TAOK2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TAOK2_MOUSE
• UniProt AC: Q6ZQ29
• Protein Name: Serine/threonine-protein kinase TAO2
• Gene Name: Taok2
• Organism: Mus musculus (Mouse).
• Sequence Length: 1240
• Subcellular Localization: Cytoplasmic vesicle membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton. Found to be perinuclear and localized to vesicular compartment..; Isoform 2: Cell projection, dendrite. In dendrites, colocalizes with PCDH8..
• Protein Description: Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. 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 upstream MAP2K3 and MAP2K6 kinases. May affect microtubule organization and stability. May play a role in the osmotic stress-MAPK8 pathway. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14/p38 MAPK activation (By similarity)..
• Protein Sequence: MPAGGRAGSLKDPDVAELFFKDDPEKLFSDLREIGHGSFGAVYFARDVRNSEVVAIKKMSYSGKQSNEKWQDIIKEVRFLQKLRHPNTIQYRGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAVTHGALQGLAYLHSHNMIHRDVKAGNILLSEPGLVKLGDFGSASIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSEVLLKHRFVLRERPPTVIMDLIQRTKDAVRELDNLQYRKMKKILFQEAPNGPGAEAPEEEELTPCSQEAEPYTHRAGTLTSLESSHSVPSMSISASSQSSSVNSLADASDNEEEEEEEEEEEEEEEEEGPESREMAMMQEGEHTVTSHSSIIHRLPGSDNLYDDPYQPEMTPGPLQPPAAPPTSTSSSARRRAYCRNRDHFATIRTASLVSRQIQEHEQDSALREQLSGYKRMRRQHQKQLLALESRLRGEREEHSGRLQRELEAQRAGFGTEAEKLARRHQAIGEKEARAAQAEERKFQQHILGQQKKELAALLEAQKRTYKLRKEQLKEELQENPSTPKREKAEWLLRQKEQLQQCQAEEEAGLLRRQRQYFELQCRQYKRKMLLARHSLDQDLLREDLNKKQTQKDLECALLLRQHEATRELELRQLQAVQRTRAELTRLQHQTELGNQLEYNKRREQELRQKHAAQVRQQPKSLKVRAGQLPMGLPATGALGPLSTGTPSEEQPCSSGQEAILDQRMLGEEEEAVPERRILGKEGTTLEPEEQRILGEEMGTFSSSPQKHRSLANEEDWDISEEMKEIRVPSLASQERNIIGQEEAAAWSLWEKEGGNLVDVEFKLGWVQGPVLTPVPEEEEEEEEEGGAPIGTHRDPGDGCPSPDIPPEPPPSHLRQYPTSQLPGLLSHGLLAGLSFAVGSSSGLLPLLLLLLLPLLAAQGGGGLQAALLALEVGLVGLGASYLFLCTALHLPPGLFLLLAQGTALLAVLSLSWRRGLMGVPLGLGAAWLLAWPSLALPLAAMAAGGKWVRQQGPQMRRGISRLWLRILLRLSPMVFRALQGCGAVGDRGLFALYPKTNKNGFRSRLPVPWPRQGNPRTTQHPLAQLTRVWAVCKGWNWRLARASHRLASCLPPWAVHILASWGLLKGERPSRIPRLLPRSQRRLGLSASRQLPPGTVAGRRSQTRRTLPPWR

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
9	Phosphorylation	PAGGRAGSLKDPDVA CCCCCCCCCCCCCHH	31.12	26824392
43	Phosphorylation	HGSFGAVYFARDVRN CCCCCCEEEEECCCC	7.32	18034455
51	Phosphorylation	FARDVRNSEVVAIKK EEECCCCCEEEEEEE	22.62	25338131
160	Phosphorylation	KAGNILLSEPGLVKL CCCCEEECCCCEEEC	38.00	28285833
174	Phosphorylation	LGDFGSASIMAPANS CCCCCCCEEEECCCC	18.00	23649490
181	Phosphorylation	SIMAPANSFVGTPYW EEEECCCCCCCCCCC	24.34	23649490
309	Phosphorylation	RELDNLQYRKMKKIL HHHHHHHHHHHHHHH	18.50	29514104
419	Phosphorylation	EGEHTVTSHSSIIHR CCCCEECCCHHHHHC	19.62	29899451
422	Phosphorylation	HTVTSHSSIIHRLPG CEECCCHHHHHCCCC	21.82	-
466	Phosphorylation	SSARRRAYCRNRDHF CHHHHHHHHCCCCCH	7.07	29514104
475	Phosphorylation	RNRDHFATIRTASLV CCCCCHHHHHHHHHH	15.28	27600695
478	Phosphorylation	DHFATIRTASLVSRQ CCHHHHHHHHHHHHH	19.42	26745281
480	Phosphorylation	FATIRTASLVSRQIQ HHHHHHHHHHHHHHH	28.79	24453211
483	Phosphorylation	IRTASLVSRQIQEHE HHHHHHHHHHHHHHH	24.62	28066266
493	Phosphorylation	IQEHEQDSALREQLS HHHHHHCHHHHHHHH	28.97	25521595
500	Phosphorylation	SALREQLSGYKRMRR HHHHHHHHHHHHHHH	39.51	29514104
502	Phosphorylation	LREQLSGYKRMRRQH HHHHHHHHHHHHHHH	7.64	29899451
610	Phosphorylation	EELQENPSTPKREKA HHHHHCCCCCHHHHH	69.77	-
611	Phosphorylation	ELQENPSTPKREKAE HHHHCCCCCHHHHHH	33.80	-
663	Phosphorylation	KMLLARHSLDQDLLR HHHHHHHCCCHHHHH	28.25	25521595
675	Acetylation	LLREDLNKKQTQKDL HHHHHHCHHHHHHHH	54.26	19857369
738	Acetylation	REQELRQKHAAQVRQ HHHHHHHHHHHHHHH	28.86	8276525
748	Acetylation	AQVRQQPKSLKVRAG HHHHHCCCCCCCCCC	65.17	8276539
782	Phosphorylation	PSEEQPCSSGQEAIL CCCCCCCCCCHHHHH	44.16	-
830	Phosphorylation	GEEMGTFSSSPQKHR HCCCCCCCCCHHHHH	29.73	26643407
831	Phosphorylation	EEMGTFSSSPQKHRS CCCCCCCCCHHHHHH	41.67	26643407
832	Phosphorylation	EMGTFSSSPQKHRSL CCCCCCCCHHHHHHH	30.10	26643407
993 (in isoform 2)	Phosphorylation	-	28.06	29514104
995 (in isoform 2)	Phosphorylation	-	7.08	29514104
997 (in isoform 2)	Phosphorylation	-	4.36	29514104
999 (in isoform 2)	Methylation	-	5.74	24129315
1009 (in isoform 2)	Phosphorylation	-	22.14	26745281
1018 (in isoform 2)	Phosphorylation	-	33.55	25521595
1021 (in isoform 2)	Phosphorylation	-	59.48	25521595
1022 (in isoform 2)	Phosphorylation	-	27.41	30372032
1037 (in isoform 2)	Phosphorylation	-	3.38	20415495
1039 (in isoform 2)	Phosphorylation	-	5.07	21183079
1041 (in isoform 2)	Phosphorylation	-	10.17	25177544
1044 (in isoform 2)	Phosphorylation	-	16.08	21183079
1054 (in isoform 2)	Phosphorylation	-	10.66	29514104
1230	Phosphorylation	GTVAGRRSQTRRTLP CCCCCCCCCCCCCCC	34.25	24719451
1232	Phosphorylation	VAGRRSQTRRTLPPW CCCCCCCCCCCCCCC	24.30	24719451

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
475	T	Phosphorylation	Kinase	MST3	Q9Y6E0	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1037	S	Phosphorylation	[Isoform 2]: Phosphorylated on Ser-1037 by MAPK14.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TAOK2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLUS_HUMAN	CLU	physical	26496610
IF4G1_HUMAN	EIF4G1	physical	26496610
RENT1_HUMAN	UPF1	physical	26496610
RCOR3_HUMAN	RCOR3	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
PPR18_HUMAN	PPP1R18	physical	26496610

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND MASSSPECTROMETRY.
PubMed: 18034455