MK01_XENLA - dbPTM
MK01_XENLA - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MK01_XENLA
UniProt AC P26696
Protein Name Mitogen-activated protein kinase 1
Gene Name mapk1
Organism Xenopus laevis (African clawed frog).
Sequence Length 361
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm . Cytoplasm, cytoskeleton, spindle . Associated with the spindle during prometaphase and metaphase in cultured XTC cells.
Protein Description Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the MAPK/ERK cascade. Depending on the cellular context, this 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. Many of the 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. Phosphorylates microtubule-associated protein 2 (MAP2), myelin basic protein (MBP) and Elk-1. Phosphorylates dual specificity protein phosphatase 1 (DUSP1) during meiosis, increasing its stability. Activated by M phase promoting factor (MPF). Plays a role in the spindle assembly checkpoint..
Protein Sequence MAAAGAASNPGGGPEMVRGQAFDVGPRYINLAYIGEGAYGMVCSAHDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFKHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADPKALDLLDKMLTFNPHKRIEVEAALAHPYLEQYYDPSDEPVAEAPFKFEMELDDLPKETLKELIFEETARFQPGY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
188PhosphorylationHDHTGFLTEYVATRW
CCCCCHHHHHHHHCC
24.021313186
190PhosphorylationHTGFLTEYVATRWYR
CCCHHHHHHHHCCCC
7.081313186

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MK01_XENLA !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MK01_XENLA !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MK01_XENLA !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MK01_XENLA !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MK01_XENLA

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Requirements for phosphorylation of MAP kinase during meiosis inXenopus oocytes.";
Posada J., Cooper J.A.;
Science 255:212-215(1992).
Cited for: PHOSPHORYLATION AT THR-188 AND TYR-190, MUTAGENESIS OF LYS-57; ILE-86;THR-188 AND TYR-190, AND ENZYME REGULATION.

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