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Protein

Extracellular signal-regulated kinase 1

Gene

CEK1

Organism
Candida albicans (strain WO-1) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951ATPPROSITE-ProRule annotation
Active sitei190 – 1901Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 809ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
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:CAWG_03179
OrganismiCandida albicans (strain WO-1) (Yeast)
Taxonomic identifieri294748 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000001429 Componenti: Chromosome 4, Supercontig 1.4

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Extracellular signal-regulated kinase 1PRO_0000413039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei226 – 2261PhosphothreonineBy similarity
Modified residuei228 – 2281PhosphotyrosineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-226 and Tyr-228, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliC4YGK0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 369304Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi226 – 2283TXY

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 4945Ala/Gln-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000233024.
OMAiHKPTNQK.
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.
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.

C4YGK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQAAA AAAAANAAAT
60 70 80 90 100
TSSSPRQVSF NVSDHYQILE IVGEGAYGIV CSAIHKPSQQ KVAIKKIEPF
110 120 130 140 150
ERSMLCLRTL RELKLLKHFN HENIISILAI QRPINYESFN EIYLIQELME
160 170 180 190 200
TDLHRVIRTQ NLSDDHIQYF IYQTLRALKA MHSANVLHRD LKPSNLLLNS
210 220 230 240 250
NCDLKICDFG LARSIASQED NYGFMTEYVA TRWYRAPEIM LTFQEYTTAI
260 270 280 290 300
DVWSVGCILA EMLSGRPLFP GRDYHNQLWL IMEVLGTPNM EDYYNIKSKR
310 320 330 340 350
AREYIRSLPF CKKIPFSELF ANTNNNTSTS NTGGRTNINP LALDLLEKLL
360 370 380 390 400
IFNPAKRITV EDALKHPYLQ LYHDPNDEPI SDKIPEDFFD FDKMKDQLTI
410
EDLKKLLYEE IMKPL
Length:415
Mass (Da):47,836
Last modified:July 28, 2009 - v1
Checksum:i572857CFD5B00B67
GO

Sequence cautioni

The sequence AAA34343.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → SS in AAA34343 (PubMed:1409649).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76585 Genomic DNA. Translation: AAA34343.2. Different initiation.
CH672349 Genomic DNA. Translation: EEQ44882.1.
PIRiA47211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76585 Genomic DNA. Translation: AAA34343.2. Different initiation.
CH672349 Genomic DNA. Translation: EEQ44882.1.
PIRiA47211.

3D structure databases

ProteinModelPortaliC4YGK0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000233024.
OMAiHKPTNQK.
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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dominant negative selection of heterologous genes: isolation of Candida albicans genes that interfere with Saccharomyces cerevisiae mating factor-induced cell cycle arrest."
    Whiteway M., Dignard D., Thomas D.Y.
    Proc. Natl. Acad. Sci. U.S.A. 89:9410-9414(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: WO-1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WO-1.

Entry informationi

Entry nameiERK1_CANAW
AccessioniPrimary (citable) accession number: C4YGK0
Secondary accession number(s): P28869
, P87079, P87080, P87081, P87082, P87083, P87084, P87085, P87086, P87322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: July 28, 2009
Last modified: February 4, 2015
This is version 39 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.