TPX2A_XENLA - dbPTM
TPX2A_XENLA - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPX2A_XENLA
UniProt AC Q6NUF4
Protein Name Targeting protein for Xklp2-A
Gene Name tpx2-a
Organism Xenopus laevis (African clawed frog).
Sequence Length 716
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Localizes during metaphase on spindle microtubules, with a strong enrichment at spindle poles. Localizes to the minus ends of spindle pole and aster microtubules in a d
Protein Description Spindle assembly factor. Required for normal assembly of mitotic spindles. Mediates the binding kif15 and aurka to spindle microtubules. Required for targeting kif15 to microtubule minus ends. Activates aurka by promoting its autophosphorylation and protects the phosphorylated residue against dephosphorylation (By similarity)..
Protein Sequence MEDTQDTYSYDAPSIFNFSSFHEDHNADSWFDQVTNAENIPPDQRRLSETSVNTEQNSKVEPVQTTPSKDDVSNSATHVCDVKSQSKRSSRRMSKKHRQKLLVKMKDTHLEKETAPPEYPPCKKLKGSSSKGRHAPVIKSQSTSSHHSMTSPKPKAQLTMPSTPTVLKRRNVLVKAKNSEEQELEKMQELQKEMLENLKKNEHSMKVAITGAGQPVKTFIPVTKPVDFHFKTDDRLKRTANQPEGDGYKAVDFASELRKHPPSPVQVTKGGHTVPKPFNLSKGKRKHEEASDYVSTAEQVIAFYKRTPARYHLRSRQREMEGPSPVKMIKTKLTNPKTPLLQTKGRHRPVTCKSAAELEAEELEMINQYKFKAQELDTRILEGGPVLLKKPLVKEPTKAIGFDLEIEKRIQQREKKEEIEEETFTFHSRPCPSKMLTDVVGVPLKKLLPVTVPQSPAFALKNRVRIPAQEEKQEEMVPVIKATRMPHYGVPFKPKLVEQRQVDVCPFSFCDRDKERQLQKEKRLDELRKDEVPKFKAQPLPQFDNIRLPEKKVKMPTQQEPFDLEIEKRGASKLQRWQQQIQEELKQQKEMVVFKARPNTVVHQEPFVPKKENRSLTESLSGSIVQEGFELATAKRAKERQEFDKCLAETEAQKSLLEEEIRKRREEEEKEEISQLRQELVHKAKPIRKYRAVEVKASDVPLTVPRSPNFSDRFKC
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
48PhosphorylationPPDQRRLSETSVNTE
CCCHHHHHCCCCCCC
36.7014701852
90PhosphorylationKSQSKRSSRRMSKKH
CCCCHHHHHHHCHHH
28.1214701852
94PhosphorylationKRSSRRMSKKHRQKL
HHHHHHHCHHHHHHH
36.4214701852
204PhosphorylationNLKKNEHSMKVAITG
HHHHCCCCCEEEECC
17.7019556869

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
48SPhosphorylationKinaseAURKAO14965
GPS
48SPhosphorylationKinaseAURKA-PhosphoELM
90SPhosphorylationKinaseAURKAO14965
GPS
90SPhosphorylationKinaseAURKA-PhosphoELM
94SPhosphorylationKinaseAURKAO14965
GPS
94SPhosphorylationKinaseAURKA-PhosphoELM
204SPhosphorylationKinasePLK1P70032
Uniprot
204SPhosphorylationKinasePLK1-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPX2A_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 TPX2A_XENLA !!

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

Oops, there are no PPI records of TPX2A_XENLA !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPX2A_XENLA

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of TPX2 by Plx1 enhances activation of Aurora A.";
Eckerdt F., Pascreau G., Phistry M., Lewellyn A.L.,DePaoli-Roach A.A., Maller J.L.;
Cell Cycle 8:2413-2419(2009).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-204, MUTAGENESIS OF SER-204, ANDINTERACTION WITH PLK1.

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