TOB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TOB2_HUMAN
• UniProt AC: Q14106
• Protein Name: Protein Tob2
• Gene Name: TOB2
• Organism: Homo sapiens (Human).
• Sequence Length: 344
• Subcellular Localization: Cytoplasm.
• Protein Description: Anti-proliferative protein inhibits cell cycle progression from the G0/G1 to S phases..
• Protein Sequence: MQLEIKVALNFIISYLYNKLPRRRADLFGEELERLLKKKYEGHWYPEKPLKGSGFRCVHIGEMVDPVVELAAKRSGLAVEDVRANVPEELSVWIDPFEVSYQIGEKGAVKVLYLDDSEGCGAPELDKEIKSSFNPDAQVFVPIGSQDSSLSNSPSPSFGQSPSPTFIPRSAQPITFTTASFAATKFGSTKMKKGGGAASGGGVASSGAGGQQPPQQPRMARSPTNSLLKHKSLSLSMHSLNFITANPAPQSQLSPNAKEFVYNGGGSPSLFFDAADGQGSGTPGPFGGSGAGTCNSSSFDMAQVFGGGANSLFLEKTPFVEGLSYNLNTMQYPSQQFQPVVLAN

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
40	Phosphorylation	ERLLKKKYEGHWYPE HHHHHHHHCCCCCCC	35.70	20090780
110	Ubiquitination	IGEKGAVKVLYLDDS ECCCCCEEEEEEECC	26.45	29967540
127	Ubiquitination	CGAPELDKEIKSSFN CCCHHHHHHHHHCCC	74.16	29967540
153	Phosphorylation	QDSSLSNSPSPSFGQ CCCCCCCCCCCCCCC	24.31	22252318
155	Phosphorylation	SSLSNSPSPSFGQSP CCCCCCCCCCCCCCC	32.75	22252318
157	Phosphorylation	LSNSPSPSFGQSPSP CCCCCCCCCCCCCCC	46.47	29802988
163	Phosphorylation	PSFGQSPSPTFIPRS CCCCCCCCCCCCCCC	41.65	22252318
170	O-linked_Glycosylation	SPTFIPRSAQPITFT CCCCCCCCCCCEEEE	26.38	31492838
193	Acetylation	FGSTKMKKGGGAASG CCCCCCEECCCCCCC	60.33	11411281
193	Ubiquitination	FGSTKMKKGGGAASG CCCCCCEECCCCCCC	60.33	29967540
199	Phosphorylation	KKGGGAASGGGVASS EECCCCCCCCCCCCC	37.12	26074081
205	Phosphorylation	ASGGGVASSGAGGQQ CCCCCCCCCCCCCCC	27.22	26074081
206	Phosphorylation	SGGGVASSGAGGQQP CCCCCCCCCCCCCCC	23.95	26074081
222	Phosphorylation	QQPRMARSPTNSLLK CCCCCCCCCCHHHHH	26.91	30266825
224	Phosphorylation	PRMARSPTNSLLKHK CCCCCCCCHHHHHHH	38.39	30266825
226	Phosphorylation	MARSPTNSLLKHKSL CCCCCCHHHHHHHHE	37.24	23403867
232	Phosphorylation	NSLLKHKSLSLSMHS HHHHHHHHEEEEECC	23.94	27251275
234	Phosphorylation	LLKHKSLSLSMHSLN HHHHHHEEEEECCCE	26.03	19690332
236	Phosphorylation	KHKSLSLSMHSLNFI HHHHEEEEECCCEEE	15.86	27251275
239	Phosphorylation	SLSLSMHSLNFITAN HEEEEECCCEEEECC	19.16	27251275
244	Phosphorylation	MHSLNFITANPAPQS ECCCEEEECCCCCHH	19.08	27251275
251	Phosphorylation	TANPAPQSQLSPNAK ECCCCCHHHCCCCCC	31.84	26657352
254	Phosphorylation	PAPQSQLSPNAKEFV CCCHHHCCCCCCHHC	14.42	21082442
317	Phosphorylation	NSLFLEKTPFVEGLS CCEEECCCCCCCEEC	16.75	-

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
254	S	Phosphorylation	Kinase	CDK1	P06493	PSP
254	S	Phosphorylation	Kinase	CDK2	P24941	PSP
254	S	Phosphorylation	Kinase	CDK4	P11802	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TOB2_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 TOB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CNOT7_HUMAN	CNOT7	physical	10602502
PABP1_HUMAN	PABPC1	physical	17785442
CAF1A_HUMAN	CHAF1A	physical	17785442
PAN2_HUMAN	PAN2	physical	17785442
CNOT7_HUMAN	CNOT7	physical	25416956
CEP76_HUMAN	CEP76	physical	25416956
PABP1_HUMAN	PABPC1	physical	23340509

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

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASSSPECTROMETRY.
PubMed: 19690332