TKTL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TKTL2_HUMAN
• UniProt AC: Q9H0I9
• Protein Name: Transketolase-like protein 2
• Gene Name: TKTL2
• Organism: Homo sapiens (Human).
• Sequence Length: 626
• Protein Description: Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis..
• Protein Sequence: MMANDAKPDVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLNLRKLHSDLERHPTPRLPFVDVATGSLGQGLGTACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQTNENLIPKSPVEDSPQISITDIKMTSPPAYKVGDKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIRTSQPETAVIYTPQENFEIGQAKVVRHGVNDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATGGRVITVEDHYREGGIGEAVCAAVSREPDILVHQLAVSGVPQRGKTSELLDMFGISTRHIIAAVTLTLMK

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
27	Phosphorylation	ANRLRIHSIRATCAS HHHHEEEEEEEEECC	16.05	24719451
123	Phosphorylation	LPFVDVATGSLGQGL CCEEEECCCCCCCCH	27.44	22210691
125	Phosphorylation	FVDVATGSLGQGLGT EEEECCCCCCCCHHH	25.60	22210691
240	Phosphorylation	SQVKNKPTAIVAKTF HHCCCCCCEEEEECC	30.53	-
280	Phosphorylation	AIVKLIESQIQTNEN HHHHHHHHHHHCCCC	26.11	30622161
284	Phosphorylation	LIESQIQTNENLIPK HHHHHHHCCCCCCCC	46.24	30622161
297	Phosphorylation	PKSPVEDSPQISITD CCCCCCCCCCEEEEE	12.75	30622161
301	Phosphorylation	VEDSPQISITDIKMT CCCCCCEEEEEEECC	17.75	30622161
303	Phosphorylation	DSPQISITDIKMTSP CCCCEEEEEEECCCC	25.53	30622161
308	Phosphorylation	SITDIKMTSPPAYKV EEEEEECCCCCCCCC	32.83	26552605
309	Phosphorylation	ITDIKMTSPPAYKVG EEEEECCCCCCCCCC	25.95	26552605
313	Phosphorylation	KMTSPPAYKVGDKIA ECCCCCCCCCCCCHH	16.39	26552605
324	Phosphorylation	DKIATQKTYGLALAK CCHHCHHHHHHHHHH	17.01	23403867
325	Phosphorylation	KIATQKTYGLALAKL CHHCHHHHHHHHHHH	19.71	23403867
410	Phosphorylation	QLRMGAISQANINLI HHHHCCCHHHCEEEE	23.78	-
542	Ubiquitination	VIDPFTIKPLDAATI EECCCCCCCCCHHHH	36.15	-
612	Phosphorylation	LLDMFGISTRHIIAA HHHHHCCCHHHHHHH	21.55	-
613	Phosphorylation	LDMFGISTRHIIAAV HHHHCCCHHHHHHHH	25.09	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TKTL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TKTL2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TKTL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPAC_HUMAN	ACP1	physical	26344197
ALDR_HUMAN	AKR1B1	physical	26344197
ESTD_HUMAN	ESD	physical	26344197
FABP7_HUMAN	FABP7	physical	26344197
GLRX1_HUMAN	GLRX	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
FBLN5_HUMAN	FBLN5	physical	28514442
UBP33_HUMAN	USP33	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-325, AND MASSSPECTROMETRY.
PubMed: 18083107