SNT2_YEAST
ID SNT2_YEAST Reviewed; 1403 AA.
AC P53127; D6VU17;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=E3 ubiquitin-protein ligase SNT2 {ECO:0000305|PubMed:22570702};
DE EC=2.3.2.27 {ECO:0000269|PubMed:22570702};
DE AltName: Full=Histone E3 ligase SNT2 {ECO:0000303|PubMed:22570702};
DE AltName: Full=RING-type E3 ubiquitin transferase SNT2 {ECO:0000305};
DE AltName: Full=SANT domain-containing protein 2 {ECO:0000303|PubMed:17142463};
GN Name=SNT2 {ECO:0000303|PubMed:17142463};
GN OrderedLocusNames=YGL131C {ECO:0000312|SGD:S000003099}; ORFNames=G2850;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1232.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840506;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<887::aid-yea971>3.0.co;2-d;
RA Escribano V., Eraso P., Portillo F., Mazon M.J.;
RT "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae
RT chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-
RT dependent enzyme and six new open reading frames.";
RL Yeast 12:887-892(1996).
RN [4]
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 [5]
RP INTERACTION WITH HISTONE H3.
RX PubMed=17142463; DOI=10.1074/jbc.c600286200;
RA Shi X., Kachirskaia I., Walter K.L., Kuo J.-H.A., Lake A., Davrazou F.,
RA Chan S.M., Martin D.G.E., Fingerman I.M., Briggs S.D., Howe L., Utz P.J.,
RA Kutateladze T.G., Lugovskoy A.A., Bedford M.T., Gozani O.;
RT "Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD
RT fingers as novel direct and selective binding modules of histone H3
RT methylated at either lysine 4 or lysine 36.";
RL J. Biol. Chem. 282:2450-2455(2007).
RN [6]
RP INTERACTION WITH ECM5 AND RPD3.
RX PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT "Chromatin Central: towards the comparative proteome by accurate mapping of
RT the yeast proteomic environment.";
RL Genome Biol. 9:R167.1-R167.22(2008).
RN [7]
RP IDENTIFICATION BY 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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ECM5 AND RPD3.
RX PubMed=23878396; DOI=10.1128/mcb.00025-13;
RA Baker L.A., Ueberheide B.M., Dewell S., Chait B.T., Zheng D., Allis C.D.;
RT "The yeast Snt2 protein coordinates the transcriptional response to
RT hydrogen peroxide-mediated oxidative stress.";
RL Mol. Cell. Biol. 33:3735-3748(2013).
CC -!- FUNCTION: Transcriptional regulator that, together with ECM5, recruits
CC histone deacetylase RPD3 to a small number of promoters of stress-
CC response genes in response to oxidative stress (PubMed:23878396).
CC Probable ubiquitin-protein ligase involved in the degradation-related
CC ubiquitination of histones. Contributes to the post-translational
CC regulation of histone protein levels by polyubiquitination of excess
CC histones for subsequent degradation (PubMed:22570702).
CC {ECO:0000269|PubMed:22570702, ECO:0000269|PubMed:23878396}.
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 -!- SUBUNIT: Component of the Snt2C complex composed of SNT2, ECM5 and
CC RPD3. Interacts with the E2 ubiquitin-conjugating enzyme UBC4 and
CC histones H3 and H4. Binding is enhanced to methylated histone H3K36me3.
CC {ECO:0000269|PubMed:17142463, ECO:0000269|PubMed:19040720,
CC ECO:0000269|PubMed:22570702, ECO:0000269|PubMed:23878396}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Note=Localizes to promoters of stress-
CC response genes in response to oxidative stress.
CC {ECO:0000269|PubMed:23878396}.
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DR EMBL; Z72654; CAA96843.1; -; Genomic_DNA.
DR EMBL; Z72652; CAA96841.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07978.1; -; Genomic_DNA.
DR PIR; S64142; S64142.
DR RefSeq; NP_011384.1; NM_001180996.1.
DR AlphaFoldDB; P53127; -.
DR BioGRID; 33120; 52.
DR ComplexPortal; CPX-1372; SNT2C histone deacetylase complex.
DR DIP; DIP-6540N; -.
DR IntAct; P53127; 17.
DR MINT; P53127; -.
DR STRING; 4932.YGL131C; -.
DR iPTMnet; P53127; -.
DR MaxQB; P53127; -.
DR PaxDb; P53127; -.
DR PRIDE; P53127; -.
DR EnsemblFungi; YGL131C_mRNA; YGL131C; YGL131C.
DR GeneID; 852746; -.
DR KEGG; sce:YGL131C; -.
DR SGD; S000003099; SNT2.
DR VEuPathDB; FungiDB:YGL131C; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_001514_2_0_1; -.
DR InParanoid; P53127; -.
DR OMA; FHVGCAH; -.
DR BioCyc; YEAST:G3O-30627-MON; -.
DR PRO; PR:P53127; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53127; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0048189; C:Lid2 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070211; C:Snt2C complex; IPI:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0036205; P:histone catabolic process; IMP:SGD.
DR GO; GO:0016574; P:histone ubiquitination; IDA:SGD.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IC:ComplexPortal.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR029617; Snt2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47672; PTHR47672; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 2.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1403
FT /note="E3 ubiquitin-protein ligase SNT2"
FT /id="PRO_0000202742"
FT DOMAIN 121..258
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 555..606
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 317..369
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1038..1097
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1041..1095
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 1105..1153
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1177..1231
FT /note="PHD-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 163203 MW; 758D3FB130DF2357 CRC64;
MPKEEDFQLP RRREAAKNVN YNEMEIDTKL VQQIQIAEKS GAKTKGSNSQ TPRNCKRTSN
PASRNEKFKY QKFLHDKNTC WNFIPTLPPS FRKNSRFSNI LDLDDAMIDL KKMSLFNTES
VLLSANDTIY MISEPAGEPY YVGRVVNFVS KPEFSNTIHE AIKTTSVFPA KFFQVRMNWF
YRPRDIQEHV NTFNPRLVYA SLHQDICPIS SYRGKCSIFH KDEVFDVLPN EKECIIRPNI
FYFDELFDRY TLKYYKVYST DKILNKWNSK SPFLYVLNRR FRYIYTEPKY PLENVLKKYV
FHELEVNELS PADYQWDKRC QFCKEWCIQK ESLSCDECGV CAHLYCMDPP LDRKPNKDVV
WTCFSCLQKQ QGTKDSHVRF LEEQALELDF IRSVRQKIEE ISSKAIKENV GYNTENCWFQ
YLGIYSISHI GDALNDSMFF PYPFKPSRVG VKYQWNGCNH NVPWRRNSYI SANSEEERGS
TKTSELAWVL DASKITTRKL SEYIEQCKSE ICPILNVRGE TCNFIDVVLK NLLFTNYDTA
EAFKKCKREL SRKFLKEPSF TAVEIRKFEE AVEKFGSELR PVCEYVGTQP MSMIVRFYYN
WKKTERGLTV RGKLSKLSKN KRKKEIANHE NDVETKYIDD SSFDTEKLSL AESSFQCMFC
KTDYSPMWYR VTGGSDDEKI KIRMQTGVNE KTEISEKSPA HSKKNEKLGA LCIRCARMWR
RYAIKWVPPL ETLRKITGTC QNSFYSAIEG IIEENNTNKF TLSPFQAHNK LLEWELVQDS
ELIIRQRMKV YKNPNSFVKM KRYSMTFHTQ LYKMAVRSYR KNEFHPETMQ RDLELFIEDN
KEVRKAIPEQ KPERAKNTKD EFPVNIIRQS PGTIKTSDTS RNRKCNDVFI EKASNNNIPK
ITNASNDLIE ISIKTGGSSS GSVSVDKGFK FVKFDNKTFQ RLRNSLKLVN NKLPKYNEPS
TKKIKMINDI ALSNPLNEPN GASYNYTVIS HSKETSVALE KYHDGNKPSK MLEKDMILKH
TKNKPKNPDT AWANNSARTF CSVCKEKFND NDNYEVVCGN CGLTVHYFCY AIKLPKDMKK
NTNLKTFKWL CDPCSNDLNP IISTTYQCSM CPTKDYDYDR YRSQSFKICP DALKCTSLGT
WVHLVCSLFN EDIKYGNGQS MQPALNTTAV LIKHSRFTCG VCRINGGGLV KCNKCQYRYH
ITCAQNSSNF KLMFEKKNMS VDTTLPCIKD VKLNDTYTLR PILICDRHDI SLEGNELYPL
SYKPQHTLSY IEQYCRYYKC ESDHSLVELR YFEQLRLRHG EMPGNSHDSA IKPKIYVLPF
ERTCPHCGTN KSLYWYEDII CHSCNLRSGA QELDFDSASA NISNDNGLPV EITQQLMEGI
EPAMFDIDIS EAGTDKNTHP SSQ
