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Reviewed, UniProtKB/Swiss-Prot Q54R82 (MKKA_DICDI)

Last modified February 9, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase kinase kinase A
    EC=2.7.11.25
Alternative name(s):
    MAPK/ERK kinase 1
      Short name=MEK kinase 1
      Short name=MEKK 1
    MAPK/ERK kinase A
      Short name=MEK kinase A
      Short name=MEKK A
      Short name=MEKKalpha
Gene names
Name: mkkA
ORF Names: DDB_G0283265
OrganismDictyostelium discoideum (Slime mold) [Complete proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Regulates cell-type differentiation and spatial patterning, required for the proper induction and maintenance of prespore cell differentiation. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q869N2

Cofactor

Magnesium By similarity. UniProtKB Q869N2

Subunit structure

Interacts with ubcB and ubpB. Ref.1

Subcellular location

Membrane; Single-pass membrane protein Potential. Note: Localized predominantly at the periphery of the cells, possibly in the cortex or the plasma membrane. Ref.1

Post-translational modification

ubcB and ubpB differentially control ubiquitination/deubiquitination and degradation in a cell-type-specific and temporally regulated manner.

Disruption phenotype

Cells develop precociously and exhibit abnormal cell-type patterning with an increase in the pstO prestalk compartment, a concomitant reduction in the prespore domain, and a loss of the sharp compartment boundaries, resulting in overlapping prestalk and prespore domains. Ref.1

Sequence similarities

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

Contains 1 F-box domain.

Contains 1 OPR domain.

Contains 1 protein kinase domain.

Contains 7 WD repeats.

Sequence caution

The sequence EAL65773.2 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 942942Mitogen-activated protein kinase kinase kinase A
PRO_0000371250

Regions

Transmembrane513 – 53321 Potential
Domain15 – 10187OPR
Domain170 – 429260Protein kinase
Domain518 – 56447F-box
Repeat607 – 64640WD 1
Repeat690 – 73344WD 2
Repeat736 – 77843WD 3
Repeat780 – 82546WD 4
Repeat828 – 86538WD 5
Repeat872 – 90938WD 6
Repeat912 – 94231WD 7
Nucleotide binding176 – 1849ATP By similarity UniProtKB P28523
Compositional bias121 – 14424Poly-Asn
Compositional bias449 – 46113Poly-Thr
Compositional bias471 – 4799Poly-Gln
Compositional bias504 – 51310Poly-Ser

Sites

Active site2971Proton acceptor By similarity UniProtKB P28523
Binding site1991ATP By similarity UniProtKB P28523

Sequences

Sequence LengthMass (Da)Tools
Q54R82-1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: C9E4928A8C7C68F7

FASTA942105,796
        10         20         30         40         50         60 
MSWLNNPSQN FVDPFIRIKC ILGDDIRIIK FNSNISYGGL MNQLEQDFQC PISIHQYEDY 

        70         80         90        100        110        120 
EGDKVTVKSK DDIMEALTMY FELKALNPTK IISTKFFLKQ LPPQSQPLSS SLSPTQSLIL 

       130        140        150        160        170        180 
NNNNNNNNNN NNNNNNNNNN NNNNIIQHTD FPSLIINEHE ELISNHNIKW QKGQILGRGG 

       190        200        210        220        230        240 
YGSVYLGLNK DTGELFAVKQ LEIVDINSDP KLKNMILSFS KEIEVMRSLR HDNIVRYLGT 

       250        260        270        280        290        300 
SLDQSFLSVF LEYIPGGSIS SLLGKFGAFS ENVIKVYTKQ ILQGLSFLHA NSIIHRDIKG 

       310        320        330        340        350        360 
ANILIDTKGI VKLSDFGCSK SFSGIVSQFK SMQGTPYWMA PEVIKQTGHG RSSDIWSLGC 

       370        380        390        400        410        420 
VIVEMATAQP PWSNITELAA VMYHIASSNS IPNIPSHMSQ EAFDFLNLCF KRDPKERPDA 

       430        440        450        460        470        480 
NQLLKHPFIM NLDDNIQLPT ISPTTTLSTN TTNTTATTTT TNNATNSNIN QQQQQQQQQP 

       490        500        510        520        530        540 
PTRTQRVSIS AGSSNNKRYT PPISTSTSSS SSSILNNFSI NIILPINLII LIFREIKPNF 

       550        560        570        580        590        600 
VNTLSRVCKH WKQIIDDDEL WNKYCSDRLI NKSKFEESIT WKSNYIKIYK QQKVWFHNKL 

       610        620        630        640        650        660 
NHSTLKGHDK GVFCVKLIDD QGMVLSGGED KKLKVWDISG NHHHNHHSGI VGSISKKSGL 

       670        680        690        700        710        720 
NIINNNNSNN SNSSSNSSSS NSRYLFSLKG HSGCIKSVDY QRQSGSDVSR VFTASADFTC 

       730        740        750        760        770        780 
KIFSLKTKKT LFTYTNHQEA VTCINYLGDV ENKCITSSLD KTIQLWDAET GSCLSTLRGH 

       790        800        810        820        830        840 
TGGIYCVKTD QVATHGNGYN HLVVSASVDK TSNVWDTRSS SKVRSFTQHT EDVLCCYVFD 

       850        860        870        880        890        900 
QKVVTGSCDG TIKLWDIGTG KTISTFIPSE TRQKNYVWTV QFDQSKIISS GKTGIIRIWD 

       910        920        930        940 
IYNERDSRSI GGHHETIFSL QFNNQKLITG SLDKLVKIWS ID 

« Hide

References

« Hide 'large scale' references
[1]"A novel, putative MEK kinase controls developmental timing and spatial patterning in Dictyostelium and is regulated by ubiquitin-mediated protein degradation."
Chung C.Y., Reddy T.B.K., Zhou K., Firtel R.A.
Genes Dev. 12:3564-3578(1998) [PubMed: 9832508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH UBC AND UPC, SUBCELLULAR LOCATION, UBIQUITINATION, DISRUPTION PHENOTYPE.
Strain: AX3-1.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed: 15875012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF093689 mRNA. Translation: AAC97114.1.
AAFI02000052 Genomic DNA. Translation: EAL65773.2. Sequence problems.
RefSeqXP_639165.2.

3D structure databases

HSSPHSSP built from PDB template 2CLQ based on UniProtKB Q99683.
SMRQ54R82. Positions 170-429.
ModBaseSearch...

Genome annotation databases

GeneID8624035.
KEGGddi:DDB_0220118.

Organism-specific databases

dictyBaseDDB_G0283265. mkkA.

Phylogenomic databases

eggNOGKOG0274.
InParanoidQ54R82.
PhylomeDBQ54R82.

Family and domain databases

InterProIPR001810. F-box.
IPR020472. G-protein_beta_WD-40_rep_reg.
IPR011009. Kinase-like_dom.
IPR015748. MAPKKK3.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019782. WD40_repeat_2.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR019781. WD40_repeat_sg.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PANTHERPTHR22986:SF64. MAPKKK3. 1 hit.
PfamPF00646. F-box. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00256. FBOX. 1 hit.
SM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
PROSITEPS50181. FBOX. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMKKA_DICDI
AccessionPrimary (citable) accession number: Q54R82
Secondary accession number(s): O96611
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: February 9, 2010
This is version 36 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents