O48788 · Y2267_ARATH
- ProteinProbable inactive receptor kinase At2g26730
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids658 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein kinase activity |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProbable inactive receptor kinase At2g26730
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO48788
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 258-278 | Helical | ||||
Sequence: IVAIIVASALVALLLLALLLF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MASISWVLNSLFSILLLTQRVNS | ||||||
Chain | PRO_0000305194 | 24-658 | Probable inactive receptor kinase At2g26730 | |||
Sequence: ESTAEKQALLTFLQQIPHENRLQWNESDSACNWVGVECNSNQSSIHSLRLPGTGLVGQIPSGSLGRLTELRVLSLRSNRLSGQIPSDFSNLTHLRSLYLQHNEFSGEFPTSFTQLNNLIRLDISSNNFTGSIPFSVNNLTHLTGLFLGNNGFSGNLPSISLGLVDFNVSNNNLNGSIPSSLSRFSAESFTGNVDLCGGPLKPCKSFFVSPSPSPSLINPSNRLSSKKSKLSKAAIVAIIVASALVALLLLALLLFLCLRKRRGSNEARTKQPKPAGVATRNVDLPPGASSSKEEVTGTSSGMGGETERNKLVFTEGGVYSFDLEDLLRASAEVLGKGSVGTSYKAVLEEGTTVVVKRLKDVMASKKEFETQMEVVGKIKHPNVIPLRAYYYSKDEKLLVFDFMPTGSLSALLHGSRGSGRTPLDWDNRMRIAITAARGLAHLHVSAKLVHGNIKASNILLHPNQDTCVSDYGLNQLFSNSSPPNRLAGYHAPEVLETRKVTFKSDVYSFGVLLLELLTGKSPNQASLGEEGIDLPRWVLSVVREEWTAEVFDVELMRYHNIEEEMVQLLQIAMACVSTVPDQRPVMQEVLRMIEDVNRSETTDDGLRQSSDDPSKGSEGQTPPGESRTPPRSVTP | ||||||
Glycosylation | 48 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 64 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 113 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 150 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 190 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 353 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 374 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 430 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 520 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 637 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 640 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O48788 | CAM4 P0DH96 | 2 | EBI-1239029, EBI-1235664 | |
BINARY | O48788 | CAM7 P59220 | 2 | EBI-1239029, EBI-1236031 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 65-89 | LRR 1 | ||||
Sequence: QSSIHSLRLPGTGLVGQIPSGSLGR | ||||||
Repeat | 90-113 | LRR 2 | ||||
Sequence: LTELRVLSLRSNRLSGQIPSDFSN | ||||||
Repeat | 115-138 | LRR 3 | ||||
Sequence: THLRSLYLQHNEFSGEFPTSFTQL | ||||||
Repeat | 139-164 | LRR 4 | ||||
Sequence: NNLIRLDISSNNFTGSIPFSVNNLTH | ||||||
Repeat | 166-183 | LRR 5 | ||||
Sequence: TGLFLGNNGFSGNLPSIS | ||||||
Repeat | 184-207 | LRR 6 | ||||
Sequence: LGLVDFNVSNNNLNGSIPSSLSRF | ||||||
Region | 289-329 | Disordered | ||||
Sequence: EARTKQPKPAGVATRNVDLPPGASSSKEEVTGTSSGMGGET | ||||||
Compositional bias | 314-328 | Polar residues | ||||
Sequence: SKEEVTGTSSGMGGE | ||||||
Domain | 351-619 | Protein kinase | ||||
Sequence: RASAEVLGKGSVGTSYKAVLEEGTTVVVKRLKDVMASKKEFETQMEVVGKIKHPNVIPLRAYYYSKDEKLLVFDFMPTGSLSALLHGSRGSGRTPLDWDNRMRIAITAARGLAHLHVSAKLVHGNIKASNILLHPNQDTCVSDYGLNQLFSNSSPPNRLAGYHAPEVLETRKVTFKSDVYSFGVLLLELLTGKSPNQASLGEEGIDLPRWVLSVVREEWTAEVFDVELMRYHNIEEEMVQLLQIAMACVSTVPDQRPVMQEVLRMIEDV | ||||||
Compositional bias | 619-634 | Basic and acidic residues | ||||
Sequence: VNRSETTDDGLRQSSD | ||||||
Region | 619-658 | Disordered | ||||
Sequence: VNRSETTDDGLRQSSDDPSKGSEGQTPPGESRTPPRSVTP | ||||||
Compositional bias | 635-658 | Polar residues | ||||
Sequence: DPSKGSEGQTPPGESRTPPRSVTP |
Domain
The protein kinase domain is predicted to be catalytically inactive.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length658
- Mass (Da)71,752
- Last updated1998-06-01 v1
- Checksum2B951D45A40485B4
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 314-328 | Polar residues | ||||
Sequence: SKEEVTGTSSGMGGE | ||||||
Sequence conflict | 403 | in Ref. 3; AAK92807 | ||||
Sequence: H → R | ||||||
Compositional bias | 619-634 | Basic and acidic residues | ||||
Sequence: VNRSETTDDGLRQSSD | ||||||
Compositional bias | 635-658 | Polar residues | ||||
Sequence: DPSKGSEGQTPPGESRTPPRSVTP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC003105 EMBL· GenBank· DDBJ | AAB95307.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC07880.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY050870 EMBL· GenBank· DDBJ | AAK92807.1 EMBL· GenBank· DDBJ | mRNA | ||
BT021127 EMBL· GenBank· DDBJ | AAX22262.1 EMBL· GenBank· DDBJ | mRNA |