GenomeNet

Database: UniProt
Entry: KEG_ARATH
LinkDB: KEG_ARATH
Original site: KEG_ARATH 
ID   KEG_ARATH               Reviewed;        1625 AA.
AC   Q9FY48; Q27YP2; Q9FY47;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   16-OCT-2019, entry version 145.
DE   RecName: Full=E3 ubiquitin-protein ligase KEG;
DE            EC=2.3.2.27;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein KEEP ON GOING;
DE   AltName: Full=RING finger protein KEG;
DE   AltName: Full=RING-type E3 ubiquitin transferase KEG {ECO:0000305};
GN   Name=KEG; OrderedLocusNames=At5g13530; ORFNames=T6I14.60, T6I14.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, PHOSPHORYLATION,
RP   UBIQUITINATION, AND INTERACTION WITH ABI5.
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   [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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA   Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT   "Evaluation and classification of RING-finger domains encoded by the
RT   Arabidopsis genome.";
RL   Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=15644464; DOI=10.1104/pp.104.052423;
RA   Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E.,
RA   Callis J.;
RT   "Functional analysis of the RING-type ubiquitin ligase family of
RT   Arabidopsis.";
RL   Plant Physiol. 137:13-30(2005).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP   GLY-1144.
RX   PubMed=18815384; DOI=10.1104/pp.108.127605;
RA   Wawrzynska A., Christiansen K.M., Lan Y., Rodibaugh N.L., Innes R.W.;
RT   "Powdery mildew resistance conferred by loss of the ENHANCED DISEASE
RT   RESISTANCE1 protein kinase is suppressed by a missense mutation in
RT   KEEP ON GOING, a regulator of abscisic acid signaling.";
RL   Plant Physiol. 148:1510-1522(2008).
RN   [7]
RP   FUNCTION, AUTOUBIQUITINATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF 29-CYS--HIS-31 AND LYS-176.
RC   STRAIN=cv. Columbia;
RX   PubMed=20682837; DOI=10.1105/tpc.110.076075;
RA   Liu H., Stone S.L.;
RT   "Abscisic acid increases Arabidopsis ABI5 transcription factor levels
RT   by promoting KEG E3 ligase self-ubiquitination and proteasomal
RT   degradation.";
RL   Plant Cell 22:2630-2641(2010).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EDR1, AND MUTAGENESIS
RP   OF GLY-1144.
RX   PubMed=21343429; DOI=10.1104/pp.110.171785;
RA   Gu Y., Innes R.W.;
RT   "The KEEP ON GOING protein of Arabidopsis recruits the ENHANCED
RT   DISEASE RESISTANCE1 protein to trans-Golgi network/early endosome
RT   vesicles.";
RL   Plant Physiol. 155:1827-1838(2011).
CC   -!- FUNCTION: Mediates E2-dependent protein ubiquitination. Acts as a
CC       negative regulator of abscisic acid signaling. Required for ABI5
CC       degradation, by mediating its ubiquitination. Together with EDR1,
CC       may regulate endocytic trafficking and/or the formation of
CC       signaling complexes on trans-Golgi network (TGN)/ early endosome
CC       (EE) vesicles during stress responses.
CC       {ECO:0000269|PubMed:18815384, ECO:0000269|PubMed:20682837,
CC       ECO:0000269|PubMed:21343429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC         protein]-L-lysine.; EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with ABI5 and EDR1.
CC       {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:21343429}.
CC   -!- INTERACTION:
CC       Q9SJN0:ABI5; NbExp=2; IntAct=EBI-1955729, EBI-1778690;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000269|PubMed:21343429}. Early endosome
CC       {ECO:0000269|PubMed:21343429}.
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=Q9FY48-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues of young seedlings.
CC       In flowering plants, only detected in the youngest part of the
CC       stem, anthers and the receptacle of immature siliques. Not found
CC       in mature leave, older parts of the stem, flower parts other than
CC       anthers or mature siliques. {ECO:0000269|PubMed:18815384}.
CC   -!- DEVELOPMENTAL STAGE: Expressed mainly in the actively growing and
CC       dividing cells. {ECO:0000269|PubMed:18815384}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- PTM: Autophosphotylated and autoubiquitinated in vitro.
CC       {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC   -!- PTM: Phosphorylation enhances self-ubiquitination.
CC       {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC   -!- PTM: Autoubiquitinated in response to abscisic acid (ABA) and
CC       subsequently targeted to proteolysis.
CC       {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC   -!- DISRUPTION PHENOTYPE: Plants are seedling lethal and are
CC       hypersensitive to glucose and abscisic acid. High accumulation of
CC       ABI5. {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC   -!- CAUTION: The protein kinase domain is predicted to be
CC       catalytically inactive but PubMed:17194765 shows an in vitro
CC       activity. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC05430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAC05431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DQ315360; ABC46683.1; -; mRNA.
DR   EMBL; AL391710; CAC05430.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL391710; CAC05431.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91908.1; -; Genomic_DNA.
DR   RefSeq; NP_196857.2; NM_121356.3. [Q9FY48-1]
DR   SMR; Q9FY48; -.
DR   BioGrid; 16475; 12.
DR   IntAct; Q9FY48; 1.
DR   STRING; 3702.AT5G13530.1; -.
DR   iPTMnet; Q9FY48; -.
DR   PaxDb; Q9FY48; -.
DR   PRIDE; Q9FY48; -.
DR   EnsemblPlants; AT5G13530.1; AT5G13530.1; AT5G13530. [Q9FY48-1]
DR   GeneID; 831197; -.
DR   Gramene; AT5G13530.1; AT5G13530.1; AT5G13530. [Q9FY48-1]
DR   KEGG; ath:AT5G13530; -.
DR   Araport; AT5G13530; -.
DR   TAIR; locus:2185061; AT5G13530.
DR   eggNOG; KOG0198; Eukaryota.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG4185; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   HOGENOM; HOG000084006; -.
DR   InParanoid; Q9FY48; -.
DR   KO; K16279; -.
DR   OMA; WVRLRNN; -.
DR   OrthoDB; 24404at2759; -.
DR   PhylomeDB; Q9FY48; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FY48; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FY48; baseline and differential.
DR   Genevisible; Q9FY48; AT.
DR   GO; GO:0005769; C:early endosome; IDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR   GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0006952; P:defense response; IMP:TAIR.
DR   GO; GO:0048589; P:developmental growth; IMP:TAIR.
DR   GO; GO:0016197; P:endosomal transport; IMP:TAIR.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IDA:TAIR.
DR   GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   GO; GO:0032940; P:secretion by cell; IMP:TAIR.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR040847; SH3_15.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF18346; SH3_15; 8.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Alternative splicing; ANK repeat;
KW   ATP-binding; Complete proteome; Endosome; Golgi apparatus; Kinase;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1625       E3 ubiquitin-protein ligase KEG.
FT                                /FTId=PRO_0000356172.
FT   DOMAIN      141    427       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REPEAT      467    496       ANK 1.
FT   REPEAT      510    540       ANK 2.
FT   REPEAT      544    573       ANK 3.
FT   REPEAT      579    608       ANK 4.
FT   REPEAT      612    641       ANK 5.
FT   REPEAT      647    676       ANK 6.
FT   REPEAT      685    720       ANK 7.
FT   REPEAT      725    754       ANK 8.
FT   REPEAT      758    787       ANK 9.
FT   REPEAT      791    826       ANK 10.
FT   REPEAT      832    863       ANK 11.
FT   ZN_FING      10     56       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   NP_BIND     147    155       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS     88    107       Asp-rich.
FT   COMPBIAS   1494   1497       Poly-Glu.
FT   BINDING     176    176       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MUTAGEN      29     31       CGH->AGA: Small sterile plants unable to
FT                                polyubiquitinate ABI5.
FT                                {ECO:0000269|PubMed:20682837}.
FT   MUTAGEN     176    176       K->R: Loss of kinase activity associated
FT                                with the loss of ABA-induced KEG
FT                                autoubiquitination and subsequent
FT                                degradation.
FT                                {ECO:0000269|PubMed:20682837}.
FT   MUTAGEN    1144   1144       G->S: In keg-4/supp69; confers resistance
FT                                to 6% glucose and suppresses abscisic
FT                                acid signaling. Suppression of EDR1
FT                                disruption- (edr1-) mediated disease
FT                                resistance. Reduced endosomal
FT                                localization but increased localization
FT                                to the endoplasmic reticulum and cytosol.
FT                                {ECO:0000269|PubMed:18815384,
FT                                ECO:0000269|PubMed:21343429}.
SQ   SEQUENCE   1625 AA;  178216 MW;  8F16ECA3DC32B9C4 CRC64;
     MVGRVKVPCC SVCHTRYNED ERVPLLLQCG HGFCKDCLSK MFSTSSDTTL TCPRCRHVSV
     VGNSVQGLRK NYAMLALIHA ASGGANFDCD YTDDEDDDDE EDGSDEDGAR AARGFHASSS
     INSLCGPVIE VGAHPEMKLV RQIGEESSSG GFGGVEMWDA TVAGGGGRCK HRVAVKKMTL
     TEDMDVEWMQ GQLESLRRAS MWCRNVCTFH GVVKMDGSLC LLMDRCFGSV QSEMQRNEGR
     LTLEQILRYG ADVARGVAEL HAAGVICMNI KPSNLLLDAS GNAVVSDYGL APILKKPTCQ
     KTRPEFDSSK VTLYTDCVTL SPHYTAPEAW GPVKKLFWED ASGVSPESDA WSFGCTLVEM
     CTGSTPWDGL SREEIFQAVV KARKVPPQYE RIVGVGIPRE LWKMIGECLQ FKPSKRPTFN
     AMLATFLRHL QEIPRSPSAS PDNGIAKICE VNIVQAPRAT NIGVFQDNPN NLHRVVLEGD
     FEGVRNILAK AAAGGGGSSV RSLLEAQNAD GQSALHLACR RGSAELVEAI LEYGEANVDI
     VDKDGDPPLV FALAAGSPQC VHVLIKKGAN VRSRLREGSG PSVAHVCSYH GQPDCMRELL
     VAGADPNAVD DEGETVLHRA VAKKYTDCAI VILENGGSRS MTVSNAKCLT PLHMCVATWN
     VAVIKRWVEV SSPEEISQAI NIPSPVGTAL CMAASIRKDH EKEGRELVQI LLAAGADPTA
     QDAQHGRTAL HTAAMANNVE LVRVILDAGV NANIRNVHNT IPLHMALARG ANSCVSLLLE
     SGSDCNIQDD EGDNAFHIAA DAAKMIRENL DWLIVMLRSP DAAVDVRNHS GKTVRDFLEA
     LPREWISEDL MEALLKRGVH LSPTIYEVGD WVKFKRGITT PLHGWQGAKP KSVGFVQTIL
     EKEDMIIAFC SGEARVLANE VVKLIPLDRG QHVRLRADVK EPRFGWRGQS RDSVGTVLCV
     DEDGILRVGF PGASRGWKAD PAEMERVEEF KVGDWVRIRQ NLTSAKHGFG SVVPGSMGIV
     YCVRPDSSLL VELSYLPNPW HCEPEEVEPV APFRIGDRVC VKRSVAEPRY AWGGETHHSV
     GKISEIENDG LLIIEIPNRP IPWQADPSDM EKIDDFKVGD WVRVKASVSS PKYGWEDITR
     NSIGVMHSLD EDGDVGIAFC FRSKPFSCSV TDVEKVTPFH VGQEIHMTPS ITQPRLGWSN
     ETPATIGKVM RIDMDGTLSA QVTGRQTLWR VSPGDAELLS GFEVGDWVRS KPSLGNRPSY
     DWSNVGRESI AVVHSIQETG YLELACCFRK GRWSTHYTDL EKIPALKVGQ FVHFQKGITE
     PRWGWRAAKP DSRGIITTVH ADGEVRVAFF GLPGLWRGDP ADLEVEPMFE VGEWVRLREG
     VSCWKSVGPG SVGVVHGVGY EGDEWDGTTS VSFCGEQERW AGPTSHLEKA KKLVVGQKTR
     VKLAVKQPRF GWSGHSHGSV GTISAIDADG KLRIYTPAGS KTWMLDPSEV ETIEEEELKI
     GDWVRVKASI TTPTYQWGEV NPSSTGVVHR MEDGDLCVSF CFLDRLWLCK AGELERIRPF
     RIGDRVKIKD GLVTPRWGWG METHASKGHV VGVDANGKLR IKFLWREGRP WIGDPADIVL
     DETSG
//
DBGET integrated database retrieval system