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Q9FY48

- KEG_ARATH

UniProt

Q9FY48 - KEG_ARATH

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Protein

E3 ubiquitin-protein ligase KEG

Gene
KEG, At5g13530, T6I14.60, T6I14.70
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mediates E2-dependent protein ubiquitination. Acts as a negative regulator of abscisic acid signaling. Required for ABI5 degradation, by mediating its ubiquitination. Together with EDR1, may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei176 – 1761ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 5647RING-typeAdd
BLAST
Nucleotide bindingi147 – 1559ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
  4. protein kinase activity Source: TAIR
  5. protein self-association Source: TAIR
  6. protein serine/threonine kinase activity Source: UniProtKB-KW
  7. ubiquitin-protein transferase activity Source: TAIR
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: TAIR
  2. defense response Source: TAIR
  3. developmental growth Source: TAIR
  4. endosomal transport Source: TAIR
  5. negative regulation of abscisic acid-activated signaling pathway Source: TAIR
  6. protein ubiquitination Source: TAIR
  7. response to abscisic acid Source: TAIR
  8. secretion by cell Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Ligase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Abscisic acid signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G13530-MONOMER.
ARA:GQT-1981-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase KEG (EC:2.7.11.1, EC:6.3.2.-)
Alternative name(s):
Protein KEEP ON GOING
RING finger protein KEG
Gene namesi
Name:KEG
Ordered Locus Names:At5g13530
ORF Names:T6I14.60, T6I14.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G13530.

Subcellular locationi

Golgi apparatustrans-Golgi network. Early endosome 1 Publication

GO - Cellular componenti

  1. early endosome Source: TAIR
  2. trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus

Pathology & Biotechi

Disruption phenotypei

Plants are seedling lethal and are hypersensitive to glucose and abscisic acid. High accumulation of ABI5.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 313CGH → AGA: Small sterile plants unable to polyubiquitinate ABI5. 1 Publication
Mutagenesisi176 – 1761K → R: Loss of kinase activity associated with the loss of ABA-induced KEG autoubiquitination and subsequent degradation. 1 Publication
Mutagenesisi1144 – 11441G → S in keg-4/supp69; confers resistance to 6% glucose and suppresses abscisic acid signaling. Suppression of EDR1 disruption- (edr1-) mediated disease resistance. Reduced endosomal localization but increased localization to the endoplasmic reticulum and cytosol. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16251625E3 ubiquitin-protein ligase KEGPRO_0000356172Add
BLAST

Post-translational modificationi

Autophosphotylated and autoubiquitinated in vitro.
Phosphorylation enhances self-ubiquitination.
Autoubiquitinated in response to abscisic acid (ABA) and subsequently targeted to proteolysis.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9FY48.
PRIDEiQ9FY48.

Expressioni

Tissue specificityi

Expressed in all tissues of young seedlings. In flowering plants, only detected in the youngest part of the stem, anthers and the receptacle of immature siliques. Not found in mature leave, older parts of the stem, flower parts other than anthers or mature siliques.1 Publication

Developmental stagei

Expressed mainly in the actively growing and dividing cells.1 Publication

Gene expression databases

GenevestigatoriQ9FY48.

Interactioni

Subunit structurei

Interacts with ABI5 and EDR1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI5Q9SJN02EBI-1955729,EBI-1778690

Protein-protein interaction databases

BioGridi16475. 6 interactions.
IntActiQ9FY48. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9FY48.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 427287Protein kinaseAdd
BLAST
Repeati467 – 49630ANK 1Add
BLAST
Repeati510 – 54031ANK 2Add
BLAST
Repeati544 – 57330ANK 3Add
BLAST
Repeati579 – 60830ANK 4Add
BLAST
Repeati612 – 64130ANK 5Add
BLAST
Repeati647 – 67630ANK 6Add
BLAST
Repeati685 – 72036ANK 7Add
BLAST
Repeati725 – 75430ANK 8Add
BLAST
Repeati758 – 78730ANK 9Add
BLAST
Repeati791 – 82636ANK 10Add
BLAST
Repeati832 – 86332ANK 11Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 10720Asp-richAdd
BLAST
Compositional biasi1494 – 14974Poly-Glu

Domaini

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme By similarity.

Sequence similaritiesi

Contains 11 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000084006.
InParanoidiQ27YP2.
KOiK16279.
OMAiVVRRWVE.
PhylomeDBiQ9FY48.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR027370. Znf-RING_LisH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FY48-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MVGRVKVPCC SVCHTRYNED ERVPLLLQCG HGFCKDCLSK MFSTSSDTTL     50
TCPRCRHVSV VGNSVQGLRK NYAMLALIHA ASGGANFDCD YTDDEDDDDE 100
EDGSDEDGAR AARGFHASSS INSLCGPVIE VGAHPEMKLV RQIGEESSSG 150
GFGGVEMWDA TVAGGGGRCK HRVAVKKMTL TEDMDVEWMQ GQLESLRRAS 200
MWCRNVCTFH GVVKMDGSLC LLMDRCFGSV QSEMQRNEGR LTLEQILRYG 250
ADVARGVAEL HAAGVICMNI KPSNLLLDAS GNAVVSDYGL APILKKPTCQ 300
KTRPEFDSSK VTLYTDCVTL SPHYTAPEAW GPVKKLFWED ASGVSPESDA 350
WSFGCTLVEM CTGSTPWDGL SREEIFQAVV KARKVPPQYE RIVGVGIPRE 400
LWKMIGECLQ FKPSKRPTFN AMLATFLRHL QEIPRSPSAS PDNGIAKICE 450
VNIVQAPRAT NIGVFQDNPN NLHRVVLEGD FEGVRNILAK AAAGGGGSSV 500
RSLLEAQNAD GQSALHLACR RGSAELVEAI LEYGEANVDI VDKDGDPPLV 550
FALAAGSPQC VHVLIKKGAN VRSRLREGSG PSVAHVCSYH GQPDCMRELL 600
VAGADPNAVD DEGETVLHRA VAKKYTDCAI VILENGGSRS MTVSNAKCLT 650
PLHMCVATWN VAVIKRWVEV SSPEEISQAI NIPSPVGTAL CMAASIRKDH 700
EKEGRELVQI LLAAGADPTA QDAQHGRTAL HTAAMANNVE LVRVILDAGV 750
NANIRNVHNT IPLHMALARG ANSCVSLLLE SGSDCNIQDD EGDNAFHIAA 800
DAAKMIRENL DWLIVMLRSP DAAVDVRNHS GKTVRDFLEA LPREWISEDL 850
MEALLKRGVH LSPTIYEVGD WVKFKRGITT PLHGWQGAKP KSVGFVQTIL 900
EKEDMIIAFC SGEARVLANE VVKLIPLDRG QHVRLRADVK EPRFGWRGQS 950
RDSVGTVLCV DEDGILRVGF PGASRGWKAD PAEMERVEEF KVGDWVRIRQ 1000
NLTSAKHGFG SVVPGSMGIV YCVRPDSSLL VELSYLPNPW HCEPEEVEPV 1050
APFRIGDRVC VKRSVAEPRY AWGGETHHSV GKISEIENDG LLIIEIPNRP 1100
IPWQADPSDM EKIDDFKVGD WVRVKASVSS PKYGWEDITR NSIGVMHSLD 1150
EDGDVGIAFC FRSKPFSCSV TDVEKVTPFH VGQEIHMTPS ITQPRLGWSN 1200
ETPATIGKVM RIDMDGTLSA QVTGRQTLWR VSPGDAELLS GFEVGDWVRS 1250
KPSLGNRPSY DWSNVGRESI AVVHSIQETG YLELACCFRK GRWSTHYTDL 1300
EKIPALKVGQ FVHFQKGITE PRWGWRAAKP DSRGIITTVH ADGEVRVAFF 1350
GLPGLWRGDP ADLEVEPMFE VGEWVRLREG VSCWKSVGPG SVGVVHGVGY 1400
EGDEWDGTTS VSFCGEQERW AGPTSHLEKA KKLVVGQKTR VKLAVKQPRF 1450
GWSGHSHGSV GTISAIDADG KLRIYTPAGS KTWMLDPSEV ETIEEEELKI 1500
GDWVRVKASI TTPTYQWGEV NPSSTGVVHR MEDGDLCVSF CFLDRLWLCK 1550
AGELERIRPF RIGDRVKIKD GLVTPRWGWG METHASKGHV VGVDANGKLR 1600
IKFLWREGRP WIGDPADIVL DETSG 1625
Length:1,625
Mass (Da):178,216
Last modified:December 16, 2008 - v2
Checksum:i8F16ECA3DC32B9C4
GO

Sequence cautioni

The sequence CAC05430.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAC05431.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ315360 mRNA. Translation: ABC46683.1.
AL391710 Genomic DNA. Translation: CAC05430.1. Sequence problems.
AL391710 Genomic DNA. Translation: CAC05431.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91908.1.
RefSeqiNP_196857.2. NM_121356.2. [Q9FY48-1]
UniGeneiAt.32056.

Genome annotation databases

EnsemblPlantsiAT5G13530.1; AT5G13530.1; AT5G13530. [Q9FY48-1]
GeneIDi831197.
KEGGiath:AT5G13530.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ315360 mRNA. Translation: ABC46683.1 .
AL391710 Genomic DNA. Translation: CAC05430.1 . Sequence problems.
AL391710 Genomic DNA. Translation: CAC05431.1 . Sequence problems.
CP002688 Genomic DNA. Translation: AED91908.1 .
RefSeqi NP_196857.2. NM_121356.2. [Q9FY48-1 ]
UniGenei At.32056.

3D structure databases

ProteinModelPortali Q9FY48.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 16475. 6 interactions.
IntActi Q9FY48. 1 interaction.

Proteomic databases

PaxDbi Q9FY48.
PRIDEi Q9FY48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G13530.1 ; AT5G13530.1 ; AT5G13530 . [Q9FY48-1 ]
GeneIDi 831197.
KEGGi ath:AT5G13530.

Organism-specific databases

TAIRi AT5G13530.

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000084006.
InParanoidi Q27YP2.
KOi K16279.
OMAi VVRRWVE.
PhylomeDBi Q9FY48.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci ARA:AT5G13530-MONOMER.
ARA:GQT-1981-MONOMER.

Gene expression databases

Genevestigatori Q9FY48.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR027370. Znf-RING_LisH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 9 hits.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and development, is involved in abscisic acid signaling."
    Stone S.L., Williams L.A., Farmer L.M., Vierstra R.D., Callis J.
    Plant Cell 18:3415-3428(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, PHOSPHORYLATION, UBIQUITINATION, INTERACTION WITH ABI5.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome."
    Kosarev P., Mayer K.F.X., Hardtke C.S.
    Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION.
  5. "Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis."
    Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.
    Plant Physiol. 137:13-30(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  6. "Powdery mildew resistance conferred by loss of the ENHANCED DISEASE RESISTANCE1 protein kinase is suppressed by a missense mutation in KEEP ON GOING, a regulator of abscisic acid signaling."
    Wawrzynska A., Christiansen K.M., Lan Y., Rodibaugh N.L., Innes R.W.
    Plant Physiol. 148:1510-1522(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLY-1144.
  7. "Abscisic acid increases Arabidopsis ABI5 transcription factor levels by promoting KEG E3 ligase self-ubiquitination and proteasomal degradation."
    Liu H., Stone S.L.
    Plant Cell 22:2630-2641(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOUBIQUITINATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 29-CYS--HIS-31 AND LYS-176.
    Strain: cv. Columbia.
  8. "The KEEP ON GOING protein of Arabidopsis recruits the ENHANCED DISEASE RESISTANCE1 protein to trans-Golgi network/early endosome vesicles."
    Gu Y., Innes R.W.
    Plant Physiol. 155:1827-1838(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EDR1, MUTAGENESIS OF GLY-1144.

Entry informationi

Entry nameiKEG_ARATH
AccessioniPrimary (citable) accession number: Q9FY48
Secondary accession number(s): Q27YP2, Q9FY47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: September 3, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

The protein kinase domain is predicted to be catalytically inactive but 1 Publication shows an in vitro activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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