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5TOS

Botrytis-induced kinase 1 (BIK1) from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002221biological_processpattern recognition receptor signaling pathway
A0002237biological_processresponse to molecule of bacterial origin
A0002376biological_processimmune system process
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0006952biological_processdefense response
A0009620biological_processresponse to fungus
A0010008cellular_componentendosome membrane
A0010119biological_processregulation of stomatal movement
A0012505cellular_componentendomembrane system
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0042742biological_processdefense response to bacterium
A0045087biological_processinnate immune response
A0050832biological_processdefense response to fungus
A0080141biological_processregulation of jasmonic acid biosynthetic process
A0080142biological_processregulation of salicylic acid biosynthetic process
A0106310molecular_functionprotein serine kinase activity
A1900424biological_processregulation of defense response to bacterium
B0000166molecular_functionnucleotide binding
B0002221biological_processpattern recognition receptor signaling pathway
B0002237biological_processresponse to molecule of bacterial origin
B0002376biological_processimmune system process
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0006952biological_processdefense response
B0009620biological_processresponse to fungus
B0010008cellular_componentendosome membrane
B0010119biological_processregulation of stomatal movement
B0012505cellular_componentendomembrane system
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0042742biological_processdefense response to bacterium
B0045087biological_processinnate immune response
B0050832biological_processdefense response to fungus
B0080141biological_processregulation of jasmonic acid biosynthetic process
B0080142biological_processregulation of salicylic acid biosynthetic process
B0106310molecular_functionprotein serine kinase activity
B1900424biological_processregulation of defense response to bacterium
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues34
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGGFGCVFkGwldestltptkpgtglviAVKK
ChainResidueDetails
AILE73-LYS106

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViYrDIKasNILL
ChainResidueDetails
AVAL198-LEU210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMotif: {"description":"Required for physical interaction with and phosphorylation of downstream signaling proteins (e.g. WRKY33, WRKY50, WRKY51 and WRKY57) to activate EFR-mediated immune signaling","evidences":[{"source":"PubMed","id":"29649442","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by EFR","evidences":[{"source":"PubMed","id":"29649442","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by EFR","evidences":[{"source":"PubMed","id":"29649442","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by EFR","evidences":[{"source":"PubMed","id":"29649442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24532660","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis and BAK1","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30212650","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24532660","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"24104392","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"32404997","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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