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Protein

Extracellular signal-regulated kinase 2

Gene

erkB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+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

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. cell division Source: UniProtKB-KW
  5. chemotaxis Source: UniProtKB-KW
  6. mitotic nuclear division Source: UniProtKB-KW
  7. negative regulation of cyclic-nucleotide phosphodiesterase activity Source: dictyBase
  8. positive regulation of cAMP biosynthetic process Source: dictyBase
  9. response to cisplatin Source: dictyBase
  10. response to lipopolysaccharide Source: dictyBase
Complete GO annotation...

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 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0283903. erkB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: dictyBase
Complete GO annotation...

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.
InParanoidiQ54QB1.
KOiK08293.
OMAiGFEYMET.
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.
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

        10         20         30         40         50
MSSEDIDKHV LRKYEVLQKI GKGAYGIVWK AIDKKTKQTV ALKKIFDAFQ
60 70 80 90 100
NATDAQRTFR EIMFLQELHG HENIIKLLNV IKADNDRDIY LVFEHMETDL
110 120 130 140 150
HAVIRAKILE EIHKQYTIYQ LLKALKYMHS ANVLHRDIKP SNLLLNSECL
160 170 180 190 200
VKVADFGLAR SITSLESIAE ANPVLTEYVA TRWYRAPEIL LGSTKYTKGV
210 220 230 240 250
DMWSIGCILG ELLGEKAMFP GNSTMNQLDL IIEVTGRPSA EDIEAIKSPF
260 270 280 290 300
AGTMLESLPP SNPRSLSDMY PSASVDALDL LKKLLQFNPD KRITAEEALA
310 320 330 340 350
HPFVTQFHNP AEEPHFDRII KISIDDGQKF PIAEYRNRLY NDIIKKKKEE
360
RKKQTNPTKP DTTAPTLST
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
L33043 mRNA. No translation available.
AAFI02000058 Genomic DNA. Translation: EAL65439.1.
PIRiA56492.
RefSeqiXP_638833.1. XM_633741.1.

3D structure databases

ProteinModelPortaliQ54QB1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ54QB1. 1 interaction.
STRINGi44689.DDB_0191457.

Proteomic databases

PRIDEiQ54QB1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

dictyBaseiDDB_G0283903. erkB.

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiQ54QB1.
KOiK08293.
OMAiGFEYMET.
PhylomeDBiQ54QB1.

Miscellaneous databases

PROiQ54QB1.

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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 83 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

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 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.