Reviewed, UniProtKB/Swiss-Prot Q54QB1 (ERK2_DICDI)

Names and origin

Protein names

Recommended 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

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chemotaxis Mitosis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Extracellular signal-regulated kinase 2		PRO_0000312369
Regions
	Domain	14 – 304	291	Protein kinase
	Nucleotide binding	20 – 28	9	ATP By similarity
	Motif	176 – 178	3	TXY
	Compositional bias	345 – 348	4	Poly-Lys
Sites
	Active site	137	1	Proton acceptor By similarity
	Binding site	43	1	ATP By similarity
Amino acid modifications
	Modified residue	176	1	Phosphothreonine By similarity
	Modified residue	178	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	17 – 18	2	LQ → FH in L33043. Ref.1
	Sequence conflict	30	1	K → E in L33043. Ref.1
	Sequence conflict	36 – 38	3	TKQ → PHH in L33043. Ref.1
	Sequence conflict	285	1	L → S in L33043. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54QB1-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 3AB5C85E6F10722B	FASTA	369	41,978
	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

References

	« Hide 'large scale' referencesShow '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: 7844154] [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: 15875012] [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: 9427685] [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: 18408056] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L33043 mRNA. No translation available. AAFI02000058 Genomic DNA. Translation: EAL65439.1.
PIR	A56492.
RefSeq	XP_638833.1.
3D structure databases
HSSP	HSSP built from PDB template 1OIQ based on UniProtKB P24941.
ModBase	Search...
Genome annotation databases
GeneID	3390365.
GenomeReviews	Gene locus erkB in contig CM000153_GR.
KEGG	ddi:DDB_0191457.
Organism-specific databases
dictyBase	DDB_G0283903. erkB.
Phylogenomic databases
OMA	VVIRANI.
Enzyme and pathway databases
BRENDA	2.7.11.24. 424.
Family and domain databases
InterPro	IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ERK2_DICDI

Accession

Primary (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:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)