HEL2_YEAST
ID HEL2_YEAST Reviewed; 639 AA.
AC Q05580; D6VSQ0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=E3 ubiquitin-protein ligase HEL2 {ECO:0000305|PubMed:22570702};
DE EC=2.3.2.27 {ECO:0000269|PubMed:22570702};
DE AltName: Full=Histone E3 ligase 2 {ECO:0000303|PubMed:22570702};
DE AltName: Full=RING-type E3 ubiquitin transferase HEL2 {ECO:0000305};
GN Name=HEL2 {ECO:0000303|PubMed:22570702};
GN OrderedLocusNames=YDR266C {ECO:0000312|SGD:S000002674};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBC4, AND INTERACTION WITH
RP HISTONES H3 AND H4.
RX PubMed=22570702; DOI=10.1371/journal.pone.0036295;
RA Singh R.K., Gonzalez M., Kabbaj M.H., Gunjan A.;
RT "Novel E3 ubiquitin ligases that regulate histone protein levels in the
RT budding yeast Saccharomyces cerevisiae.";
RL PLoS ONE 7:E36295-E36295(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Probable ubiquitin-protein ligase involved in the
CC degradation-related ubiquitination of histones. Contributes to the
CC post-translational regulation of histone protein levels by
CC polyubiquitination of excess histones for subsequent degradation.
CC {ECO:0000269|PubMed:22570702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:22570702};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with the E2 ubiquitin-conjugating enzyme UBC4 and
CC histones H3 and H4. {ECO:0000269|PubMed:22570702}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U51030; AAB64455.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12110.1; -; Genomic_DNA.
DR PIR; S70126; S70126.
DR RefSeq; NP_010552.3; NM_001180574.3.
DR AlphaFoldDB; Q05580; -.
DR BioGRID; 32322; 107.
DR DIP; DIP-5369N; -.
DR IntAct; Q05580; 12.
DR MINT; Q05580; -.
DR STRING; 4932.YDR266C; -.
DR iPTMnet; Q05580; -.
DR MaxQB; Q05580; -.
DR PaxDb; Q05580; -.
DR PRIDE; Q05580; -.
DR EnsemblFungi; YDR266C_mRNA; YDR266C; YDR266C.
DR GeneID; 851859; -.
DR KEGG; sce:YDR266C; -.
DR SGD; S000002674; HEL2.
DR VEuPathDB; FungiDB:YDR266C; -.
DR eggNOG; KOG2231; Eukaryota.
DR GeneTree; ENSGT00390000014178; -.
DR HOGENOM; CLU_008515_2_0_1; -.
DR InParanoid; Q05580; -.
DR OMA; HTTCHKC; -.
DR BioCyc; YEAST:G3O-29836-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q05580; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05580; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0036205; P:histone catabolic process; IMP:SGD.
DR GO; GO:0016574; P:histone ubiquitination; IDA:SGD.
DR GO; GO:0061157; P:mRNA destabilization; IMP:SGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938; PTHR22938; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..639
FT /note="E3 ubiquitin-protein ligase HEL2"
FT /id="PRO_0000253811"
FT DOMAIN 222..292
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT ZN_FING 64..104
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 639 AA; 72756 MW; F9C28DFD6342B939 CRC64;
MSESVKENVT PTRNFRRTQG PQNNTKPHND RKNFRRKQKK NNLSAEPNLT TSSADDTDEE
NELCVICARK LTYVSLTPCH HKTCHICGFR QRALYNKKSC LICRTENEEV MFTDRIDGDI
SDKYNFCEKN EKYGINFTSE EVATETLNLL KFFCPLSKDE QVCDFGSFKK YNEHLKSEHN
RMICLICATH KHAFPCELEI FTQNQLRNHQ TKGNSEGFKG HPMCAFCSGK RFYSDDELYI
HMRNQHEKCH ICDKMNPASP QYFKDYNQLF DHFKHSHYVC TVQTCLDNKF VVFKDELELQ
AHILQEHGNI LKGKPKFFQS ELSTFISAPS RVIRERDDYD LPSISSLPGS SSGSRTDVRS
ASSPEESRLR LAERAKYYLE NSKEDFNKFS SYNEDYSKGR LSAEKLLESY KLLFTKPNAD
VYLLIHNLAE TFPKNSSKYN NLNAIYEQRE QTLARQTSLP SLSSDSSLSM SIGRGHWGGT
NDGGSAGAAL GVRNIKNLPT LKSPSASYDP FATTVKKNTL RPVQNIKRTT PQSVSYRTST
NTVAFSPTYL ESKKGSSSTS LNNSKDKLKS LNLPQLPPPK PKVQIPGLNR PQIADPKQWG
KKSSTQDTNV HDNLRELNTT SGGNKKKGKQ KQLLFHIGV
