TIF9_ARATH
ID TIF9_ARATH Reviewed; 197 AA.
AC Q93ZM9; C0JPT8; Q3E9I1; Q3E9I2; Q9LYV4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Protein TIFY 9;
DE AltName: Full=Jasmonate ZIM domain-containing protein 10;
DE AltName: Full=Protein JASMONATE-ASSOCIATED 1;
DE AltName: Full=Protein JAZ10;
GN Name=TIFY9; Synonyms=JAS1, JAZ10; OrderedLocusNames=At5g13220;
GN ORFNames=T31B5.40;
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), FUNCTION, INTERACTION WITH MYC2;
RP COI1; TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6B/JAZ3; TIFY6A/JAZ4; TIFY11B/JAZ6;
RP TIFY5A/JAZ8; TIFY7/JAZ9; TIFY3A/JAZ11 AND TIFY3B/JAZ12, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF THR-106; ILE-107; PHE-108; TYR-109 AND GLY-111, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19151223; DOI=10.1105/tpc.108.064097;
RA Chung H.S., Howe G.A.;
RT "A critical role for the TIFY motif in repression of jasmonate signaling by
RT a stabilized splice variant of the JASMONATE ZIM-domain protein JAZ10 in
RT Arabidopsis.";
RL Plant Cell 21:131-145(2009).
RN [2]
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 [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 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP INDUCTION BY JASMONATE.
RX PubMed=17637677; DOI=10.1038/nature05960;
RA Thines B., Katsir L., Melotto M., Niu Y., Mandaokar A., Liu G., Nomura K.,
RA He S.Y., Howe G.A., Browse J.;
RT "JAZ repressor proteins are targets of the SCF(COI1) complex during
RT jasmonate signalling.";
RL Nature 448:661-665(2007).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17637675; DOI=10.1038/nature06006;
RA Chini A., Fonseca S., Fernandez G., Adie B., Chico J.M., Lorenzo O.,
RA Garcia-Casado G., Lopez-Vidriero I., Lozano F.M., Ponce M.R., Micol J.L.,
RA Solano R.;
RT "The JAZ family of repressors is the missing link in jasmonate
RT signalling.";
RL Nature 448:666-671(2007).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17499004; DOI=10.1016/j.tplants.2007.04.004;
RA Vanholme B., Grunewald W., Bateman A., Kohchi T., Gheysen G.;
RT "The tify family previously known as ZIM.";
RL Trends Plant Sci. 12:239-244(2007).
RN [9]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND
RP DOMAIN.
RX PubMed=17675405; DOI=10.1105/tpc.107.050708;
RA Yan Y., Stolz S., Chetelat A., Reymond P., Pagni M., Dubugnon L.,
RA Farmer E.E.;
RT "A downstream mediator in the growth repression limb of the jasmonate
RT pathway.";
RL Plant Cell 19:2470-2483(2007).
RN [10]
RP INDUCTION BY WOUNDING AND HERBIVORY.
RX PubMed=18223147; DOI=10.1104/pp.107.115691;
RA Chung H.S., Koo A.J., Gao X., Jayanty S., Thines B., Jones A.D., Howe G.A.;
RT "Regulation and function of Arabidopsis JASMONATE ZIM-domain genes in
RT response to wounding and herbivory.";
RL Plant Physiol. 146:952-964(2008).
RN [11]
RP INTERACTION WITH MYC2.
RX PubMed=19309455; DOI=10.1111/j.1365-313x.2009.03852.x;
RA Chini A., Fonseca S., Chico J.M., Fernandez-Calvo P., Solano R.;
RT "The ZIM domain mediates homo- and heteromeric interactions between
RT Arabidopsis JAZ proteins.";
RL Plant J. 59:77-87(2009).
RN [12]
RP INTERACTION WITH AFPH2/NINJA.
RX PubMed=20360743; DOI=10.1038/nature08854;
RA Pauwels L., Barbero G.F., Geerinck J., Tilleman S., Grunewald W.,
RA Perez A.C., Chico J.M., Bossche R.V., Sewell J., Gil E., Garcia-Casado G.,
RA Witters E., Inze D., Long J.A., De Jaeger G., Solano R., Goossens A.;
RT "NINJA connects the co-repressor TOPLESS to jasmonate signalling.";
RL Nature 464:788-791(2010).
RN [13]
RP FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH MYC2; MYC3; MYC4 AND
RP AFPH2/NINJA, MUTAGENESIS OF 32-ARG--ARG-34; THR-106 AND ILE-107, AND
RP INDUCTION BY JASMONIC ACID.
RX PubMed=23632853; DOI=10.1104/pp.113.218164;
RA Moreno J.E., Shyu C., Campos M.L., Patel L.C., Chung H.S., Yao J., He S.Y.,
RA Howe G.A.;
RT "Negative feedback control of jasmonate signaling by an alternative splice
RT variant of JAZ10.";
RL Plant Physiol. 162:1006-1017(2013).
RN [14]
RP FUNCTION, AND INTERACTION WITH RHD6 AND RSL1.
RX PubMed=31988260; DOI=10.1105/tpc.19.00617;
RA Han X., Zhang M., Yang M., Hu Y.;
RT "Arabidopsis JAZ proteins interact with and suppress RHD6 transcription
RT factor to regulate jasmonate-stimulated root hair development.";
RL Plant Cell 32:1049-1062(2020).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 16-58 AND 166-192.
RX PubMed=28137867; DOI=10.1073/pnas.1616938114;
RA Zhang F., Ke J., Zhang L., Chen R., Sugimoto K., Howe G.A., Xu H.E.,
RA Zhou M., He S.Y., Melcher K.;
RT "Structural insights into alternative splicing-mediated desensitization of
RT jasmonate signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:1720-1725(2017).
CC -!- FUNCTION: [Isoform 3]: Repressor of jasmonate (JA) responses that lacks
CC the entire Jas domain and possesses severe JA insensitivity and
CC resistance to JA-induced degradation (PubMed:19151223, PubMed:17675405,
CC PubMed:23632853). Acts as an endogenous repressor of JA signal output
CC in JA-stimulated cells (PubMed:19151223). Modulator of JA-controlled
CC growth inhibition in response to wounding (PubMed:17675405).
CC {ECO:0000269|PubMed:17675405, ECO:0000269|PubMed:19151223,
CC ECO:0000269|PubMed:23632853}.
CC -!- FUNCTION: [Isoform 2]: Repressor of jasmonate (JA) responses that lacks
CC part of the Jas domain and possesses JA insensitivity and partial
CC resistance to JA-induced degradation. {ECO:0000269|PubMed:19151223}.
CC -!- FUNCTION: Repressor of jasmonate (JA) responses (PubMed:19151223).
CC Interacts with and suppresses RHD6 and RSL1 transcription factor
CC activities to negatively regulate jasmonate-stimulated root hair
CC development (PubMed:31988260). {ECO:0000269|PubMed:19151223,
CC ECO:0000269|PubMed:31988260}.
CC -!- SUBUNIT: Homo- and heterodimer. Interacts with MYC2, MYC3, MYC4,
CC AFPH2/NINJA, TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY6B/JAZ3, TIFY6A/JAZ4,
CC TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY7/JAZ9, TIFY3A/JAZ11 and TIFY3B/JAZ12.
CC Isoform 1 and isoform 2 interact with COI1. Isoform 3 does not interact
CC with COI1 (PubMed:19151223, PubMed:19309455, PubMed:20360743,
CC PubMed:23632853). Interacts with RHD6 and RSL1 (PubMed:31988260).
CC {ECO:0000269|PubMed:19151223, ECO:0000269|PubMed:19309455,
CC ECO:0000269|PubMed:20360743, ECO:0000269|PubMed:23632853,
CC ECO:0000269|PubMed:31988260}.
CC -!- INTERACTION:
CC Q93ZM9; Q9SV55: AFPH2; NbExp=7; IntAct=EBI-2312172, EBI-1787005;
CC Q93ZM9; Q9LNJ5: BHLH13; NbExp=4; IntAct=EBI-2312172, EBI-4434261;
CC Q93ZM9; Q39204: MYC2; NbExp=2; IntAct=EBI-2312172, EBI-1792336;
CC Q93ZM9; O49687: MYC4; NbExp=3; IntAct=EBI-2312172, EBI-15406909;
CC Q93ZM9; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2312172, EBI-4426144;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:17675405, ECO:0000269|PubMed:19151223}. Note=Isoform
CC 1, isoform 2 and isoform 3 are localized to the nucleus.
CC {ECO:0000269|PubMed:19151223}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=JAZ10.1;
CC IsoId=Q93ZM9-1; Sequence=Displayed;
CC Name=2; Synonyms=JAZ10.3;
CC IsoId=Q93ZM9-2; Sequence=VSP_027854;
CC Name=3; Synonyms=JAZ10.4;
CC IsoId=Q93ZM9-3; Sequence=VSP_053475, VSP_053476;
CC -!- INDUCTION: Up-regulated by jasmonate, wounding and herbivory.
CC {ECO:0000269|PubMed:17637677, ECO:0000269|PubMed:17675405,
CC ECO:0000269|PubMed:18223147, ECO:0000269|PubMed:23632853}.
CC -!- DOMAIN: The tify domain is required for dimerization.
CC {ECO:0000269|PubMed:19151223}.
CC -!- DOMAIN: The jas domain (168-193) is required for interaction with COI1.
CC {ECO:0000269|PubMed:19151223}.
CC -!- DOMAIN: [Isoform 3]: Binds to MYC2 via a cryptic CMID domain (16-58)
CC instead of the absent jas domain. {ECO:0000269|PubMed:19151223}.
CC -!- PTM: Ubiquitinated. Targeted for degradation by the SCF(COI1) E3
CC ubiquitin ligase-proteasome pathway during jasmonate signaling.
CC {ECO:0000269|PubMed:23632853}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks the entire Jas domain and is highly
CC resistant to jasmonate-induced degradation mediated by the 26S-
CC proteasome pathway. {ECO:0000269|PubMed:19151223}.
CC -!- MISCELLANEOUS: [Isoform 1]: Not involved in jasmonate responses
CC regulation.
CC -!- SIMILARITY: Belongs to the TIFY/JAZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86629.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ417331; ACN58542.1; -; mRNA.
DR EMBL; AL163491; CAB86629.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91865.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91866.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91867.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91868.1; -; Genomic_DNA.
DR EMBL; AY056444; AAL08300.1; -; mRNA.
DR EMBL; AY081715; AAL87368.1; -; mRNA.
DR EMBL; BX833870; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T48569; T48569.
DR RefSeq; NP_001154713.1; NM_001161241.2. [Q93ZM9-3]
DR RefSeq; NP_568287.1; NM_121325.3. [Q93ZM9-1]
DR RefSeq; NP_974775.1; NM_203046.3. [Q93ZM9-2]
DR RefSeq; NP_974776.1; NM_203047.3. [Q93ZM9-2]
DR PDB; 5T0F; X-ray; 2.40 A; B=16-58.
DR PDB; 5T0Q; X-ray; 2.15 A; B=166-192.
DR PDBsum; 5T0F; -.
DR PDBsum; 5T0Q; -.
DR AlphaFoldDB; Q93ZM9; -.
DR SMR; Q93ZM9; -.
DR BioGRID; 16440; 24.
DR DIP; DIP-53276N; -.
DR ELM; Q93ZM9; -.
DR IntAct; Q93ZM9; 9.
DR STRING; 3702.AT5G13220.1; -.
DR PaxDb; Q93ZM9; -.
DR ProteomicsDB; 234330; -. [Q93ZM9-1]
DR EnsemblPlants; AT5G13220.1; AT5G13220.1; AT5G13220. [Q93ZM9-1]
DR EnsemblPlants; AT5G13220.2; AT5G13220.2; AT5G13220. [Q93ZM9-2]
DR EnsemblPlants; AT5G13220.3; AT5G13220.3; AT5G13220. [Q93ZM9-2]
DR EnsemblPlants; AT5G13220.4; AT5G13220.4; AT5G13220. [Q93ZM9-3]
DR GeneID; 831162; -.
DR Gramene; AT5G13220.1; AT5G13220.1; AT5G13220. [Q93ZM9-1]
DR Gramene; AT5G13220.2; AT5G13220.2; AT5G13220. [Q93ZM9-2]
DR Gramene; AT5G13220.3; AT5G13220.3; AT5G13220. [Q93ZM9-2]
DR Gramene; AT5G13220.4; AT5G13220.4; AT5G13220. [Q93ZM9-3]
DR KEGG; ath:AT5G13220; -.
DR Araport; AT5G13220; -.
DR TAIR; locus:2183921; AT5G13220.
DR eggNOG; ENOG502RZEQ; Eukaryota.
DR HOGENOM; CLU_124666_0_0_1; -.
DR InParanoid; Q93ZM9; -.
DR OMA; NRNPVDW; -.
DR PhylomeDB; Q93ZM9; -.
DR PRO; PR:Q93ZM9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZM9; baseline and differential.
DR Genevisible; Q93ZM9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031347; P:regulation of defense response; IBA:GO_Central.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR InterPro; IPR018467; CCT_CS.
DR InterPro; IPR040390; TIFY/JAZ.
DR InterPro; IPR010399; Tify_dom.
DR PANTHER; PTHR33077; PTHR33077; 1.
DR Pfam; PF09425; Jas_motif; 1.
DR Pfam; PF06200; tify; 1.
DR SMART; SM00979; TIFY; 1.
DR PROSITE; PS51320; TIFY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Jasmonic acid signaling pathway;
KW Nucleus; Plant defense; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..197
FT /note="Protein TIFY 9"
FT /id="PRO_0000300651"
FT DOMAIN 98..132
FT /note="Tify"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00650"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..193
FT /note="Jas"
FT /evidence="ECO:0000255"
FT MOTIF 170..177
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 57..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 148..167
FT /note="VILPTTLRPKLFGQNLEGDL -> IFPSQGESHCNVFSRSARRD (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:19151223"
FT /id="VSP_053475"
FT VAR_SEQ 168..197
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19151223"
FT /id="VSP_053476"
FT VAR_SEQ 186..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_027854"
FT MUTAGEN 32..34
FT /note="RRR->AAA: In isoform 3; no effect on dimerization
FT but loss of interaction with MYC2. In isoform 1; no effect
FT on dimerization or interaction with MYC2."
FT /evidence="ECO:0000269|PubMed:23632853"
FT MUTAGEN 32..34
FT /note="RRR->ARA: In isoform 3; no effect on dimerization or
FT interaction with MYC2."
FT /evidence="ECO:0000269|PubMed:23632853"
FT MUTAGEN 32..33
FT /note="RR->AA: In isoform 3; no effect on dimerization or
FT interaction with MYC2."
FT MUTAGEN 33..34
FT /note="RR->AA: In isoform 3; no effect on dimerization or
FT interaction with MYC2."
FT MUTAGEN 106
FT /note="T->A: No effect on dimerization and interactions
FT with TIFY11B/JAZ6 and AFPH2/NINJA."
FT /evidence="ECO:0000269|PubMed:19151223,
FT ECO:0000269|PubMed:23632853"
FT MUTAGEN 107
FT /note="I->A: Loss of dimerization, loss of interaction with
FT TIFY11B/JAZ6 and strongly decreased interaction with
FT AFPH2/NINJA."
FT /evidence="ECO:0000269|PubMed:19151223,
FT ECO:0000269|PubMed:23632853"
FT MUTAGEN 108
FT /note="F->A: No effect on dimerization and interaction with
FT TIFY11B/JAZ6."
FT /evidence="ECO:0000269|PubMed:19151223"
FT MUTAGEN 109
FT /note="Y->A: No effect on dimerization and interaction with
FT TIFY11B/JAZ6."
FT /evidence="ECO:0000269|PubMed:19151223"
FT MUTAGEN 111
FT /note="G->A: Loss of dimerization and loss of interaction
FT with TIFY11B/JAZ6."
FT /evidence="ECO:0000269|PubMed:19151223"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:5T0F"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:5T0F"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:5T0Q"
SQ SEQUENCE 197 AA; 21813 MW; 475DADBCEDC540E1 CRC64;
MSKATIELDF LGLEKKQTNN APKPKFQKFL DRRRSFRDIQ GAISKIDPEI IKSLLASTGN
NSDSSAKSRS VPSTPREDQP QIPISPVHAS LARSSTELVS GTVPMTIFYN GSVSVFQVSR
NKAGEIMKVA NEAASKKDES SMETDLSVIL PTTLRPKLFG QNLEGDLPIA RRKSLQRFLE
KRKERLVSTS PYYPTSA
