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Protein

Mitogen-activated protein kinase 16

Gene

MPK16

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: TAIR

GO - Biological processi

  • MAPK cascade Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G19010-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 16 (EC:2.7.11.24)
Short name:
AtMPK16
Short name:
MAP kinase 16
Gene namesi
Name:MPK16
Ordered Locus Names:At5g19010
ORF Names:T16G12.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G19010.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Mitogen-activated protein kinase 16PRO_0000245816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei187 – 1871PhosphothreonineBy similarity
Modified residuei189 – 1891PhosphotyrosineBy similarity
Modified residuei192 – 1921PhosphothreonineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-187 and Tyr-189, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8W4J2.
PRIDEiQ8W4J2.

Interactioni

Protein-protein interaction databases

BioGridi17295. 1 interaction.
IntActiQ8W4J2. 1 interaction.
STRINGi3702.AT5G19010.1.

Structurei

3D structure databases

ProteinModelPortaliQ8W4J2.
SMRiQ8W4J2. Positions 11-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 316292Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi187 – 1893TXY

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

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiQ8W4J2.
OMAiSHKFPHA.
PhylomeDBiQ8W4J2.

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.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8W4J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPDHRKKSS VEVDFFTEYG EGSRYRIEEV IGKGSYGVVC SAYDTHTGEK
60 70 80 90 100
VAIKKINDIF EHVSDATRIL REIKLLRLLR HPDIVEIKHI LLPPSRREFR
110 120 130 140 150
DIYVVFELME SDLHQVIKAN DDLTPEHYQF FLYQLLRGLK YIHTANVFHR
160 170 180 190 200
DLKPKNILAN ADCKLKICDF GLARVAFNDT PTAIFWTDYV ATRWYRAPEL
210 220 230 240 250
CGSFFSKYTP AIDIWSIGCI FAELLTGKPL FPGKNVVHQL DLMTDMLGTP
260 270 280 290 300
SAEAIGRVRN EKARRYLSSM RKKKPIPFSH KFPHTDPLAL RLLEKMLSFE
310 320 330 340 350
PKDRPTAEEA LADVYFKGLA KVEREPSAQP VTKLEFEFER RRITKEDVRE
360 370 380 390 400
LIYRESLEYH PKMLKEYLDG SEPTNFMYPS AVEHFKKQFA YLEEHYKNGT
410 420 430 440 450
SHNPPERQQH ASLPRACVLY SDNNHPVAQQ SSAEVTDGLS KCSIRDERPR
460 470 480 490 500
GADRNAQMPM SRIPINVPQT IQGAAVARPG KVVGSVLRYN NCGAATGVEA
510 520 530 540 550
LEQQQRRMVR NPAAASQYPK RTQPCKSNRG DEDCATAAEG PSRLKPNTQY
560
IPQKVSAAQD TAMSRWY
Length:567
Mass (Da):64,912
Last modified:September 5, 2006 - v2
Checksum:iF6D817F558EFCC33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971K → R in AAL32607 (PubMed:14593172).Curated
Sequence conflicti397 – 3971K → R in AAN15447 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC068809 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92639.1.
AY062529 mRNA. Translation: AAL32607.1.
BT000128 mRNA. Translation: AAN15447.1.
RefSeqiNP_197402.1. NM_121906.3.
UniGeneiAt.19792.
At.20179.

Genome annotation databases

EnsemblPlantsiAT5G19010.1; AT5G19010.1; AT5G19010.
GeneIDi832019.
KEGGiath:AT5G19010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC068809 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92639.1.
AY062529 mRNA. Translation: AAL32607.1.
BT000128 mRNA. Translation: AAN15447.1.
RefSeqiNP_197402.1. NM_121906.3.
UniGeneiAt.19792.
At.20179.

3D structure databases

ProteinModelPortaliQ8W4J2.
SMRiQ8W4J2. Positions 11-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17295. 1 interaction.
IntActiQ8W4J2. 1 interaction.
STRINGi3702.AT5G19010.1.

Proteomic databases

PaxDbiQ8W4J2.
PRIDEiQ8W4J2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G19010.1; AT5G19010.1; AT5G19010.
GeneIDi832019.
KEGGiath:AT5G19010.

Organism-specific databases

GeneFarmi1568. 89.
TAIRiAT5G19010.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiQ8W4J2.
OMAiSHKFPHA.
PhylomeDBiQ8W4J2.

Enzyme and pathway databases

BioCyciARA:AT5G19010-MONOMER.

Miscellaneous databases

PROiQ8W4J2.

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.
[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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
    , 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].
    Strain: cv. Columbia.
  4. "Mitogen-activated protein kinase cascades in plants: a new nomenclature."
    MAPK group
    Trends Plant Sci. 7:301-308(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  5. Cited for: GENE FAMILY.

Entry informationi

Entry nameiMPK16_ARATH
AccessioniPrimary (citable) accession number: Q8W4J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: September 5, 2006
Last modified: June 24, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.