2 and SIR1
RT   at HMR and telomeres in yeast.";
RL   J. Mol. Biol. 375:1178-1187(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-362, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [16]
RP   FUNCTION, AND RNA-BINDING.
RX   PubMed=18805955; DOI=10.1261/rna.1016508;
RA   Hasegawa Y., Irie K., Gerber A.P.;
RT   "Distinct roles for Khd1p in the localization and expression of bud-
RT   localized mRNAs in yeast.";
RL   RNA 14:2333-2347(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [18]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20953064; DOI=10.1247/csf.10011;
RA   Mauchi N., Ohtake Y., Irie K.;
RT   "Stability control of MTL1 mRNA by the RNA-binding protein Khd1p in
RT   yeast.";
RL   Cell Struct. Funct. 35:95-105(2010).
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 such as the MTL1 mRNA. Involved in structural and
CC       functional organization of telomeric chromatin and regulates silencing
CC       at the HMR locus. {ECO:0000269|PubMed:11739741,
CC       ECO:0000269|PubMed:11867544, ECO:0000269|PubMed:17588515,
CC       ECO:0000269|PubMed:18067921, ECO:0000269|PubMed:18805955,
CC       ECO:0000269|PubMed:20953064}.
CC   -!- SUBUNIT: Binds RNA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. Nucleus.
CC       Chromosome, telomere.
CC   -!- PTM: Phosphorylated by the plasma membrane-anchored casein kinase YCK1.
CC       Phosphorylation at its C-terminus reduces its RNA-binding capacity.
CC       {ECO:0000269|PubMed:17588515}.
CC   -!- MISCELLANEOUS: Present with 15600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HEK2 family. {ECO:0000305}.
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DR   EMBL; X77291; CAA54496.1; -; Genomic_DNA.
DR   EMBL; Z35793; CAA84852.1; -; Genomic_DNA.
DR   EMBL; AY692814; AAT92833.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07087.1; -; Genomic_DNA.
DR   PIR; S45766; S45766.
DR   RefSeq; NP_009521.1; NM_001178272.1.
DR   AlphaFoldDB; P38199; -.
DR   SMR; P38199; -.
DR   BioGRID; 32665; 1194.
DR   DIP; DIP-3934N; -.
DR   IntAct; P38199; 51.
DR   MINT; P38199; -.
DR   STRING; 4932.YBL032W; -.
DR   iPTMnet; P38199; -.
DR   MaxQB; P38199; -.
DR   PaxDb; 4932-YBL032W; -.
DR   PeptideAtlas; P38199; -.
DR   EnsemblFungi; YBL032W_mRNA; YBL032W; YBL032W.
DR   GeneID; 852248; -.
DR   KEGG; sce:YBL032W; -.
DR   AGR; SGD:S000000128; -.
DR   SGD; S000000128; HEK2.
DR   VEuPathDB; FungiDB:YBL032W; -.
DR   eggNOG; KOG2190; Eukaryota.
DR   GeneTree; ENSGT00940000153434; -.
DR   HOGENOM; CLU_022670_2_0_1; -.
DR   InParanoid; P38199; -.
DR   OMA; TERSYFP; -.
DR   OrthoDB; 378620at2759; -.
DR   BioCyc; YEAST:G3O-28935-MONOMER; -.
DR   Reactome; R-SCE-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   BioGRID-ORCS; 852248; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P38199; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38199; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IDA:SGD.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0008298; P:intracellular mRNA localization; IDA:SGD.
DR   GO; GO:0048255; P:mRNA stabilization; IMP:SGD.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IGI:SGD.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR   CDD; cd00105; KH-I; 1.
DR   CDD; cd22455; KH-I_Rnc1_rpt1; 1.
DR   CDD; cd22456; KH-I_Rnc1_rpt2; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR10288:SF142; RNA-BINDING PROTEIN PASILLA; 1.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Cytoplasm; mRNA transport; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Telomere;
KW   Translation regulation; Transport.
FT   CHAIN           1..381
FT                   /note="Heterogeneous nuclear rnp K-like protein 2"
FT                   /id="PRO_0000050161"
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:0007744|PubMed:17287358"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        362
FT                   /note="S -> P (in Ref. 4; AAT92833)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41683 MW;  0A8752961EB77DC9 CRC64;
     MSQFFEAATP VAIPTNNTNG GSSDAGSAAT GGAPVVGTTA QPTINHRLLL SLKEAAKIIG
     TKGSTISRIR AANAVKIGIS 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 QENHDNKEEQ S
//