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Q54QB1 (ERK2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular signal-regulated kinase 2

Short name=ERK2
EC=2.7.11.24
Alternative name(s):
Defective in aggregation protein C
MAP kinase 2
Gene names
Name:erkB
Synonyms:dagC, erk2
ORF Names:DDB_G0283903
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation By similarity.

Domain

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

Post-translational modification

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

Disruption phenotype

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. Ref.3 Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gpaDP340422EBI-2905550,EBI-2905587

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Extracellular signal-regulated kinase 2
PRO_0000312369

Regions

Domain14 – 304291Protein kinase
Nucleotide binding20 – 289ATP By similarity
Motif176 – 1783TXY
Compositional bias345 – 3484Poly-Lys

Sites

Active site1371Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue1761Phosphothreonine By similarity
Modified residue1781Phosphotyrosine By similarity

Experimental info

Sequence conflict17 – 182LQ → FH in L33043. Ref.1
Sequence conflict301K → E in L33043. Ref.1
Sequence conflict36 – 383TKQ → PHH in L33043. Ref.1
Sequence conflict2851L → S in L33043. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q54QB1 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 3AB5C85E6F10722B

FASTA36941,978
        10         20         30         40         50         60 
MSSEDIDKHV LRKYEVLQKI GKGAYGIVWK AIDKKTKQTV ALKKIFDAFQ NATDAQRTFR 

        70         80         90        100        110        120 
EIMFLQELHG HENIIKLLNV IKADNDRDIY LVFEHMETDL HAVIRAKILE EIHKQYTIYQ 

       130        140        150        160        170        180 
LLKALKYMHS ANVLHRDIKP SNLLLNSECL VKVADFGLAR SITSLESIAE ANPVLTEYVA 

       190        200        210        220        230        240 
TRWYRAPEIL LGSTKYTKGV DMWSIGCILG ELLGEKAMFP GNSTMNQLDL IIEVTGRPSA 

       250        260        270        280        290        300 
EDIEAIKSPF AGTMLESLPP SNPRSLSDMY PSASVDALDL LKKLLQFNPD KRITAEEALA 

       310        320        330        340        350        360 
HPFVTQFHNP AEEPHFDRII KISIDDGQKF PIAEYRNRLY NDIIKKKKEE RKKQTNPTKP 


DTTAPTLST 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33043 mRNA. No translation available.
AAFI02000058 Genomic DNA. Translation: EAL65439.1.
PIRA56492.
RefSeqXP_638833.1. XM_633741.1.

3D structure databases

ProteinModelPortalQ54QB1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ54QB1. 1 interaction.
STRING44689.DDB_0191457.

Proteomic databases

PRIDEQ54QB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191457; DDB0191457; DDB_G0283903.
GeneID8624357.
KEGGddi:DDB_G0283903.

Organism-specific databases

dictyBaseDDB_G0283903. erkB.

Phylogenomic databases

eggNOGCOG0515.
OMASAEIESH.
PhylomeDBQ54QB1.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ54QB1.

Entry information

Entry nameERK2_DICDI
AccessionPrimary (citable) accession number: Q54QB1
Secondary accession number(s): Q7M445
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: May 24, 2005
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase