Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitogen-activated protein kinase homolog D5

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATPPROSITE-ProRule annotation
Active sitei188 – 1881Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 769ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 4872.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase homolog D5 (EC:2.7.11.24)
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Mitogen-activated protein kinase homolog D5PRO_0000186319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201PhosphothreonineBy similarity
Modified residuei222 – 2221PhosphotyrosineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-220 and Tyr-222, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ06060.

Expressioni

Tissue specificityi

Leaves, roots, root apices, and dormant and growing axillary buds.

Structurei

3D structure databases

ProteinModelPortaliQ06060.
SMRiQ06060. Positions 51-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 347286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi220 – 2223TXY

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

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.
IPR008271. Ser/Thr_kinase_AS.
[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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06060-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGGGGAPAA DAVMEDAAPQ QQEPQQQAAM GIENIPATLS HGGRFIQYNI
60 70 80 90 100
FGNIFEVTAK YRPPIMPIGK GAYGIVCSAH NSETNEHVAV KKIANAFDNK
110 120 130 140 150
IDAKRTLREI KLVRHMDHEN VVAIRDIVPP PQREVFNDVY IAYELMDTDL
160 170 180 190 200
HQIIRSNQAL SEEHCQYFLY QILRGLKYIH SANVLHRDLK PSNLLLNANC
210 220 230 240 250
DLKICDFGLA RVTSETDFMT EYVVTRWYRA PELLLNSSDY TAAIDVWSVG
260 270 280 290 300
CIFMELMDRK PLFPGRDHVH QLRLLMELIG TPSEADLGFL NENAKRYIRQ
310 320 330 340 350
LPLYRRQSFQ EKFPHVHPEA IDLVEKMLTF DPRQRITVEN ALAHPYLTSL
360 370 380 390
HDISDEPVCT TPFSFDFEQH ALTEEQMKEL IYREALAFNP EYQQ
Length:394
Mass (Da):45,145
Last modified:October 1, 1994 - v1
Checksum:iE7B4758EBD8F24A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70703 mRNA. Translation: CAA50036.1.
PIRiS33635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70703 mRNA. Translation: CAA50036.1.
PIRiS33635.

3D structure databases

ProteinModelPortaliQ06060.
SMRiQ06060. Positions 51-394.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ06060.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.7.11.24. 4872.

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.
IPR008271. Ser/Thr_kinase_AS.
[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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of a MAP kinase homologue from pea."
    Stafstrom J.P., Altschuler M., Anderson D.H.
    Plant Mol. Biol. 22:83-90(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Alaska.
    Tissue: Seedling.

Entry informationi

Entry nameiMPK_PEA
AccessioniPrimary (citable) accession number: Q06060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 24, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1, Met-14 or Met-30 is the initiator.Curated

Documents

  1. 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.