Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1

Gene

BAK1

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

Functioni

Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interactions with FLS2 and EFR, and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway (PubMed:17583510, PubMed:17600708, PubMed:18667726, PubMed:18694562, PubMed:19124768, PubMed:20018402, PubMed:20404519, PubMed:21350342, PubMed:21693696). Phosphorylates BIR2 and thus promotes interaction with BIR2. This interaction prevents interaction with FLS2 in the absence of pathogen-associated molecular patterns (PAMP) (PubMed:24388849, PubMed:24556575).11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521flg221 Publication
Binding sitei54 – 541flg22; via amide nitrogen1 Publication
Binding sitei297 – 2971ATP; via carbonyl oxygen1 Publication
Binding sitei317 – 3171ATPPROSITE-ProRule annotation
Active sitei416 – 4161Proton acceptorPROSITE-ProRule annotation
Binding sitei418 – 4181ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi295 – 3039ATPPROSITE-ProRule annotation
Nucleotide bindingi364 – 3663ATP1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G33430-MONOMER.
ARA:GQT-1669-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 (EC:2.7.10.1, EC:2.7.11.1)
Short name:
AtBAK1
Short name:
BRI1-associated receptor kinase 1
Alternative name(s):
Protein ELONGATED
Somatic embryogenesis receptor kinase 3
Short name:
AtSERK3
Somatic embryogenesis receptor-like kinase 3
Gene namesi
Name:BAK1
Synonyms:ELG, SERK3
Ordered Locus Names:At4g33430
ORF Names:F17M5.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G33430.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 225200ExtracellularSequence analysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence analysisAdd
BLAST
Topological domaini247 – 615369CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endosome membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Semi-dwarfed phenotype, altered leaf morphology and reduced sensitivity to brassinolide and flagellin. Enhanced chlorosis and lesion formation upon pathogen infection. Bak1 and bkk1 double mutants are seedling lethal.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301D → Y: No effect on flg22 induced FLS2-BAK1 heterodimerization. 1 Publication
Mutagenesisi32 – 321L → E: Loss of binding to BRI1, but no effect on kinase activity. 1 Publication
Mutagenesisi46 – 461L → E: Loss of binding to BRI1 and loss of kinase activity. 1 Publication
Mutagenesisi60 – 601F → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication
Mutagenesisi64 – 641C → Y: No effect. 1 Publication
Mutagenesisi94 – 941L → E: No effect. 1 Publication
Mutagenesisi96 – 961Y → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication
Mutagenesisi121 – 1211L → E: No effect. 1 Publication
Mutagenesisi122 – 1221D → N: Hypersensitivity to brassinosteroids and enhanced high-light phototropism. 1 Publication
Mutagenesisi144 – 1441F → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication
Mutagenesisi172 – 1721S → F: No effect. 1 Publication
Mutagenesisi286 – 2861S → A: No effect.
Mutagenesisi286 – 2861S → D: Loss of kinase activity.
Mutagenesisi290 – 2901S → A: Reduced kinase activity. Reduced interaction with BIR2. 1 Publication
Mutagenesisi290 – 2901S → D: Normal interaction with BIR2. 1 Publication
Mutagenesisi304 – 3041Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi312 – 3121T → A: No effect on the kinase activity or on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. 2 Publications
Mutagenesisi312 – 3121T → D: Reduced interaction with BIR2. 1 Publication
Mutagenesisi317 – 3171K → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB, but no effect on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. 5 Publications
Mutagenesisi363 – 3631Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi363 – 3631Y → G or A: Loss of autophosphorylation. 1 Publication
Mutagenesisi365 – 3651Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi403 – 4031Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi416 – 4161D → A: Loss of phosphorylation. 1 Publication
Mutagenesisi421 – 4211N → A: Loss of phosphorylation. 1 Publication
Mutagenesisi439 – 4391K → A: No effect on some phosphorylation sites. 1 Publication
Mutagenesisi443 – 4431Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi446 – 4461T → A or D: No effect. Reduced interaction with BIR2. Loss of kinase activity; when associated with D-449 and D-450. 2 Publications
Mutagenesisi449 – 4491T → A or D: Slight decrease of kinase activity but loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. Loss of kinase activity; when associated with A-446 and D-450. 3 Publications
Mutagenesisi450 – 4501T → A or D: Loss of interaction with hopAB2/AvrPtoB and loss of phosphorylation. Reduced interaction with BIR2. Loss of kinase activity; when associated with A-446 and D-449. 4 Publications
Mutagenesisi451 – 4511A → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. 2 Publications
Mutagenesisi452 – 4521V → D: Strongly decreased kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication
Mutagenesisi453 – 4531R → A: No effect on some phosphorylation sites. 1 Publication
Mutagenesisi455 – 4551T → A, D or E: Loss of kinase activity. 2 Publications
Mutagenesisi455 – 4551T → N: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication
Mutagenesisi456 – 4561I → D: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication
Mutagenesisi458 – 4581H → D: Loss of kinase activity, loss of phosphorylation and loss of interaction with hopAB2/AvrPtoB. 2 Publications
Mutagenesisi463 – 4631Y → F: Loss of kinase activity and loss of autophosphorylation. 1 Publication
Mutagenesisi464 – 4641L → D: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication
Mutagenesisi478 – 4781Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi495 – 4951A → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication
Mutagenesisi530 – 5301Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi546 – 5461T → A: 60% decrease of binding to the FHA domain of KAPP. 1 Publication
Mutagenesisi587 – 5871Y → F: No effect on autophosphorylation. 1 Publication
Mutagenesisi610 – 6101Y → E: Loss of brassinosteroid signaling but no effect on programmed cell death inhibition. 1 Publication
Mutagenesisi610 – 6101Y → F: Decreased autophosphorylation on tyrosine, loss of transphosphorylation and activation of BRI1 but no effect on the binding to BRI1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 615590BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1PRO_0000024304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 642 Publications
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence analysis
Modified residuei286 – 2861Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine4 Publications
Modified residuei312 – 3121Phosphothreonine2 Publications
Modified residuei370 – 3701PhosphoserineBy similarity
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei446 – 4461Phosphothreonine5 Publications
Modified residuei449 – 4491Phosphothreonine5 Publications
Modified residuei450 – 4501Phosphothreonine4 Publications
Modified residuei455 – 4551Phosphothreonine4 Publications
Modified residuei463 – 4631PhosphotyrosineBy similarity
Modified residuei465 – 4651PhosphoserineBy similarity
Modified residuei466 – 4661PhosphothreonineBy similarity
Modified residuei470 – 4701PhosphoserineBy similarity
Modified residuei546 – 5461PhosphothreonineCurated
Modified residuei589 – 5891Phosphothreonine1 Publication
Modified residuei595 – 5951Phosphoserine1 Publication
Modified residuei604 – 6041Phosphoserine1 Publication
Modified residuei610 – 6101Phosphotyrosine1 Publication
Modified residuei612 – 6121Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated on Ser-290, Thr-312, Thr-446, Thr-449, Thr-455 and Tyr-610. Probable autophosphorylation on additional Tyr residues. Transphosphorylated by BRI1. It is not sure whether Thr-589 or Ser-595 is the target of the phosphorylation. The phosphorylations on Thr and Tyr are induced by brassinolide. Phosphorylation on Tyr-610 is required for brassinolide signaling, but not for flagellin signaling. Phosphorylation at Ser-286, Ser-290 Thr-446 or Thr-449 is not critical for flagellin signaling.9 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ94F62.

PTM databases

iPTMnetiQ94F62.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Inductioni

Up-regulated by flagellin and harpin.1 Publication

Gene expression databases

ExpressionAtlasiQ94F62. baseline and differential.
GenevisibleiQ94F62. AT.

Interactioni

Subunit structurei

Interacts constitutively with BIR2, thereby preventing interaction with the ligand-binding LRR-RLK FLS2. Upon infection, pathogen-associated molecular patterns (PAMP) perception leads to BIR2 release from the BAK1 complex and enables the recruitment of BAK1 into the FLS2 complex (PubMed:24388849, PubMed:24556575). Heterodimer with FLS2 (PubMed:24114786). Monomer. Heterodimer with BRI1 in the endosomes. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Interacts with the P.syringae AvrPto and hopAB2/AvrPtoB, ERD13, PEPR1 and PEPR2. Interacts (via extracellular region) with MSBP1. Interacts with the EF-Tu receptor EFR and FLS2 in a specific ligand-induced manner. Interacts with TMK4/BARK1.21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
At5g48380Q9ASS44EBI-617138,EBI-6298290
BRI1O224765EBI-617138,EBI-1797828
BRL1Q9ZWC85EBI-617138,EBI-590903
FLS2Q9FL283EBI-617138,EBI-1799448

GO - Molecular functioni

  • receptor serine/threonine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi14764. 22 interactions.
DIPiDIP-34976N.
IntActiQ94F62. 8 interactions.

Structurei

Secondary structure

1
615
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 3711Combined sources
Helixi45 – 484Combined sources
Beta strandi53 – 597Combined sources
Beta strandi62 – 643Combined sources
Beta strandi70 – 745Combined sources
Beta strandi81 – 833Combined sources
Helixi86 – 905Combined sources
Beta strandi96 – 983Combined sources
Helixi110 – 1145Combined sources
Beta strandi120 – 1223Combined sources
Helixi134 – 1374Combined sources
Beta strandi144 – 1463Combined sources
Helixi158 – 1614Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi183 – 1864Combined sources
Turni192 – 1943Combined sources
Beta strandi195 – 1984Combined sources
Helixi280 – 2834Combined sources
Turni284 – 2874Combined sources
Helixi291 – 2933Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi299 – 3068Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi314 – 3185Combined sources
Helixi330 – 3367Combined sources
Helixi337 – 3393Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi360 – 3645Combined sources
Helixi371 – 3766Combined sources
Helixi387 – 40620Combined sources
Beta strandi407 – 4104Combined sources
Beta strandi421 – 4244Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi443 – 4464Combined sources
Helixi456 – 4583Combined sources
Helixi461 – 4666Combined sources
Beta strandi467 – 4693Combined sources
Helixi471 – 48717Combined sources
Helixi494 – 4974Combined sources
Turni498 – 5003Combined sources
Helixi505 – 5095Combined sources
Turni510 – 5134Combined sources
Helixi518 – 5203Combined sources
Helixi524 – 5263Combined sources
Beta strandi527 – 5304Combined sources
Helixi532 – 54514Combined sources
Helixi550 – 5523Combined sources
Helixi556 – 5649Combined sources
Beta strandi569 – 5713Combined sources
Helixi577 – 5815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TL8X-ray2.50A/D/G/H250-590[»]
3UIMX-ray2.20A258-583[»]
3ULZX-ray2.60A258-583[»]
4M7EX-ray3.60C/D26-220[»]
4MN8X-ray3.06B1-220[»]
ProteinModelPortaliQ94F62.
SMRiQ94F62. Positions 26-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati93 – 11624LRR 1Add
BLAST
Repeati117 – 14024LRR 2Add
BLAST
Repeati141 – 16323LRR 3Add
BLAST
Repeati165 – 18723LRR 4Add
BLAST
Domaini289 – 576288Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 624Brassinolide binding1 Publication

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 648Cys pair

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 21727Pro-richAdd
BLAST

Domaini

Contains one leucine-zipper motif and one pair of conservatively spaced Cys (Cys pair) involved in forming heterodimers.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000116554.
InParanoidiQ94F62.
KOiK13416.
PhylomeDBiQ94F62.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR031048. SERK.
[Graphical view]
PANTHERiPTHR27001:SF1. PTHR27001:SF1. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q94F62-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERRLMIPCF FWLILVLDLV LRVSGNAEGD ALSALKNSLA DPNKVLQSWD
60 70 80 90 100
ATLVTPCTWF HVTCNSDNSV TRVDLGNANL SGQLVMQLGQ LPNLQYLELY
110 120 130 140 150
SNNITGTIPE QLGNLTELVS LDLYLNNLSG PIPSTLGRLK KLRFLRLNNN
160 170 180 190 200
SLSGEIPRSL TAVLTLQVLD LSNNPLTGDI PVNGSFSLFT PISFANTKLT
210 220 230 240 250
PLPASPPPPI SPTPPSPAGS NRITGAIAGG VAAGAALLFA VPAIALAWWR
260 270 280 290 300
RKKPQDHFFD VPAEEDPEVH LGQLKRFSLR ELQVASDNFS NKNILGRGGF
310 320 330 340 350
GKVYKGRLAD GTLVAVKRLK EERTQGGELQ FQTEVEMISM AVHRNLLRLR
360 370 380 390 400
GFCMTPTERL LVYPYMANGS VASCLRERPE SQPPLDWPKR QRIALGSARG
410 420 430 440 450
LAYLHDHCDP KIIHRDVKAA NILLDEEFEA VVGDFGLAKL MDYKDTHVTT
460 470 480 490 500
AVRGTIGHIA PEYLSTGKSS EKTDVFGYGV MLLELITGQR AFDLARLAND
510 520 530 540 550
DDVMLLDWVK GLLKEKKLEA LVDVDLQGNY KDEEVEQLIQ VALLCTQSSP
560 570 580 590 600
MERPKMSEVV RMLEGDGLAE RWEEWQKEEM FRQDFNYPTH HPAVSGWIIG
610
DSTSQIENEY PSGPR
Length:615
Mass (Da):68,161
Last modified:March 28, 2003 - v2
Checksum:i547B3F38FB46E1DD
GO

Sequence cautioni

The sequence CAB38801.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB80060.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121W → G in AAK68074 (PubMed:11706164).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384970 mRNA. Translation: AAK68074.1.
FJ708762 mRNA. Translation: ACN59355.1.
AL035678 Genomic DNA. Translation: CAB38801.1. Sequence problems.
AL161583 Genomic DNA. Translation: CAB80060.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86223.1.
PIRiT05994.
RefSeqiNP_567920.1. NM_119497.4. [Q94F62-1]
UniGeneiAt.376.

Genome annotation databases

EnsemblPlantsiAT4G33430.1; AT4G33430.1; AT4G33430. [Q94F62-1]
GeneIDi829480.
KEGGiath:AT4G33430.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384970 mRNA. Translation: AAK68074.1.
FJ708762 mRNA. Translation: ACN59355.1.
AL035678 Genomic DNA. Translation: CAB38801.1. Sequence problems.
AL161583 Genomic DNA. Translation: CAB80060.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86223.1.
PIRiT05994.
RefSeqiNP_567920.1. NM_119497.4. [Q94F62-1]
UniGeneiAt.376.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TL8X-ray2.50A/D/G/H250-590[»]
3UIMX-ray2.20A258-583[»]
3ULZX-ray2.60A258-583[»]
4M7EX-ray3.60C/D26-220[»]
4MN8X-ray3.06B1-220[»]
ProteinModelPortaliQ94F62.
SMRiQ94F62. Positions 26-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14764. 22 interactions.
DIPiDIP-34976N.
IntActiQ94F62. 8 interactions.

PTM databases

iPTMnetiQ94F62.

Proteomic databases

PRIDEiQ94F62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G33430.1; AT4G33430.1; AT4G33430. [Q94F62-1]
GeneIDi829480.
KEGGiath:AT4G33430.

Organism-specific databases

TAIRiAT4G33430.

Phylogenomic databases

HOGENOMiHOG000116554.
InParanoidiQ94F62.
KOiK13416.
PhylomeDBiQ94F62.

Enzyme and pathway databases

BioCyciARA:AT4G33430-MONOMER.
ARA:GQT-1669-MONOMER.

Miscellaneous databases

PROiQ94F62.

Gene expression databases

ExpressionAtlasiQ94F62. baseline and differential.
GenevisibleiQ94F62. AT.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR031048. SERK.
[Graphical view]
PANTHERiPTHR27001:SF1. PTHR27001:SF1. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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. "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture."
    Hecht V.F.G., Vielle-Calzada J.-P., Hartog M.V., Schmidt E.D.L., Boutilier K., Grossniklaus U., de Vries S.C.
    Plant Physiol. 127:803-816(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
  2. "BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling."
    Li J., Wen J., Lease K.A., Doke J.T., Tax F.E., Walker J.C.
    Cell 110:213-222(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE.
  3. "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 [MRNA].
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Molecular characterisation of two novel maize LRR receptor-like kinases, which belong to the SERK gene family."
    Baudino S., Hansen S., Brettschneider R., Hecht V.F.G., Dresselhaus T., Loerz H., Dumas C., Rogowsky P.M.
    Planta 213:1-10(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling."
    Nam K.H., Li J.
    Cell 110:203-212(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1.
  8. "Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1)."
    Russinova E., Borst J.-W., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries S.C.
    Plant Cell 16:3216-3229(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BRI1.
  9. "Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase."
    Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J., Asami T., Yoshida S., Huber S.C., Clouse S.D.
    Plant Cell 17:1685-1703(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1.
  10. "A brassinosteroid-hypersensitive mutant of BAK1 indicates that a convergence of photomorphogenic and hormonal signaling modulates phototropism."
    Whippo C.W., Hangarter R.P.
    Plant Physiol. 139:448-457(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-122.
  11. "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein complex includes BRASSINOSTEROID-INSENSITIVE1."
    Karlova R., Boeren S., Russinova E., Aker J., Vervoort J., de Vries S.C.
    Plant Cell 18:626-638(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SERK1 COMPLEX.
  12. "The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants."
    Heese A., Hann D.R., Gimenez-Ibanez S., Jones A.M.E., He K., Li J., Schroeder J.I., Peck S.C., Rathjen J.P.
    Proc. Natl. Acad. Sci. U.S.A. 104:12217-12222(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLS2.
  13. "BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways."
    He K., Gou X., Yuan T., Lin H., Asami T., Yoshida S., Russell S.D., Li J.
    Curr. Biol. 17:1109-1115(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. Cited for: FUNCTION.
  15. "A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence."
    Chinchilla D., Zipfel C., Robatzek S., Kemmerling B., Nuernberger T., Jones J.D.G., Felix G., Boller T.
    Nature 448:497-500(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLS2, DISRUPTION PHENOTYPE.
  16. "Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase."
    Ding Z., Wang H., Liang X., Morris E.R., Gallazzi F., Pandit S., Skolnick J., Walker J.C., Van Doren S.R.
    Biochemistry 46:2684-2696(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-312; LYS-317 AND THR-546, INTERACTION WITH THE KINASE-INTERACTING FHA DOMAIN OF KAPP.
  17. "Fluorescence fluctuation analysis of Arabidopsis thaliana somatic embryogenesis receptor-like kinase and brassinosteroid insensitive 1 receptor oligomerization."
    Hink M.A., Shah K., Russinova E., de Vries S.C., Visser A.J.
    Biophys. J. 94:1052-1062(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  18. "Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity."
    Shan L., He P., Li J., Heese A., Peck S.C., Nurnberger T., Martin G.B., Sheen J.
    Cell Host Microbe 4:17-27(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO AND AVRPTOB/HOPAB2.
  19. "Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling."
    Wang X., Kota U., He K., Blackburn K., Li J., Goshe M.B., Huber S.C., Clouse S.D.
    Dev. Cell 15:220-235(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-286; SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, INTERACTION WITH BRI1, MUTAGENESIS OF THR-455.
  20. "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and -independent signaling pathways."
    Albrecht C., Russinova E., Kemmerling B., Kwaaitaal M., de Vries S.C.
    Plant Physiol. 148:611-619(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Modulations of AtGSTF10 expression induce stress tolerance and BAK1-mediated cell death."
    Ryu H.Y., Kim S.Y., Park H.M., You J.Y., Kim B.H., Lee J.S., Nam K.H.
    Biochem. Biophys. Res. Commun. 379:417-422(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERD13.
  22. "Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1."
    Song L., Shi Q.M., Yang X.H., Xu Z.H., Xue H.W.
    Cell Res. 19:864-876(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MSBP1.
  23. "Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases."
    Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J., Vervoort J., de Vries S.C.
    Proteomics 9:368-379(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.
  24. "Analysis of phosphorylation of the BRI1/BAK1 complex in arabidopsis reveals amino acid residues critical for receptor formation and activation of BR signaling."
    Yun H.S., Bae Y.H., Lee Y.J., Chang S.C., Kim S.-K., Li J., Nam K.H.
    Mol. Cells 27:183-190(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-32; LEU-46; CYS-64; LEU-94; LEU-121; SER-172; LYS-317; THR-446; THR-449; THR-450 AND THR-455.
  25. "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis."
    Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION.
  26. "The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity."
    Postel S., Kuefner I., Beuter C., Mazzotta S., Schwedt A., Borlotti A., Halter T., Kemmerling B., Nuernberger T.
    Eur. J. Cell Biol. 89:169-174(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, INTERACTION WITH PEPR1 AND PEPR2.
  27. "Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1."
    Schulze B., Mentzel T., Jehle A.K., Mueller K., Beeler S., Boller T., Felix G., Chinchilla D.
    J. Biol. Chem. 285:9444-9451(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLS2, PHOSPHORYLATION.
  28. "Phosphorylation of receptor-like cytoplasmic kinases by bacterial flagellin."
    Lu D., Wu S., He P., Shan L.
    Plant Signal. Behav. 5:598-600(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression."
    Oh M.H., Wang X., Wu X., Zhao Y., Clouse S.D., Huber S.C.
    Proc. Natl. Acad. Sci. U.S.A. 107:17827-17832(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-304; TYR-363; TYR-365; TYR-403; TYR-443; TYR-463; TYR-478; TYR-530; TYR-587 AND TYR-610, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-610.
  30. "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens."
    Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N., Malinovsky F.G., Tor M., de Vries S., Zipfel C.
    Plant Cell 23:2440-2455(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EFR AND FLS2.
    Strain: cv. Columbia.
  31. "Functional importance of BAK1 tyrosine phosphorylation in vivo."
    Oh M.H., Wu X., Clouse S.D., Huber S.C.
    Plant Signal. Behav. 6:400-405(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH BRI1.
  32. "Identification of Arabidopsis BAK1-associating receptor-like kinase 1 (BARK1) and characterization of its gene expression and brassinosteroid-regulated root phenotypes."
    Kim M.H., Kim Y., Kim J.W., Lee H.S., Lee W.S., Kim S.K., Wang Z.Y., Kim S.H.
    Plant Cell Physiol. 54:1620-1634(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMK4/BARK1.
  33. Cited for: FUNCTION, MUTAGENESIS OF SER-290; THR-312; LYS-317; THR-446; THR-449; THR-450 AND THR-455, INTERACTION WITH BIR2, AUTOPHOSPHORYLATION.
    Strain: cv. Columbia.
  34. "Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated immune signaling in Arabidopsis."
    Blaum B.S., Mazzotta S., Noeldeke E.R., Halter T., Madlung J., Kemmerling B., Stehle T.
    J. Struct. Biol. 186:112-121(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIR2.
  35. "Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector."
    Cheng W., Munkvold K.R., Gao H., Mathieu J., Schwizer S., Wang S., Yan Y.B., Wang J., Martin G.B., Chai J.
    Cell Host Microbe 10:616-626(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 250-590 IN COMPLEX WITH HOPAB2/AVRPTOB, PHOSPHORYLATION AT THR-446; THR-449 AND THR-450, MUTAGENESIS OF LYS-317; THR-449; THR-450; ALA-451; VAL-452; THR-455; ILE-456; HIS-458; LEU-464 AND ALA-495.
  36. "Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1."
    Yan L., Ma Y., Liu D., Wei X., Sun Y., Chen X., Zhao H., Zhou J., Wang Z., Shui W., Lou Z.
    Cell Res. 22:1304-1308(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 258-583 IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.
  37. "Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex."
    Sun Y., Li L., Macho A.P., Han Z., Hu Z., Zipfel C., Zhou J.M., Chai J.
    Science 342:624-628(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 1-220 IN COMPLEX WITH FLS2 AND FLG22, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF ASP-30; PHE-60; TYR-96 AND PHE-144.
  38. "Structural insight into BL-induced activation of the BRI1-BAK1 complex."
    Sun Y., Han Z., Chai J.
    Submitted (AUG-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 26-220 IN COMPLEX WITH BRASSINOLIDE, DISULFIDE BONDS.

Entry informationi

Entry nameiBAK1_ARATH
AccessioniPrimary (citable) accession number: Q94F62
Secondary accession number(s): C0LGS0, Q9SZC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: June 8, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Interaction with BRI1 activates both receptor kinases and the full activation of either receptor kinase requires transphosphorylation by their partners. This interaction in vitro is magnesium dependent. Instantaneous heteromeric complex formation between FLS2 and BAK1 and reciprocal transphosphorylation after binding of the flagellin flg22 ligand to FLS2. The kinase activity is not required for the complex formation.
The interaction with the bacterial effectors AvrPto and AvrPtoB/hopAB2 interfers with FLS2 binding and plant immunity.
Phosphorylated residues T-450 and T-455 have stronger functional effects than other phosphorylated residues by interacting with both the catalytic and activation loops to achieve a conformational stability, locking BAK1 kinase in the active conformation.1 Publication

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.