UniProt ID | TAOK1_MOUSE | |
---|---|---|
UniProt AC | Q5F2E8 | |
Protein Name | Serine/threonine-protein kinase TAO1 | |
Gene Name | Taok1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1001 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade (By similarity).. | |
Protein Sequence | MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGVGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDASDDKSELDMMEGDHTVMSNSSVIHLKPEEENYQEEGDPRTRASDPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMANEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASSWSHNPTGGPGPHWGHPMGGTPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSMGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Phosphorylation | PSTNRAGSLKDPEIA CCCCCCCCCCCHHHH | 31.12 | 26824392 | |
11 | Ubiquitination | TNRAGSLKDPEIAEL CCCCCCCCCHHHHHH | 73.30 | - | |
43 | Phosphorylation | HGSFGAVYFARDVRT CCCCCCEEEEECCCC | 7.32 | 22817900 | |
88 | Phosphorylation | QRIKHPNSIEYKGCY HHCCCCCCCCCCEEE | 22.65 | 26643407 | |
91 | Phosphorylation | KHPNSIEYKGCYLRE CCCCCCCCCEEEHHH | 15.83 | 26643407 | |
172 | Phosphorylation | VKLADFGSASMASPA EEECCCCCCCCCCCC | 19.71 | 23649490 | |
174 | Phosphorylation | LADFGSASMASPANS ECCCCCCCCCCCCCC | 19.31 | 23649490 | |
177 | Phosphorylation | FGSASMASPANSFVG CCCCCCCCCCCCCCC | 18.86 | 23649490 | |
181 | Phosphorylation | SMASPANSFVGTPYW CCCCCCCCCCCCCCC | 24.34 | 22322096 | |
185 | Phosphorylation | PANSFVGTPYWMAPE CCCCCCCCCCCCCCH | 14.11 | 23649490 | |
187 | Phosphorylation | NSFVGTPYWMAPEVI CCCCCCCCCCCCHHE | 13.98 | 23737553 | |
277 | Ubiquitination | PTSEELLKHMFVLRE CCHHHHHHHHHHHCC | 45.72 | - | |
309 | Phosphorylation | RELDNLQYRKMKKLL HHHHHHHHHHHHHHH | 18.50 | 29514104 | |
314 | Ubiquitination | LQYRKMKKLLFQEAH HHHHHHHHHHHHHHH | 47.10 | - | |
414 | Phosphorylation | QEEGDPRTRASDPQS CCCCCCCCCCCCCCC | 35.66 | 29472430 | |
417 | Phosphorylation | GDPRTRASDPQSPPQ CCCCCCCCCCCCCCC | 46.67 | 25619855 | |
421 | Phosphorylation | TRASDPQSPPQVSRH CCCCCCCCCCCHHHC | 43.89 | 27087446 | |
426 | Phosphorylation | PQSPPQVSRHKSHYR CCCCCCHHHCHHHHC | 24.34 | 25619855 | |
432 | Phosphorylation | VSRHKSHYRNREHFA HHHCHHHHCCHHHHH | 19.37 | 29514104 | |
440 | Phosphorylation | RNREHFATIRTASLV CCHHHHHHHHHHHHH | 15.28 | 26824392 | |
443 | Phosphorylation | EHFATIRTASLVTRQ HHHHHHHHHHHHHHH | 19.42 | 22817900 | |
445 | Phosphorylation | FATIRTASLVTRQMQ HHHHHHHHHHHHHHH | 23.82 | 25521595 | |
448 | Phosphorylation | IRTASLVTRQMQEHE HHHHHHHHHHHHHHH | 22.07 | 22324799 | |
458 | Phosphorylation | MQEHEQDSELREQMS HHHHHHCHHHHHHHH | 37.92 | 25338131 | |
465 | Phosphorylation | SELREQMSGYKRMRR HHHHHHHHHHHHHHH | 38.37 | 25338131 | |
480 | Phosphorylation | QHQKQLMTLENKLKA HHHHHHHHHHHHHHH | 39.24 | 25521595 | |
575 | Phosphorylation | EELNENQSTPKKEKQ HHHHHCCCCCHHHHH | 59.25 | 25619855 | |
576 | Phosphorylation | ELNENQSTPKKEKQE HHHHCCCCCHHHHHH | 29.39 | 25619855 | |
610 | Phosphorylation | LLRRQRQYLELECRR HHHHHHHHHHHHHHH | 12.34 | 29514104 | |
669 | Phosphorylation | LEFRHLNTIQKMRCE HHHHHHHHHHHHHHH | 31.01 | 29899451 | |
818 | Ubiquitination | LLNAYQSKIKMQAEA HHHHHHHHHHHHHHH | 30.71 | - | |
958 | Phosphorylation | MQGVPRGSSMGVRNS CCCCCCCCCCCCCCC | 20.59 | 26643407 | |
959 | Phosphorylation | QGVPRGSSMGVRNSP CCCCCCCCCCCCCCH | 23.52 | 26643407 | |
965 | Phosphorylation | SSMGVRNSPQALRRT CCCCCCCCHHHHHHH | 14.07 | 25521595 | |
972 | Phosphorylation | SPQALRRTASGGRTE CHHHHHHHCCCCCCC | 20.81 | 29550500 | |
974 | Phosphorylation | QALRRTASGGRTEQG HHHHHHCCCCCCCCC | 40.96 | 25266776 | |
978 | Phosphorylation | RTASGGRTEQGMSRS HHCCCCCCCCCCCCC | 35.62 | 29550500 | |
983 | Phosphorylation | GRTEQGMSRSTSVTS CCCCCCCCCCEEECC | 29.88 | 29514104 | |
985 | Phosphorylation | TEQGMSRSTSVTSQI CCCCCCCCEEECCCC | 20.09 | 30635358 | |
986 | Phosphorylation | EQGMSRSTSVTSQIS CCCCCCCEEECCCCC | 26.55 | 30635358 | |
987 | Phosphorylation | QGMSRSTSVTSQISN CCCCCCEEECCCCCC | 25.33 | 23684622 | |
989 | Phosphorylation | MSRSTSVTSQISNGS CCCCEEECCCCCCCC | 18.06 | 30635358 | |
990 | Phosphorylation | SRSTSVTSQISNGSH CCCEEECCCCCCCCC | 24.30 | 30635358 | |
993 | Phosphorylation | TSVTSQISNGSHMSY EEECCCCCCCCCCCC | 27.74 | 22006019 | |
996 | Phosphorylation | TSQISNGSHMSYT-- CCCCCCCCCCCCC-- | 21.92 | 25338131 | |
999 | Phosphorylation | ISNGSHMSYT----- CCCCCCCCCC----- | 21.87 | 25338131 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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440 | T | Phosphorylation | Kinase | MST3 | Q9Y6E0 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TAOK1_MOUSE !! |
* 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 TAOK1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of TAOK1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, AND MASSSPECTROMETRY. | |
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-421, AND MASSSPECTROMETRY. |