SNL2_ARATH
ID SNL2_ARATH Reviewed; 1367 AA.
AC Q9LFQ3; Q8GWB6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Paired amphipathic helix protein Sin3-like 2;
GN Name=SNL2; OrderedLocusNames=At5g15020; ORFNames=F2G14.140;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-551.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
RA Conlan R.S.;
RT "PAH-domain-specific interactions of the Arabidopsis transcription
RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS
RT EARLY2 Myb-DNA binding factors.";
RL J. Mol. Biol. 395:937-949(2010).
CC -!- FUNCTION: Acts as a transcriptional repressor. Plays roles in
CC regulating gene expression and genome stability (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LFQ3-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43533.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAC01821.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391146; CAC01821.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92105.1; -; Genomic_DNA.
DR EMBL; AK118953; BAC43533.1; ALT_SEQ; mRNA.
DR PIR; T51447; T51447.
DR RefSeq; NP_197006.2; NM_121506.4. [Q9LFQ3-1]
DR AlphaFoldDB; Q9LFQ3; -.
DR SMR; Q9LFQ3; -.
DR BioGRID; 16631; 3.
DR IntAct; Q9LFQ3; 1.
DR STRING; 3702.AT5G15020.1; -.
DR iPTMnet; Q9LFQ3; -.
DR PaxDb; Q9LFQ3; -.
DR PRIDE; Q9LFQ3; -.
DR ProteomicsDB; 232644; -. [Q9LFQ3-1]
DR EnsemblPlants; AT5G15020.1; AT5G15020.1; AT5G15020. [Q9LFQ3-1]
DR GeneID; 831354; -.
DR Gramene; AT5G15020.1; AT5G15020.1; AT5G15020. [Q9LFQ3-1]
DR KEGG; ath:AT5G15020; -.
DR Araport; AT5G15020; -.
DR TAIR; locus:2147845; AT5G15020.
DR eggNOG; KOG4204; Eukaryota.
DR InParanoid; Q9LFQ3; -.
DR OrthoDB; 253485at2759; -.
DR PhylomeDB; Q9LFQ3; -.
DR PRO; PR:Q9LFQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFQ3; baseline and differential.
DR Genevisible; Q9LFQ3; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0016580; C:Sin3 complex; IDA:TAIR.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.1160.11; -; 3.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1367
FT /note="Paired amphipathic helix protein Sin3-like 2"
FT /id="PRO_0000394041"
FT DOMAIN 46..116
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 130..200
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 327..396
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 14..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..989
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1017
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1367 AA; 155119 MW; 7C47897854F9B2B4 CRC64;
MKRIRDDIYA TGSQFKRPLG SSRGESYEQS PITGGGSIGE GGINTQKLTT DDALTYLKEV
KEMFQDQRDK YDMFLEVMKD FKAQKTDTSG VISRVKELFK GHNNLIFGFN TFLPKGFEIT
LDDVEAPSKK TVEFEEAISF VNKIKTRFQH NELVYKSFLE ILNMYRKDNK DITEVYNEVS
TLFEDHSDLL EEFTRFLPDS LAPHTEAQLL RSQAQRYDDR GSGPPLVRRM FMEKDRRRER
TVASRGDRDH SVDRSDLNDD KSMVKMHRDQ RKRVDKDNRE RRSRDLEDGE AEQDNLQHFS
EKRKSSRRME GFEAYSGPAS HSEKNNLKSM YNQAFLFCEK VKERLCSQDD YQAFLKCLNM
FSNGIIQRKD LQNLVSDVLG KFPDLMDEFN QFFERCESID GFQHLAGVMS KKSLGSEENL
SRSVKGEEKD REHKRDVEAA KEKERSKDKY MGKSIQELDL SDCERCTPSY RLLPPDYPIP
SVRHRQKSGA AVLNDHWVSV TSGSEDYSFK HMRRNQYEES LFRCEDDRFE LDMLLESVGS
AAKSAEELLN IIIDKKISFE GSFRIEDHFT ALNLRCIERL YGDHGLDVTD LIRKNPAAAL
PVILTRLKQK QDEWTKCREG FNVVWADVYA KNHYKSLDHR SFYFKQQDSK NLSAKALVSE
VKDLKEKSQK EDDVVLSISA GYRQPIIPHL EYDYLDRAIH EDLFKLVQFS CEEICSTKEQ
TGKVLKLWAN FLELMLDVAP RAKGSDSVED VVETQHQRAF TSGEANESSD AISLVSRQLK
FATNGDVHAS SGVSKHGETG LLNRDSSGKE NLKDGDLANK DVATCAEKPQ KDQEIGNGAA
KRSGDVDERV ATSSSSFPSG VENNNGKVGS RDSSGSRGIL SKPSEAIDKV DSIQHTQGVD
IGRIIVLGNG LQSDTSKANS NYDESGGPSK IEKEEGELSP VGDSEDNFVV YEDRELKATA
KTEHSVEAEG ENDEDADDED GDDASEAGED ASGTESIGDE CSQDDNGVEE EGEHDEIDGK
AESEGEAEGM ESHLIEDKGL FPSSERVLLS VKPLSKHIAA AALVDEKKKD SRVFYGNDDF
YVLFRLHRVS AIDSYDLLSH ILYERILSAK TYCSGSEMKL RNTKDTCSPD PYARFMNALF
SLLNGSAENS KFEDECRAII GNQSYVLFTL EKLIYKLVKQ LQAVVADDMD NKLLQLYEYE
NSRRPGRVFD SVYYENARIL LHEENIYRLE CSSSPSRLSI QLMDNIIEKP DAYAVSMEPT
FTSYLQNEFL SNSSGKKELQ DIVLQRNMRG YNGLDDLAVA CKAMEGVQVI NGLECKMSCS
SYKISYVLDT EDFFHRKKKQ KKSNNLSLAK LSQNRIARFH KFLSASR
