PTTG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PTTG_HUMAN
• UniProt AC: P53801
• Protein Name: Pituitary tumor-transforming gene 1 protein-interacting protein
• Gene Name: PTTG1IP
• Organism: Homo sapiens (Human).
• Sequence Length: 180
• Subcellular Localization: Membrane ; Single-pass type I membrane protein . Cytoplasm . Nucleus . According to PubMed:10781616, it is found in the cytoplasm and the nucleus.
• Protein Description: May facilitate PTTG1 nuclear translocation..
• Protein Sequence: MAPGVARGPTPYWRLRLGGAALLLLLIPVAAAQEPPGAACSQNTNKTCEECLKNVSCLWCNTNKACLDYPVTSVLPPASLCKLSSARWGVCWVNFEALIITMSVVGGTLLLGIAICCCCCCRRKRSRKPDRSEEKAMREREERRIRQEERRAEMKTRHDEIRKKYGLFKEENPYARFENN

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
45	N-linked_Glycosylation	AACSQNTNKTCEECL CCCCCCCCCCHHHHH	45.23	UniProtKB CARBOHYD
54	N-linked_Glycosylation	TCEECLKNVSCLWCN CHHHHHHHCCEEEEC	20.27	17660510
132	Phosphorylation	RSRKPDRSEEKAMRE CCCCCCHHHHHHHHH	58.44	29514088
135	Ubiquitination	KPDRSEEKAMREREE CCCHHHHHHHHHHHH	43.35	-
156	Phosphorylation	ERRAEMKTRHDEIRK HHHHHHHHHHHHHHH	31.74	-
164	Ubiquitination	RHDEIRKKYGLFKEE HHHHHHHHHCCCCCC	34.40	21890473
165	Phosphorylation	HDEIRKKYGLFKEEN HHHHHHHHCCCCCCC	23.30	21082442
169	Ubiquitination	RKKYGLFKEENPYAR HHHHCCCCCCCCCCC	69.98	21890473
169	Sumoylation	RKKYGLFKEENPYAR HHHHCCCCCCCCCCC	69.98	-
174	Phosphorylation	LFKEENPYARFENN- CCCCCCCCCCCCCC-	23.22	25159151

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
174	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PTTG_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 PTTG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB4A_HUMAN	RAB4A	physical	21988832
P53_HUMAN	TP53	physical	24506068
CLC7A_HUMAN	CLEC7A	physical	25416956
LRAD1_HUMAN	LDLRAD1	physical	25416956
P53_HUMAN	TP53	physical	25408419

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

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-174, AND MASSSPECTROMETRY.
PubMed: 19534553

"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-174, AND MASSSPECTROMETRY.
PubMed: 17389395

"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-165 AND TYR-174, ANDMASS SPECTROMETRY.
PubMed: 18083107