PIPNA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIPNA_HUMAN
• UniProt AC: Q00169
• Protein Name: Phosphatidylinositol transfer protein alpha isoform
• Gene Name: PITPNA
• Organism: Homo sapiens (Human).
• Sequence Length: 270
• Subcellular Localization: Cytoplasm.
• Protein Description: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes..
• Protein Sequence: MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTMDDIRRMEEETKRQLDEMRQKDPVKGMTADD

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
5	Sumoylation	---MVLLKEYRVILP ---CCEEEEEEEEEE	48.84	-
5	Ubiquitination	---MVLLKEYRVILP ---CCEEEEEEEEEE	48.84	-
5	Sumoylation	---MVLLKEYRVILP ---CCEEEEEEEEEE	48.84	-
7	Phosphorylation	-MVLLKEYRVILPVS -CCEEEEEEEEEEEE	14.48	24043423
14	Phosphorylation	YRVILPVSVDEYQVG EEEEEEEECCEEEHH	23.16	22817901
18	Phosphorylation	LPVSVDEYQVGQLYS EEEECCEEEHHHEEE	12.20	24043423
24	Phosphorylation	EYQVGQLYSVAEASK EEEHHHEEEHHHHHC	8.00	24043423
25	Phosphorylation	YQVGQLYSVAEASKN EEHHHEEEHHHHHCC	24.36	24043423
30	Phosphorylation	LYSVAEASKNETGGG EEEHHHHHCCCCCCC	27.76	24043423
50	Acetylation	LVNEPYEKDGEKGQY EECCCCCCCCCCCCC	66.25	66693765
50	Ubiquitination	LVNEPYEKDGEKGQY EECCCCCCCCCCCCC	66.25	21906983
54	Ubiquitination	PYEKDGEKGQYTHKI CCCCCCCCCCCEEHH	57.77	-
57	Phosphorylation	KDGEKGQYTHKIYHL CCCCCCCCEEHHEEH	21.34	18083107
58	Phosphorylation	DGEKGQYTHKIYHLQ CCCCCCCEEHHEEHH	14.59	15322105
60	Ubiquitination	EKGQYTHKIYHLQSK CCCCCEEHHEEHHHC	36.84	-
62	Phosphorylation	GQYTHKIYHLQSKVP CCCEEHHEEHHHCCC	10.98	29496907
67	Ubiquitination	KIYHLQSKVPTFVRM HHEEHHHCCCCHHHH	38.99	-
74	Sulfoxidation	KVPTFVRMLAPEGAL CCCCHHHHHCCCCCC	2.92	21406390
86	Ubiquitination	GALNIHEKAWNAYPY CCCCHHHHHHHHCCC	44.53	21890473
91	Phosphorylation	HEKAWNAYPYCRTVI HHHHHHHCCCCCEEE	7.48	28152594
93	Phosphorylation	KAWNAYPYCRTVITN HHHHHCCCCCEEECC	5.06	20090780
110	Ubiquitination	MKEDFLIKIETWHKP HHHCEEEEEEECCCC	36.32	-
127	Ubiquitination	GTQENVHKLEPEAWK CCCCCHHHCCHHHHH	50.71	-
134	Acetylation	KLEPEAWKHVEAVYI HCCHHHHHCCEEEEE	44.83	27452117
140	Phosphorylation	WKHVEAVYIDIADRS HHCCEEEEEECHHHH	10.42	24927040
146	Methylation	VYIDIADRSQVLSKD EEEECHHHHHHHCCC	21.70	115487595
147	Phosphorylation	YIDIADRSQVLSKDY EEECHHHHHHHCCCC	25.78	27282143
152	Ubiquitination	DRSQVLSKDYKAEED HHHHHHCCCCCCCCC	62.00	21890473
162	Acetylation	KAEEDPAKFKSIKTG CCCCCHHHCCCCCCC	59.73	25953088
162	Ubiquitination	KAEEDPAKFKSIKTG CCCCCHHHCCCCCCC	59.73	21890473
165	Phosphorylation	EDPAKFKSIKTGRGP CCHHHCCCCCCCCCC	32.24	15322105
178	Ubiquitination	GPLGPNWKQELVNQK CCCCCCHHHHHHCCC	40.30	21890473
185	Ubiquitination	KQELVNQKDCPYMCA HHHHHCCCCCCCEEE	56.97	-
199	Acetylation	AYKLVTVKFKWWGLQ EEEEEEEEHHHHHCH	31.68	25953088
201	Ubiquitination	KLVTVKFKWWGLQNK EEEEEEHHHHHCHHH	36.00	21890473
201	Acetylation	KLVTVKFKWWGLQNK EEEEEEHHHHHCHHH	36.00	25953088
208	Ubiquitination	KWWGLQNKVENFIHK HHHHCHHHHHHHHHH	37.66	21890473
215	Ubiquitination	KVENFIHKQERRLFT HHHHHHHHHHHHHHH	49.38	19608861
215	Acetylation	KVENFIHKQERRLFT HHHHHHHHHHHHHHH	49.38	19608861

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
58	T	Phosphorylation	Kinase	PRKCA	P05696	GPS
165	S	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
165	S	Phosphorylation	Kinase	PRKCA	P05696	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIPNA_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 PIPNA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PMVK_HUMAN	PMVK	physical	17353931
MO4L2_HUMAN	MORF4L2	physical	17353931
MLKL_HUMAN	MLKL	physical	17353931
NLTP_HUMAN	SCP2	physical	15182174
UB2L3_HUMAN	UBE2L3	physical	26344197

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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND MASS SPECTROMETRY.
PubMed: 19608861

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-57, AND MASSSPECTROMETRY.
PubMed: 18083107