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Protein

Extracellular signal-regulated kinase 2

Gene

erkB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei43ATPPROSITE-ProRule annotation1
Active sitei137Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 28ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: dictyBase
  • MAP kinase activity Source: dictyBase

GO - Biological processi

  • activation of adenylate cyclase activity Source: dictyBase
  • aggregation involved in sorocarp development Source: dictyBase
  • cAMP-mediated signaling Source: dictyBase
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell surface receptor signaling pathway Source: dictyBase
  • chemotaxis to cAMP Source: dictyBase
  • chemotaxis to folate Source: dictyBase
  • G-protein coupled receptor signaling pathway Source: dictyBase
  • negative regulation of cyclic-nucleotide phosphodiesterase activity Source: dictyBase
  • positive regulation of gene expression Source: dictyBase
  • protein autophosphorylation Source: dictyBase
  • response to cisplatin Source: dictyBase
  • response to differentiation-inducing factor 1 Source: dictyBase
  • response to lipopolysaccharide Source: dictyBase
  • sorocarp spore cell differentiation Source: dictyBase

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Chemotaxis, Mitosis
LigandATP-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 lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0283903 erkB

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: dictyBase
  • nucleus 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)DescriptionActionsGraphical viewLength
ChainiPRO_00003123691 – 369Extracellular signal-regulated kinase 2Add BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei176PhosphothreonineBy similarity1
Modified residuei178PhosphotyrosineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ54QB1
PRIDEiQ54QB1

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

IntActiQ54QB1, 1 interactor
STRINGi44689.DDB0191457

Structurei

3D structure databases

ProteinModelPortaliQ54QB1
SMRiQ54QB1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 304Protein kinasePROSITE-ProRule annotationAdd BLAST291

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi176 – 178TXY3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi345 – 348Poly-Lys4

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0660 Eukaryota
ENOG410XNY0 LUCA
InParanoidiQ54QB1
KOiK19603
OMAiASDEPDC
PhylomeDBiQ54QB1

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti17 – 18LQ → FH in L33043 (PubMed:7844154).Curated2
Sequence conflicti30K → E in L33043 (PubMed:7844154).Curated1
Sequence conflicti36 – 38TKQ → PHH in L33043 (PubMed:7844154).Curated3
Sequence conflicti285L → S in L33043 (PubMed:7844154).Curated1

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

EnsemblProtistsiEAL65439; EAL65439; DDB_G0283903
GeneIDi8624357
KEGGiddi:DDB_G0283903

Similar proteinsi

Entry informationi

Entry nameiERK2_DICDI
AccessioniPrimary (citable) accession number: Q54QB1
Secondary accession number(s): Q7M445
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: May 24, 2005
Last modified: April 25, 2018
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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