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Q9FY48 (KEG_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KEG
Ordered Locus Names:At5g13530
ORF Names:T6I14.60, T6I14.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1625 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with ABI5 and EDR1. Ref.1 Ref.8

Subcellular location

Golgi apparatustrans-Golgi network. Early endosome Ref.8.

Tissue specificity

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. Ref.6

Developmental stage

Expressed mainly in the actively growing and dividing cells. Ref.6

Domain

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

Post-translational modification

Autophosphotylated and autoubiquitinated in vitro.

Phosphorylation enhances self-ubiquitination.

Autoubiquitinated in response to abscisic acid (ABA) and subsequently targeted to proteolysis.

Disruption phenotype

Plants are seedling lethal and are hypersensitive to glucose and abscisic acid. High accumulation of ABI5. Ref.1 Ref.7

Sequence similarities

Contains 11 ANK repeats.

Contains 1 protein kinase domain.

Contains 1 RING-type zinc finger.

Caution

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

Sequence caution

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.

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
Ubl conjugation pathway
   Cellular componentEndosome
Golgi apparatus
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Ligase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid-activated signaling pathway

Inferred from mutant phenotype Ref.1Ref.6. Source: TAIR

defense response

Inferred from mutant phenotype Ref.6. Source: TAIR

developmental growth

Inferred from mutant phenotype Ref.1. Source: TAIR

endosomal transport

Inferred from mutant phenotype PubMed 23192225. Source: TAIR

negative regulation of abscisic acid-activated signaling pathway

Inferred from mutant phenotype Ref.7. Source: TAIR

protein ubiquitination

Inferred from direct assay Ref.1. Source: TAIR

response to abscisic acid

Inferred from mutant phenotype Ref.7. Source: TAIR

secretion by cell

Inferred from mutant phenotype PubMed 23192225. Source: TAIR

   Cellular_componentearly endosome

Inferred from direct assay Ref.8. Source: TAIR

trans-Golgi network

Inferred from direct assay Ref.8PubMed 23192225. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.1. Source: TAIR

protein self-association

Inferred from physical interaction Ref.8. Source: TAIR

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein transferase activity

Inferred from direct assay Ref.1Ref.6. Source: TAIR

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABI5Q9SJN02EBI-1955729,EBI-1778690

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FY48-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16251625E3 ubiquitin-protein ligase KEG
PRO_0000356172

Regions

Domain141 – 427287Protein kinase
Repeat467 – 49630ANK 1
Repeat510 – 54031ANK 2
Repeat544 – 57330ANK 3
Repeat579 – 60830ANK 4
Repeat612 – 64130ANK 5
Repeat647 – 67630ANK 6
Repeat685 – 72036ANK 7
Repeat725 – 75430ANK 8
Repeat758 – 78730ANK 9
Repeat791 – 82636ANK 10
Repeat832 – 86332ANK 11
Zinc finger10 – 5647RING-type
Nucleotide binding147 – 1559ATP By similarity
Compositional bias88 – 10720Asp-rich
Compositional bias1494 – 14974Poly-Glu

Sites

Binding site1761ATP By similarity

Experimental info

Mutagenesis29 – 313CGH → AGA: Small sterile plants unable to polyubiquitinate ABI5. Ref.7
Mutagenesis1761K → R: Loss of kinase activity associated with the loss of ABA-induced KEG autoubiquitination and subsequent degradation. Ref.7
Mutagenesis11441G → 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. Ref.6 Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 8F16ECA3DC32B9C4

FASTA1,625178,216
        10         20         30         40         50         60 
MVGRVKVPCC SVCHTRYNED ERVPLLLQCG HGFCKDCLSK MFSTSSDTTL TCPRCRHVSV 

        70         80         90        100        110        120 
VGNSVQGLRK NYAMLALIHA ASGGANFDCD YTDDEDDDDE EDGSDEDGAR AARGFHASSS 

       130        140        150        160        170        180 
INSLCGPVIE VGAHPEMKLV RQIGEESSSG GFGGVEMWDA TVAGGGGRCK HRVAVKKMTL 

       190        200        210        220        230        240 
TEDMDVEWMQ GQLESLRRAS MWCRNVCTFH GVVKMDGSLC LLMDRCFGSV QSEMQRNEGR 

       250        260        270        280        290        300 
LTLEQILRYG ADVARGVAEL HAAGVICMNI KPSNLLLDAS GNAVVSDYGL APILKKPTCQ 

       310        320        330        340        350        360 
KTRPEFDSSK VTLYTDCVTL SPHYTAPEAW GPVKKLFWED ASGVSPESDA WSFGCTLVEM 

       370        380        390        400        410        420 
CTGSTPWDGL SREEIFQAVV KARKVPPQYE RIVGVGIPRE LWKMIGECLQ FKPSKRPTFN 

       430        440        450        460        470        480 
AMLATFLRHL QEIPRSPSAS PDNGIAKICE VNIVQAPRAT NIGVFQDNPN NLHRVVLEGD 

       490        500        510        520        530        540 
FEGVRNILAK AAAGGGGSSV RSLLEAQNAD GQSALHLACR RGSAELVEAI LEYGEANVDI 

       550        560        570        580        590        600 
VDKDGDPPLV FALAAGSPQC VHVLIKKGAN VRSRLREGSG PSVAHVCSYH GQPDCMRELL 

       610        620        630        640        650        660 
VAGADPNAVD DEGETVLHRA VAKKYTDCAI VILENGGSRS MTVSNAKCLT PLHMCVATWN 

       670        680        690        700        710        720 
VAVIKRWVEV SSPEEISQAI NIPSPVGTAL CMAASIRKDH EKEGRELVQI LLAAGADPTA 

       730        740        750        760        770        780 
QDAQHGRTAL HTAAMANNVE LVRVILDAGV NANIRNVHNT IPLHMALARG ANSCVSLLLE 

       790        800        810        820        830        840 
SGSDCNIQDD EGDNAFHIAA DAAKMIRENL DWLIVMLRSP DAAVDVRNHS GKTVRDFLEA 

       850        860        870        880        890        900 
LPREWISEDL MEALLKRGVH LSPTIYEVGD WVKFKRGITT PLHGWQGAKP KSVGFVQTIL 

       910        920        930        940        950        960 
EKEDMIIAFC SGEARVLANE VVKLIPLDRG QHVRLRADVK EPRFGWRGQS RDSVGTVLCV 

       970        980        990       1000       1010       1020 
DEDGILRVGF PGASRGWKAD PAEMERVEEF KVGDWVRIRQ NLTSAKHGFG SVVPGSMGIV 

      1030       1040       1050       1060       1070       1080 
YCVRPDSSLL VELSYLPNPW HCEPEEVEPV APFRIGDRVC VKRSVAEPRY AWGGETHHSV 

      1090       1100       1110       1120       1130       1140 
GKISEIENDG LLIIEIPNRP IPWQADPSDM EKIDDFKVGD WVRVKASVSS PKYGWEDITR 

      1150       1160       1170       1180       1190       1200 
NSIGVMHSLD EDGDVGIAFC FRSKPFSCSV TDVEKVTPFH VGQEIHMTPS ITQPRLGWSN 

      1210       1220       1230       1240       1250       1260 
ETPATIGKVM RIDMDGTLSA QVTGRQTLWR VSPGDAELLS GFEVGDWVRS KPSLGNRPSY 

      1270       1280       1290       1300       1310       1320 
DWSNVGRESI AVVHSIQETG YLELACCFRK GRWSTHYTDL EKIPALKVGQ FVHFQKGITE 

      1330       1340       1350       1360       1370       1380 
PRWGWRAAKP DSRGIITTVH ADGEVRVAFF GLPGLWRGDP ADLEVEPMFE VGEWVRLREG 

      1390       1400       1410       1420       1430       1440 
VSCWKSVGPG SVGVVHGVGY EGDEWDGTTS VSFCGEQERW AGPTSHLEKA KKLVVGQKTR 

      1450       1460       1470       1480       1490       1500 
VKLAVKQPRF GWSGHSHGSV GTISAIDADG KLRIYTPAGS KTWMLDPSEV ETIEEEELKI 

      1510       1520       1530       1540       1550       1560 
GDWVRVKASI TTPTYQWGEV NPSSTGVVHR MEDGDLCVSF CFLDRLWLCK AGELERIRPF 

      1570       1580       1590       1600       1610       1620 
RIGDRVKIKD GLVTPRWGWG METHASKGHV VGVDANGKLR IKFLWREGRP WIGDPADIVL 


DETSG 

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References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_196857.2. NM_121356.2. [Q9FY48-1]
UniGeneAt.32056.

3D structure databases

ProteinModelPortalQ9FY48.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16475. 6 interactions.
IntActQ9FY48. 1 interaction.

Proteomic databases

PaxDbQ9FY48.
PRIDEQ9FY48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G13530.1; AT5G13530.1; AT5G13530. [Q9FY48-1]
GeneID831197.
KEGGath:AT5G13530.

Organism-specific databases

TAIRAT5G13530.

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000084006.
InParanoidQ27YP2.
KOK16279.
OMAVVRRWVE.
PhylomeDBQ9FY48.

Enzyme and pathway databases

BioCycARA:AT5G13530-MONOMER.
ARA:GQT-1981-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ9FY48.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
InterProIPR002110. 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]
PfamPF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 9 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. 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]
ProtoNetSearch...

Entry information

Entry nameKEG_ARATH
AccessionPrimary (citable) accession number: Q9FY48
Secondary accession number(s): Q27YP2, Q9FY47
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names