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Protein

Somatic embryogenesis receptor kinase 1

Gene

SERK1

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. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway.2 Publications

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by manganese.

Kineticsi

  1. KM=4 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei330ATPPROSITE-ProRule annotation1
    Active sitei429Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi308 – 316ATPPROSITE-ProRule annotation9

    GO - Molecular functioni

    GO - Biological processi

    • brassinosteroid mediated signaling pathway Source: TAIR
    • embryo development ending in seed dormancy Source: TAIR
    • floral organ abscission Source: TAIR
    • Golgi organization Source: TAIR
    • microsporogenesis Source: TAIR
    • pollen maturation Source: TAIR
    • protein autophosphorylation Source: TAIR
    • protein phosphorylation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Somatic embryogenesis receptor kinase 1 (EC:2.7.10.1, EC:2.7.11.1)
    Short name:
    AtSERK1
    Alternative name(s):
    Somatic embryogenesis receptor-like kinase 1
    Gene namesi
    Name:SERK1
    Ordered Locus Names:At1g71830
    ORF Names:F14O23.21, F14O23_24
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G71830.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini24 – 238ExtracellularSequence analysisAdd BLAST215
    Transmembranei239 – 259HelicalSequence analysisAdd BLAST21
    Topological domaini260 – 625CytoplasmicSequence analysisAdd BLAST366

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Serk1 and serk2 double mutants are completely male sterile due to a failure in tapetum specification.2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi330K → E: Loss of kinase activity. 1 Publication1
    Mutagenesisi459T → A or E: No effect. 1 Publication1
    Mutagenesisi462T → A or E: Decreased kinase activity. Loss of kinase activity; when associated with A,E-463 and A,E-468. 1 Publication1
    Mutagenesisi463T → A or E: Loss of autophosphorylation. Loss of kinase activity; when associated with A,E-462 and A,E-468. 1 Publication1
    Mutagenesisi468T → A or E: Loss of kinase activity. Loss of kinase activity; when associated with A,E-462 and A,E-463. 1 Publication1
    Mutagenesisi541T → A: No effect. Reduction of autophosphorylation; when associated with A-570. 1 Publication1
    Mutagenesisi562S → A: Loss of autophosphorylation. 1 Publication1
    Mutagenesisi570S → A: No effect. Reduction of autophosphorylation; when associated with A-541. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 23Sequence analysisAdd BLAST23
    ChainiPRO_000037959624 – 625Somatic embryogenesis receptor kinase 1Add BLAST602

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi115N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi150N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi163N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi184N-linked (GlcNAc...)Sequence analysis1
    Modified residuei291Phosphoserine1 Publication1
    Modified residuei299Phosphoserine1 Publication1
    Modified residuei303Phosphoserine1 Publication1
    Modified residuei325Phosphothreonine1 Publication1
    Modified residuei337Phosphothreonine1 Publication1
    Modified residuei346Phosphothreonine1 Publication1
    Modified residuei352Phosphoserine1 Publication1
    Modified residuei383Phosphoserine1 Publication1
    Modified residuei386PhosphoserineBy similarity1
    Modified residuei394Phosphoserine1 Publication1
    Modified residuei402Phosphothreonine1 Publication1
    Modified residuei415Phosphoserine1 Publication1
    Modified residuei456Phosphotyrosine1 Publication1
    Modified residuei459Phosphothreonine1 Publication1
    Modified residuei462Phosphothreonine1 Publication1
    Modified residuei463Phosphothreonine1 Publication1
    Modified residuei468Phosphothreonine1 Publication1
    Modified residuei476Phosphotyrosine1 Publication1
    Modified residuei478Phosphoserine1 Publication1
    Modified residuei479Phosphothreonine1 Publication1
    Modified residuei483Phosphoserine1 Publication1
    Modified residuei541Phosphothreonine1 Publication1
    Modified residuei543Phosphotyrosine1 Publication1
    Modified residuei559Phosphothreonine1 Publication1
    Modified residuei606Phosphoserine1 Publication1
    Modified residuei612Phosphoserine1 Publication1
    Modified residuei613Phosphothreonine1 Publication1
    Modified residuei614Phosphotyrosine1 Publication1
    Modified residuei622Phosphoserine1 Publication1

    Post-translational modificationi

    Glycosylated. Important for targeting to the plasma membrane.
    Intermolecular autophosphorylation. The catalytic activity of SERK1 depends on the presence of a phosphorylated Thr residue in SERK1. The phosphorylation is induced by brassinosteroids. Transphosphorylation by BRI1 occurs only on Ser-299 and Thr-462. Dephosphorylation of threonine residues by the kinase-associated protein phosphatase (KAPP) is involved in SERK1 endocytosis.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ94AG2.
    PRIDEiQ94AG2.

    PTM databases

    iPTMnetiQ94AG2.

    Expressioni

    Tissue specificityi

    Expressed in flowers, tapetum, developing microspores, all cells of the embryo sac, provascular strands and developing vascular bundles. Low expression in adult vascular tissue. Detected in root meristem.4 Publications

    Developmental stagei

    Expressed during pollen development and megasporogenesis in the nucellus of developing ovules, in all cells of the embryo sac up to fertilization and in all cells of the developing embryo until the heart-shaped stage. Found in epidermal and vascular cells of the late torpedo and cotyledon stages embryos.3 Publications

    Gene expression databases

    GenevisibleiQ94AG2. AT.

    Interactioni

    Subunit structurei

    Monomer, homo- and heterodimer. Interacts with KAPP, CDC48A, GRF6 or GRF7, SERK2, BRI1 and SERK3/BAK1 to form the SERK1 signaling complex. Interacts with the EF-Tu receptor EFR and FLS2 in a specific ligand-induced manner.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1555537,EBI-1555537
    BRI1O224765EBI-1555537,EBI-1797828
    CDC48AP5460912EBI-1555537,EBI-1563238
    GRF6P483496EBI-1555537,EBI-1633785

    GO - Molecular functioni

    • receptor serine/threonine kinase binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi28733. 14 interactors.
    DIPiDIP-38028N.
    IntActiQ94AG2. 10 interactors.
    STRINGi3702.AT1G71830.1.

    Structurei

    Secondary structure

    1625
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi28 – 39Combined sources12
    Turni46 – 49Combined sources4
    Beta strandi54 – 56Combined sources3
    Helixi57 – 59Combined sources3
    Beta strandi63 – 65Combined sources3
    Beta strandi71 – 75Combined sources5
    Beta strandi82 – 84Combined sources3
    Helixi87 – 91Combined sources5
    Beta strandi97 – 99Combined sources3
    Beta strandi102 – 108Combined sources7
    Helixi113 – 115Combined sources3
    Beta strandi120 – 123Combined sources4
    Beta strandi126 – 131Combined sources6
    Helixi135 – 139Combined sources5
    Beta strandi145 – 147Combined sources3
    Beta strandi150 – 155Combined sources6
    Helixi159 – 163Combined sources5
    Beta strandi169 – 171Combined sources3
    Beta strandi174 – 180Combined sources7
    Helixi185 – 189Combined sources5
    Helixi192 – 194Combined sources3
    Beta strandi199 – 203Combined sources5
    Turni204 – 207Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4LSCX-ray1.53A24-213[»]
    4LSXX-ray3.30C/D24-213[»]
    4Z64X-ray2.66C1-213[»]
    5IYXX-ray2.43C24-213[»]
    ProteinModelPortaliQ94AG2.
    SMRiQ94AG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Repeati94 – 117LRR 1Add BLAST24
    Repeati118 – 140LRR 2Add BLAST23
    Repeati142 – 165LRR 3Add BLAST24
    Repeati166 – 188LRR 4Add BLAST23
    Domaini302 – 589Protein kinasePROSITE-ProRule annotationAdd BLAST288

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi204 – 231Pro-richAdd BLAST28
    Compositional biasi239 – 260Ala-richAdd BLAST22

    Domaini

    The extracellular domain (26-234) is required for dimerization.

    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

    eggNOGiENOG410IGSH. Eukaryota.
    ENOG410ZNK7. LUCA.
    HOGENOMiHOG000116554.
    InParanoidiQ94AG2.
    KOiK13418.
    OMAiWQKVEIL.
    OrthoDBiEOG093605SM.
    PhylomeDBiQ94AG2.

    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.
    IPR013210. LRR_N_plant-typ.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF08263. LRRNT_2. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52058. SSF52058. 2 hits.
    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.

    Q94AG2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MESSYVVFIL LSLILLPNHS LWLASANLEG DALHTLRVTL VDPNNVLQSW
    60 70 80 90 100
    DPTLVNPCTW FHVTCNNENS VIRVDLGNAE LSGHLVPELG VLKNLQYLEL
    110 120 130 140 150
    YSNNITGPIP SNLGNLTNLV SLDLYLNSFS GPIPESLGKL SKLRFLRLNN
    160 170 180 190 200
    NSLTGSIPMS LTNITTLQVL DLSNNRLSGS VPDNGSFSLF TPISFANNLD
    210 220 230 240 250
    LCGPVTSHPC PGSPPFSPPP PFIQPPPVST PSGYGITGAI AGGVAAGAAL
    260 270 280 290 300
    LFAAPAIAFA WWRRRKPLDI FFDVPAEEDP EVHLGQLKRF SLRELQVASD
    310 320 330 340 350
    GFSNKNILGR GGFGKVYKGR LADGTLVAVK RLKEERTPGG ELQFQTEVEM
    360 370 380 390 400
    ISMAVHRNLL RLRGFCMTPT ERLLVYPYMA NGSVASCLRE RPPSQPPLDW
    410 420 430 440 450
    PTRKRIALGS ARGLSYLHDH CDPKIIHRDV KAANILLDEE FEAVVGDFGL
    460 470 480 490 500
    AKLMDYKDTH VTTAVRGTIG HIAPEYLSTG KSSEKTDVFG YGIMLLELIT
    510 520 530 540 550
    GQRAFDLARL ANDDDVMLLD WVKGLLKEKK LEMLVDPDLQ TNYEERELEQ
    560 570 580 590 600
    VIQVALLCTQ GSPMERPKMS EVVRMLEGDG LAEKWDEWQK VEILREEIDL
    610 620
    SPNPNSDWIL DSTYNLHAVE LSGPR
    Length:625
    Mass (Da):69,022
    Last modified:July 28, 2009 - v2
    Checksum:i98F6B69126DB664A
    GO

    Sequence cautioni

    The sequence AAF43236 differs from that shown. Reason: Erroneous gene model prediction.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti53T → R in AAK82463 (PubMed:14593172).Curated1
    Sequence conflicti53T → R in AAN72307 (PubMed:14593172).Curated1
    Sequence conflicti251L → P in CAB42254 (PubMed:11706164).Curated1
    Sequence conflicti266K → S in CAB42254 (PubMed:11706164).Curated1
    Sequence conflicti327V → I in AAK82463 (PubMed:14593172).Curated1
    Sequence conflicti327V → I in AAN72307 (PubMed:14593172).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    A67827 Unassigned DNA. Translation: CAB42254.1.
    A67815 Unassigned DNA. No translation available.
    FJ708676 mRNA. Translation: ACN59271.1.
    AC012654 Genomic DNA. Translation: AAF43236.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE35238.1.
    AY048200 mRNA. Translation: AAK82463.1.
    BT002217 mRNA. Translation: AAN72307.1.
    PIRiH96740.
    RefSeqiNP_177328.1. NM_105841.4.
    UniGeneiAt.12027.
    At.72107.

    Genome annotation databases

    EnsemblPlantsiAT1G71830.1; AT1G71830.1; AT1G71830.
    GeneIDi843513.
    GrameneiAT1G71830.1; AT1G71830.1; AT1G71830.
    KEGGiath:AT1G71830.

    Cross-referencesi

    Web resourcesi

    PlantP kinase Classification PPC

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    A67827 Unassigned DNA. Translation: CAB42254.1.
    A67815 Unassigned DNA. No translation available.
    FJ708676 mRNA. Translation: ACN59271.1.
    AC012654 Genomic DNA. Translation: AAF43236.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE35238.1.
    AY048200 mRNA. Translation: AAK82463.1.
    BT002217 mRNA. Translation: AAN72307.1.
    PIRiH96740.
    RefSeqiNP_177328.1. NM_105841.4.
    UniGeneiAt.12027.
    At.72107.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4LSCX-ray1.53A24-213[»]
    4LSXX-ray3.30C/D24-213[»]
    4Z64X-ray2.66C1-213[»]
    5IYXX-ray2.43C24-213[»]
    ProteinModelPortaliQ94AG2.
    SMRiQ94AG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi28733. 14 interactors.
    DIPiDIP-38028N.
    IntActiQ94AG2. 10 interactors.
    STRINGi3702.AT1G71830.1.

    PTM databases

    iPTMnetiQ94AG2.

    Proteomic databases

    PaxDbiQ94AG2.
    PRIDEiQ94AG2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G71830.1; AT1G71830.1; AT1G71830.
    GeneIDi843513.
    GrameneiAT1G71830.1; AT1G71830.1; AT1G71830.
    KEGGiath:AT1G71830.

    Organism-specific databases

    TAIRiAT1G71830.

    Phylogenomic databases

    eggNOGiENOG410IGSH. Eukaryota.
    ENOG410ZNK7. LUCA.
    HOGENOMiHOG000116554.
    InParanoidiQ94AG2.
    KOiK13418.
    OMAiWQKVEIL.
    OrthoDBiEOG093605SM.
    PhylomeDBiQ94AG2.

    Miscellaneous databases

    PROiQ94AG2.

    Gene expression databases

    GenevisibleiQ94AG2. 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.
    IPR013210. LRR_N_plant-typ.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF08263. LRRNT_2. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52058. SSF52058. 2 hits.
    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...

    Entry informationi

    Entry nameiSERK1_ARATH
    AccessioniPrimary (citable) accession number: Q94AG2
    Secondary accession number(s): C0LGI6, Q9M9G3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: July 28, 2009
    Last modified: November 2, 2016
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Seems to be related with early development of tissues in general rather than with embryogenesis.

    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.