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Q5A1D3 (ERK1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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 1

Short name=ERK1
EC=2.7.11.24
Alternative name(s):
MAP kinase 1
Short name=MAPK 1
Gene names
Name:CEK1
Synonyms:ERK1
ORF Names:CaO19.10404, CaO19.2886
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Post-translational modification

Dually phosphorylated on Thr-231 and Tyr-233, which activates the enzyme By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence EAK96519.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAK96578.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from genetic interaction PubMed 9596738. Source: CGD

cellular response to drug

Inferred from mutant phenotype PubMed 16304189PubMed 17604452PubMed 20140194. Source: CGD

cellular response to heat

Inferred from mutant phenotype PubMed 9493378. Source: CGD

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 16079350. Source: CGD

cellular response to reactive oxygen species

Inferred from mutant phenotype PubMed 16179009. Source: CGD

cellular response to starvation

Inferred from mutant phenotype PubMed 12773383PubMed 9398674PubMed 9596738. Source: CGD

filamentous growth

Inferred from mutant phenotype PubMed 12773383PubMed 15800048PubMed 9398674PubMed 9596738. Source: CGD

filamentous growth of a population of unicellular organisms

Inferred from genetic interaction PubMed 9596738. Source: CGD

filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype PubMed 12773383PubMed 9596738. Source: CGD

filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype PubMed 12773383PubMed 9398674PubMed 9493378PubMed 9596738. Source: CGD

fungal-type cell wall biogenesis

Inferred from mutant phenotype PubMed 19563901. Source: CGD

fungal-type cell wall organization

Inferred from mutant phenotype PubMed 16467475PubMed 9493378. Source: CGD

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

parasexual conjugation with cellular fusion

Inferred from mutant phenotype PubMed 12453219. Source: CGD

pathogenesis

Inferred from mutant phenotype PubMed 12381467PubMed 16179009PubMed 24363364PubMed 9009353PubMed 9596738PubMed 9741091. Source: CGD

positive regulation of filamentous growth of a population of unicellular organisms

Inferred from genetic interaction PubMed 9596738. Source: CGD

positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype PubMed 9596738. Source: CGD

positive regulation of filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype PubMed 9398674PubMed 9493378PubMed 9596738. Source: CGD

protein phosphorylation

Inferred from genetic interaction PubMed 7891715. Source: CGD

regulation of single-species biofilm formation on inanimate substrate

Inferred from mutant phenotype PubMed 15800048. Source: CGD

retrograde transport, endosome to Golgi

Inferred from mutant phenotype PubMed 24363364. Source: CGD

signal transduction

Inferred from genetic interaction PubMed 7891715. Source: CGD

single-species biofilm formation on inanimate substrate

Inferred from mutant phenotype PubMed 15800048. Source: CGD

stress-activated protein kinase signaling cascade

Inferred from expression pattern PubMed 15800048. Source: CGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from genetic interaction PubMed 12075459PubMed 7891715. Source: CGD

protein binding

Inferred from physical interaction PubMed 23953117. Source: IntAct

protein kinase activity

Inferred from sequence or structural similarity PubMed 1409649. Source: CGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STE5P329172EBI-8783371,EBI-18373From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Extracellular signal-regulated kinase 1
PRO_0000186325

Regions

Domain71 – 376306Protein kinase
Nucleotide binding77 – 859ATP By similarity
Motif231 – 2333TXY
Compositional bias5 – 5349Ala/Gln-rich

Sites

Active site1951Proton acceptor By similarity
Binding site1001ATP By similarity

Amino acid modifications

Modified residue2311Phosphothreonine By similarity
Modified residue2331Phosphotyrosine By similarity

Natural variations

Natural variant32 – 354Missing in strain: ATCC 60193 / S-24; in allele 237 B.
Natural variant331Q → QA in strain: R-2617; in allele 249 D.
Natural variant34 – 352QQ → AQAQA in strain: R-2805; in allele 255 A.
Natural variant341Q → A in strain: R-2617, R-2624, R-2777 and R-2805; in allele 246 D, 249 E, 249 C and 246 E.
Natural variant38 – 436Missing in strain: ATCC 36232; in allele 225 A.
Natural variant38 – 414Missing in strain: R-2621; in allele 237 A.
Natural variant411Q → QQ in strain: R-2621; in allele 249 B.
Natural variant411Missing in strain: R-2540; in allele 243 A.
Natural variant521A → T in strain: R-2617; in allele 246 D.

Sequences

Sequence LengthMass (Da)Tools
Q5A1D3 [UniParc].

Last modified October 19, 2011. Version 2.
Checksum: 471BE4423FDAAAD5

FASTA42248,623
        10         20         30         40         50         60 
MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQQQQ QAAAAAAAAN AAATTSSSSP 

        70         80         90        100        110        120 
RQVSFNVSDH YQILEIVGEG AYGIVCSAIH KPSQQKVAIK KIEPFERSML CLRTLRELKL 

       130        140        150        160        170        180 
LKHFNHENII SILAIQRPIN YESFNEIYLI QELMETDLHR VIRTQNLSDD HIQYFIYQTL 

       190        200        210        220        230        240 
RALKAMHSAN VLHRDLKPSN LLLNSNCDLK ICDFGLARSI ASQEDNYGFM TEYVATRWYR 

       250        260        270        280        290        300 
APEIMLTFQE YTTAIDVWSV GCILAEMLSG RPLFPGRDYH NQLWLIMEVL GTPNMEDYYN 

       310        320        330        340        350        360 
IKSKRAREYI RSLPFCKKIP FSELFANTNN NTSTSTSNTG GRTNINPLAL DLLEKLLIFN 

       370        380        390        400        410        420 
PAKRITVEDA LKHPYLQLYH DPNDEPISDK IPEDFFDFDK MKDQLTIEDL KKLLYEEIMK 


PL 

« Hide

References

« Hide 'large scale' references
[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[2]"Sequence analysis of a compound coding-region microsatellite in Candida albicans resolves homoplasies and provides a high-resolution tool for genotyping."
Metzgar D., Field D., Haubrich R., Wills C.
FEMS Immunol. Med. Microbiol. 20:103-109(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
Strain: ATCC 36232, ATCC 60193 / S-24, R-2436, R-2535, R-2540, R-2607, R-2617, R-2621, R-2624, R-2777 and R-2805.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000084 Genomic DNA. Translation: EAK96519.1. Different initiation.
AACQ01000083 Genomic DNA. Translation: EAK96578.1. Different initiation.
U95784 Genomic DNA. Translation: AAB88588.1.
U95785 Genomic DNA. Translation: AAB88589.1.
U95786 Genomic DNA. Translation: AAB88590.1.
U95787 Genomic DNA. Translation: AAB88591.1.
U95788 Genomic DNA. Translation: AAB88592.1.
U95789 Genomic DNA. Translation: AAB88593.1.
U95790 Genomic DNA. Translation: AAB88594.1.
U95791 Genomic DNA. Translation: AAB88595.1.
U95792 Genomic DNA. Translation: AAB88596.1.
U95793 Genomic DNA. Translation: AAB88597.1.
U95794 Genomic DNA. Translation: AAB88598.1.
U95795 Genomic DNA. Translation: AAB88599.1.
U95796 Genomic DNA. Translation: AAB88600.1.
U95797 Genomic DNA. Translation: AAB88601.1.
U95798 Genomic DNA. Translation: AAB88602.1.
RefSeqXP_715542.1. XM_710449.1.
XP_715598.1. XM_710505.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1225883. 5 interactions.
IntActQ5A1D3. 2 interactions.
STRING5476.CAL0005224.

Proteomic databases

PRIDEQ5A1D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3642743.
3642789.
KEGGcal:CaO19.10404.
cal:CaO19.2886.

Organism-specific databases

CGDCAL0005224. CEK1.

Phylogenomic databases

eggNOGCOG0515.
KOK04371.
OrthoDBEOG7K3TWD.

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...

Entry information

Entry nameERK1_CANAL
AccessionPrimary (citable) accession number: Q5A1D3
Secondary accession number(s): O13435 expand/collapse secondary AC list , P28869, P87079, P87080, P87081, P87082, P87083, P87084, P87085, P87086, P87322, Q6LC13
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Candida albicans

Candida albicans: entries and gene names