MAPK1Mitogen-activated protein kinase 1

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P63086"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10617468"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10637505"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11154262"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12110590"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12356731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12792650"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12794087"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12974390"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15184391"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15241487"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15616583"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15664191"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15788397"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15952796"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16581800"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18794356"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19265199"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19879846"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22033920"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "26942675"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32721402"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "35831023"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "7588608"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "8622688"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9480836"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9596579"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9649500"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9687510"
        },
        {
          "evidenceCode": "ECO:0000303",
          "source": "PubMed",
          "id": "15526160"
        },
        {
          "evidenceCode": "ECO:0000303",
          "source": "PubMed",
          "id": "16393692"
        },
        {
          "evidenceCode": "ECO:0000303",
          "source": "PubMed",
          "id": "19565474"
        },
        {
          "evidenceCode": "ECO:0000303",
          "source": "PubMed",
          "id": "21779493"
        }
      ],
      "value": "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 also plays 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 FXR1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2, GLI1 or GRB10) (PubMed:35831023). 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 response to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity). Phosphorylates phosphoglycerate kinase PGK1 under hypoxic conditions to promote its targeting to the mitochondrion and suppress the formation of acetyl-coenzyme A from pyruvate (PubMed:26942675). Phosphorylates GJA1 at 'Ser-279' and 'Ser-282' resulting in an increase in GJA1 ubiquitination and ultimately lysosomal degradation (By similarity). Acts as a positive regulator of smoothened signaling by mediating phosphorylation of GLI1 in response to smoothened activation, promoting its dissociation from SUFU inhibitor and translocation to the nucleus (PubMed:35831023)"
    }
  ],
  "commentType": "FUNCTION"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19879846"
        }
      ],
      "value": "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"
    }
  ],
  "commentType": "FUNCTION"
}

{
  "commentType": "CATALYTIC ACTIVITY",
  "reaction": {
    "name": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)",
    "reactionCrossReferences": [
      {
        "database": "Rhea",
        "id": "RHEA:17989"
      },
      {
        "database": "Rhea",
        "id": "RHEA-COMP:9863"
      },
      {
        "database": "Rhea",
        "id": "RHEA-COMP:11604"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:15378"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:29999"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:30616"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:83421"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:456216"
      }
    ],
    "ecNumber": "2.7.11.24",
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "26942675"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "35831023"
      }
    ]
  }
}

{
  "commentType": "CATALYTIC ACTIVITY",
  "reaction": {
    "name": "L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)",
    "reactionCrossReferences": [
      {
        "database": "Rhea",
        "id": "RHEA:46608"
      },
      {
        "database": "Rhea",
        "id": "RHEA-COMP:11060"
      },
      {
        "database": "Rhea",
        "id": "RHEA-COMP:11605"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:15378"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:30013"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:30616"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:61977"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:456216"
      }
    ],
    "ecNumber": "2.7.11.24"
  }
}

{
  "commentType": "COFACTOR",
  "cofactors": [
    {
      "name": "Mg(2+)",
      "evidences": [
        {
          "evidenceCode": "ECO:0000250"
        }
      ],
      "cofactorCrossReference": {
        "database": "ChEBI",
        "id": "CHEBI:18420"
      }
    }
  ]
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12356731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19060905"
        }
      ],
      "value": "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 DUSP1, DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors"
    }
  ],
  "commentType": "ACTIVITY REGULATION"
}

Eukaryota → Metazoa → Chordata → Craniata → Vertebrata → Euteleostomi → Mammalia → Eutheria → Euarchontoglires → Primates → Haplorrhini → Catarrhini → Hominidae → Homo

{
  "names": {
    "recommendedName": {
      "fullName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000305"
          }
        ],
        "value": "Mitogen-activated protein kinase 1"
      },
      "shortNames": [
        {
          "value": "MAP kinase 1"
        },
        {
          "value": "MAPK 1"
        }
      ],
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000269",
              "source": "PubMed",
              "id": "26942675"
            },
            {
              "evidenceCode": "ECO:0000269",
              "source": "PubMed",
              "id": "35831023"
            }
          ],
          "value": "2.7.11.24"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "ERT1"
        }
      },
      {
        "fullName": {
          "value": "Extracellular signal-regulated kinase 2"
        },
        "shortNames": [
          {
            "value": "ERK-2"
          }
        ]
      },
      {
        "fullName": {
          "value": "MAP kinase isoform p42"
        },
        "shortNames": [
          {
            "value": "p42-MAPK"
          }
        ]
      },
      {
        "fullName": {
          "value": "Mitogen-activated protein kinase 2"
        },
        "shortNames": [
          {
            "value": "MAP kinase 2"
          },
          {
            "value": "MAPK 2"
          }
        ]
      }
    ]
  },
  "genes": [
    {
      "geneName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000312",
            "source": "HGNC",
            "id": "HGNC:6871"
          }
        ],
        "value": "MAPK1"
      },
      "synonyms": [
        {
          "value": "ERK2"
        },
        {
          "value": "PRKM1"
        },
        {
          "value": "PRKM2"
        }
      ]
    }
  ]
}

{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Noonan syndrome 13",
    "diseaseAccession": "DI-05961",
    "acronym": "NS13",
    "description": "A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. NS13 inheritance is autosomal dominant. There is considerable variability in severity.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "619087"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "32721402"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250"
        },
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P63085"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16288922"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17274988"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18760948"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19053285"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19060905"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19265199"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19447520"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19494114"
        }
      ],
      "value": "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. Dephosphorylated by DUSP1 and DUSP2 at Thr-185 and Tyr-187 (By similarity) (PubMed:16288922)"
    }
  ],
  "commentType": "PTM"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250"
        }
      ],
      "value": "ISGylated"
    }
  ],
  "commentType": "PTM"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "34497368"
        }
      ],
      "value": "Ubiquitinated by TRIM15 via 'Lys-63'-linked ubiquitination; leading to activation. Deubiquitinated by CYLD"
    }
  ],
  "commentType": "PTM"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P63085"
        },
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P63086"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11912194"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12356731"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15358203"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15616583"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16139248"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16242327"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16581800"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17194451"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17300186"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18211802"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18296648"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18435604"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18760948"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18794356"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19060905"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19447520"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19827834"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22033920"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23847209"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "26942675"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32051553"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32721402"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9596579"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9788880"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9827991"
        }
      ],
      "value": "Binds both upstream activators and downstream substrates in multimolecular complexes. This interaction inhibits its tyrosine-kinase activity. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, NISCH, SGK1, and isoform 1 of NEK2. Interacts (via phosphorylated form) with TPR (via C-terminal region and phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases following EGF stimulation (PubMed:18794356). Interacts with MAP2K1 (PubMed:32721402). Interacts with DUSP6 (PubMed:32721402, PubMed:9596579). 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. Interacts with CDK2AP2. Interacts with CAVIN4 (By similarity). Interacts with DUSP7; the interaction enhances DUSP7 phosphatase activity (PubMed:9788880). Interacts with GIT1; this interaction is necessary for MAPK1 localization to focal adhesions (By similarity). Interacts with ZNF263 (PubMed:32051553). Interacts with phosphoglycerate kinase PGK1; the interaction is direct, occurs under hypoxic conditions, and promotes interaction between PGK1 and PIN1 (PubMed:26942675)"
    }
  ],
  "commentType": "SUBUNIT"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "8794306"
        }
      ],
      "value": "(Microbial infection) Interacts with HIV-1 Nef through its SH3 domain"
    }
  ],
  "commentType": "SUBUNIT"
}

{
  "texts": [
    {
      "value": "The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases"
    }
  ],
  "commentType": "DOMAIN"
}

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily"
    }
  ],
  "commentType": "SIMILARITY"
}

Alternative splicing

{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "isoformIds": [
        "P28482-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "isoformIds": [
        "P28482-2"
      ],
      "sequenceIds": [
        "VSP_047815"
      ],
      "isoformSequenceStatus": "Described"
    }
  ]
}

• P28482-1 · 1 · Displayed
  Complete source annotation

  {
    "name": {
      "value": "1"
    },
    "isoformIds": [
      "P28482-1"
    ],
    "isoformSequenceStatus": "Displayed"
  }

• P28482-2 · 2 · Described · VSP_047815
  Complete source annotation

  {
    "name": {
      "value": "2"
    },
    "isoformIds": [
      "P28482-2"
    ],
    "sequenceIds": [
      "VSP_047815"
    ],
    "isoformSequenceStatus": "Described"
  }

• UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:00.665019+00:00
• InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:00.619412+00:00
• AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:02.555561+00:00
• UniProt / The UniProt Consortium ↗ · 2026-11-09T11:41:00.665019+00:00
• InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:41:00.619412+00:00
• AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:41:02.555561+00:00
• UniProt overview ↗ · 2026-11-10T20:42:46.095741+00:00
• www.ebi.ac.uk ↗ · 2026-11-10T21:11:51.375871+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:51.424773+00:00
• www.ebi.ac.uk ↗ · 2026-11-10T21:11:51.461512+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:51.466342+00:00
• www.ebi.ac.uk ↗ · 2026-11-10T21:11:51.496852+00:00
• omabrowser.org ↗ · 2026-11-10T21:11:51.553144+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:51.567945+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:51.649742+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:52.349584+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:52.447985+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:53.184697+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:53.259969+00:00
• rest.uniprot.org ↗ · 2026-11-10T21:11:54.209129+00:00
• omabrowser.org ↗ · 2026-11-10T21:11:56.688922+00:00