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P27361

- MK03_HUMAN

UniProt

P27361 - MK03_HUMAN

Protein

Mitogen-activated protein kinase 3

Gene

MAPK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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, 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.12 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-202 and Tyr-204 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. Dephosphorylated and inactivated by DUSP3, DUSP6 and DUSP9.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711ATPPROSITE-ProRule annotation
    Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 569ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB
    3. phosphatase binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: Reactome
    2. activation of MAPKK activity Source: Reactome
    3. apoptotic process Source: UniProtKB-KW
    4. axon guidance Source: Reactome
    5. blood coagulation Source: Reactome
    6. BMP signaling pathway Source: BHF-UCL
    7. cartilage development Source: Ensembl
    8. caveolin-mediated endocytosis Source: UniProtKB
    9. cell cycle Source: UniProtKB-KW
    10. cellular response to mechanical stimulus Source: UniProtKB
    11. cytokine-mediated signaling pathway Source: Reactome
    12. DNA damage induced protein phosphorylation Source: UniProtKB
    13. epidermal growth factor receptor signaling pathway Source: Reactome
    14. Fc-epsilon receptor signaling pathway Source: Reactome
    15. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    16. fibroblast growth factor receptor signaling pathway Source: Reactome
    17. gene expression Source: Reactome
    18. innate immune response Source: Reactome
    19. insulin receptor signaling pathway Source: Reactome
    20. interleukin-1-mediated signaling pathway Source: BHF-UCL
    21. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    22. lipopolysaccharide-mediated signaling pathway Source: Ensembl
    23. MAPK cascade Source: BHF-UCL
    24. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    25. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    26. negative regulation of apolipoprotein binding Source: Ensembl
    27. neurotrophin TRK receptor signaling pathway Source: Reactome
    28. organ morphogenesis Source: Ensembl
    29. peptidyl-tyrosine autophosphorylation Source: UniProtKB
    30. phosphorylation Source: UniProtKB
    31. platelet activation Source: Reactome
    32. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    33. positive regulation of histone acetylation Source: BHF-UCL
    34. positive regulation of histone phosphorylation Source: BHF-UCL
    35. positive regulation of protein phosphorylation Source: BHF-UCL
    36. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    37. protein phosphorylation Source: UniProtKB
    38. Ras protein signal transduction Source: Reactome
    39. regulation of cytoskeleton organization Source: UniProtKB
    40. regulation of early endosome to late endosome transport Source: UniProtKB
    41. regulation of Golgi inheritance Source: UniProtKB
    42. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    43. regulation of stress-activated MAPK cascade Source: UniProtKB
    44. response to epidermal growth factor Source: UniProtKB
    45. response to exogenous dsRNA Source: Ensembl
    46. sensory perception of pain Source: Ensembl
    47. small GTPase mediated signal transduction Source: Reactome
    48. stress-activated MAPK cascade Source: Reactome
    49. toll-like receptor 10 signaling pathway Source: Reactome
    50. toll-like receptor 2 signaling pathway Source: Reactome
    51. toll-like receptor 3 signaling pathway Source: Reactome
    52. toll-like receptor 4 signaling pathway Source: Reactome
    53. toll-like receptor 5 signaling pathway Source: Reactome
    54. toll-like receptor 9 signaling pathway Source: Reactome
    55. toll-like receptor signaling pathway Source: Reactome
    56. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    57. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    58. transcription from RNA polymerase I promoter Source: Reactome
    59. transcription initiation from RNA polymerase I promoter Source: Reactome
    60. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    61. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle, Host-virus interaction

    Keywords - Ligandi

    ATP-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_115831. ISG15 antiviral mechanism.
    REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_1391. ERK1 activation.
    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_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_2232. RNA Polymerase I Promoter Opening.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.
    REACT_508. Signal attenuation.
    REACT_9470. Signaling by FGFR.
    SignaLinkiP27361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 3 (EC:2.7.11.24)
    Short name:
    MAP kinase 3
    Short name:
    MAPK 3
    Alternative name(s):
    ERT2
    Extracellular signal-regulated kinase 1
    Short name:
    ERK-1
    Insulin-stimulated MAP2 kinase
    MAP kinase isoform p44
    Short name:
    p44-MAPK
    Microtubule-associated protein 2 kinase
    p44-ERK1
    Gene namesi
    Name:MAPK3
    Synonyms:ERK1, PRKM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:6877. MAPK3.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Autophosphorylation at Thr-207 promotes nuclear localization.

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. early endosome Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. focal adhesion Source: UniProtKB
    7. Golgi apparatus Source: UniProtKB
    8. late endosome Source: UniProtKB
    9. microtubule cytoskeleton Source: HPA
    10. mitochondrion Source: UniProtKB
    11. nucleoplasm Source: Reactome
    12. nucleus Source: UniProtKB
    13. pseudopodium Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30622.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 379378Mitogen-activated protein kinase 3PRO_0000186251Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei170 – 1701Phosphoserine
    Modified residuei198 – 1981Phosphothreonine1 Publication
    Modified residuei202 – 2021Phosphothreonine; by MAP2K1 and MAP2K23 Publications
    Modified residuei204 – 2041Phosphotyrosine; by MAP2K1 and MAP2K25 Publications
    Modified residuei207 – 2071Phosphothreonine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylated upon KIT and FLT3 signaling By similarity. Dually phosphorylated on Thr-202 and Tyr-204, which activates the enzyme. Ligand-activated ALK induces tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-204.By similarity9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP27361.
    PaxDbiP27361.
    PRIDEiP27361.

    PTM databases

    PhosphoSiteiP27361.

    Expressioni

    Gene expression databases

    ArrayExpressiP27361.
    BgeeiP27361.
    CleanExiHS_MAPK3.
    GenevestigatoriP27361.

    Organism-specific databases

    HPAiCAB002683.
    HPA003995.
    HPA005700.

    Interactioni

    Subunit structurei

    Binds both upstream activators and downstream substrates in multimolecular complexes. Found in a complex with at least BRAF, HRAS, MAP2K1/MEK1, MAPK3 and RGS14 By similarity. Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine-kinase activity. Interacts with ADAM15, ARRB2, CANX, DAPK1 (via death domain), HSF4, IER3, MAP2K1/MEK1, MORG1, NISCH, and SGK1. Interacts with PEA15 and MKNK2 By similarity. MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation By similarity. Interacts with TPR.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAPK1P533555EBI-73995,EBI-358616
    DUSP1P285625EBI-73995,EBI-975493
    ELK1P194192EBI-73995,EBI-726632
    MAP2K1Q027502EBI-73995,EBI-492564
    MAPK1P284823EBI-73995,EBI-959949
    MAPK14Q165395EBI-73995,EBI-73946
    NsmfQ9EPI62EBI-73995,EBI-6899705From a different organism.
    PKMP14618-13EBI-73995,EBI-4304679
    PTPRBP234672EBI-73995,EBI-1265766
    PTPRJQ129135EBI-73995,EBI-2264500
    PtprrQ621323EBI-73995,EBI-6954051From a different organism.
    RPS6KA2Q153492EBI-73995,EBI-1384149
    SCRIBQ141602EBI-73995,EBI-357345

    Protein-protein interaction databases

    BioGridi111581. 114 interactions.
    DIPiDIP-30985N.
    IntActiP27361. 59 interactions.
    MINTiMINT-99599.
    STRINGi9606.ENSP00000263025.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni39 – 413
    Beta strandi42 – 498
    Beta strandi55 – 617
    Turni62 – 654
    Beta strandi66 – 738
    Helixi79 – 9416
    Beta strandi104 – 1074
    Turni112 – 1143
    Beta strandi118 – 1236
    Beta strandi126 – 1283
    Helixi129 – 1357
    Helixi140 – 15920
    Beta strandi171 – 1744
    Beta strandi180 – 1823
    Helixi193 – 1953
    Helixi208 – 2103
    Helixi214 – 2174
    Helixi225 – 24016
    Helixi252 – 26110
    Turni266 – 2683
    Helixi275 – 2839
    Helixi292 – 2954
    Helixi301 – 31010
    Turni315 – 3173
    Helixi321 – 3255
    Helixi328 – 3303
    Turni331 – 3333
    Helixi336 – 3383
    Helixi352 – 3543
    Helixi357 – 36711
    Helixi369 – 3713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZOQX-ray2.39A/B1-379[»]
    ProteinModelPortaliP27361.
    SMRiP27361. Positions 24-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27361.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 330289Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi202 – 2043TXY

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiP27361.
    KOiK04371.
    OMAiAEMLSNK.
    OrthoDBiEOG7M3J0K.
    PhylomeDBiP27361.
    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_dom.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P27361-1) [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

    MAAAAAQGGG GGEPRRTEGV GPGVPGEVEM VKGQPFDVGP RYTQLQYIGE    50
    GAYGMVSSAY DHVRKTRVAI KKISPFEHQT YCQRTLREIQ ILLRFRHENV 100
    IGIRDILRAS TLEAMRDVYI VQDLMETDLY KLLKSQQLSN DHICYFLYQI 150
    LRGLKYIHSA NVLHRDLKPS NLLINTTCDL KICDFGLARI ADPEHDHTGF 200
    LTEYVATRWY RAPEIMLNSK GYTKSIDIWS VGCILAEMLS NRPIFPGKHY 250
    LDQLNHILGI LGSPSQEDLN CIINMKARNY LQSLPSKTKV AWAKLFPKSD 300
    SKALDLLDRM LTFNPNKRIT VEEALAHPYL EQYYDPTDEP VAEEPFTFAM 350
    ELDDLPKERL KELIFQETAR FQPGVLEAP 379
    Length:379
    Mass (Da):43,136
    Last modified:January 23, 2007 - v4
    Checksum:iE6020CE413EC41F7
    GO
    Isoform 2 (identifier: P27361-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         259-302: Missing.

    Show »
    Length:335
    Mass (Da):38,275
    Checksum:i54DA760A09F1F2F5
    GO
    Isoform 3 (identifier: P27361-3) [UniParc]FASTAAdd to Basket

    Also known as: ERK1b

    The sequence of this isoform differs from the canonical sequence as follows:
         340-379: PVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP → VGQSPAAVGLGAGEQGGT

    Show »
    Length:357
    Mass (Da):40,088
    Checksum:iF2C6D29C623AC072
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti174 – 1741I → S in CAA42744. (PubMed:7687743)Curated
    Sequence conflicti174 – 1741I → S in AAK52329. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti323 – 3231E → K.1 Publication
    Corresponds to variant rs55859133 [ dbSNP | Ensembl ].
    VAR_042253

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei259 – 30244Missing in isoform 2. 1 PublicationVSP_041906Add
    BLAST
    Alternative sequencei340 – 37940PVAEE…VLEAP → VGQSPAAVGLGAGEQGGT in isoform 3. 1 PublicationVSP_041907Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60188 mRNA. Translation: CAA42744.1.
    AY033607 mRNA. Translation: AAK52329.1.
    DQ399291 mRNA. Translation: ABD60302.1.
    EU332853 Genomic DNA. Translation: ABY87542.1.
    AC012645 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW79912.1.
    CH471238 Genomic DNA. Translation: EAW79915.1.
    BC013992 mRNA. Translation: AAH13992.1.
    M84490 mRNA. Translation: AAA36142.1.
    Z11696 mRNA. Translation: CAA77754.1.
    CCDSiCCDS10672.1. [P27361-1]
    CCDS42148.1. [P27361-2]
    CCDS42149.1. [P27361-3]
    PIRiA48082.
    RefSeqiNP_001035145.1. NM_001040056.2. [P27361-3]
    NP_001103361.1. NM_001109891.1. [P27361-2]
    NP_002737.2. NM_002746.2. [P27361-1]
    UniGeneiHs.861.

    Genome annotation databases

    EnsembliENST00000263025; ENSP00000263025; ENSG00000102882. [P27361-1]
    ENST00000322266; ENSP00000327293; ENSG00000102882. [P27361-2]
    ENST00000395199; ENSP00000378625; ENSG00000102882. [P27361-3]
    ENST00000395202; ENSP00000378628; ENSG00000102882. [P27361-2]
    GeneIDi5595.
    KEGGihsa:5595.
    UCSCiuc002dwr.3. human. [P27361-1]
    uc002dwt.3. human. [P27361-3]
    uc002dwv.4. human. [P27361-2]

    Polymorphism databases

    DMDMi232066.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60188 mRNA. Translation: CAA42744.1 .
    AY033607 mRNA. Translation: AAK52329.1 .
    DQ399291 mRNA. Translation: ABD60302.1 .
    EU332853 Genomic DNA. Translation: ABY87542.1 .
    AC012645 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW79912.1 .
    CH471238 Genomic DNA. Translation: EAW79915.1 .
    BC013992 mRNA. Translation: AAH13992.1 .
    M84490 mRNA. Translation: AAA36142.1 .
    Z11696 mRNA. Translation: CAA77754.1 .
    CCDSi CCDS10672.1. [P27361-1 ]
    CCDS42148.1. [P27361-2 ]
    CCDS42149.1. [P27361-3 ]
    PIRi A48082.
    RefSeqi NP_001035145.1. NM_001040056.2. [P27361-3 ]
    NP_001103361.1. NM_001109891.1. [P27361-2 ]
    NP_002737.2. NM_002746.2. [P27361-1 ]
    UniGenei Hs.861.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZOQ X-ray 2.39 A/B 1-379 [» ]
    ProteinModelPortali P27361.
    SMRi P27361. Positions 24-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111581. 114 interactions.
    DIPi DIP-30985N.
    IntActi P27361. 59 interactions.
    MINTi MINT-99599.
    STRINGi 9606.ENSP00000263025.

    Chemistry

    BindingDBi P27361.
    ChEMBLi CHEMBL1907606.
    DrugBanki DB01169. Arsenic trioxide.
    DB01064. Isoproterenol.
    DB00641. Simvastatin.
    DB00605. Sulindac.
    GuidetoPHARMACOLOGYi 1494.

    PTM databases

    PhosphoSitei P27361.

    Polymorphism databases

    DMDMi 232066.

    Proteomic databases

    MaxQBi P27361.
    PaxDbi P27361.
    PRIDEi P27361.

    Protocols and materials databases

    DNASUi 5595.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263025 ; ENSP00000263025 ; ENSG00000102882 . [P27361-1 ]
    ENST00000322266 ; ENSP00000327293 ; ENSG00000102882 . [P27361-2 ]
    ENST00000395199 ; ENSP00000378625 ; ENSG00000102882 . [P27361-3 ]
    ENST00000395202 ; ENSP00000378628 ; ENSG00000102882 . [P27361-2 ]
    GeneIDi 5595.
    KEGGi hsa:5595.
    UCSCi uc002dwr.3. human. [P27361-1 ]
    uc002dwt.3. human. [P27361-3 ]
    uc002dwv.4. human. [P27361-2 ]

    Organism-specific databases

    CTDi 5595.
    GeneCardsi GC16M030125.
    HGNCi HGNC:6877. MAPK3.
    HPAi CAB002683.
    HPA003995.
    HPA005700.
    MIMi 601795. gene.
    neXtProti NX_P27361.
    PharmGKBi PA30622.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi P27361.
    KOi K04371.
    OMAi AEMLSNK.
    OrthoDBi EOG7M3J0K.
    PhylomeDBi P27361.
    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_115831. ISG15 antiviral mechanism.
    REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_1391. ERK1 activation.
    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_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_2232. RNA Polymerase I Promoter Opening.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.
    REACT_508. Signal attenuation.
    REACT_9470. Signaling by FGFR.
    SignaLinki P27361.

    Miscellaneous databases

    EvolutionaryTracei P27361.
    GeneWikii MAPK3.
    GenomeRNAii 5595.
    NextBioi 21714.
    PROi P27361.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27361.
    Bgeei P27361.
    CleanExi HS_MAPK3.
    Genevestigatori P27361.

    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_dom.
    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

    1. "Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1."
      Charest D.L., Jirik F., Harder K., Pelech S.L., Mordret G.
      Mol. Cell. Biol. 13:4679-4690(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Hepatoma.
    2. "Properties of human ERK1b."
      Aebersold D.M., Yung Y., Seger R.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    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).
    4. SeattleSNPs variation discovery resource
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Lymph.
    8. Bienvenut W.V., Dhillon A.S., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 33-41; 88-94; 117-131; 212-220; 279-287; 303-318 AND 360-370, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    9. "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] OF 14-379 (ISOFORM 1).
    10. "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] OF 25-379 (ISOFORM 1).
    11. "Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase."
      Marklund U., Brattsand G., Shingler V., Gullberg M.
      J. Biol. Chem. 268:15039-15047(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STMN1.
    12. "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.
    13. "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates."
      Fukunaga R., Hunter T.
      EMBO J. 16:1921-1933(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MKNK1/MNK1.
    14. "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.
    15. "Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes."
      Chevet E., Wong H.N., Gerber D., Cochet C., Fazel A., Cameron P.H., Gushue J.N., Thomas D.Y., Bergeron J.J.
      EMBO J. 18:3655-3666(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CANX, INTERACTION WITH CANX.
    16. "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.
    17. "Identification of a cytoplasmic-retention sequence in ERK2."
      Rubinfeld H., Hanoch T., Seger R.
      J. Biol. Chem. 274:30349-30352(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MAP2K1/MEK1, DOMAIN.
    18. "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.
    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. "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.
    22. "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.
    23. "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: INTERACTION WITH DAPK1.
    24. "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.
    25. "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.
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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.
    31. "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.
    32. "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.
    33. "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: INTERACTION WITH TPR.
    34. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. "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].
    36. "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.
    37. "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-204, DEPHOSPHORYLATION AT TYR-204 BY PTPRJ.
    38. "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: INTERACTION WITH SGK1.
    39. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "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-207, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
    41. "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.
    42. "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.
    43. "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-202 AND TYR-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    44. "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.
    45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    46. "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.
    47. "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-202 AND TYR-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    48. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    49. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    50. Cited for: X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS), PHOSPHORYLATION AT TYR-204.
    51. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-323.

    Entry informationi

    Entry nameiMK03_HUMAN
    AccessioniPrimary (citable) accession number: P27361
    Secondary accession number(s): A8CZ58, B0LPG3, Q8NHX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 170 of the entry and version 4 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3