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P43294 (MHK_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase MHK

EC=2.7.11.22
Gene names
Name:MHK
Ordered Locus Names:At4g13020
ORF Names:F25G13.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a role in the regulation of plant growth and development.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Tissue specificity

Roots, leaves and stems.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P43294-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P43294-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MMVFVVFVMC → ME

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Serine/threonine-protein kinase MHK
PRO_0000086325

Regions

Domain12 – 291280Protein kinase
Nucleotide binding18 – 269ATP By similarity

Sites

Active site1331Proton acceptor By similarity
Binding site411ATP By similarity

Amino acid modifications

Modified residue1641Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 1010MMVFVVFVMC → ME in isoform Short.
VSP_004861

Experimental info

Sequence conflict661N → K in AAA18854. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: AF92A2233B673F0F

FASTA44350,896
        10         20         30         40         50         60 
MMVFVVFVMC RYKILEELGD GTCGSVYKAV NLETYEVVAV KKMKRKFYYW EECVNLREVK 

        70         80         90        100        110        120 
ALRKLNHPHI IKLKEIVREH NELFFIFECM DHNLYHIMKE RERPFSEGEI RSFMSQMLQG 

       130        140        150        160        170        180 
LAHMHKNGYF HRDLKPENLL VTNNILKIAD FGLAREVASM PPYTEYVSTR WYRAPEVLLQ 

       190        200        210        220        230        240 
SSLYTPAVDM WAVGAILAEL YALTPLFPGE SEIDQLYKIC CVLGKPDWTT FPEAKSISRI 

       250        260        270        280        290        300 
MSISHTEFPQ TRIADLLPNA APEAIDLINR LCSWDPLKRP TADEALNHPF FSMATQASYP 

       310        320        330        340        350        360 
IHDLELRLDN MAALPNLELN LWDFNREPEE CFLGLTLAVK PSAPKLEMLR NVSQDMSENF 

       370        380        390        400        410        420 
LFCPGVNNDR EPSVFWSLLS PDENGLHAPV ESSPLSLSFS PMQQHTVGPP QSSGFTMTSS 

       430        440 
MQPNMLDRPW MAVSAPFQQS HYL 

« Hide

Isoform Short [UniParc].

Checksum: E4837811577EB337
Show »

FASTA43549,968

References

« Hide 'large scale' references
[1]"Molecular cloning of two novel protein kinase genes from Arabidopsis thaliana."
Moran T.V., Walker J.C.
Biochim. Biophys. Acta 1216:9-14(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], ALTERNATIVE SPLICING.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07249 mRNA. Translation: AAA18854.1.
AL079349 Genomic DNA. Translation: CAB45501.1.
AL161535 Genomic DNA. Translation: CAB78344.1.
CP002687 Genomic DNA. Translation: AEE83214.1.
CP002687 Genomic DNA. Translation: AEE83215.1.
AF360324 mRNA. Translation: AAK26034.1.
AY056332 mRNA. Translation: AAL07181.1.
PIRC85140.
S38327.
RefSeqNP_193038.1. NM_117371.1. [P43294-1]
NP_849370.1. NM_179039.3. [P43294-2]
UniGeneAt.236.

3D structure databases

ProteinModelPortalP43294.
SMRP43294. Positions 11-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid12212. 1 interaction.
IntActP43294. 9 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G13020.2; AT4G13020.2; AT4G13020. [P43294-1]
GeneID826915.
KEGGath:AT4G13020.

Organism-specific databases

TAIRAT4G13020.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidP43294.
PhylomeDBP43294.

Enzyme and pathway databases

BioCycARA:AT4G13020-MONOMER.
ARA:GQT-448-MONOMER.
ARA:GQT-597-MONOMER.
ARA:GQT-598-MONOMER.
ARA:GQT-599-MONOMER.
BRENDA2.7.11.22. 399.

Gene expression databases

ArrayExpressP43294.
GenevestigatorP43294.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMHK_ARATH
AccessionPrimary (citable) accession number: P43294
Secondary accession number(s): Q9C5D4, Q9SV67
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 6, 2002
Last modified: May 14, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names