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Protein

Chitin elicitor receptor kinase 1

Gene

CERK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI).8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Enzyme regulationi

Activated by chitin-mediated homodimerization.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei349 – 3491ATPPROSITE-ProRule annotation
Active sitei441 – 4411Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi328 – 3369ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chitin binding Source: UniProtKB
  • chitosan binding Source: UniProtKB
  • kinase activity Source: TAIR
  • protein homodimerization activity Source: UniProtKB
  • protein self-association Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • transmembrane receptor protein kinase activity Source: TAIR

GO - Biological processi

  • cell surface pattern recognition receptor signaling pathway Source: UniProtKB
  • cellular response to chitin Source: UniProtKB
  • cellular response to molecule of bacterial origin Source: UniProtKB
  • defense response to bacterium Source: UniProtKB
  • defense response to fungus, incompatible interaction Source: TAIR
  • detection of molecule of fungal origin Source: TAIR
  • detection of peptidoglycan Source: TAIR
  • innate immune response Source: TAIR
  • intracellular signal transduction Source: TAIR
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: TAIR
  • response to chitin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Plant defense

Keywords - Ligandi

ATP-binding, Chitin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G21630-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitin elicitor receptor kinase 1 (EC:2.7.11.1)
Short name:
AtCERK1
Alternative name(s):
LysM domain receptor-like kinase 1
Short name:
LysM RLK1
Short name:
LysM-containing receptor-like kinase 1
Gene namesi
Name:CERK1
Synonyms:LYK1, RLK1
Ordered Locus Names:At3g21630
ORF Names:MIL23.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G21630.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 232209ExtracellularSequence analysisAdd
BLAST
Transmembranei233 – 25321HelicalSequence analysisAdd
BLAST
Topological domaini254 – 617364CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Complete loss of response to the chitin elicitor, including loss of MAPK activation, generation of reactive oxygen species, and transcriptional activation. Impaired chitin-mediated resistance against biotic and abiotic stresses such as tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection. Reduced resistance to incompatible fungi such as Erysiphe cichoracearum and Alternaria brassicicola. Enhanced susceptibility to Pseudomonas syringae pv. tomato DC3000 associated with peptidoglycan insensitivity.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381A → H: Slower chitin-mediated phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 617594Chitin elicitor receptor kinase 1PRO_0000420826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 93
Disulfide bondi29 ↔ 155
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence analysis
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Disulfide bondi91 ↔ 153
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence analysis
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence analysis
Modified residuei266 – 2661Phosphoserine1 Publication
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei270 – 2701Phosphoserine1 Publication
Modified residuei274 – 2741Phosphoserine1 Publication
Modified residuei519 – 5191Phosphothreonine1 Publication

Post-translational modificationi

Autophosphorylated. Autophosphorylation is induced by chitin and derivatives.2 Publications
Ubiquitinated and targeted to the proteasome by hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiA8R7E6.
PRIDEiA8R7E6.

PTM databases

iPTMnetiA8R7E6.

Expressioni

Tissue specificityi

Expressed ubiquitously, with lowest expression in pollen.1 Publication

Inductioni

Induced upon treatment with chitin oligosaccharide elicitor and flagellin (e.g. flg22).2 Publications

Gene expression databases

GenevisibleiA8R7E6. AT.

Interactioni

Subunit structurei

Forms homodimers and homooligomers. Homodimerization is required to trigger plant defenses. Binds to chitin, chitosan and chito-oligomer oligosaccharide elicitors. Interaction with chitin octamer (NAG8) promotes homodimerization while shorter chitin oligomers inhibit homodimerization. Interacts with Pseudomonas syringae hopAB2/avrPtoB.6 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi7049. 63 interactions.
STRINGi3702.AT3G21630.1.

Structurei

Secondary structure

1
617
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 376Combined sources
Helixi44 – 507Combined sources
Beta strandi54 – 563Combined sources
Helixi64 – 674Combined sources
Beta strandi84 – 896Combined sources
Beta strandi92 – 943Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 1069Combined sources
Helixi113 – 1186Combined sources
Turni119 – 1235Combined sources
Helixi127 – 1337Combined sources
Helixi138 – 1403Combined sources
Beta strandi146 – 1527Combined sources
Turni158 – 1603Combined sources
Beta strandi167 – 1715Combined sources
Helixi178 – 1858Combined sources
Helixi189 – 1957Combined sources
Beta strandi205 – 2117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EBYX-ray1.65A25-230[»]
4EBZX-ray1.79A25-230[»]
ProteinModelPortaliA8R7E6.
SMRiA8R7E6. Positions 25-224, 289-590.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 7429LysM 1; degenerateAdd
BLAST
Domaini108 – 14033LysM 2; degenerateAdd
BLAST
Domaini168 – 21144LysM 3PROSITE-ProRule annotationAdd
BLAST
Domaini322 – 594273Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1157Chitin-binding
Regioni137 – 1437Chitin-binding

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 3 LysM domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II96. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000116550.
InParanoidiA8R7E6.
KOiK13429.
OMAiFFFAVES.
PhylomeDBiA8R7E6.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.10.350.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR018392. LysM_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF01476. LysM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51782. LYSM. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A8R7E6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLKISLIAP ILLLFSFFFA VESKCRTSCP LALASYYLEN GTTLSVINQN
60 70 80 90 100
LNSSIAPYDQ INFDPILRYN SNIKDKDRIQ MGSRVLVPFP CECQPGDFLG
110 120 130 140 150
HNFSYSVRQE DTYERVAISN YANLTTMESL QARNPFPATN IPLSATLNVL
160 170 180 190 200
VNCSCGDESV SKDFGLFVTY PLRPEDSLSS IARSSGVSAD ILQRYNPGVN
210 220 230 240 250
FNSGNGIVYV PGRDPNGAFP PFKSSKQDGV GAGVIAGIVI GVIVALLLIL
260 270 280 290 300
FIVYYAYRKN KSKGDSFSSS IPLSTKADHA SSTSLQSGGL GGAGVSPGIA
310 320 330 340 350
AISVDKSVEF SLEELAKATD NFNLSFKIGQ GGFGAVYYAE LRGEKAAIKK
360 370 380 390 400
MDMEASKQFL AELKVLTRVH HVNLVRLIGY CVEGSLFLVY EYVENGNLGQ
410 420 430 440 450
HLHGSGREPL PWTKRVQIAL DSARGLEYIH EHTVPVYVHR DIKSANILID
460 470 480 490 500
QKFRAKVADF GLTKLTEVGG SATRGAMGTF GYMAPETVYG EVSAKVDVYA
510 520 530 540 550
FGVVLYELIS AKGAVVKMTE AVGEFRGLVG VFEESFKETD KEEALRKIID
560 570 580 590 600
PRLGDSYPFD SVYKMAELGK ACTQENAQLR PSMRYIVVAL STLFSSTGNW
610
DVGNFQNEDL VSLMSGR
Length:617
Mass (Da):67,315
Last modified:January 15, 2008 - v1
Checksum:iCF5019DB428CFE1E
GO

Sequence cautioni

The sequence BAB02358.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB367524 mRNA. Translation: BAF92788.1.
AB019232 Genomic DNA. Translation: BAB02358.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE76532.1.
RefSeqiNP_566689.2. NM_113058.3.
UniGeneiAt.5663.

Genome annotation databases

EnsemblPlantsiAT3G21630.1; AT3G21630.1; AT3G21630.
GeneIDi821717.
GrameneiAT3G21630.1; AT3G21630.1; AT3G21630.
KEGGiath:AT3G21630.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB367524 mRNA. Translation: BAF92788.1.
AB019232 Genomic DNA. Translation: BAB02358.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE76532.1.
RefSeqiNP_566689.2. NM_113058.3.
UniGeneiAt.5663.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EBYX-ray1.65A25-230[»]
4EBZX-ray1.79A25-230[»]
ProteinModelPortaliA8R7E6.
SMRiA8R7E6. Positions 25-224, 289-590.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi7049. 63 interactions.
STRINGi3702.AT3G21630.1.

PTM databases

iPTMnetiA8R7E6.

Proteomic databases

PaxDbiA8R7E6.
PRIDEiA8R7E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G21630.1; AT3G21630.1; AT3G21630.
GeneIDi821717.
GrameneiAT3G21630.1; AT3G21630.1; AT3G21630.
KEGGiath:AT3G21630.

Organism-specific databases

TAIRiAT3G21630.

Phylogenomic databases

eggNOGiENOG410II96. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000116550.
InParanoidiA8R7E6.
KOiK13429.
OMAiFFFAVES.
PhylomeDBiA8R7E6.

Enzyme and pathway databases

BioCyciARA:AT3G21630-MONOMER.

Miscellaneous databases

PROiA8R7E6.

Gene expression databases

GenevisibleiA8R7E6. AT.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.10.350.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR018392. LysM_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF01476. LysM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51782. LYSM. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis."
    Miya A., Albert P., Shinya T., Desaki Y., Ichimura K., Shirasu K., Narusaka Y., Kawakami N., Kaku H., Shibuya N.
    Proc. Natl. Acad. Sci. U.S.A. 104:19613-19618(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AUTOPHOSPHORYLATION, INDUCTION BY CHITIN, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(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. "A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis."
    Wan J., Zhang X.-C., Neece D., Ramonell K.M., Clough S., Kim S.-Y., Stacey M.G., Stacey G.
    Plant Cell 20:471-481(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  5. "AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants."
    Gimenez-Ibanez S., Hann D.R., Ntoukakis V., Petutschnig E., Lipka V., Rathjen J.P.
    Curr. Biol. 19:423-429(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH PSEUDOMONAS SYRINGAE HOPAB2/AVRPTOB.
    Strain: cv. Columbia and cv. Wassilewskija-4.
  6. "The LysM receptor kinase CERK1 mediates bacterial perception in Arabidopsis."
    Gimenez-Ibanez S., Ntoukakis V., Rathjen J.P.
    Plant Signal. Behav. 4:539-541(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, REVIEW.
    Strain: cv. Columbia.
  7. "Direct binding of a plant LysM receptor-like kinase, LysM RLK1/CERK1, to chitin in vitro."
    Iizasa E., Mitsutomi M., Nagano Y.
    J. Biol. Chem. 285:2996-3004(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHITIN, AUTOPHOSPHORYLATION.
  8. "The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation."
    Petutschnig E.K., Jones A.M.E., Serazetdinova L., Lipka U., Lipka V.
    J. Biol. Chem. 285:28902-28911(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CHITIN AND DERIVATIVES, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-266; SER-268; SER-274 AND THR-519.
  9. "Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection."
    Willmann R., Lajunen H.M., Erbs G., Newman M.-A., Kolb D., Tsuda K., Katagiri F., Fliegmann J., Bono J.-J., Cullimore J.V., Jehle A.K., Goetz F., Kulik A., Molinaro A., Lipka V., Gust A.A., Nuernberger T.
    Proc. Natl. Acad. Sci. U.S.A. 108:19824-19829(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  10. "The LysM receptor-like kinase LysM RLK1 is required to activate defense and abiotic-stress responses induced by overexpression of fungal chitinases in Arabidopsis plants."
    Brotman Y., Landau U., Pnini S., Lisec J., Balazadeh S., Mueller-Roeber B., Zilberstein A., Willmitzer L., Chet I., Viterbo A.
    Mol. Plant 5:1113-1124(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "Functional characterization of CEBiP and CERK1 homologs in Arabidopsis and rice reveals the presence of different chitin receptor systems in plants."
    Shinya T., Motoyama N., Ikeda A., Wada M., Kamiya K., Hayafune M., Kaku H., Shibuya N.
    Plant Cell Physiol. 53:1696-1706(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHITIN.
    Strain: cv. Columbia.
  12. "LYK4, a lysin motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis."
    Wan J., Tanaka K., Zhang X.-C., Son G.H., Brechenmacher L., Nguyen T.H.N., Stacey G.
    Plant Physiol. 160:396-406(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY CHITIN AND FLAGELLIN.
  13. "How plant lysin motif receptors get activated: lessons learned from structural biology."
    Willmann R., Nuernberger T.
    Sci. Signal. 5:PE28-PE28(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHITIN, HOMODIMER.
  14. "Chitin-induced dimerization activates a plant immune receptor."
    Liu T., Liu Z., Song C., Hu Y., Han Z., She J., Fan F., Wang J., Jin C., Chang J., Zhou J.-M., Chai J.
    Science 336:1160-1164(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-230 IN COMPLEX WITH CHITIN OLIGOMERS, HOMODIMER, ENZYME REGULATION, MUTAGENESIS OF ALA-138, PHOSPHORYLATION.

Entry informationi

Entry nameiCERK1_ARATH
AccessioniPrimary (citable) accession number: A8R7E6
Secondary accession number(s): Q9LVE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: January 15, 2008
Last modified: May 11, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.