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Q42371 (ERECT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LRR receptor-like serine/threonine-protein kinase ERECTA

EC=2.7.11.1
Alternative name(s):
Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1
Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1
Protein TRANSPIRATION EFFICIENCY 1
Gene names
Name:ERECTA
Synonyms:ER, QRP1, QRS1, TE1
Ordered Locus Names:At2g26330
ORF Names:T1D16.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length976 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor kinase that, together with ERL1 and ERL2, regulates aerial architecture, including inflorescence (e.g. shoot apical meristem-originating organ shape, elongation of the internode and pedicels, and adaxial-abaxial polarity), and stomatal patterning (e.g. density and clustering), probably by tuning cell division and expansion. Modulates plant transpiration efficiency by controlling stomatal density, leaf photosynthetic capacity, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. Probable major trait regulating canalization (maintenance of phenotype despite varying environment) in many aspect of the plant physiology (e.g. plant morphology, light-dependent leaves number, branch number, flowering time, phytate and mineral concentrations) by transducing microenvironmental variation into phenotypic differentiation (ecological amplifier). May maintain development integrity in heat stress conditions. Regulates cell wall composition and structure. Confers resistance to the pathogenic bacteria Ralstonia solanacearum and to the necrotrophic fungi Plectosphaerella cucumerina and Pythium irregulare, and required for callose deposition upon infection. Resistance to P.cucumerina seems cell wall-mediated. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Mostly expressed in shoot apical meristems (SAM), organ primordia, flowers, siliques and young rosette leaves, and, to a lower extent, in stems and cauline leaves. Ref.1 Ref.8

Developmental stage

Strongly expressed in organ primordia and immature organs but weakly in mature organs. Observed in SAM at low levels during the vegetative growth with an increase at the transition to the reproductive growth phase. At the reproductive stage, localized in the young developing flowers. Expressed in inflorescence meristem and is up-regulated during flower initiation and formation of flower organs. Also found in cells that differentiate into pedicels. Ref.8 Ref.13

Polymorphism

The cultivar Landsberg erecta (cv. Ler) derives from cv. Landsberg (cv. La-0) in which ERECTA is mutated at Ile-750 (variant er).

Disruption phenotype

In er-104 and er-105, small curly leaves and compact inflorescence with short thick siliques, increased canalization of rosette leaf number during long days. Ref.1 Ref.22

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 20 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Plant defense
   Cellular componentMembrane
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from mutant phenotype Ref.12. Source: UniProtKB

defense response to fungus

Inferred from mutant phenotype Ref.17. Source: TAIR

inflorescence morphogenesis

Inferred from mutant phenotype Ref.10. Source: UniProtKB

leaf morphogenesis

Inferred from mutant phenotype Ref.16. Source: TAIR

plant-type cell wall organization

Inferred from mutant phenotype Ref.25. Source: UniProtKB

polarity specification of adaxial/abaxial axis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of cell adhesion

Inferred from mutant phenotype Ref.16. Source: TAIR

regulation of cell division

Inferred from genetic interaction Ref.18. Source: UniProtKB

regulation of cell growth

Inferred from genetic interaction Ref.18. Source: UniProtKB

regulation of organ morphogenesis

Inferred from mutant phenotype Ref.1. Source: TAIR

stomatal complex morphogenesis

Inferred from mutant phenotype Ref.19. Source: TAIR

transpiration

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay PubMed 14671022. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay. Source: UniProtKB

transmembrane receptor protein kinase activity

Inferred from sequence or structural similarity Ref.1. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 976952LRR receptor-like serine/threonine-protein kinase ERECTA
PRO_0000389000

Regions

Topological domain25 – 580556Extracellular Potential
Transmembrane581 – 60121Helical; Potential
Topological domain602 – 976375Cytoplasmic Potential
Repeat69 – 9224LRR 1
Repeat93 – 11523LRR 2
Repeat117 – 14024LRR 3
Repeat141 – 16323LRR 4
Repeat165 – 18723LRR 5
Repeat189 – 21224LRR 6
Repeat213 – 23523LRR 7
Repeat237 – 25923LRR 8
Repeat260 – 28223LRR 9
Repeat284 – 30623LRR 10
Repeat308 – 33023LRR 11
Repeat332 – 35524LRR 12
Repeat356 – 37924LRR 13
Repeat380 – 40122LRR 14
Repeat404 – 42522LRR 15
Repeat428 – 44922LRR 16
Repeat452 – 47322LRR 17
Repeat476 – 49823LRR 18
Repeat500 – 52223LRR 19
Repeat523 – 54523LRR 20
Domain648 – 918271Protein kinase
Nucleotide binding654 – 6629ATP By similarity

Sites

Active site7731Proton acceptor By similarity
Binding site6761ATP By similarity

Amino acid modifications

Modified residue6451Phosphothreonine By similarity
Modified residue7211Phosphotyrosine By similarity
Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation2211N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation3051N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation5431N-linked (GlcNAc...) Potential

Natural variations

Natural variant7501I → K Er-1 in strain: cv. Landsberg erecta; round leaves, compact inflorescence, blunt fruits, short and thick siliques and petioles, susceptibility to pathogens such as R.solanacearum, P.irregulare and P.cucumerina, abnormal cell-wall composition and increased canalization of rosette leaf number during long days. In er-101 and er-102, compact inflorescence with short siliques and pedicels. Ref.1 Ref.9 Ref.12 Ref.17 Ref.21 Ref.25
Natural variant8861V → M in strain: cv. Mt-0. Ref.7

Experimental info

Mutagenesis2821M → I in er-103; compact inflorescence with short siliques, but normal leaves. Ref.1 Ref.18
Mutagenesis4891G → D in er-117; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina. Ref.9 Ref.17
Mutagenesis8311D → N in er-114; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina. Ref.9 Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q42371 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0E51D46A4AB94C8D

FASTA976107,334
        10         20         30         40         50         60 
MALFRDIVLL GFLFCLSLVA TVTSEEGATL LEIKKSFKDV NNVLYDWTTS PSSDYCVWRG 

        70         80         90        100        110        120 
VSCENVTFNV VALNLSDLNL DGEISPAIGD LKSLLSIDLR GNRLSGQIPD EIGDCSSLQN 

       130        140        150        160        170        180 
LDLSFNELSG DIPFSISKLK QLEQLILKNN QLIGPIPSTL SQIPNLKILD LAQNKLSGEI 

       190        200        210        220        230        240 
PRLIYWNEVL QYLGLRGNNL VGNISPDLCQ LTGLWYFDVR NNSLTGSIPE TIGNCTAFQV 

       250        260        270        280        290        300 
LDLSYNQLTG EIPFDIGFLQ VATLSLQGNQ LSGKIPSVIG LMQALAVLDL SGNLLSGSIP 

       310        320        330        340        350        360 
PILGNLTFTE KLYLHSNKLT GSIPPELGNM SKLHYLELND NHLTGHIPPE LGKLTDLFDL 

       370        380        390        400        410        420 
NVANNDLEGP IPDHLSSCTN LNSLNVHGNK FSGTIPRAFQ KLESMTYLNL SSNNIKGPIP 

       430        440        450        460        470        480 
VELSRIGNLD TLDLSNNKIN GIIPSSLGDL EHLLKMNLSR NHITGVVPGD FGNLRSIMEI 

       490        500        510        520        530        540 
DLSNNDISGP IPEELNQLQN IILLRLENNN LTGNVGSLAN CLSLTVLNVS HNNLVGDIPK 

       550        560        570        580        590        600 
NNNFSRFSPD SFIGNPGLCG SWLNSPCHDS RRTVRVSISR AAILGIAIGG LVILLMVLIA 

       610        620        630        640        650        660 
ACRPHNPPPF LDGSLDKPVT YSTPKLVILH MNMALHVYED IMRMTENLSE KYIIGHGASS 

       670        680        690        700        710        720 
TVYKCVLKNC KPVAIKRLYS HNPQSMKQFE TELEMLSSIK HRNLVSLQAY SLSHLGSLLF 

       730        740        750        760        770        780 
YDYLENGSLW DLLHGPTKKK TLDWDTRLKI AYGAAQGLAY LHHDCSPRII HRDVKSSNIL 

       790        800        810        820        830        840 
LDKDLEARLT DFGIAKSLCV SKSHTSTYVM GTIGYIDPEY ARTSRLTEKS DVYSYGIVLL 

       850        860        870        880        890        900 
ELLTRRKAVD DESNLHHLIM SKTGNNEVME MADPDITSTC KDLGVVKKVF QLALLCTKRQ 

       910        920        930        940        950        960 
PNDRPTMHQV TRVLGSFMLS EQPPAATDTS ATLAGSCYVD EYANLKTPHS VNCSSMSASD 

       970 
AQLFLRFGQV ISQNSE 

« Hide

References

« Hide 'large scale' references
[1]"The Arabidopsis ERECTA gene encodes a putative receptor protein kinase with extracellular leucine-rich repeats."
Torii K.U., Mitsukawa N., Oosumi T., Matsuura Y., Yokoyama R., Whittier R.F., Komeda Y.
Plant Cell 8:735-746(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ER-1 LYS-750, FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF MET-282.
Strain: cv. Columbia and cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-976.
Strain: cv. Columbia.
[7]"The genetic architecture of shoot branching in Arabidopsis thaliana: a comparative assessment of candidate gene associations vs. quantitative trait locus mapping."
Ehrenreich I.M., Stafford P.A., Purugganan M.D.
Genetics 176:1223-1236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 791-935, VARIANT MET-886.
Strain: cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1, cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1 and cv. Wassilewskija.
[8]"The Arabidopsis ERECTA gene is expressed in the shoot apical meristem and organ primordia."
Yokoyama R., Takahashi T., Kato A., Torii K.U., Komeda Y.
Plant J. 15:301-310(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]"Receptor serine/threonine protein kinases in signalling: analysis of the erecta receptor-like kinase of Arabidopsis thaliana."
Lease K.A., Lau N.Y., Schuster R.A., Torii K.U., Walker J.C.
New Phytol. 151:133-144(2001)
Cited for: FUNCTION, CHARACTERIZATION OF VARIANT ER-1 LYS-750, MUTAGENESIS OF GLY-489 AND ASP-831.
[10]"KNAT1 and ERECTA regulate inflorescence architecture in Arabidopsis."
Douglas S.J., Chuck G., Dengler R.E., Pelecanda L., Riggs C.D.
Plant Cell 14:547-558(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Novel as1 and as2 defects in leaf adaxial-abaxial polarity reveal the requirement for ASYMMETRIC LEAVES1 and 2 and ERECTA functions in specifying leaf adaxial identity."
Xu L., Xu Y., Dong A., Sun Y., Pi L., Xu Y., Huang H.
Development 130:4097-4107(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"ERECTA, an LRR receptor-like kinase protein controlling development pleiotropically affects resistance to bacterial wilt."
Godiard L., Sauviac L., Torii K.U., Grenon O., Mangin B., Grimsley N.H., Marco Y.
Plant J. 36:353-365(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT ER-1 LYS-750.
[13]"Synergistic interaction of three ERECTA-family receptor-like kinases controls Arabidopsis organ growth and flower development by promoting cell proliferation."
Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.
Development 131:1491-1501(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[14]"ERECTA is required for protection against heat-stress in the AS1/ AS2 pathway to regulate adaxial-abaxial leaf polarity in Arabidopsis."
Qi Y., Sun Y., Xu L., Xu Y., Huang H.
Planta 219:270-276(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Pedicel development in Arabidopsis thaliana: contribution of vascular positioning and the role of the BREVIPEDICELLUS and ERECTA genes."
Douglas S.J., Riggs C.D.
Dev. Biol. 284:451-463(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"The ERECTA gene regulates plant transpiration efficiency in Arabidopsis."
Masle J., Gilmore S.R., Farquhar G.D.
Nature 436:866-870(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"ERECTA receptor-like kinase and heterotrimeric G protein from Arabidopsis are required for resistance to the necrotrophic fungus Plectosphaerella cucumerina."
Llorente F., Alonso-Blanco C., Sanchez-Rodriguez C., Jorda L., Molina A.
Plant J. 43:165-180(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-489 AND ASP-831, VARIANT ER-1 LYS-750.
[18]"Interaction of auxin and ERECTA in elaborating Arabidopsis inflorescence architecture revealed by the activation tagging of a new member of the YUCCA family putative flavin monooxygenases."
Woodward C., Bemis S.M., Hill E.J., Sawa S., Koshiba T., Torii K.U.
Plant Physiol. 139:192-203(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF MET-282.
[19]"Stomatal patterning and differentiation by synergistic interactions of receptor kinases."
Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.
Science 309:290-293(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"Haploinsufficiency after successive loss of signaling reveals a role for ERECTA-family genes in Arabidopsis ovule development."
Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.
Development 134:3099-3109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"ABA is an essential signal for plant resistance to pathogens affecting JA biosynthesis and the activation of defenses in Arabidopsis."
Adie B.A.T., Perez-Perez J., Perez-Perez M.M., Godoy M., Sanchez-Serrano J.-J., Schmelz E.A., Solano R.
Plant Cell 19:1665-1681(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT ER-1 LYS-750.
[22]"Genetics of microenvironmental canalization in Arabidopsis thaliana."
Hall M.C., Dworkin I., Ungerer M.C., Purugganan M.
Proc. Natl. Acad. Sci. U.S.A. 104:13717-13722(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[23]"Polymorphic genes of major effect: consequences for variation, selection and evolution in Arabidopsis thaliana."
Stinchcombe J.R., Weinig C., Heath K.D., Brock M.T., Schmitt J.
Genetics 182:911-922(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"A strong effect of growth medium and organ type on the identification of QTLs for phytate and mineral concentrations in three Arabidopsis thaliana RIL populations."
Ghandilyan A., Ilk N., Hanhart C., Mbengue M., Barboza L., Schat H., Koornneef M., El-Lithy M., Vreugdenhil D., Reymond M., Aarts M.G.M.
J. Exp. Bot. 60:1409-1425(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"The ERECTA receptor-like kinase regulates cell wall-mediated resistance to pathogens in Arabidopsis thaliana."
Sanchez-Rodriguez C., Estevez J.M., Llorente F., Hernandez-Blanco C., Jorda L., Pagan I., Berrocal M., Marco Y., Somerville S., Molina A.
Mol. Plant Microbe Interact. 22:953-963(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT ER-1 LYS-750.
[26]"The many functions of ERECTA."
van Zanten M., Snoek L.B., Proveniers M.C.G., Peeters A.J.M.
Trends Plant Sci. 14:214-218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Web resources

PlantP kinase Classification PPC
Protein Spotlight

A complicated affair - Issue 116 of April 2010

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D83257 Genomic DNA. Translation: BAA11869.1.
U47029 mRNA. Translation: AAC49302.1.
AC004484 Genomic DNA. Translation: AAC14518.1.
CP002685 Genomic DNA. Translation: AEC07825.1.
AY035110 mRNA. Translation: AAK59615.1.
FJ708701 mRNA. Translation: ACN59296.1.
AK221886 mRNA. Translation: BAD94220.1.
EF598332 Genomic DNA. Translation: ABR08864.1.
EF598333 Genomic DNA. Translation: ABR08865.1.
EF598334 Genomic DNA. Translation: ABR08866.1.
EF598335 Genomic DNA. Translation: ABR08867.1.
EF598336 Genomic DNA. Translation: ABR08868.1.
EF598337 Genomic DNA. Translation: ABR08869.1.
EF598338 Genomic DNA. Translation: ABR08870.1.
EF598339 Genomic DNA. Translation: ABR08871.1.
EF598340 Genomic DNA. Translation: ABR08872.1.
EF598341 Genomic DNA. Translation: ABR08873.1.
EF598342 Genomic DNA. Translation: ABR08874.1.
EF598343 Genomic DNA. Translation: ABR08875.1.
EF598344 Genomic DNA. Translation: ABR08876.1.
EF598345 Genomic DNA. Translation: ABR08877.1.
EF598346 Genomic DNA. Translation: ABR08878.1.
EF598347 Genomic DNA. Translation: ABR08879.1.
EF598348 Genomic DNA. Translation: ABR08880.1.
EF598349 Genomic DNA. Translation: ABR08881.1.
EF598350 Genomic DNA. Translation: ABR08882.1.
EF598351 Genomic DNA. Translation: ABR08883.1.
EF598352 Genomic DNA. Translation: ABR08884.1.
EF598353 Genomic DNA. Translation: ABR08885.1.
EF598354 Genomic DNA. Translation: ABR08886.1.
PIRB84659.
RefSeqNP_180201.1. NM_128190.2.
UniGeneAt.10804.

3D structure databases

ProteinModelPortalQ42371.
SMRQ42371. Positions 23-567, 638-947.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid2525. 5 interactions.
STRING3702.AT2G26330.1-P.

Proteomic databases

PaxDbQ42371.
PRIDEQ42371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G26330.1; AT2G26330.1; AT2G26330.
GeneID817173.
KEGGath:AT2G26330.

Organism-specific databases

GeneFarm2563. 221.
TAIRAT2G26330.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000116551.
InParanoidQ42371.
OMATASNAVM.
PhylomeDBQ42371.

Enzyme and pathway databases

BioCycARA:AT2G26330-MONOMER.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 5 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51450. LRR. 17 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERECT_ARATH
AccessionPrimary (citable) accession number: Q42371
Secondary accession number(s): A5YYA0, A5YYB1, Q56WZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

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