SIZ1_ARATH
ID SIZ1_ARATH Reviewed; 884 AA.
AC Q680Q4; B9DG12; Q56YS2; Q56ZS1; Q67ZL3; Q9FKK4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=E3 SUMO-protein ligase SIZ1 {ECO:0000303|PubMed:15894620};
DE EC=2.3.2.- {ECO:0000305};
DE AltName: Full=E3 SUMO-protein transferase SIZ1 {ECO:0000305};
GN Name=SIZ1 {ECO:0000303|PubMed:15894620};
GN OrderedLocusNames=At5g60410 {ECO:0000312|Araport:AT5G60410};
GN ORFNames=MUF9.5 {ECO:0000312|EMBL:BAB08225.1}, MUF9.70;
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 [MRNA] (ISOFORM 3).
RA Ouyang J., Chua N.-H.;
RT "Arabidopsis thaliana SUMO E3 ligase.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15894620; DOI=10.1073/pnas.0500778102;
RA Miura K., Rus A., Sharkhuu A., Yokoi S., Karthikeyan A.S., Raghothama K.G.,
RA Baek D., Koo Y.D., Jin J.B., Bressan R.A., Yun D.-J., Hasegawa P.M.;
RT "The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7760-7765(2005).
RN [8]
RP STRUCTURE BY NMR OF 104-168.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PHD domain in DNA-binding family protein AAM98074.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17041025; DOI=10.1104/pp.106.088831;
RA Yoo C.Y., Miura K., Jin J.B., Lee J., Park H.C., Salt D.E., Yun D.J.,
RA Bressan R.A., Hasegawa P.M.;
RT "SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal
RT thermotolerance in Arabidopsis independent of salicylic acid.";
RL Plant Physiol. 142:1548-1558(2006).
RN [10]
RP FUNCTION.
RX PubMed=17416732; DOI=10.1105/tpc.106.048397;
RA Miura K., Jin J.B., Lee J., Yoo C.Y., Stirm V., Miura T., Ashworth E.N.,
RA Bressan R.A., Yun D.J., Hasegawa P.M.;
RT "SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and
RT freezing tolerance in Arabidopsis.";
RL Plant Cell 19:1403-1414(2007).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17905899; DOI=10.1105/tpc.106.049981;
RA Catala R., Ouyang J., Abreu I.A., Hu Y., Seo H., Zhang X., Chua N.H.;
RT "The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought
RT responses.";
RL Plant Cell 19:2952-2966(2007).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17163880; DOI=10.1111/j.1365-313x.2006.02947.x;
RA Lee J., Nam J., Park H.C., Na G., Miura K., Jin J.B., Yoo C.Y., Baek D.,
RA Kim D.H., Jeong J.C., Kim D., Lee S.Y., Salt D.E., Mengiste T., Gong Q.,
RA Ma S., Bohnert H.J., Kwak S.S., Bressan R.A., Hasegawa P.M., Yun D.J.;
RT "Salicylic acid-mediated innate immunity in Arabidopsis is regulated by
RT SIZ1 SUMO E3 ligase.";
RL Plant J. 49:79-90(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17644626; DOI=10.1104/pp.107.102285;
RA Saracco S.A., Miller M.J., Kurepa J., Vierstra R.D.;
RT "Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and
RT SUMO2 to nuclear proteins is essential.";
RL Plant Physiol. 145:119-134(2007).
RN [14]
RP FUNCTION, AUTOSUMOYLATION AT LYS-100 AND LYS-488, INTERACTION WITH SCE1;
RP GTE3 AND GTE5, DOMAIN, AND MUTAGENESIS OF LYS-100 AND LYS-488.
RX PubMed=18502747; DOI=10.1074/jbc.m708176200;
RA Garcia-Dominguez M., March-Diaz R., Reyes J.C.;
RT "The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain
RT GTE proteins.";
RL J. Biol. Chem. 283:21469-21477(2008).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18069938; DOI=10.1111/j.1365-313x.2007.03359.x;
RA Jin J.B., Jin Y.H., Lee J., Miura K., Yoo C.Y., Kim W.Y., Van Oosten M.,
RA Hyun Y., Somers D.E., Lee I., Yun D.J., Bressan R.A., Hasegawa P.M.;
RT "The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic
RT acid-mediated floral promotion pathway and through affects on FLC chromatin
RT structure.";
RL Plant J. 53:530-540(2008).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19276109; DOI=10.1073/pnas.0811088106;
RA Miura K., Lee J., Jin J.B., Yoo C.Y., Miura T., Hasegawa P.M.;
RT "Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively
RT regulates abscisic acid signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5418-5423(2009).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF CYS-379.
RX PubMed=26662259; DOI=10.1111/tpj.13096;
RA Crozet P., Margalha L., Butowt R., Fernandes N., Elias C.A., Orosa B.,
RA Tomanov K., Teige M., Bachmair A., Sadanandom A., Baena-Gonzalez E.;
RT "SUMOylation represses SnRK1 signaling in Arabidopsis.";
RL Plant J. 85:120-133(2016).
CC -!- FUNCTION: E3 SUMO protein ligase involved in regulation processes.
CC Mediates SUMO/ attachment to PHR1, a MYB transcriptional activator
CC controlling the phosphate deficiency responses (PubMed:15894620).
CC Functions as an upstream negative regulator of salicylic acid (SA)
CC accumulation and subsequent SA-mediated systemic acquired resistance
CC (SAR) signaling. Probably not involved in jasmonic acid (JA)-mediated
CC defense response. Participates in abiotic stress-induced sumoylation.
CC Controls heat shock-induced SUMO1 and SUMO2 conjugation and facilitates
CC basal thermotolerance. Involved in freezing tolerance by mediating
CC sumoylation of ICE1, a transcription activator of the cold signaling
CC regulator CBF3/DREB1A. Acts as positive regulator of drought stress
CC tolerance. Acts as floral repressor that promotes FLC expression by
CC repressing FLD activity through sumoylation. Acts as negative regulator
CC of abscisic acid (ABA) signaling through ABI5 sumoylation. Mediates
CC sumoylation of SCE1, GTE3 and GTE5. Functions as negative regulator of
CC SnRK1 signaling through sumoylation of several components of the SnRK1
CC complex (PubMed:26662259). {ECO:0000269|PubMed:15894620,
CC ECO:0000269|PubMed:17041025, ECO:0000269|PubMed:17163880,
CC ECO:0000269|PubMed:17416732, ECO:0000269|PubMed:17644626,
CC ECO:0000269|PubMed:17905899, ECO:0000269|PubMed:18069938,
CC ECO:0000269|PubMed:18502747, ECO:0000269|PubMed:19276109,
CC ECO:0000269|PubMed:26662259}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts (via PHD domain) with SCE1, GTE3 and GTE5.
CC {ECO:0000269|PubMed:18502747}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15894620}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q680Q4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q680Q4-2; Sequence=VSP_015483, VSP_015484;
CC Name=3;
CC IsoId=Q680Q4-3; Sequence=VSP_015486, VSP_015487;
CC Name=4;
CC IsoId=Q680Q4-4; Sequence=VSP_015485;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17905899}.
CC -!- DOMAIN: The PHD-type zinc finger mediates interaction with SCE1, GTE3
CC and GTE5 and is required for E3 activity.
CC {ECO:0000269|PubMed:18502747}.
CC -!- PTM: Autosumoylated at Lys-100 and Lys-488.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype. Heat-sensitive phenotype. Early
CC flowering under short day. Elevated level of salicylic acid (SA),
CC increased expression of pathogenesis-related (PR) genes and increased
CC resistance to the bacterial pathogen P.syringae. ABA hypersensitivity
CC during seed germination primary root growth. Exaggerated prototypical
CC Pi-starvation responses, including increased root-shoot mass ratio and
CC greater anthocyanin accumulation (PubMed:15894620).
CC {ECO:0000269|PubMed:15894620, ECO:0000269|PubMed:17041025,
CC ECO:0000269|PubMed:17163880, ECO:0000269|PubMed:17644626,
CC ECO:0000269|PubMed:17905899, ECO:0000269|PubMed:18069938,
CC ECO:0000269|PubMed:19276109}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; AY700572; AAU00414.1; -; mRNA.
DR EMBL; AB011483; BAB08225.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97324.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97325.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97326.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97327.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97328.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70389.1; -; Genomic_DNA.
DR EMBL; AY139752; AAM98074.1; -; mRNA.
DR EMBL; BT004542; AAO42788.1; -; mRNA.
DR EMBL; AK175813; BAD43576.1; -; mRNA.
DR EMBL; AK221190; BAD95283.1; -; mRNA.
DR EMBL; AK220973; BAD94544.1; -; mRNA.
DR EMBL; AK221249; BAD93882.1; -; mRNA.
DR EMBL; AK221292; BAD94016.1; -; mRNA.
DR EMBL; AK220890; BAD94301.1; -; mRNA.
DR EMBL; AK176104; BAD43867.1; -; mRNA.
DR EMBL; AK316983; BAH19679.1; -; mRNA.
DR RefSeq; NP_001032108.1; NM_001037031.1. [Q680Q4-2]
DR RefSeq; NP_001032109.2; NM_001037032.2. [Q680Q4-1]
DR RefSeq; NP_001119465.1; NM_001125993.1. [Q680Q4-4]
DR RefSeq; NP_001332003.1; NM_001345415.1. [Q680Q4-3]
DR RefSeq; NP_200849.2; NM_125434.4. [Q680Q4-3]
DR RefSeq; NP_974969.1; NM_203240.3. [Q680Q4-4]
DR PDB; 1WEW; NMR; -; A=104-168.
DR PDBsum; 1WEW; -.
DR AlphaFoldDB; Q680Q4; -.
DR SMR; Q680Q4; -.
DR BioGRID; 21407; 18.
DR STRING; 3702.AT5G60410.2; -.
DR iPTMnet; Q680Q4; -.
DR PaxDb; Q680Q4; -.
DR PRIDE; Q680Q4; -.
DR ProteomicsDB; 232620; -. [Q680Q4-1]
DR EnsemblPlants; AT5G60410.1; AT5G60410.1; AT5G60410. [Q680Q4-3]
DR EnsemblPlants; AT5G60410.2; AT5G60410.2; AT5G60410. [Q680Q4-4]
DR EnsemblPlants; AT5G60410.3; AT5G60410.3; AT5G60410. [Q680Q4-2]
DR EnsemblPlants; AT5G60410.4; AT5G60410.4; AT5G60410. [Q680Q4-1]
DR EnsemblPlants; AT5G60410.5; AT5G60410.5; AT5G60410. [Q680Q4-4]
DR EnsemblPlants; AT5G60410.6; AT5G60410.6; AT5G60410. [Q680Q4-3]
DR GeneID; 836163; -.
DR Gramene; AT5G60410.1; AT5G60410.1; AT5G60410. [Q680Q4-3]
DR Gramene; AT5G60410.2; AT5G60410.2; AT5G60410. [Q680Q4-4]
DR Gramene; AT5G60410.3; AT5G60410.3; AT5G60410. [Q680Q4-2]
DR Gramene; AT5G60410.4; AT5G60410.4; AT5G60410. [Q680Q4-1]
DR Gramene; AT5G60410.5; AT5G60410.5; AT5G60410. [Q680Q4-4]
DR Gramene; AT5G60410.6; AT5G60410.6; AT5G60410. [Q680Q4-3]
DR KEGG; ath:AT5G60410; -.
DR Araport; AT5G60410; -.
DR TAIR; locus:2175148; AT5G60410.
DR eggNOG; KOG2169; Eukaryota.
DR InParanoid; Q680Q4; -.
DR OMA; PYGHAKR; -.
DR OrthoDB; 141085at2759; -.
DR PhylomeDB; Q680Q4; -.
DR UniPathway; UPA00886; -.
DR EvolutionaryTrace; Q680Q4; -.
DR PRO; PR:Q680Q4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q680Q4; baseline and differential.
DR Genevisible; Q680Q4; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0032183; F:SUMO binding; IPI:TAIR.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010247; P:detection of phosphate ion; IDA:TAIR.
DR GO; GO:0048589; P:developmental growth; IMP:UniProtKB.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IMP:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0010113; P:negative regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IMP:TAIR.
DR GO; GO:0090352; P:regulation of nitrate assimilation; IMP:TAIR.
DR GO; GO:2000070; P:regulation of response to water deprivation; IMP:TAIR.
DR GO; GO:0010337; P:regulation of salicylic acid metabolic process; IMP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR GO; GO:0062210; P:shoot regeneration; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR031141; SIZ1_plant.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF85; PTHR10782:SF85; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Flowering; Isopeptide bond;
KW Metal-binding; Nucleus; Plant defense; Reference proteome; Stress response;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..884
FT /note="E3 SUMO-protein ligase SIZ1"
FT /id="PRO_0000218984"
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT ZN_FING 112..168
FT /note="PHD-type"
FT ZN_FING 346..429
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 828..832
FT /note="ASLLL -> GLFPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT /id="VSP_015483"
FT VAR_SEQ 833..884
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT /id="VSP_015484"
FT VAR_SEQ 860..884
FT /note="NNEQDHQTRHRSLNKICIILCAGKN -> VRPRMYLSIDSDSETMNRIIRQD
FT TGV (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015485"
FT VAR_SEQ 860..873
FT /note="NNEQDHQTRHRSLN -> VRPRMYLSIDSDSE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.5"
FT /id="VSP_015486"
FT VAR_SEQ 874..884
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.5"
FT /id="VSP_015487"
FT MUTAGEN 100
FT /note="K->R: Strongly reduces autosumoylation; when
FT associated with R-488."
FT /evidence="ECO:0000269|PubMed:18502747"
FT MUTAGEN 379
FT /note="C->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:26662259"
FT MUTAGEN 488
FT /note="K->R: Strongly reduces autosumoylation; when
FT associated with R-100."
FT /evidence="ECO:0000269|PubMed:18502747"
FT CONFLICT 335
FT /note="I -> S (in Ref. 5; BAD94301/BAD43867)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="E -> D (in Ref. 5; BAD43867)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="D -> G (in Ref. 5; BAD43867)"
FT /evidence="ECO:0000305"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1WEW"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1WEW"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1WEW"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1WEW"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1WEW"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1WEW"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1WEW"
SQ SEQUENCE 884 AA; 97034 MW; 5E44EA57FE896113 CRC64;
MDLEANCKEK LSYFRIKELK DVLTQLGLSK QGKKQELVDR ILTLLSDEQA ARLLSKKNTV
AKEAVAKLVD DTYRKMQVSG ASDLASKGQV SSDTSNLKVK GEPEDPFQPE IKVRCVCGNS
LETDSMIQCE DPRCHVWQHV GCVILPDKPM DGNPPLPESF YCEICRLTRA DPFWVTVAHP
LSPVRLTATT IPNDGASTMQ SVERTFQITR ADKDLLAKPE YDVQAWCMLL NDKVLFRMQW
PQYADLQVNG VPVRAINRPG GQLLGVNGRD DGPIITSCIR DGVNRISLSG GDVRIFCFGV
RLVKRRTLQQ VLNLIPEEGK GETFEDALAR VRRCIGGGGG DDNADSDSDI EVVADFFGVN
LRCPMSGSRI KVAGRFLPCV HMGCFDLDVF VELNQRSRKW QCPICLKNYS VEHVIVDPYF
NRITSKMKHC DEEVTEIEVK PDGSWRVKFK RESERRELGE LSQWHAPDGS LCPSAVDIKR
KMEMLPVKQE GYSDGPAPLK LGIRKNRNGI WEVSKPNTNG LSSSNRQEKV GYQEKNIIPM
SSSATGSGRD GDDASVNQDA IGTFDFVANG MELDSISMNV DSGYNFPDRN QSGEGGNNEV
IVLSDSDDEN DLVITPGPAY SGCQTDGGLT FPLNPPGIIN SYNEDPHSIA GGSSGLGLFN
DDDEFDTPLW SFPSETPEAP GFQLFRSDAD VSGGLVGLHH HSPLNCSPEI NGGYTMAPET
SMASVPVVPG STGRSEANDG LVDNPLAFGR DDPSLQIFLP TKPDASAQSG FKNQADMSNG
LRSEDWISLR LGDSASGNHG DPATTNGINS SHQMSTREGS MDTTTETASL LLGMNDSRQD
KAKKQRSDNP FSFPRQKRSN NEQDHQTRHR SLNKICIILC AGKN
