PMYT1_XENLA - dbPTM
PMYT1_XENLA - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMYT1_XENLA
UniProt AC Q91618
Protein Name Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
Gene Name pkmyt1
Organism Xenopus laevis (African clawed frog).
Sequence Length 548
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein . Golgi apparatus membrane
Peripheral membrane protein .
Protein Description Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins. Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. May be a downstream target of Notch signaling pathway during eye development..
Protein Sequence MPVPGDDMGETPLTRTPIPMPAYFSQAEQSFSLKKRGRSLCYTLPPRPPVKSALPVSRIFPNKQRSWSQPRPQSVSFRSPQNKTPASKLYDQSKGDTFFKQCFKSICKLGRGSFGEVYKVQSLEDGCFYAVKRSVSPFRGESDRQRKLQEVRKHERVGEHPNCLRFVRAWEEKRMLYLQTELCAGSLQQHSEEFAGSLPPRRVWNITCDLLHGLKHLHDRNLLHLDIKPANVFISFSGVCKLGDFGLMVELDGTEGSGEAQEGDPRYMAPELLDGIFSKAADVFSLGMSLLEVACNMELPKGGDGWQQLRQGHLPTEFTSDLPPDFLKVLSAMLEPDYRRRATVDWLLSLPAIRNAERWRMVTLAQERTLGKIIAVYQFIVWLLSFVFQWLNRPVIGFLHYCGLRALPRSPPCSPFPNHLGESSFSSDWDDESLGDDVFEVPPSPLATHRNLTYHGQELIGRHSPDLLSRPSLGSTSTPRNLSPEFSMRKRSALPLTPNVSRISQDSTGKSRSPSTSHSSSGFVDAEVQRTLFLPRNLLGMFDDATEQ
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
478PhosphorylationPSLGSTSTPRNLSPE
CCCCCCCCCCCCCCC
26.7615692562

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
66SPhosphorylationKinasePKMYT1-GPS
76SPhosphorylationKinasePKMYT1-GPS
410SPhosphorylationKinaseCDK1-GPS
410SPhosphorylationKinaseCDK2-GPS
414SPhosphorylationKinaseCDK1-GPS
414SPhosphorylationKinaseCDK2-GPS
424SPhosphorylationKinasePLK1-GPS
444SPhosphorylationKinaseCDK1-GPS
444SPhosphorylationKinaseCDK2-GPS
478TPhosphorylationKinaseCDK2-GPS
478TPhosphorylationKinaseCDK1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMYT1_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 PMYT1_XENLA !!

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

Oops, there are no PPI records of PMYT1_XENLA !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMYT1_XENLA

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The Polo-like kinase Plx1 interacts with and inhibits Myt1 afterfertilization of Xenopus eggs.";
Inoue D., Sagata N.;
EMBO J. 24:1057-1067(2005).
Cited for: PHOSPHORYLATION AT THR-478 BY CDK1, AND PHOSPHORYLATION BY PLK1.

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