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P43068

- MKC1_CANAX

UniProt

P43068 - MKC1_CANAX

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Protein

Mitogen-activated protein kinase MKC1

Gene
MKC1
Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 sitei74 – 741ATP By similarity
Active sitei174 – 1741Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase MKC1 (EC:2.7.11.24)
Short name:
MAP kinase MKC1
Gene namesi
Name:MKC1
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Mitogen-activated protein kinase MKC1PRO_0000186334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111Phosphothreonine By similarity
Modified residuei213 – 2131Phosphotyrosine By similarity

Post-translational modificationi

Dually phosphorylated on Thr-211 and Tyr-213, which activates the enzyme By similarity.

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliP43068.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 339312Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi211 – 2133TXY

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43068-1 [UniParc]FASTAAdd to Basket

« Hide

MDQQEAPIYY GRSVNKVYNQ EFIIDSRFKI VKELGHGAYG IVCSAKYDNG    50
SKKVPDSNNG NASSSANASF VAIKKITNIF SKNILCKRAL RELKLLQFFR 100
GHKNITCLYD LDIIPNPMTG EFNEIYLYEE LMECDMHQII RSGQPLSDQH 150
YQSFIYQVLC GLNFIHSADV LHRDLKPGNL LVNADCELKI CDFGLARGFS 200
ENPDENAGFM TEYVATRWYR APEIMLSFTN YTKAIDIWSV GCILAELLGG 250
KPLFRGKDYV DQLNQILMIL GTPPESTLQR IGSHRAQNYV RSLPITRKAS 300
YEELFPDANP LALDLLERML TLDPRERITV RDALNHKYLE LWHDPKEEIE 350
CQVKFDFKSF ETVDGLDEMK QLIMDEVQKF REFVRKPIEE QQRIQMQLHM 400
QKREEQRQEE EEKELLEQQR QFPAQESMDI SQTPYNNLET NIGTPQVEDD 450
YPRPQELDEF TFSNLESSSS MNLFQDMAKP SGEEYIKLEE ELGFGLDWCY 500
V 501
Length:501
Mass (Da):58,192
Last modified:November 1, 1995 - v1
Checksum:i0EA9F8B6CB97AB07
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76708 Genomic DNA. Translation: CAA54129.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76708 Genomic DNA. Translation: CAA54129.1 .

3D structure databases

ProteinModelPortali P43068.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0515.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Functional characterization of the MKC1 gene of Candida albicans, which encodes a mitogen-activated protein kinase homolog related to cell integrity."
    Navarro-Garcia F., Sanchez M., Pla J., Nombela C.
    Mol. Cell. Biol. 15:2197-2206(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 64385 / 1001.

Entry informationi

Entry nameiMKC1_CANAX
AccessioniPrimary (citable) accession number: P43068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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