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Q5A1D3

- ERK1_CANAL

UniProt

Q5A1D3 - ERK1_CANAL

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Protein
Extracellular signal-regulated kinase 1
Gene
CEK1, ERK1, CaO19.10404, CaO19.2886
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001ATP By similarity
Active sitei195 – 1951Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 859ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: CGD
  3. protein binding Source: IntAct
  4. protein kinase activity Source: CGD

GO - Biological processi

  1. MAPK cascade Source: CGD
  2. cellular response to drug Source: CGD
  3. cellular response to heat Source: CGD
  4. cellular response to oxidative stress Source: CGD
  5. cellular response to reactive oxygen species Source: CGD
  6. cellular response to starvation Source: CGD
  7. filamentous growth Source: CGD
  8. filamentous growth of a population of unicellular organisms Source: CGD
  9. filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
  10. filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
  11. fungal-type cell wall biogenesis Source: CGD
  12. fungal-type cell wall organization Source: CGD
  13. mitotic nuclear division Source: UniProtKB-KW
  14. parasexual conjugation with cellular fusion Source: CGD
  15. pathogenesis Source: CGD
  16. positive regulation of filamentous growth of a population of unicellular organisms Source: CGD
  17. positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
  18. positive regulation of filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
  19. protein phosphorylation Source: CGD
  20. regulation of single-species biofilm formation on inanimate substrate Source: CGD
  21. retrograde transport, endosome to Golgi Source: CGD
  22. signal transduction Source: CGD
  23. single-species biofilm formation on inanimate substrate Source: CGD
  24. stress-activated protein kinase signaling cascade Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular signal-regulated kinase 1 (EC:2.7.11.24)
Short name:
ERK1
Alternative name(s):
MAP kinase 1
Short name:
MAPK 1
Gene namesi
Name:CEK1
Synonyms:ERK1
ORF Names:CaO19.10404, CaO19.2886
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0005224. CEK1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Extracellular signal-regulated kinase 1
PRO_0000186325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311Phosphothreonine By similarity
Modified residuei233 – 2331Phosphotyrosine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5A1D3.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
STE5P329172EBI-8783371,EBI-18373From a different organism.

Protein-protein interaction databases

BioGridi1225883. 5 interactions.
IntActiQ5A1D3. 2 interactions.
STRINGi5476.CAL0005224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 376306Protein kinase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi231 – 2333TXY

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 5349Ala/Gln-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
KOiK04371.
OrthoDBiEOG7K3TWD.

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_dom.
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.

Q5A1D3-1 [UniParc]FASTAAdd to Basket

« Hide

MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQQQQ QAAAAAAAAN    50
AAATTSSSSP RQVSFNVSDH YQILEIVGEG AYGIVCSAIH KPSQQKVAIK 100
KIEPFERSML CLRTLRELKL LKHFNHENII SILAIQRPIN YESFNEIYLI 150
QELMETDLHR VIRTQNLSDD HIQYFIYQTL RALKAMHSAN VLHRDLKPSN 200
LLLNSNCDLK ICDFGLARSI ASQEDNYGFM TEYVATRWYR APEIMLTFQE 250
YTTAIDVWSV GCILAEMLSG RPLFPGRDYH NQLWLIMEVL GTPNMEDYYN 300
IKSKRAREYI RSLPFCKKIP FSELFANTNN NTSTSTSNTG GRTNINPLAL 350
DLLEKLLIFN PAKRITVEDA LKHPYLQLYH DPNDEPISDK IPEDFFDFDK 400
MKDQLTIEDL KKLLYEEIMK PL 422
Length:422
Mass (Da):48,623
Last modified:October 19, 2011 - v2
Checksum:i471BE4423FDAAAD5
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 354Missing in strain: ATCC 60193 / S-24; in allele 237 B.
Natural varianti33 – 331Q → QA in strain: R-2617; in allele 249 D.
Natural varianti34 – 352QQ → AQAQA in strain: R-2805; in allele 255 A.
Natural varianti34 – 341Q → A in strain: R-2617, R-2624, R-2777 and R-2805; in allele 246 D, 249 E, 249 C and 246 E.
Natural varianti38 – 436Missing in strain: ATCC 36232; in allele 225 A.
Natural varianti38 – 414Missing in strain: R-2621; in allele 237 A.
Natural varianti41 – 411Q → QQ in strain: R-2621; in allele 249 B.
Natural varianti41 – 411Missing in strain: R-2540; in allele 243 A.
Natural varianti52 – 521A → T in strain: R-2617; in allele 246 D.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiXP_715542.1. XM_710449.1.
XP_715598.1. XM_710505.1.

Genome annotation databases

GeneIDi3642743.
3642789.
KEGGical:CaO19.10404.
cal:CaO19.2886.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi XP_715542.1. XM_710449.1.
XP_715598.1. XM_710505.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1225883. 5 interactions.
IntActi Q5A1D3. 2 interactions.
STRINGi 5476.CAL0005224.

Proteomic databases

PRIDEi Q5A1D3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3642743.
3642789.
KEGGi cal:CaO19.10404.
cal:CaO19.2886.

Organism-specific databases

CGDi CAL0005224. CEK1.

Phylogenomic databases

eggNOGi COG0515.
KOi K04371.
OrthoDBi EOG7K3TWD.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiERK1_CANAL
AccessioniPrimary (citable) accession number: Q5A1D3
Secondary accession number(s): O13435
, P28869, P87079, P87080, P87081, P87082, P87083, P87084, P87085, P87086, P87322, Q6LC13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: September 3, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi