Any feedback?
Information on EC 2.7.12.1 - dual-specificity kinase and Organism(s) Arabidopsis thaliana and UniProt Accession P51566
for references in articles please use BRENDA:EC2.7.12.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.12.1 dual-specificity kinaseIUBMB Comments
This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
Specify your search results
Word Map
- 2.7.12.1
- alzheimer
-
dyrks
- autophosphorylation
- tau
- deficit
-
intellectual
- disability
- harmine
- neurodegenerative
-
neurogenesis
- microcephaly
-
trisomic
-
neurodevelopmental
-
ts65dn
- nfat
-
tyrosine-phosphorylated
-
neurofibrillary
-
hyperphosphorylation
-
autism
-
haploinsufficiency
-
tangle
-
cdc2-like
- biliverdin
-
kinome
- ck2
-
proline-directed
- medicine
-
euploid
- gli1
-
atp-competitive
- rcan1
- dscr1
- analysis
- diagnostics
- drug development
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
dyrk1a, dyrk2, dyrk1b, dyrk3, dual-specificity kinase, dyrk1, dual specificity kinase, dual-specificity tyrosine phosphorylation-regulated kinase 1a, dual-specificity protein kinase, dyrk1a kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Clik1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating)
This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
CAS REGISTRY NUMBER
COMMENTARY
134549-83-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + annexin 1
ADP + phospho-annexin 1
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 2
ADP + phospho-annexin 2
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 4
ADP + phospho-annexin 4
phosphorylation at tyrosine residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
phosphorylation at serine/threonine residues
-
-
?
additional information
?
-
the enzyme activates STE12-dependent processes in Saccharomyces cerevisiae
-
-
?
additional information
?
-
the enzyme activates STE12-dependent processes in Saccharomyces cerevisiae
-
-
?
additional information
?
-
the enzyme activates STE12-dependent processes in Saccharomyces cerevisiae
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Mg-chelatase and chlorophyll biosynthesis
-
-
?
additional information
?
-
substrate specificity, overview. No activity with Rubisco activase and chlorophyll A/B binding protein 3
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with Rubisco activase and chlorophyll A/B binding protein 3
-
-
?
additional information
?
-
-
the enzyme autophosphorylates on both serine/threonine and tyrosine residues
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + annexin 1
ADP + phospho-annexin 1
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 2
ADP + phospho-annexin 2
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 4
ADP + phospho-annexin 4
phosphorylation at tyrosine residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
phosphorylation at serine/threonine residues
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Mg-chelatase and chlorophyll biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
enzme Yak1 is a member of dual-specificity Tyr phosphorylation-regulated kinases (DYRKs) that are evolutionarily conserved
malfunction
-
a T-DNA insertion mutant of AtSARK shows significantly delayed senescence, while inducible overexpression of AtSARK in Arabidopsis thaliana causes precocious senescence and abnormal floral organ development. phenotypes of transgenic lines, overview
physiological function
physiological function
AtYak1 is a dual specificity protein kinase in Arabidopsis that may regulate the phosphorylation status of the annexin family proteins
physiological function
kinase YAK1 interacts with LIGHT-REGULATED WD1 (LWD1). YAK1 is an important regulator for various light responses, including the circadian clock, photomorphogenesis and reproductive development. AtYAK1 can antagonize the function of LIGHT-REGULATED WDs in regulating the circadian clock and photoperiodic flowering. YAK1 regulates light-induced period-length shortening and photomorphogenic development. YAK1 mediates plant fertility especially under inferior light conditions including low light and short-day length
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AFC1_ARATH
467
0
54198
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an universal stress induced protein associated domain, USPA, and a C-terminal GUN4 domain, the latter binds magnesium-protoporphyrin IX
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
the enzyme autophosphorylates on both serine/threonine and tyrosine residues
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
atyak1-1 (SAIL_31_C10) and atyak1-2 (SALK_0746) T-DNA insertion mutants
additional information
-
atyak1-1 (SAIL_31_C10) and atyak1-2 (SALK_0746) T-DNA insertion mutants
additional information
-
construction of a a T-DNA insertion mutant of AtSARK that shows significantly delayed senescence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtSARK, the gene gene consists of 11 exons, quantitative RT-PCR analysis, inducible overexpression of AtSARK in Arabidopsis thaliana causes precocious senescence and abnormal floral organ development
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mayer, K.; Schuller, C.; Wambutt, R.; Murphy, G.; et al.
Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana
Nature
402
769-777
1999
Arabidopsis thaliana (P51567), Arabidopsis thaliana (P51568)
Salanoubat, M.; Lemcke, K.; Rieger, M.; Ansorge, W.; Unseld, M.; et al.
Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana
Nature
408
820-822
2000
Arabidopsis thaliana (P51566)
Bender, J.; Fink, G.R.
AFC1, a LAMMER kinase from Arabidopsis thaliana, activates STE12-dependent processes in yeast
Proc. Natl. Acad. Sci. USA
91
12105-12109
1994
Arabidopsis thaliana (P51566), Arabidopsis thaliana (P51567), Arabidopsis thaliana (P51568)
Krupa, A.; Srinivasan, N.
Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes
BMC Genet.
6
129
2005
Arabidopsis thaliana, Bradyrhizobium japonicum, Chlamydia sp., Chloroflexus aurantiacus, Clostridium acetobutylicum, Acetivibrio thermocellus, Deinococcus radiodurans, Halobacterium salinarum, Leptospira interrogans, Mesorhizobium loti, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanosarcina mazei, Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycobacterium avium subsp. paratuberculosis, Nitrosomonas europaea, Nostoc punctiforme, Nostoc sp., Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas syringae, Streptomyces avermitilis, Streptomyces coelicolor, Saccharolobus solfataricus, Thermobifida fusca, Thermoplasma acidophilum, Thermoplasma volcanium, Methanosarcina acetivorans, Gloeobacter violaceus, Trichodesmium erythraeum, Pirellula sp., Thermospora curvatum, Sulfurisphaera tokodaii, Mycobacterium tuberculosis variant bovis AF2, Mycobacterium tuberculosis CDC 1551
Kim, D.; Ntui, V.O.; Zhang, N.; Xiong, L.
Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase
FEBS Lett.
589
3321-3327
2015
Arabidopsis thaliana (Q8RWH3), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q8RWH3)
Xu, F.; Meng, T.; Li, P.; Yu, Y.; Cui, Y.; Wang, Y.; Gong, Q.; Wang, N.N.
A soybean dual-specificity kinase, GmSARK, and its Arabidopsis homolog, AtSARK, regulate leaf senescence through synergistic actions of auxin and ethylene
Plant Physiol.
157
2131-2153
2011
Arabidopsis thaliana, Glycine max
EXTERNAL LINKS (specific for EC-Number 2.7.12.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
