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Q54QB1

- ERK2_DICDI

UniProt

Q54QB1 - ERK2_DICDI

Protein

Extracellular signal-regulated kinase 2

Gene

erkB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Implicated in the relay of the cAMP chemotactic signal and cell differentiation. Important for receptor-mediated activation of adenylyl cyclase.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431ATPPROSITE-ProRule annotation
    Active sitei137 – 1371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: dictyBase
    2. aggregation involved in sorocarp development Source: dictyBase
    3. cAMP-mediated signaling Source: dictyBase
    4. chemotaxis Source: UniProtKB-KW
    5. mitotic nuclear division Source: UniProtKB-KW
    6. negative regulation of cyclic-nucleotide phosphodiesterase activity Source: dictyBase
    7. positive regulation of cAMP biosynthetic process Source: dictyBase
    8. response to cisplatin Source: dictyBase
    9. response to lipopolysaccharide Source: dictyBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Chemotaxis, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extracellular signal-regulated kinase 2 (EC:2.7.11.24)
    Short name:
    ERK2
    Alternative name(s):
    Defective in aggregation protein C
    MAP kinase 2
    Gene namesi
    Name:erkB
    Synonyms:dagC, erk2
    ORF Names:DDB_G0283903
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 4, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0283903. erkB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: dictyBase

    Pathology & Biotechi

    Disruption phenotypei

    Cells, starved for 8 hours, exhibited a decrease in motility and a severe chemotaxis defect toward a cAMP gradient. Aberrancy in chemotaxis was aggravated in the presence of a strong cAMP gradient. Cells also display defective cytoskeletal remodeling in response to chemoattractant stimulation. Cells are defective in aggregation and display multiple crown-like membranous protrusions, which were enriched not only in F-actin but also in myosin II. This aberrant structure, which was proposed to be less stable and unable to provide necessary traction force for cells to move, is believed to be the reason why cells are less motile than wild-type cells.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Extracellular signal-regulated kinase 2PRO_0000312369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei176 – 1761PhosphothreonineBy similarity
    Modified residuei178 – 1781PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-176 and Tyr-178, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ54QB1.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    gpaDP340422EBI-2905550,EBI-2905587

    Protein-protein interaction databases

    IntActiQ54QB1. 1 interaction.
    STRINGi44689.DDB_0191457.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54QB1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 304291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi176 – 1783TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi345 – 3484Poly-Lys

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    KOiK08293.
    OMAiSAEIESH.
    PhylomeDBiQ54QB1.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q54QB1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSEDIDKHV LRKYEVLQKI GKGAYGIVWK AIDKKTKQTV ALKKIFDAFQ    50
    NATDAQRTFR EIMFLQELHG HENIIKLLNV IKADNDRDIY LVFEHMETDL 100
    HAVIRAKILE EIHKQYTIYQ LLKALKYMHS ANVLHRDIKP SNLLLNSECL 150
    VKVADFGLAR SITSLESIAE ANPVLTEYVA TRWYRAPEIL LGSTKYTKGV 200
    DMWSIGCILG ELLGEKAMFP GNSTMNQLDL IIEVTGRPSA EDIEAIKSPF 250
    AGTMLESLPP SNPRSLSDMY PSASVDALDL LKKLLQFNPD KRITAEEALA 300
    HPFVTQFHNP AEEPHFDRII KISIDDGQKF PIAEYRNRLY NDIIKKKKEE 350
    RKKQTNPTKP DTTAPTLST 369
    Length:369
    Mass (Da):41,978
    Last modified:May 24, 2005 - v1
    Checksum:i3AB5C85E6F10722B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 182LQ → FH in L33043. (PubMed:7844154)Curated
    Sequence conflicti30 – 301K → E in L33043. (PubMed:7844154)Curated
    Sequence conflicti36 – 383TKQ → PHH in L33043. (PubMed:7844154)Curated
    Sequence conflicti285 – 2851L → S in L33043. (PubMed:7844154)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33043 mRNA. No translation available.
    AAFI02000058 Genomic DNA. Translation: EAL65439.1.
    PIRiA56492.
    RefSeqiXP_638833.1. XM_633741.1.

    Genome annotation databases

    EnsemblProtistsiDDB0191457; DDB0191457; DDB_G0283903.
    GeneIDi8624357.
    KEGGiddi:DDB_G0283903.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33043 mRNA. No translation available.
    AAFI02000058 Genomic DNA. Translation: EAL65439.1 .
    PIRi A56492.
    RefSeqi XP_638833.1. XM_633741.1.

    3D structure databases

    ProteinModelPortali Q54QB1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q54QB1. 1 interaction.
    STRINGi 44689.DDB_0191457.

    Proteomic databases

    PRIDEi Q54QB1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0191457 ; DDB0191457 ; DDB_G0283903 .
    GeneIDi 8624357.
    KEGGi ddi:DDB_G0283903.

    Organism-specific databases

    dictyBasei DDB_G0283903. erkB.

    Phylogenomic databases

    eggNOGi COG0515.
    KOi K08293.
    OMAi SAEIESH.
    PhylomeDBi Q54QB1.

    Miscellaneous databases

    PROi Q54QB1.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A MAP kinase necessary for receptor-mediated activation of adenylyl cyclase in Dictyostelium."
      Segall J.E., Kuspa A., Shaulsky G., Ecke M., Maeda M., Gaskins C., Firtel R.A., Loomis W.F.
      J. Cell Biol. 128:405-413(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: AX4.
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "MAP kinase function in amoeboid chemotaxis."
      Wang Y., Liu J., Segall J.E.
      J. Cell Sci. 111:373-383(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    4. "MPL1, a novel phosphatase with leucine-rich repeats, is essential for proper ERK2 phosphorylation and cell motility."
      Rodriguez M., Kim B., Lee N.-S., Veeranki S., Kim L.
      Eukaryot. Cell 7:958-966(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiERK2_DICDI
    AccessioniPrimary (citable) accession number: Q54QB1
    Secondary accession number(s): Q7M445
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3