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Protein

Mitogen-activated protein kinase homolog MMK2

Gene

MMK2

Organism
Medicago sativa (Alfalfa)
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)DescriptionActionsGraphical viewLength
Binding sitei66ATPPROSITE-ProRule annotation1
Active sitei163Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 51ATPPROSITE-ProRule annotation9

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 3078.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase homolog MMK2 (EC:2.7.11.24)
Gene namesi
Name:MMK2
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863181 – 371Mitogen-activated protein kinase homolog MMK2Add BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei195PhosphothreonineBy similarity1
Modified residuei197PhosphotyrosineBy similarity1

Post-translational modificationi

Dually phosphorylated on Thr-195 and Tyr-197, which activates the enzyme (By similarity). Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ40353.

Structurei

3D structure databases

ProteinModelPortaliQ40353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 323Protein kinasePROSITE-ProRule annotationAdd BLAST287

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi195 – 197TXY3

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.
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.

Q40353-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVESAENNI RGVPTHGGRY LQYNIYGNLF EVSRKYVPPI RSVGRGAYGI
60 70 80 90 100
VCAAVNAETR EEVAIKKIGN AFDNRIDAKR TLREIKLLRH MDHENVMSIK
110 120 130 140 150
DIIRPPQKEN FNHVYIVSEL MDTDLHQIIR SNQPMTDDHC RYFVYQLLRG
160 170 180 190 200
LKYVHSANVL HRDLKPSNLL LNANCDLKIG DFGLARTTSE TDFMTEYVVT
210 220 230 240 250
RWYRAPELLL NCSDYTAAID IWSVGCILGE IVTRQPLFPG RDYVHQLRLV
260 270 280 290 300
TELIGSPDDA SLGFLRSENA RRYVRQLPQY PKQNFSARFP NMSPGAVDLL
310 320 330 340 350
EKMLIFDPSK RIKVDEALCH PYMAPLHDIN EEPVCARPFS FDFEEPMFTE
360 370
EDIKELIWKE SVRFNPDPPI N
Length:371
Mass (Da):42,794
Last modified:November 1, 1996 - v1
Checksum:i1903E2D43158A4EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82268 mRNA. Translation: CAA57719.1.
PIRiS60121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82268 mRNA. Translation: CAA57719.1.
PIRiS60121.

3D structure databases

ProteinModelPortaliQ40353.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ40353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.7.11.24. 3078.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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...

Entry informationi

Entry nameiMMK2_MEDSA
AccessioniPrimary (citable) accession number: Q40353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.