O64783 · Y1137_ARATH

Function

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site507-515ATP (UniProtKB | ChEBI)
Binding site529ATP (UniProtKB | ChEBI)
Active site626Proton acceptor

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functioncalmodulin binding
Molecular Functioncarbohydrate binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionubiquitin protein ligase binding
Biological Processrecognition of pollen

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    G-type lectin S-receptor-like serine/threonine-protein kinase At1g61370
  • EC number

Gene names

    • ORF names
      T1F9.14
    • Ordered locus names
      At1g61370

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    O64783

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain26-433Extracellular
Transmembrane434-454Helical
Topological domain455-814Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000040131626-814G-type lectin S-receptor-like serine/threonine-protein kinase At1g61370
Glycosylation43N-linked (GlcNAc...) asparagine
Glycosylation54N-linked (GlcNAc...) asparagine
Glycosylation89N-linked (GlcNAc...) asparagine
Glycosylation95N-linked (GlcNAc...) asparagine
Glycosylation253N-linked (GlcNAc...) asparagine
Glycosylation271N-linked (GlcNAc...) asparagine
Disulfide bond286↔298
Disulfide bond292↔306
Glycosylation324N-linked (GlcNAc...) asparagine
Glycosylation334N-linked (GlcNAc...) asparagine
Glycosylation340N-linked (GlcNAc...) asparagine
Disulfide bond376↔397
Disulfide bond380↔386
Glycosylation383N-linked (GlcNAc...) asparagine
Modified residue535Phosphoserine
Modified residue550Phosphoserine
Modified residue630Phosphoserine
Modified residue643Phosphoserine
Modified residue660Phosphothreonine
Modified residue703Phosphoserine
Modified residue704Phosphoserine
Modified residue797Phosphoserine
Modified residue802Phosphoserine
Modified residue809Phosphothreonine

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain26-145Bulb-type lectin
Domain282-318EGF-like
Domain337-423PAN
Domain501-786Protein kinase
Region590-607CaM-binding

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    814
  • Mass (Da)
    90,857
  • Last updated
    2010-11-30 v2
  • Checksum
    1D9DFEA059F7B296
MGKIGIVFFASLLFLLIIFPSCAFAAITRASPLSIGQTLSSPNGTYELGFFSPNNSRNQYVGIWFKNITPRVVVWVANRDKPVTNNAANLTINSNGSLILVEREQNVVWSIGETFSSNELRAELLENGNLVLIDGVSERNLWESFEHLGDTMLLESSVMYDVPNNKKRVLSSWKNPTDPSPGEFVAELTTQVPPQGFIMRGSRPYWRGGPWARVRFTGIPEMDGSHVSKFDISQDVAAGTGSLTYSLERRNSNLSYTTLTSAGSLKIIWNNGSGWVTDLEAPVSSCDVYNTCGPFGLCIRSNPPKCECLKGFVPKSDEEWNKRNWTGGCMRRTNLSCDVNSSATAQANNGDIFDIVANVKPPDFYEYLSLINEEDCQQRCLGNCSCTAFSYIEQIGCLVWNRELVDVMQFVAGGETLSIRLASSELAGSNRVKIIVASIVSISVFMILVFASYWYWRYKAKQNDSNPIPLETSQDAWREQLKPQDVNFFDMQTILTITNNFSMENKLGQGGFGPVYKGNLQDGKEIAIKRLSSTSGQGLEEFMNEIILISKLQHRNLVRLLGCCIEGEEKLLIYEFMANKSLNTFIFDSTKKLELDWPKRFEIIQGIACGLLYLHRDSCLRVVHRDMKVSNILLDEEMNPKISDFGLARMFQGTQHQANTRRVVGTLGYMSPEYAWTGMFSEKSDIYAFGVLLLEIITGKRISSFTIGEEGKTLLEFAWDSWCESGGSDLLDQDISSSGSESEVARCVQIGLLCIQQQAGDRPNIAQVMSMLTTTMDLPKPKQPVFAMQVQESDSESKTMYSVNNITQTAIVGR

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8AWT8A0A1P8AWT8_ARATHAt1g61370663

Sequence caution

The sequence AAC13904.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC004255
EMBL· GenBank· DDBJ
AAC13904.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002684
EMBL· GenBank· DDBJ
AEE33828.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp