ABI5_ARATH
ID ABI5_ARATH Reviewed; 442 AA.
AC Q9SJN0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein ABSCISIC ACID-INSENSITIVE 5;
DE AltName: Full=Dc3 promoter-binding factor 1;
DE Short=AtDPBF1;
DE AltName: Full=Protein GROWTH-INSENSITIVITY TO ABA 1;
DE AltName: Full=bZIP transcription factor 39;
DE Short=AtbZIP39;
GN Name=ABI5; Synonyms=BZIP39, DPBF1, GIA1, NEM1; OrderedLocusNames=At2g36270;
GN ORFNames=F2H17.12;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=10760247; DOI=10.2307/3871072;
RA Finkelstein R.R., Lynch T.J.;
RT "The Arabidopsis abscisic acid response gene ABI5 encodes a basic leucine
RT zipper transcription factor.";
RL Plant Cell 12:599-609(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY, DNA-BINDING, AND
RP HETERODIMERIZATION.
RX PubMed=12376636; DOI=10.1104/pp.003566;
RA Kim S.Y., Ma J., Perret P., Li Z., Thomas T.L.;
RT "Arabidopsis ABI5 subfamily members have distinct DNA-binding and
RT transcriptional activities.";
RL Plant Physiol. 130:688-697(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10929936; DOI=10.1093/pcp/41.5.541;
RA Lopez-Molina L., Chua N.H.;
RT "A null mutation in a bZIP factor confers ABA-insensitivity in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 41:541-547(2000).
RN [7]
RP INTERACTION WITH ABI3, AND HOMODIMERIZATION.
RX PubMed=11489176; DOI=10.1046/j.1365-313x.2001.01069.x;
RA Nakamura S., Lynch T.J., Finkelstein R.R.;
RT "Physical interactions between ABA response loci of Arabidopsis.";
RL Plant J. 26:627-635(2001).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=11287670; DOI=10.1073/pnas.081594298;
RA Lopez-Molina L., Mongrand S., Chua N.-H.;
RT "A postgermination developmental arrest checkpoint is mediated by abscisic
RT acid and requires the ABI5 transcription factor in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4782-4787(2001).
RN [9]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12084834; DOI=10.1105/tpc.000869;
RA Bensmihen S., Rippa S., Lambert G., Jublot D., Pautot V., Granier F.,
RA Giraudat J., Parcy F.;
RT "The homologous ABI5 and EEL transcription factors function
RT antagonistically to fine-tune gene expression during late embryogenesis.";
RL Plant Cell 14:1391-1403(2002).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12000684; DOI=10.1046/j.1365-313x.2002.01295.x;
RA Carles C., Bies-Etheve N., Aspart L., Leon-Kloosterziel K.M., Koornneef M.,
RA Echeverria M., Delseny M.;
RT "Regulation of Arabidopsis thaliana Em genes: role of ABI5.";
RL Plant J. 30:373-383(2002).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, PHOSPHORYLATION AT SER-42;
RP SER-145 AND THR-201, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12410810; DOI=10.1046/j.1365-313x.2002.01430.x;
RA Lopez-Molina L., Mongrand S., McLachlin D.T., Chait B.T., Chua N.-H.;
RT "ABI5 acts downstream of ABI3 to execute an ABA-dependent growth arrest
RT during germination.";
RL Plant J. 32:317-328(2002).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=12177466; DOI=10.1104/pp.005793;
RA Brocard I.M., Lynch T.J., Finkelstein R.R.;
RT "Regulation and role of the Arabidopsis abscisic acid-insensitive 5 gene in
RT abscisic acid, sugar, and stress response.";
RL Plant Physiol. 129:1533-1543(2002).
RN [13]
RP FUNCTION.
RX PubMed=12434021; DOI=10.1073/pnas.242607499;
RA Lu C., Han M.-H., Guevara-Garcia A., Fedoroff N.V.;
RT "Mitogen-activated protein kinase signaling in postgermination arrest of
RT development by abscisic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15812-15817(2002).
RN [14]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [15]
RP PROTEIN DEGRADATION, AND INTERACTION WITH AFP1.
RX PubMed=12569131; DOI=10.1101/gad.1055803;
RA Lopez-Molina L., Mongrand S., Kinoshita N., Chua N.-H.;
RT "AFP is a novel negative regulator of ABA signaling that promotes ABI5
RT protein degradation.";
RL Genes Dev. 17:410-418(2003).
RN [16]
RP PROTEIN DEGRADATION.
RX PubMed=12671091; DOI=10.1105/tpc.009217;
RA Smalle J., Kurepa J., Yang P., Emborg T.J., Babiychuk E., Kushnir S.,
RA Vierstra R.D.;
RT "The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis
RT growth and development supports a substrate-specific function in abscisic
RT acid signaling.";
RL Plant Cell 15:965-980(2003).
RN [17]
RP INDUCTION.
RX PubMed=12970489; DOI=10.1104/pp.103.021089;
RA Arroyo A., Bossi F., Finkelstein R.R., Leon P.;
RT "Three genes that affect sugar sensing (abscisic acid insensitive 4,
RT abscisic acid insensitive 5, and constitutive triple response 1) are
RT differentially regulated by glucose in Arabidopsis.";
RL Plant Physiol. 133:231-242(2003).
RN [18]
RP FUNCTION.
RX PubMed=15118859; DOI=10.1007/s00425-004-1279-5;
RA Pourtau N., Mares M., Purdy S., Quentin N., Rueel A., Wingler A.;
RT "Interactions of abscisic acid and sugar signalling in the regulation of
RT leaf senescence.";
RL Planta 219:765-772(2004).
RN [19]
RP FUNCTION, AND INTERACTION WITH ABI3.
RX PubMed=16247556; DOI=10.1007/s11103-005-8767-2;
RA Finkelstein R.R., Gampala S.S., Lynch T.J., Thomas T.L., Rock C.D.;
RT "Redundant and distinct functions of the ABA response loci ABA-
RT INSENSITIVE(ABI)5 and ABRE-BINDING FACTOR (ABF)3.";
RL Plant Mol. Biol. 59:253-267(2005).
RN [20]
RP PROTEIN DEGRADATION, AND INTERACTION WITH KEG.
RX PubMed=17194765; DOI=10.1105/tpc.106.046532;
RA Stone S.L., Williams L.A., Farmer L.M., Vierstra R.D., Callis J.;
RT "KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and
RT development, is involved in abscisic acid signaling.";
RL Plant Cell 18:3415-3428(2006).
RN [21]
RP FUNCTION, AND INDUCTION.
RX PubMed=16463099; DOI=10.1007/s11103-005-2418-5;
RA Nakashima K., Fujita Y., Katsura K., Maruyama K., Narusaka Y., Seki M.,
RA Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Transcriptional regulation of ABI3- and ABA-responsive genes including
RT RD29B and RD29A in seeds, germinating embryos, and seedlings of
RT Arabidopsis.";
RL Plant Mol. Biol. 60:51-68(2006).
RN [22]
RP PHOSPHORYLATION BY SRK2D AND SRK2I.
RX PubMed=17307925; DOI=10.1105/tpc.106.048538;
RA Fujii H., Verslues P.E., Zhu J.-K.;
RT "Identification of two protein kinases required for abscisic acid
RT regulation of seed germination, root growth, and gene expression in
RT Arabidopsis.";
RL Plant Cell 19:485-494(2007).
RN [23]
RP INTERACTION WITH AFP1; AFP2; AFP3 AND AFP4.
RX PubMed=18484180; DOI=10.1007/s11103-008-9344-2;
RA Garcia M.E., Lynch T.J., Peeters J., Snowden C., Finkelstein R.R.;
RT "A small plant-specific protein family of ABI five binding proteins (AFPs)
RT regulates stress response in germinating Arabidopsis seeds and seedlings.";
RL Plant Mol. Biol. 67:643-658(2008).
RN [24]
RP INDUCTION.
RX PubMed=18332440; DOI=10.1073/pnas.0710778105;
RA Chen H., Zhang J., Neff M.M., Hong S.-W., Zhang H., Deng X.-W., Xiong L.;
RT "Integration of light and abscisic acid signaling during seed germination
RT and early seedling development.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4495-4500(2008).
RN [25]
RP SUMOYLATION AT LYS-391, AND MUTAGENESIS OF LYS-391.
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 [26]
RP INTERACTION WITH FYPP1 AND FYPP3.
RX PubMed=22715043; DOI=10.1105/tpc.112.098905;
RA Dai M., Zhang C., Kania U., Chen F., Xue Q., McCray T., Li G., Qin G.,
RA Wakeley M., Terzaghi W., Wan J., Zhao Y., Xu J., Friml J., Deng X.W.,
RA Wang H.;
RT "A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation
RT and auxin efflux in Arabidopsis.";
RL Plant Cell 24:2497-2514(2012).
RN [27]
RP INTERACTION WITH MED25.
RX PubMed=22822206; DOI=10.1105/tpc.112.098277;
RA Chen R., Jiang H., Li L., Zhai Q., Qi L., Zhou W., Liu X., Li H., Zheng W.,
RA Sun J., Li C.;
RT "The Arabidopsis mediator subunit MED25 differentially regulates jasmonate
RT and abscisic acid signaling through interacting with the MYC2 and ABI5
RT transcription factors.";
RL Plant Cell 24:2898-2916(2012).
RN [28]
RP INTERACTION WITH TAP46 AND PP2A.
RX PubMed=24357600; DOI=10.1104/pp.113.233684;
RA Hu R., Zhu Y., Shen G., Zhang H.;
RT "TAP46 plays a positive role in the ABSCISIC ACID INSENSITIVE5-regulated
RT gene expression in Arabidopsis.";
RL Plant Physiol. 164:721-734(2014).
RN [29]
RP INTERACTION WITH FREE1.
RX PubMed=30962512; DOI=10.1038/s41477-019-0400-5;
RA Li H., Li Y., Zhao Q., Li T., Wei J., Li B., Shen W., Yang C., Zeng Y.,
RA Rodriguez P.L., Zhao Y., Jiang L., Wang X., Gao C.;
RT "The plant ESCRT component FREE1 shuttles to the nucleus to attenuate
RT abscisic acid signalling.";
RL Nat. Plants 5:512-524(2019).
CC -!- FUNCTION: Participates in ABA-regulated gene expression during seed
CC development and subsequent vegetative stage by acting as the major
CC mediator of ABA repression of growth. Binds to the embryo specification
CC element and the ABA-responsive element (ABRE) of the Dc3 gene promoter
CC and to the ABRE of the Em1 and Em6 genes promoters. Can also trans-
CC activate its own promoter, suggesting that it is autoregulated. Plays a
CC role in sugar-mediated senescence. {ECO:0000269|PubMed:11287670,
CC ECO:0000269|PubMed:12000684, ECO:0000269|PubMed:12084834,
CC ECO:0000269|PubMed:12177466, ECO:0000269|PubMed:12410810,
CC ECO:0000269|PubMed:12434021, ECO:0000269|PubMed:15118859,
CC ECO:0000269|PubMed:16247556, ECO:0000269|PubMed:16463099}.
CC -!- SUBUNIT: DNA-binding homodimer. DNA-binding heterodimer with
CC AREB3/DPBF3 or EEL/DPBF4. Interacts with ABI3, KEG, the mediator
CC subunit MED25, and the AFP proteins AFP1, AFP2, AFP3 and AFP4.
CC Interacts with TAP46. Interacts with the 36 kDa catalytic subunit
CC (subunit C) of PP2A (PubMed:11489176, PubMed:12569131, PubMed:16247556,
CC PubMed:17194765, PubMed:18484180, PubMed:22822206, PubMed:24357600).
CC Interacts with FYPP1 and FYPP3 (PubMed:22715043). Interacts with FREE1
CC (via C-terminus) (PubMed:30962512). {ECO:0000269|PubMed:11489176,
CC ECO:0000269|PubMed:12569131, ECO:0000269|PubMed:16247556,
CC ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:18484180,
CC ECO:0000269|PubMed:22715043, ECO:0000269|PubMed:22822206,
CC ECO:0000269|PubMed:24357600, ECO:0000269|PubMed:30962512}.
CC -!- INTERACTION:
CC Q9SJN0; Q9M1R4: IAA30; NbExp=3; IntAct=EBI-1778690, EBI-3946710;
CC Q9SJN0; Q9FY48: KEG; NbExp=2; IntAct=EBI-1778690, EBI-1955729;
CC Q9SJN0; P43291: SRK2A; NbExp=3; IntAct=EBI-1778690, EBI-401164;
CC Q9SJN0; P55852: SUMO1; NbExp=2; IntAct=EBI-1778690, EBI-15763381;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:12410810}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in seeds.
CC {ECO:0000269|PubMed:10760247, ECO:0000269|PubMed:12376636}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo during the latest stages of
CC seed maturation. {ECO:0000269|PubMed:12084834}.
CC -!- INDUCTION: Up-regulated by drought, salt, abscisic acid (ABA) and
CC glucose or 2-deoxy-glucose (2DG). Autoregulated. Positively regulated
CC by the light-signaling component HY5. {ECO:0000269|PubMed:11287670,
CC ECO:0000269|PubMed:12177466, ECO:0000269|PubMed:12376636,
CC ECO:0000269|PubMed:12970489, ECO:0000269|PubMed:16463099,
CC ECO:0000269|PubMed:18332440}.
CC -!- PTM: Phosphorylated by SRK2D and SRK2I in vitro.
CC {ECO:0000269|PubMed:17307925}.
CC -!- PTM: Ubiquitinated. AFP1, KEG and RPN10 mediate its proteasome-
CC dependent degradation. Its stability or degradation plays a central
CC role in abscisic acid response. Sumoylated at Lys-391 by SIZ1.
CC Sumoylation protects ABI5 from proteasome degradation, attenuating ABA
CC signaling and sensitivity to ABA. {ECO:0000269|PubMed:19276109}.
CC -!- DISRUPTION PHENOTYPE: Exhibits abscisic acid (ABA) insensitivity.
CC {ECO:0000269|PubMed:10929936}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
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DR EMBL; AF334206; AAK19599.1; -; mRNA.
DR EMBL; AC006921; AAD21438.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09226.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62587.1; -; Genomic_DNA.
DR EMBL; BT026517; ABH04624.1; -; mRNA.
DR PIR; G84778; G84778.
DR RefSeq; NP_001324735.1; NM_001336590.1.
DR RefSeq; NP_565840.1; NM_129185.4.
DR AlphaFoldDB; Q9SJN0; -.
DR SMR; Q9SJN0; -.
DR BioGRID; 3543; 82.
DR DIP; DIP-40551N; -.
DR IntAct; Q9SJN0; 29.
DR STRING; 3702.AT2G36270.1; -.
DR iPTMnet; Q9SJN0; -.
DR PaxDb; Q9SJN0; -.
DR PRIDE; Q9SJN0; -.
DR ProteomicsDB; 244371; -.
DR EnsemblPlants; AT2G36270.1; AT2G36270.1; AT2G36270.
DR EnsemblPlants; AT2G36270.2; AT2G36270.2; AT2G36270.
DR GeneID; 818199; -.
DR Gramene; AT2G36270.1; AT2G36270.1; AT2G36270.
DR Gramene; AT2G36270.2; AT2G36270.2; AT2G36270.
DR KEGG; ath:AT2G36270; -.
DR Araport; AT2G36270; -.
DR TAIR; locus:2049425; AT2G36270.
DR eggNOG; ENOG502QPJH; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR InParanoid; Q9SJN0; -.
DR OMA; GYNGMAI; -.
DR PhylomeDB; Q9SJN0; -.
DR PRO; PR:Q9SJN0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJN0; baseline and differential.
DR Genevisible; Q9SJN0; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IEP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR InterPro; IPR029803; ABI5.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043452; BZIP46-like.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR22952; PTHR22952; 1.
DR PANTHER; PTHR22952:SF430; PTHR22952:SF430; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..442
FT /note="Protein ABSCISIC ACID-INSENSITIVE 5"
FT /id="PRO_0000369605"
FT DOMAIN 355..418
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..376
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 383..404
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 414..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:12410810"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:12410810"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:12410810"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:19276109"
FT MUTAGEN 391
FT /note="K->R: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:19276109"
SQ SEQUENCE 442 AA; 47007 MW; F879F51B99A99140 CRC64;
MVTRETKLTS EREVESSMAQ ARHNGGGGGE NHPFTSLGRQ SSIYSLTLDE FQHALCENGK
NFGSMNMDEF LVSIWNAEEN NNNQQQAAAA AGSHSVPANH NGFNNNNNNG GEGGVGVFSG
GSRGNEDANN KRGIANESSL PRQGSLTLPA PLCRKTVDEV WSEIHRGGGS GNGGDSNGRS
SSSNGQNNAQ NGGETAARQP TFGEMTLEDF LVKAGVVREH PTNPKPNPNP NQNQNPSSVI
PAAAQQQLYG VFQGTGDPSF PGQAMGVGDP SGYAKRTGGG GYQQAPPVQA GVCYGGGVGF
GAGGQQMGMV GPLSPVSSDG LGHGQVDNIG GQYGVDMGGL RGRKRVVDGP VEKVVERRQR
RMIKNRESAA RSRARKQAYT VELEAELNQL KEENAQLKHA LAELERKRKQ QYFESLKSRA
QPKLPKSNGR LRTLMRNPSC PL
