SGF11_ARATH
ID SGF11_ARATH Reviewed; 181 AA.
AC Q94BV2;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=SAGA-associated factor 11 {ECO:0000305};
GN Name=SGF11 {ECO:0000303|PubMed:29588169};
GN OrderedLocusNames=At5g58575 {ECO:0000312|Araport:AT5G58575};
GN ORFNames=MZN1 {ECO:0000312|EMBL:AB020755};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH
RP ENY2, AND DISRUPTION PHENOTYPE.
RX PubMed=29588169; DOI=10.1016/j.jmb.2018.03.018;
RA Pfab A., Bruckmann A., Nazet J., Merkl R., Grasser K.D.;
RT "The adaptor protein ENY2 is a component of the deubiquitination module of
RT the Arabidopsis SAGA transcriptional co-activator complex but not of the
RT TREX-2 complex.";
RL J. Mol. Biol. 430:1479-1494(2018).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH
RP DDA1, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=30192741; DOI=10.7554/elife.37892;
RA Nassrallah A., Rougee M., Bourbousse C., Drevensek S., Fonseca S.,
RA Iniesto E., Ait-Mohamed O., Deton-Cabanillas A.F., Zabulon G., Ahmed I.,
RA Stroebel D., Masson V., Lombard B., Eeckhout D., Gevaert K., Loew D.,
RA Genovesio A., Breyton C., de Jaeger G., Bowler C., Rubio V., Barneche F.;
RT "DET1-mediated degradation of a SAGA-like deubiquitination module controls
RT H2Bub homeostasis.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Component of a deubiquitination module (DUB module) that
CC specifically deubiquinates monoubiquinated histone H2B (H2Bub)
CC (PubMed:29588169, PubMed:30192741). Does not seem to be a component of
CC the TREX-2 complex (PubMed:29588169). Seems to act independently of the
CC SAGA multiprotein complex (PubMed:30192741). The DUB module is
CC responsible for the major H2Bub deubiquitinase activity in Arabidopsis
CC (PubMed:30192741). {ECO:0000269|PubMed:29588169,
CC ECO:0000269|PubMed:30192741}.
CC -!- SUBUNIT: Component of a deubiquitination module (DUB module) formed by
CC ENY2, SGF11, and UBP22 in Arabidopsis (PubMed:29588169,
CC PubMed:30192741). Interacts directly with ENY2 and UBP22
CC (PubMed:29588169, PubMed:30192741). Interacts with DDA1
CC (PubMed:30192741). {ECO:0000269|PubMed:29588169,
CC ECO:0000269|PubMed:30192741}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:30192741}. Note=Displays a rather patchy
CC distribution forming a punctuated pattern in the euchromatin
CC (PubMed:30192741). Does not localize in the heterochromatic
CC chromocenters or nucleolus (PubMed:30192741).
CC {ECO:0000269|PubMed:30192741}.
CC -!- PTM: Ubiquitinated in DET1-dependent manner (PubMed:30192741).
CC Ubiquitination probably leads to its subsequent proteasomal degradation
CC (PubMed:30192741). {ECO:0000269|PubMed:30192741}.
CC -!- DISRUPTION PHENOTYPE: Delayed flowering and increased levels of histone
CC H2B monoubiquitination. {ECO:0000269|PubMed:29588169}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000305}.
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DR EMBL; AB020755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED97071.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70291.1; -; Genomic_DNA.
DR EMBL; AY039865; AAK63969.1; -; mRNA.
DR EMBL; AY077659; AAL76137.1; -; mRNA.
DR RefSeq; NP_001318831.1; NM_001345305.1.
DR RefSeq; NP_200665.2; NM_125243.5.
DR AlphaFoldDB; Q94BV2; -.
DR IntAct; Q94BV2; 8.
DR STRING; 3702.AT5G58575.1; -.
DR PaxDb; Q94BV2; -.
DR PRIDE; Q94BV2; -.
DR ProteomicsDB; 189271; -.
DR EnsemblPlants; AT5G58575.1; AT5G58575.1; AT5G58575.
DR EnsemblPlants; AT5G58575.2; AT5G58575.2; AT5G58575.
DR GeneID; 835971; -.
DR Gramene; AT5G58575.1; AT5G58575.1; AT5G58575.
DR Gramene; AT5G58575.2; AT5G58575.2; AT5G58575.
DR KEGG; ath:AT5G58575; -.
DR Araport; AT5G58575; -.
DR TAIR; locus:505006700; AT5G58575.
DR eggNOG; KOG2612; Eukaryota.
DR HOGENOM; CLU_110436_0_0_1; -.
DR InParanoid; Q94BV2; -.
DR OMA; IFGQSHP; -.
DR OrthoDB; 1407283at2759; -.
DR PhylomeDB; Q94BV2; -.
DR PRO; PR:Q94BV2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BV2; baseline and differential.
DR GO; GO:0071819; C:DUBm complex; IPI:TAIR.
DR GO; GO:0070461; C:SAGA-type complex; IPI:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; IMP:TAIR.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR Pfam; PF08209; Sgf11; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..181
FT /note="SAGA-associated factor 11"
FT /id="PRO_0000446675"
FT ZN_FING 93..114
FT /note="SGF11-type"
FT /evidence="ECO:0000255"
FT REGION 116..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 19677 MW; C98A997A9AB6D374 CRC64;
MSGAEDNKSS HAQLSSQIFL DLVDSVIADV ASECHRVARL GLDRDLDIVE EELRLSVEAR
AKIADPSNNL ETNTKYVVDI FGQTHPPVAS EVFNCMNCGR QIVAGRFAPH LEKCMGKGRK
ARAKTTRSTT AAQNRNARRS PNPRYSPYPN SASENQLASG SPGVAGEDCS NFTVRENVKG
D
