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Information on EC 2.7.11.24 - mitogen-activated protein kinase and Organism(s) Danio rerio

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EC Tree
IUBMB Comments
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline . A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
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This record set is specific for:
Danio rerio
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
mapk, p38, erk1/2, p38 mapk, mitogen-activated protein kinase, map kinase, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, p38mapk, p38 map kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cp38a
-
-
-
-
cp38b
-
-
-
-
CSAID binding protein
-
-
-
-
CSBP
-
-
-
-
Cytokine suppressive anti-inflammatory drug binding protein
-
-
-
-
ERK5
-
-
-
-
MAP kinase MXI2
-
-
-
-
MAP kinase p38 beta
-
-
-
-
MAP kinase p38 delta
-
-
-
-
MAP kinase p38 gamma
-
-
-
-
MAP kinase p38a
-
-
-
-
MAP kinase p38alpha
-
-
-
-
MAP kinase p38b
-
-
-
-
MAPK
-
-
-
-
mitogen-activated protein kinase
-
-
-
-
mitogen-activated protein kinase 14B
-
mitogen-activated protein kinase 8
-
Mitogen-activated protein kinase p38 beta
-
-
-
-
Mitogen-activated protein kinase p38 delta
-
-
-
-
Mitogen-activated protein kinase p38 gamma
-
-
-
-
Mitogen-activated protein kinase p38a
-
-
-
-
Mitogen-activated protein kinase p38alpha
-
-
-
-
Mitogen-activated protein kinase p38b
-
-
-
-
p38 MAP kinase
-
p38b
-
-
-
-
SAPK2A
-
-
-
-
stress-activated protein kinase 2a
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (MAPKK-activated)
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline [6]. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
CAS REGISTRY NUMBER
COMMENTARY hide
142243-02-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
molecular mechanism of negative regulation of Ras/ERK signaling, Sef negatively regulates ERK phosphorylation by blocking dissocation of MEK and ERK
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
phosphorylation activates ERK
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
ERK localization is controlled by the cytoplasmic ERK anchoring proteins that have a nuclear export signal, ERK forms complexes with MEK, EC 2.7.11.25, in the cytoplasm, in response to activation ERK dissociates from MEK and is translocated to the nucleus
Manually annotated by BRENDA team
-
ERK colocalizes with MEK and Sef
Manually annotated by BRENDA team
-
ERK localization is controlled by the cytoplasmic ERK anchoring proteins that have a nuclear export signal, ERK forms complexes with MEK, EC 2.7.11.25, in the cytoplasm, in response to activation ERK dissociates from MEK and is translocated to the nucleus, mechanism
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MK08_DANRE
384
0
44140
Swiss-Prot
other Location (Reliability: 2)
MK12_DANRE
363
0
41971
Swiss-Prot
other Location (Reliability: 5)
MK14A_DANRE
361
0
41633
Swiss-Prot
other Location (Reliability: 3)
MK14B_DANRE
348
0
39998
Swiss-Prot
other Location (Reliability: 5)
E9QBW8_DANRE
427
0
48440
TrEMBL
other Location (Reliability: 2)
I3VB57_DANRE
292
0
33571
TrEMBL
other Location (Reliability: 5)
A0A8M1P824_DANRE
361
0
41370
TrEMBL
other Location (Reliability: 5)
A0A0R4IIR5_DANRE
523
0
58697
TrEMBL
other Location (Reliability: 1)
A0A0R4IKK9_DANRE
472
0
53527
TrEMBL
other Location (Reliability: 5)
F1RAA2_DANRE
361
0
41370
TrEMBL
other Location (Reliability: 5)
E9QB50_DANRE
428
0
48531
TrEMBL
other Location (Reliability: 2)
A0A8M1P8D2_DANRE
384
0
44126
TrEMBL
other Location (Reliability: 2)
A0A8M1MZX2_DANRE
361
0
41672
TrEMBL
other Location (Reliability: 5)
Q6P023_DANRE
369
0
42147
TrEMBL
other Location (Reliability: 4)
F1RCB7_DANRE
260
2
29826
TrEMBL
other Location (Reliability: 2)
Q803M9_DANRE
674
0
75912
TrEMBL
other Location (Reliability: 2)
A0A8M1NF54_DANRE
427
0
48213
TrEMBL
other Location (Reliability: 2)
A0A2R8QEM3_DANRE
354
0
40500
TrEMBL
other Location (Reliability: 4)
Q0H1F2_DANRE
729
0
83196
TrEMBL
other Location (Reliability: 1)
B3IWJ8_DANRE
452
0
51079
TrEMBL
other Location (Reliability: 4)
E9QJ67_DANRE
256
2
29275
TrEMBL
other Location (Reliability: 2)
E7F292_DANRE
362
0
41837
TrEMBL
other Location (Reliability: 2)
Q9DGR5_DANRE
369
0
42068
TrEMBL
other Location (Reliability: 3)
Q0H1F4_DANRE
862
0
94962
TrEMBL
other Location (Reliability: 1)
Q7ZVK8_DANRE
392
0
44099
TrEMBL
other Location (Reliability: 3)
Q4VH14_DANRE
369
0
42088
TrEMBL
other Location (Reliability: 4)
A0A2R8Q3H6_DANRE
349
0
40358
TrEMBL
other Location (Reliability: 3)
A0A2R8QE41_DANRE
361
0
41451
TrEMBL
other Location (Reliability: 3)
Q6IQ84_DANRE
361
0
41672
TrEMBL
other Location (Reliability: 5)
Q567M5_DANRE
329
0
36193
TrEMBL
other Location (Reliability: 4)
A4QP40_DANRE
384
0
44054
TrEMBL
other Location (Reliability: 2)
A8KB80_DANRE
359
0
41096
TrEMBL
other Location (Reliability: 4)
A0A8M1N8E9_DANRE
430
0
49434
TrEMBL
other Location (Reliability: 5)
A0A0R4IN30_DANRE
210
0
24226
TrEMBL
other Location (Reliability: 4)
Q5U3S2_DANRE
363
0
41984
TrEMBL
other Location (Reliability: 5)
A0A8M1N660_DANRE
523
0
58697
TrEMBL
other Location (Reliability: 1)
Q9DGR6_DANRE
391
0
44126
TrEMBL
other Location (Reliability: 2)
Q5RHW0_DANRE
364
0
42217
TrEMBL
Mitochondrion (Reliability: 3)
F1QHF2_DANRE
359
0
41082
TrEMBL
other Location (Reliability: 4)
A0A8M1PG17_DANRE
475
0
52662
TrEMBL
other Location (Reliability: 4)
Q6P580_DANRE
361
0
41398
TrEMBL
other Location (Reliability: 5)
A8WG58_DANRE
427
0
48213
TrEMBL
other Location (Reliability: 2)
B0V361_DANRE
246
0
27721
TrEMBL
other Location (Reliability: 2)
Q7ZW72_DANRE
369
0
42075
TrEMBL
other Location (Reliability: 4)
E7F1L8_DANRE
533
0
58881
TrEMBL
other Location (Reliability: 4)
E9QEY0_DANRE
1080
0
118241
TrEMBL
other Location (Reliability: 1)
B2GPM7_DANRE
361
0
41633
TrEMBL
other Location (Reliability: 3)
A0A8M1NFM4_DANRE
452
0
51079
TrEMBL
other Location (Reliability: 4)
X1WHK9_DANRE
384
0
41952
TrEMBL
Mitochondrion (Reliability: 3)
A9ZMG5_DANRE
457
0
51609
TrEMBL
other Location (Reliability: 5)
Q1LVN7_DANRE
363
0
41971
TrEMBL
other Location (Reliability: 5)
Q6P3M1_DANRE
361
0
41386
TrEMBL
other Location (Reliability: 5)
Q503Q2_DANRE
524
0
58825
TrEMBL
other Location (Reliability: 1)
E9QJI8_DANRE
88
0
10036
TrEMBL
other Location (Reliability: 2)
F1QQ40_DANRE
361
0
41445
TrEMBL
other Location (Reliability: 5)
Q502A0_DANRE
260
2
29794
TrEMBL
other Location (Reliability: 2)
B0V360_DANRE
674
0
75898
TrEMBL
other Location (Reliability: 2)
Q6TNT1_DANRE
361
0
41409
TrEMBL
other Location (Reliability: 5)
F1R202_DANRE
348
0
40042
TrEMBL
other Location (Reliability: 5)
A0A8M1P821_DANRE
472
0
53527
TrEMBL
other Location (Reliability: 5)
A0A8M1P270_DANRE
486
0
55245
TrEMBL
other Location (Reliability: 5)
Q32LV0_DANRE
430
0
49434
TrEMBL
other Location (Reliability: 5)
A0A0R4I9H8_DANRE
384
0
44126
TrEMBL
other Location (Reliability: 2)
Q6Q382_DANRE
475
0
52662
TrEMBL
other Location (Reliability: 4)
A0A0R4IB91_DANRE
433
0
49812
TrEMBL
Mitochondrion (Reliability: 5)
E9QE29_DANRE
421
0
47920
TrEMBL
other Location (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
phosphorylation activates ERK
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujii, R.; Yamashita, S.; Hibi, M.; Hirano, T.
Asymmetric p38 activation in zebrafish: its possible role in symmetric and synchronous cleavage
J. Cell. Biol.
150
1335-1348
2000
Danio rerio (Q9DGD9), Danio rerio (Q9DGE1), Danio rerio (Q9DGE2), Danio rerio
Manually annotated by BRENDA team
Torii, S.; Nakayama, K.; Yamamoto, T.; Nishida, E.
Regulatory mechanisms and function of ERK MAP kinases
J. Biochem.
136
557-561
2004
Danio rerio, vertebrata
Manually annotated by BRENDA team