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P28482

- MK01_HUMAN

UniProt

P28482 - MK01_HUMAN

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Protein

Mitogen-activated protein kinase 1

Gene

MAPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.
Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-185 and Tyr-187 in response to external stimuli like insulin or NGF. Both phosphorylations are required for activity. This phosphorylation causes dramatic conformational changes, which enable full activation and interaction of MAPK1/ERK2 with its substrates. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Binding sitei54 – 541Inhibitor6 Publications
Binding sitei108 – 1081Inhibitor; via amide nitrogen and carbonyl oxygen6 Publications
Binding sitei114 – 1141Inhibitor6 Publications
Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation
Binding sitei154 – 1541Inhibitor6 Publications
Binding sitei166 – 1661Inhibitor6 Publications
Binding sitei167 – 1671Inhibitor6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation
DNA bindingi259 – 27719Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. MAP kinase activity Source: ProtInc
  4. phosphatase binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: Reactome
  2. activation of MAPKK activity Source: Reactome
  3. apoptotic process Source: ProtInc
  4. axon guidance Source: Reactome
  5. B cell receptor signaling pathway Source: Ensembl
  6. blood coagulation Source: Reactome
  7. caveolin-mediated endocytosis Source: UniProtKB
  8. cell cycle Source: UniProtKB-KW
  9. cellular response to DNA damage stimulus Source: Ensembl
  10. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: Ensembl
  11. chemotaxis Source: ProtInc
  12. cytosine metabolic process Source: Ensembl
  13. epidermal growth factor receptor signaling pathway Source: Reactome
  14. ERBB signaling pathway Source: UniProtKB
  15. ERK1 and ERK2 cascade Source: UniProtKB
  16. Fc-epsilon receptor signaling pathway Source: Reactome
  17. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  18. fibroblast growth factor receptor signaling pathway Source: Reactome
  19. innate immune response Source: Reactome
  20. insulin receptor signaling pathway Source: Reactome
  21. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  22. labyrinthine layer blood vessel development Source: Ensembl
  23. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  24. mammary gland epithelial cell proliferation Source: Ensembl
  25. MAPK cascade Source: Reactome
  26. MAPK import into nucleus Source: Ensembl
  27. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  28. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  29. negative regulation of cell differentiation Source: Ensembl
  30. neurotrophin TRK receptor signaling pathway Source: Reactome
  31. organ morphogenesis Source: Ensembl
  32. peptidyl-serine phosphorylation Source: BHF-UCL
  33. peptidyl-threonine phosphorylation Source: UniProtKB
  34. platelet activation Source: Reactome
  35. positive regulation of cell migration Source: Ensembl
  36. positive regulation of cell proliferation Source: Ensembl
  37. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  38. positive regulation of transcription, DNA-templated Source: Ensembl
  39. positive regulation of translation Source: Ensembl
  40. Ras protein signal transduction Source: Reactome
  41. regulation of cytoskeleton organization Source: UniProtKB
  42. regulation of early endosome to late endosome transport Source: UniProtKB
  43. regulation of Golgi inheritance Source: UniProtKB
  44. regulation of protein stability Source: UniProtKB
  45. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  46. regulation of stress-activated MAPK cascade Source: UniProtKB
  47. response to epidermal growth factor Source: UniProtKB
  48. response to estrogen Source: Ensembl
  49. response to exogenous dsRNA Source: Ensembl
  50. response to stress Source: ProtInc
  51. response to toxic substance Source: Ensembl
  52. sensory perception of pain Source: Ensembl
  53. signal transduction Source: ProtInc
  54. small GTPase mediated signal transduction Source: Reactome
  55. stress-activated MAPK cascade Source: Reactome
  56. synaptic transmission Source: Reactome
  57. T cell receptor signaling pathway Source: Ensembl
  58. toll-like receptor 10 signaling pathway Source: Reactome
  59. toll-like receptor 2 signaling pathway Source: Reactome
  60. toll-like receptor 3 signaling pathway Source: Reactome
  61. toll-like receptor 4 signaling pathway Source: Reactome
  62. toll-like receptor 5 signaling pathway Source: Reactome
  63. toll-like receptor 9 signaling pathway Source: Reactome
  64. toll-like receptor signaling pathway Source: Reactome
  65. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  66. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  67. transcription, DNA-templated Source: UniProtKB-KW
  68. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  69. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Repressor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 2681.
ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_111133. Growth hormone receptor signaling.
REACT_111184. Negative regulation of FGFR signaling.
REACT_1183. ERK2 activation.
REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_15466. phospho-PLA2 pathway.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_163701. FCERI mediated MAPK activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_20510. RSK activation.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
REACT_22272. Signal transduction by L1.
REACT_22365. Recycling pathway of L1.
REACT_25195. Advanced glycosylation endproduct receptor signaling.
REACT_508. Signal attenuation.
REACT_9470. Signaling by FGFR.
SignaLinkiP28482.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 1 (EC:2.7.11.24)
Short name:
MAP kinase 1
Short name:
MAPK 1
Alternative name(s):
ERT1
Extracellular signal-regulated kinase 2
Short name:
ERK-2
MAP kinase isoform p42
Short name:
p42-MAPK
Mitogen-activated protein kinase 2
Short name:
MAP kinase 2
Short name:
MAPK 2
Gene namesi
Name:MAPK1
Synonyms:ERK2, PRKM1, PRKM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6871. MAPK1.

Subcellular locationi

Cytoplasmcytoskeletonspindle By similarity. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasm
Note: Associated with the spindle during prometaphase and metaphase By similarity. PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention. Phosphorylation at Ser- 246 and Ser-248 as well as autophosphorylation at Thr-190 promote nuclear localization.By similarity

GO - Cellular componenti

  1. caveola Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: UniProtKB
  5. dendrite cytoplasm Source: Ensembl
  6. early endosome Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProt
  8. focal adhesion Source: UniProtKB
  9. Golgi apparatus Source: UniProtKB
  10. late endosome Source: UniProtKB
  11. microtubule cytoskeleton Source: HPA
  12. mitochondrion Source: UniProtKB
  13. mitotic spindle Source: UniProtKB
  14. nucleoplasm Source: Reactome
  15. nucleus Source: UniProtKB
  16. perikaryon Source: Ensembl
  17. protein complex Source: Ensembl
  18. pseudopodium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541K → R: Does not inhibit interaction with MAP2K1. 1 Publication
Mutagenesisi176 – 1794Missing: Inhibits homodimerization and interaction with TPR. 1 Publication
Mutagenesisi185 – 1851T → A: Inhibits interaction with TPR; when associated with A-187. 1 Publication
Mutagenesisi187 – 1871Y → A: Inhibits interaction with TPR; when associated with A-185. 1 Publication
Mutagenesisi234 – 2341L → A: Inhibits interaction with TPR. 1 Publication
Mutagenesisi318 – 3181D → A: Loss of dephosphorylation by PTPRJ. 2 Publications
Mutagenesisi318 – 3181D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-321. 2 Publications
Mutagenesisi321 – 3211D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-318. 1 Publication

Organism-specific databases

Orphaneti261330. Distal 22q11.2 microdeletion syndrome.
PharmGKBiPA30616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 360359Mitogen-activated protein kinase 1PRO_0000186247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei29 – 291Phosphoserine; by SGK11 Publication
Modified residuei185 – 1851Phosphothreonine; by MAP2K1 and MAP2K23 Publications
Modified residuei187 – 1871Phosphotyrosine; by MAP2K1 and MAP2K25 Publications
Modified residuei190 – 1901Phosphothreonine; by autocatalysis1 Publication
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated upon KIT and FLT3 signaling By similarity. Dually phosphorylated on Thr-185 and Tyr-187, which activates the enzyme. Undergoes regulatory phosphorylation on additional residues such as Ser-246 and Ser-248 in the kinase insert domain (KID) These phosphorylations, which are probably mediated by more than one kinase, are important for binding of MAPK1/ERK2 to importin-7 (IPO7) and its nuclear translocation. In addition, autophosphorylation of Thr-190 was shown to affect the subcellular localization of MAPK1/ERK2 as well. Ligand-activated ALK induces tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-187. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. DUSP3 and DUSP6 dephosphorylate specifically MAPK1/ERK2 and MAPK3/ERK1 whereas DUSP9 dephosphorylates a broader range of MAPKs.By similarity11 Publications
ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP28482.
PaxDbiP28482.
PeptideAtlasiP28482.
PRIDEiP28482.

2D gel databases

OGPiP28482.

PTM databases

PhosphoSiteiP28482.

Expressioni

Gene expression databases

BgeeiP28482.
CleanExiHS_MAPK1.
ExpressionAtlasiP28482. baseline and differential.
GenevestigatoriP28482.

Organism-specific databases

HPAiCAB004229.
HPA003995.
HPA005700.
HPA030069.

Interactioni

Subunit structurei

Binds both upstream activators and downstream substrates in multimolecular complexes. Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine-kinase activity. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with MORG1, PEA15 and MKNK2 By similarity. MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation By similarity. Interacts with DCC By similarity. The phosphorylated form interacts with PML (isoform PML-4). Interacts with STYX.By similarity22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB2P321213EBI-959949,EBI-714559
cicQ9U1H02EBI-959949,EBI-98330From a different organism.
DUSP1P285626EBI-959949,EBI-975493
Dusp2Q059222EBI-959949,EBI-7898692From a different organism.
DUSP5Q166904EBI-959949,EBI-7487376
ETS1P149213EBI-959949,EBI-913209
MAP2K1Q027502EBI-959949,EBI-492564
MAPK14Q16539-35EBI-959949,EBI-6932370
MAPK3P273613EBI-959949,EBI-73995
MBPP026872EBI-959949,EBI-908215From a different organism.
PPM1AP3581319EBI-959949,EBI-989143
PTPN7P352366EBI-959949,EBI-2265723
PTPRJQ129137EBI-959949,EBI-2264500
PTPRRQ152563EBI-959949,EBI-2265659
RPS6KA3P518123EBI-959949,EBI-1046616
U24Q695592EBI-959949,EBI-8015758From a different organism.

Protein-protein interaction databases

BioGridi111580. 190 interactions.
DIPiDIP-519N.
IntActiP28482. 72 interactions.
MINTiMINT-144006.
STRINGi9606.ENSP00000215832.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 198
Turni22 – 243
Beta strandi25 – 339
Beta strandi38 – 447
Turni45 – 484
Beta strandi49 – 568
Beta strandi59 – 613
Helixi62 – 7716
Beta strandi88 – 903
Turni95 – 973
Beta strandi101 – 1066
Beta strandi109 – 1113
Helixi112 – 1187
Helixi123 – 14220
Helixi152 – 1543
Beta strandi155 – 1573
Turni159 – 1613
Beta strandi163 – 1653
Helixi168 – 1703
Helixi176 – 1783
Turni181 – 1855
Helixi191 – 1933
Helixi196 – 2005
Beta strandi202 – 2054
Helixi208 – 22316
Helixi233 – 24412
Helixi249 – 2524
Beta strandi253 – 2553
Helixi258 – 2669
Helixi275 – 2784
Beta strandi279 – 2824
Helixi284 – 29310
Helixi298 – 3003
Helixi304 – 3085
Helixi311 – 3133
Turni314 – 3163
Helixi319 – 3213
Turni335 – 3373
Helixi340 – 35112
Helixi352 – 3543
Turni356 – 3583

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMEX-ray2.00A1-360[»]
1TVOX-ray2.50A1-360[»]
1WZYX-ray2.50A1-360[»]
2OJGX-ray2.00A2-360[»]
2OJIX-ray2.60A2-360[»]
2OJJX-ray2.40A2-360[»]
2Y9QX-ray1.55A1-360[»]
3D42X-ray2.46B184-191[»]
3D44X-ray1.90B184-191[»]
3I5ZX-ray2.20A1-360[»]
3I60X-ray2.50A1-360[»]
3SA0X-ray1.59A1-360[»]
3TEIX-ray2.40A1-360[»]
3W55X-ray3.00A1-360[»]
4FMQX-ray2.10A1-360[»]
4FUXX-ray2.20A1-360[»]
4FUYX-ray2.00A1-360[»]
4FV0X-ray2.10A1-360[»]
4FV1X-ray1.99A1-360[»]
4FV2X-ray2.00A1-360[»]
4FV3X-ray2.20A1-360[»]
4FV4X-ray2.50A1-360[»]
4FV5X-ray2.40A1-360[»]
4FV6X-ray2.50A1-360[»]
4FV7X-ray1.90A1-360[»]
4FV8X-ray2.00A1-360[»]
4FV9X-ray2.11A1-360[»]
4G6NX-ray2.00A1-360[»]
4G6OX-ray2.20A1-360[»]
4H3PX-ray2.30A/D1-360[»]
4H3QX-ray2.20A1-360[»]
4IZ5X-ray3.19A/B/C/D8-360[»]
4IZ7X-ray1.80A/C8-360[»]
4IZAX-ray1.93A/C8-360[»]
4N0SX-ray1.80A1-360[»]
4O6EX-ray1.95A13-360[»]
4QTAX-ray1.45A1-360[»]
4QTEX-ray1.50A1-360[»]
ProteinModelPortaliP28482.
SMRiP28482. Positions 9-358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28482.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 313289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1084Inhibitor-binding
Regioni153 – 1542Inhibitor-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi185 – 1873TXY
Motifi318 – 3225Cytoplasmic retention motif
Motifi327 – 3337Nuclear translocation motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 98Poly-Ala

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.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP28482.
KOiK04371.
OMAiVCSAYDR.
OrthoDBiEOG7M3J0K.
PhylomeDBiP28482.
TreeFamiTF105097.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
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]
PRINTSiPR01770. ERK1ERK2MAPK.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28482-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR
60 70 80 90 100
VAIKKISPFE HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD
110 120 130 140 150
VYIVQDLMET DLYKLLKTQH LSNDHICYFL YQILRGLKYI HSANVLHRDL
160 170 180 190 200
KPSNLLLNTT CDLKICDFGL ARVADPDHDH TGFLTEYVAT RWYRAPEIML
210 220 230 240 250
NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI LGILGSPSQE
260 270 280 290 300
DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK
310 320 330 340 350
RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE
360
TARFQPGYRS
Length:360
Mass (Da):41,390
Last modified:January 23, 2007 - v3
Checksum:iE85D0B2A5D2D724E
GO
Isoform 2 (identifier: P28482-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     242-285: Missing.

Show »
Length:316
Mass (Da):36,432
Checksum:i6076E1767B603945
GO

Sequence cautioni

The sequence CAA77753.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911R → Q in CAA77752. (PubMed:1319925)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei242 – 28544Missing in isoform 2. 1 PublicationVSP_047815Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84489 mRNA. Translation: AAA58459.1.
Z11694 mRNA. Translation: CAA77752.1.
Z11695 mRNA. Translation: CAA77753.1. Different initiation.
DQ399292 mRNA. Translation: ABD60303.1.
AP000553 Genomic DNA. No translation available.
AP000554 Genomic DNA. No translation available.
AP000555 Genomic DNA. No translation available.
BC017832 mRNA. Translation: AAH17832.1.
CCDSiCCDS13795.1. [P28482-1]
PIRiJQ1400.
RefSeqiNP_002736.3. NM_002745.4. [P28482-1]
NP_620407.1. NM_138957.3. [P28482-1]
UniGeneiHs.431850.

Genome annotation databases

EnsembliENST00000215832; ENSP00000215832; ENSG00000100030. [P28482-1]
ENST00000398822; ENSP00000381803; ENSG00000100030. [P28482-1]
ENST00000544786; ENSP00000440842; ENSG00000100030. [P28482-2]
GeneIDi5594.
KEGGihsa:5594.
UCSCiuc002zvn.3. human. [P28482-1]

Polymorphism databases

DMDMi119554.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Extracellular signal-regulated kinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84489 mRNA. Translation: AAA58459.1 .
Z11694 mRNA. Translation: CAA77752.1 .
Z11695 mRNA. Translation: CAA77753.1 . Different initiation.
DQ399292 mRNA. Translation: ABD60303.1 .
AP000553 Genomic DNA. No translation available.
AP000554 Genomic DNA. No translation available.
AP000555 Genomic DNA. No translation available.
BC017832 mRNA. Translation: AAH17832.1 .
CCDSi CCDS13795.1. [P28482-1 ]
PIRi JQ1400.
RefSeqi NP_002736.3. NM_002745.4. [P28482-1 ]
NP_620407.1. NM_138957.3. [P28482-1 ]
UniGenei Hs.431850.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PME X-ray 2.00 A 1-360 [» ]
1TVO X-ray 2.50 A 1-360 [» ]
1WZY X-ray 2.50 A 1-360 [» ]
2OJG X-ray 2.00 A 2-360 [» ]
2OJI X-ray 2.60 A 2-360 [» ]
2OJJ X-ray 2.40 A 2-360 [» ]
2Y9Q X-ray 1.55 A 1-360 [» ]
3D42 X-ray 2.46 B 184-191 [» ]
3D44 X-ray 1.90 B 184-191 [» ]
3I5Z X-ray 2.20 A 1-360 [» ]
3I60 X-ray 2.50 A 1-360 [» ]
3SA0 X-ray 1.59 A 1-360 [» ]
3TEI X-ray 2.40 A 1-360 [» ]
3W55 X-ray 3.00 A 1-360 [» ]
4FMQ X-ray 2.10 A 1-360 [» ]
4FUX X-ray 2.20 A 1-360 [» ]
4FUY X-ray 2.00 A 1-360 [» ]
4FV0 X-ray 2.10 A 1-360 [» ]
4FV1 X-ray 1.99 A 1-360 [» ]
4FV2 X-ray 2.00 A 1-360 [» ]
4FV3 X-ray 2.20 A 1-360 [» ]
4FV4 X-ray 2.50 A 1-360 [» ]
4FV5 X-ray 2.40 A 1-360 [» ]
4FV6 X-ray 2.50 A 1-360 [» ]
4FV7 X-ray 1.90 A 1-360 [» ]
4FV8 X-ray 2.00 A 1-360 [» ]
4FV9 X-ray 2.11 A 1-360 [» ]
4G6N X-ray 2.00 A 1-360 [» ]
4G6O X-ray 2.20 A 1-360 [» ]
4H3P X-ray 2.30 A/D 1-360 [» ]
4H3Q X-ray 2.20 A 1-360 [» ]
4IZ5 X-ray 3.19 A/B/C/D 8-360 [» ]
4IZ7 X-ray 1.80 A/C 8-360 [» ]
4IZA X-ray 1.93 A/C 8-360 [» ]
4N0S X-ray 1.80 A 1-360 [» ]
4O6E X-ray 1.95 A 13-360 [» ]
4QTA X-ray 1.45 A 1-360 [» ]
4QTE X-ray 1.50 A 1-360 [» ]
ProteinModelPortali P28482.
SMRi P28482. Positions 9-358.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111580. 190 interactions.
DIPi DIP-519N.
IntActi P28482. 72 interactions.
MINTi MINT-144006.
STRINGi 9606.ENSP00000215832.

Chemistry

BindingDBi P28482.
ChEMBLi CHEMBL4040.
DrugBanki DB01169. Arsenic trioxide.
DB01064. Isoprenaline.
GuidetoPHARMACOLOGYi 1495.

PTM databases

PhosphoSitei P28482.

Polymorphism databases

DMDMi 119554.

2D gel databases

OGPi P28482.

Proteomic databases

MaxQBi P28482.
PaxDbi P28482.
PeptideAtlasi P28482.
PRIDEi P28482.

Protocols and materials databases

DNASUi 5594.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215832 ; ENSP00000215832 ; ENSG00000100030 . [P28482-1 ]
ENST00000398822 ; ENSP00000381803 ; ENSG00000100030 . [P28482-1 ]
ENST00000544786 ; ENSP00000440842 ; ENSG00000100030 . [P28482-2 ]
GeneIDi 5594.
KEGGi hsa:5594.
UCSCi uc002zvn.3. human. [P28482-1 ]

Organism-specific databases

CTDi 5594.
GeneCardsi GC22M022108.
HGNCi HGNC:6871. MAPK1.
HPAi CAB004229.
HPA003995.
HPA005700.
HPA030069.
MIMi 176948. gene.
neXtProti NX_P28482.
Orphaneti 261330. Distal 22q11.2 microdeletion syndrome.
PharmGKBi PA30616.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074298.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P28482.
KOi K04371.
OMAi VCSAYDR.
OrthoDBi EOG7M3J0K.
PhylomeDBi P28482.
TreeFami TF105097.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
Reactomei REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_111133. Growth hormone receptor signaling.
REACT_111184. Negative regulation of FGFR signaling.
REACT_1183. ERK2 activation.
REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_15466. phospho-PLA2 pathway.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_163701. FCERI mediated MAPK activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_20510. RSK activation.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
REACT_22272. Signal transduction by L1.
REACT_22365. Recycling pathway of L1.
REACT_25195. Advanced glycosylation endproduct receptor signaling.
REACT_508. Signal attenuation.
REACT_9470. Signaling by FGFR.
SignaLinki P28482.

Miscellaneous databases

ChiTaRSi MAPK1. human.
EvolutionaryTracei P28482.
GeneWikii MAPK1.
GenomeRNAii 5594.
NextBioi 21708.
PROi P28482.
SOURCEi Search...

Gene expression databases

Bgeei P28482.
CleanExi HS_MAPK1.
ExpressionAtlasi P28482. baseline and differential.
Genevestigatori P28482.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01770. ERK1ERK2MAPK.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs."
    Owaki H., Makar R., Boulton T.G., Cobb M.H., Geppert T.D.
    Biochem. Biophys. Res. Commun. 182:1416-1422(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Heterogeneous expression of four MAP kinase isoforms in human tissues."
    Gonzalez F.A., Raden D.L., Rigby M.R., Davis R.J.
    FEBS Lett. 304:170-178(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Identification of dominant negative Erk1/2 variants in cancer cells."
    Cheng H., Ren S., Qiu R., Wang M., Feng Y.H.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  7. "ERF: an ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation."
    Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G., Mavrothalassitis G.J.
    EMBO J. 14:4781-4793(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ERF.
  8. "3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region."
    Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G.
    , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.
    Mol. Cell. Biol. 16:868-876(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPKAPK3.
  9. "Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity."
    Greenway A.L., Azad A., Mills J., McPhee D.A.
    J. Virol. 70:6701-6708(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 NEF.
  10. "MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase."
    Ni H., Wang X.S., Diener K., Yao Z.
    Biochem. Biophys. Res. Commun. 243:492-496(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPKAPK5.
  11. "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
    Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
    EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KA5/MSK1.
  12. "Antigen receptor signaling induces MAP kinase-mediated phosphorylation and degradation of the BCL-6 transcription factor."
    Niu H., Ye B.H., Dalla-Favera R.
    Genes Dev. 12:1953-1961(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BCL6.
  13. "Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase."
    Camps M., Nichols A., Gillieron C., Antonsson B., Muda M., Chabert C., Boschert U., Arkinstall S.
    Science 280:1262-1265(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP6, FUNCTION.
  14. "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway."
    Todd J.L., Tanner K.G., Denu J.M.
    J. Biol. Chem. 274:13271-13280(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY DUSP3.
  15. "ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry."
    Cruzalegui F.H., Cano E., Treisman R.
    Oncogene 18:7948-7957(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ELK1.
  16. "Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation."
    Brondello J.M., Pouyssegur J., McKenzie F.R.
    Science 286:2514-2517(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DUSP1.
  17. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
    Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
    Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MKNK2 KINASE.
  18. "Growth factors can activate ATF2 via a two-step mechanism: phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69 through RalGDS-Src-p38."
    Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P., Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A., van Dam H.
    EMBO J. 21:3782-3793(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ATF2.
  19. "IEX-1: a new ERK substrate involved in both ERK survival activity and ERK activation."
    Garcia J., Ye Y., Arranz V., Letourneux C., Pezeron G., Porteu F.
    EMBO J. 21:5151-5163(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF IER3, INTERACTION WITH IER3, ENZYME REGULATION.
  20. "Insulin receptor substrate 4 associates with the protein IRAS."
    Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
    J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NISCH.
  21. "EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2."
    Wu Y., Chen Z., Ullrich A.
    Biol. Chem. 384:1215-1226(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2.
  22. "Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446."
    Masuda K., Shima H., Katagiri C., Kikuchi K.
    J. Biol. Chem. 278:32448-32456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DUSP16.
  23. "Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK."
    Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.
    Nat. Cell Biol. 5:647-654(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CASP9.
  24. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK2.
  25. "Signal transduction via the stem cell factor receptor/c-Kit."
    Ronnstrand L.
    Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN KIT SIGNALING.
  26. "Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin."
    Mitsushima M., Suwa A., Amachi T., Ueda K., Kioka N.
    J. Biol. Chem. 279:34570-34577(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SORBS3.
  27. "MCL1 is phosphorylated in the PEST region and stabilized upon ERK activation in viable cells, and at additional sites with cytotoxic okadaic acid or taxol."
    Domina A.M., Vrana J.A., Gregory M.A., Hann S.R., Craig R.W.
    Oncogene 23:5301-5315(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MCL1.
  28. "Phosphorylation of Grb10 by mitogen-activated protein kinase: identification of Ser150 and Ser476 of human Grb10zeta as major phosphorylation sites."
    Langlais P., Wang C., Dong L.Q., Carroll C.A., Weintraub S.T., Liu F.
    Biochemistry 44:8890-8897(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GRB10.
  29. "Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK."
    Chen C.H., Wang W.J., Kuo J.C., Tsai H.C., Lin J.R., Chang Z.F., Chen R.H.
    EMBO J. 24:294-304(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK1, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
  30. "Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces Pin-1 binding in cytoplasm and cell death."
    Hong J.W., Ryu M.S., Lim I.K.
    J. Biol. Chem. 280:21256-21263(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BTG2.
  31. Cited for: FUNCTION IN PHOSPHORYLATION OF RAF1.
  32. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA."
    Fujishiro S.H., Tanimura S., Mure S., Kashimoto Y., Watanabe K., Kohno M.
    Biochem. Biophys. Res. Commun. 368:162-167(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF2.
  34. "Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26."
    Hu Y., Mivechi N.F.
    Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSF4.
  35. "ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation."
    Degoutin J., Vigny M., Gouzi J.Y.
    FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  36. "Mutations of beta-arrestin 2 that limit self-association also interfere with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs."
    Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R., Kolch W., Houslay M.D., Milligan G.
    Biochem. J. 413:51-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  37. "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
    Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
    Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAM15.
  38. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  39. "Identification and characterization of a general nuclear translocation signal in signaling proteins."
    Chuderland D., Konson A., Seger R.
    Mol. Cell 31:850-861(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-246 AND SER-248, INTERACTION WITH IPO7, SUBCELLULAR LOCATION.
  40. "Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction."
    Vomastek T., Iwanicki M.P., Burack W.R., Tiwari D., Kumar D., Parsons J.T., Weber M.J., Nandicoori V.K.
    Mol. Cell. Biol. 28:6954-6966(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TPR, INTERACTION WITH TPR, MUTAGENESIS OF LYS-54; 176-PRO--ASP-179; THR-185; TYR-187; LEU-234; ASP-318 AND ASP-321.
  41. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  42. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. "Profiling the human protein-DNA interactome reveals ERK2 as a transcriptional repressor of interferon signaling."
    Hu S., Xie Z., Onishi A., Yu X., Jiang L., Lin J., Rho H.-S., Woodard C., Wang H., Jeong J.-S., Long S., He X., Wade H., Blackshaw S., Qian J., Zhu H.
    Cell 139:610-622(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, DNA-BINDING.
  44. "The D816V mutation of c-Kit circumvents a requirement for Src family kinases in c-Kit signal transduction."
    Sun J., Pedersen M., Ronnstrand L.
    J. Biol. Chem. 284:11039-11047(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KIT SIGNALING PATHWAY, PHOSPHORYLATION.
  45. "Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases."
    Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P., Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.
    J. Biol. Chem. 284:22048-22058(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-187, DEPHOSPHORYLATION AT TYR-187 BY PTPRJ, MUTAGENESIS OF ASP-318.
  46. "Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration."
    Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J., Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M., Hur G.M.
    J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-29 BY SGK1, INTERACTION WITH SGK1.
  47. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  48. "A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy."
    Lorenz K., Schmitt J.P., Schmitteckert E.M., Lohse M.J.
    Nat. Med. 15:75-83(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-190, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
  49. "The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions."
    Yoon S., Seger R.
    Growth Factors 24:21-44(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  50. "The ERK signaling cascade--views from different subcellular compartments."
    Yao Z., Seger R.
    BioFactors 35:407-416(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, REVIEW ON SUBCELLULAR LOCATION.
  51. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  52. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  53. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  54. "The ERK cascade: distinct functions within various subcellular organelles."
    Wortzel I., Seger R.
    Genes Cancer 2:195-209(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  55. "Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover."
    Lim J.H., Liu Y., Reineke E., Kao H.Y.
    J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PML.
  56. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  57. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  58. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  59. "Pseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2."
    Reiterer V., Fey D., Kolch W., Kholodenko B.N., Farhan H.
    Proc. Natl. Acad. Sci. U.S.A. 110:E2934-2943(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STYX.
  60. "A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase."
    Fox T., Coll J.T., Xie X., Ford P.J., Germann U.A., Porter M.D., Pazhanisamy S., Fleming M.A., Galullo V., Su M.S., Wilson K.P.
    Protein Sci. 7:2249-2255(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  61. "Identification of a selective ERK inhibitor and structural determination of the inhibitor-ERK2 complex."
    Ohori M., Kinoshita T., Okubo M., Sato K., Yamazaki A., Arakawa H., Nishimura S., Inamura N., Nakajima H., Neya M., Miyake H., Fujii T.
    Biochem. Biophys. Res. Commun. 336:357-363(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  62. "Crystal structure of human ERK2 complexed with a pyrazolo[3,4-c]pyridazine derivative."
    Kinoshita T., Warizaya M., Ohori M., Sato K., Neya M., Fujii T.
    Bioorg. Med. Chem. Lett. 16:55-58(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  63. "Role of a cysteine residue in the active site of ERK and the MAPKK family."
    Ohori M., Kinoshita T., Yoshimura S., Warizaya M., Nakajima H., Miyake H.
    Biochem. Biophys. Res. Commun. 353:633-637(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  64. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
  65. "Structural basis of substrate recognition by hematopoietic tyrosine phosphatase."
    Critton D.A., Tortajada A., Stetson G., Peti W., Page R.
    Biochemistry 47:13336-13345(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 186-191, PHOSPHORYLATION AT TYR-187.
  66. "Structure-guided design of potent and selective pyrimidylpyrrole inhibitors of extracellular signal-regulated kinase (ERK) using conformational control."
    Aronov A.M., Tang Q., Martinez-Botella G., Bemis G.W., Cao J., Chen G., Ewing N.P., Ford P.J., Germann U.A., Green J., Hale M.R., Jacobs M., Janetka J.W., Maltais F., Markland W., Namchuk M.N., Nanthakumar S., Poondru S.
    , Straub J., ter Haar E., Xie X.
    J. Med. Chem. 52:6362-6368(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiMK01_HUMAN
AccessioniPrimary (citable) accession number: P28482
Secondary accession number(s): A8CZ64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3