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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei330 – 3301ATPPROSITE-ProRule annotation
    Active sitei429 – 4291Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi308 – 3169ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • identical protein binding Source: IntAct
    • receptor serine/threonine kinase binding Source: UniProtKB
    • transmembrane receptor protein serine/threonine kinase activity Source: TAIR
    • transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    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
    • transmembrane receptor protein serine/threonine kinase signaling pathway Source: GOC
    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:AT1G71830-MONOMER.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 238215ExtracellularSequence analysisAdd
    BLAST
    Transmembranei239 – 25921HelicalSequence analysisAdd
    BLAST
    Topological domaini260 – 625366CytoplasmicSequence analysisAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi330 – 3301K → E: Loss of kinase activity. 1 Publication
    Mutagenesisi459 – 4591T → A or E: No effect. 1 Publication
    Mutagenesisi462 – 4621T → A or E: Decreased kinase activity. Loss of kinase activity; when associated with A,E-463 and A,E-468. 1 Publication
    Mutagenesisi463 – 4631T → A or E: Loss of autophosphorylation. Loss of kinase activity; when associated with A,E-462 and A,E-468. 1 Publication
    Mutagenesisi468 – 4681T → A or E: Loss of kinase activity. Loss of kinase activity; when associated with A,E-462 and A,E-463. 1 Publication
    Mutagenesisi541 – 5411T → A: No effect. Reduction of autophosphorylation; when associated with A-570. 1 Publication
    Mutagenesisi562 – 5621S → A: Loss of autophosphorylation. 1 Publication
    Mutagenesisi570 – 5701S → A: No effect. Reduction of autophosphorylation; when associated with A-541. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence analysisAdd
    BLAST
    Chaini24 – 625602Somatic embryogenesis receptor kinase 1PRO_0000379596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence analysis
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence analysis
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence analysis
    Modified residuei291 – 2911Phosphoserine1 Publication
    Modified residuei299 – 2991Phosphoserine1 Publication
    Modified residuei303 – 3031Phosphoserine1 Publication
    Modified residuei325 – 3251Phosphothreonine1 Publication
    Modified residuei337 – 3371Phosphothreonine1 Publication
    Modified residuei346 – 3461Phosphothreonine1 Publication
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei383 – 3831Phosphoserine1 Publication
    Modified residuei386 – 3861PhosphoserineBy similarity
    Modified residuei394 – 3941Phosphoserine1 Publication
    Modified residuei402 – 4021Phosphothreonine1 Publication
    Modified residuei415 – 4151Phosphoserine1 Publication
    Modified residuei456 – 4561Phosphotyrosine1 Publication
    Modified residuei459 – 4591Phosphothreonine1 Publication
    Modified residuei462 – 4621Phosphothreonine1 Publication
    Modified residuei463 – 4631Phosphothreonine1 Publication
    Modified residuei468 – 4681Phosphothreonine1 Publication
    Modified residuei476 – 4761Phosphotyrosine1 Publication
    Modified residuei478 – 4781Phosphoserine1 Publication
    Modified residuei479 – 4791Phosphothreonine1 Publication
    Modified residuei483 – 4831Phosphoserine1 Publication
    Modified residuei541 – 5411Phosphothreonine1 Publication
    Modified residuei543 – 5431Phosphotyrosine1 Publication
    Modified residuei559 – 5591Phosphothreonine1 Publication
    Modified residuei606 – 6061Phosphoserine1 Publication
    Modified residuei612 – 6121Phosphoserine1 Publication
    Modified residuei613 – 6131Phosphothreonine1 Publication
    Modified residuei614 – 6141Phosphotyrosine1 Publication
    Modified residuei622 – 6221Phosphoserine1 Publication

    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

    • identical protein binding Source: IntAct
    • receptor serine/threonine kinase binding Source: UniProtKB

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    625
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 3912Combined sources
    Turni46 – 494Combined sources
    Helixi57 – 593Combined sources
    Beta strandi63 – 653Combined sources
    Beta strandi71 – 755Combined sources
    Beta strandi82 – 843Combined sources
    Helixi87 – 915Combined sources
    Beta strandi97 – 993Combined sources
    Beta strandi102 – 1076Combined sources
    Helixi113 – 1153Combined sources
    Beta strandi120 – 1234Combined sources
    Beta strandi126 – 1316Combined sources
    Helixi135 – 1395Combined sources
    Beta strandi145 – 1473Combined sources
    Beta strandi150 – 1556Combined sources
    Helixi159 – 1635Combined sources
    Beta strandi169 – 1713Combined sources
    Beta strandi174 – 1807Combined sources
    Helixi185 – 1895Combined sources
    Helixi192 – 1943Combined sources
    Beta strandi199 – 2035Combined sources
    Turni204 – 2074Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LSCX-ray1.53A24-213[»]
    4LSXX-ray3.30C/D24-213[»]
    4Z64X-ray2.66C1-213[»]
    ProteinModelPortaliQ94AG2.
    SMRiQ94AG2. Positions 27-211, 251-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati94 – 11724LRR 1Add
    BLAST
    Repeati118 – 14023LRR 2Add
    BLAST
    Repeati142 – 16524LRR 3Add
    BLAST
    Repeati166 – 18823LRR 4Add
    BLAST
    Domaini302 – 589288Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi204 – 23128Pro-richAdd
    BLAST
    Compositional biasi239 – 26022Ala-richAdd
    BLAST

    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.
    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.
    IPR001611. Leu-rich_rpt.
    IPR013210. LRR_N_plant-typ.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00560. LRR_1. 2 hits.
    PF08263. 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 AAF43236.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531T → R in AAK82463 (PubMed:14593172).Curated
    Sequence conflicti53 – 531T → R in AAN72307 (PubMed:14593172).Curated
    Sequence conflicti251 – 2511L → P in CAB42254 (PubMed:11706164).Curated
    Sequence conflicti266 – 2661K → S in CAB42254 (PubMed:11706164).Curated
    Sequence conflicti327 – 3271V → I in AAK82463 (PubMed:14593172).Curated
    Sequence conflicti327 – 3271V → I in AAN72307 (PubMed:14593172).Curated

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LSCX-ray1.53A24-213[»]
    4LSXX-ray3.30C/D24-213[»]
    4Z64X-ray2.66C1-213[»]
    ProteinModelPortaliQ94AG2.
    SMRiQ94AG2. Positions 27-211, 251-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi28733. 14 interactions.
    DIPiDIP-38028N.
    IntActiQ94AG2. 10 interactions.
    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.
    PhylomeDBiQ94AG2.

    Enzyme and pathway databases

    BioCyciARA:AT1G71830-MONOMER.

    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.
    IPR001611. Leu-rich_rpt.
    IPR013210. LRR_N_plant-typ.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00560. LRR_1. 2 hits.
    PF08263. 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...

    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 [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    2. "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.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Subcellular localization and oligomerization of the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein."
      Shah K., Gadella T.W.J. Jr., van Erp H., Hecht V., de Vries S.C.
      J. Mol. Biol. 309:641-655(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    7. "Role of threonines in the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 activation loop in phosphorylation."
      Shah K., Vervoort J., de Vries S.C.
      J. Biol. Chem. 276:41263-41269(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-330; THR-459; THR-462; THR-463 AND THR-468, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1."
      Shah K., Russinova E., Gadella T.W. Jr., Willemse J., de Vries S.C.
      Genes Dev. 16:1707-1720(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAPP, SUBUNIT.
    9. "The Arabidopsis thaliana SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASES1 and 2 control male sporogenesis."
      Albrecht C., Russinova E., Hecht V.F.G., Baaijens E., de Vries S.
      Plant Cell 17:3337-3349(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SERK2, SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    10. "The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP."
      Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.
      Planta 221:394-405(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC48A; GRF6 AND KAPP.
    11. "Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein is present in sporophytic and gametophytic cells and undergoes endocytosis."
      Kwaaitaal M.A.C.J., de Vries S.C., Russinova E.
      Protoplasma 226:55-65(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    12. "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASES1 and 2 are essential for tapetum development and microspore maturation."
      Colcombet J., Boisson-Dernier A., Ros-Palau R., Vera C.E., Schroeder J.I.
      Plant Cell 17:3350-3361(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "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: INTERACTION WITH BRI1; BAK1/SERK3; CDC48A; GRF7 AND KAPP.
    14. "The Arabidopsis thaliana AAA protein CDC48A interacts in vivo with the somatic embryogenesis receptor-like kinase 1 receptor at the plasma membrane."
      Aker J., Borst J.W., Karlova R., de Vries S.C.
      J. Struct. Biol. 156:62-71(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CDC48A.
    15. "In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy."
      Aker J., Hesselink R., Engel R., Karlova R., Borst J.W., Visser A.J.W.G., de Vries S.C.
      Plant Physiol. 145:339-350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC48A.
    16. "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.
    17. "AtSERK1 expression precedes and coincides with early somatic embryogenesis in Arabidopsis thaliana."
      Salaj J., von Recklinghausen I.R., Hecht V., de Vries S.C., Schel J.H.N., van Lammeren A.A.M.
      Plant Physiol. Biochem. 46:709-714(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    18. "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: MUTAGENESIS OF THR-541; SER-562 AND SER-570, PHOSPHORYLATION AT SER-291; SER-299; SER-303; THR-325; THR-337; THR-346; SER-352; SER-383; SER-394; THR-402; SER-415; TYR-456; THR-459; THR-462; THR-463; THR-468; TYR-476; SER-478; THR-479; SER-483; THR-541; TYR-543; THR-559; SER-606; SER-612; THR-613; TYR-614 AND SER-622.
    19. "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: INTERACTION WITH EFR AND FLS2.
      Strain: cv. Columbia.

    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: May 11, 2016
    This is version 121 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.