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Protein

Mitogen-activated protein kinase MKC1

Gene

MKC1

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei74ATPPROSITE-ProRule annotation1
Active sitei174Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 42ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle
LigandATP-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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863341 – 501Mitogen-activated protein kinase MKC1Add BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei211PhosphothreonineBy similarity1
Modified residuei213PhosphotyrosineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP43068

Structurei

3D structure databases

ProteinModelPortaliP43068
SMRiP43068
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 339Protein kinasePROSITE-ProRule annotationAdd BLAST312

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi211 – 213TXY3

Domaini

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

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008352 MAPK_p38-like
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PRINTSiPR01773 P38MAPKINASE
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

P43068-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQQEAPIYY GRSVNKVYNQ EFIIDSRFKI VKELGHGAYG IVCSAKYDNG
60 70 80 90 100
SKKVPDSNNG NASSSANASF VAIKKITNIF SKNILCKRAL RELKLLQFFR
110 120 130 140 150
GHKNITCLYD LDIIPNPMTG EFNEIYLYEE LMECDMHQII RSGQPLSDQH
160 170 180 190 200
YQSFIYQVLC GLNFIHSADV LHRDLKPGNL LVNADCELKI CDFGLARGFS
210 220 230 240 250
ENPDENAGFM TEYVATRWYR APEIMLSFTN YTKAIDIWSV GCILAELLGG
260 270 280 290 300
KPLFRGKDYV DQLNQILMIL GTPPESTLQR IGSHRAQNYV RSLPITRKAS
310 320 330 340 350
YEELFPDANP LALDLLERML TLDPRERITV RDALNHKYLE LWHDPKEEIE
360 370 380 390 400
CQVKFDFKSF ETVDGLDEMK QLIMDEVQKF REFVRKPIEE QQRIQMQLHM
410 420 430 440 450
QKREEQRQEE EEKELLEQQR QFPAQESMDI SQTPYNNLET NIGTPQVEDD
460 470 480 490 500
YPRPQELDEF TFSNLESSSS MNLFQDMAKP SGEEYIKLEE ELGFGLDWCY

V
Length:501
Mass (Da):58,192
Last modified:November 1, 1995 - v1
Checksum:i0EA9F8B6CB97AB07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76708 Genomic DNA Translation: CAA54129.1

Similar proteinsi

Entry informationi

Entry nameiMKC1_CANAX
AccessioniPrimary (citable) accession number: P43068
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health