dbPTM

PI42C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PI42C_HUMAN
UniProt AC	Q8TBX8
Protein Name	Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
Gene Name	PIP4K2C
Organism	Homo sapiens (Human).
Sequence Length	421
Subcellular Localization	Cytoplasm. Membrane. Mostly found in the cytosol and surrounding plasma membrane. However, its presence in the endoplasmic reticulum seems to be a prerequisite for PIP2 synthesis (By similarity)..
Protein Description	May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum..
Protein Sequence	MASSSVPPATVSAATAGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFGIDDQDYLVSLTRNPPSESEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVDNEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKIFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEAPVREDESEVDGDCSLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPQKEVYFMGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFITNIFA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASSSVPPA ------CCCCCCCCC	20.37	19413330
3	Phosphorylation	-----MASSSVPPAT -----CCCCCCCCCE	23.11	28270605
4	Phosphorylation	----MASSSVPPATV ----CCCCCCCCCEE	26.30	28270605
5	Phosphorylation	---MASSSVPPATVS ---CCCCCCCCCEEC	35.83	28270605
10	Phosphorylation	SSSVPPATVSAATAG CCCCCCCEECCCCCC	22.29	28270605
12	Phosphorylation	SVPPATVSAATAGPG CCCCCEECCCCCCCC	14.08	28270605
15	Phosphorylation	PATVSAATAGPGPGF CCEECCCCCCCCCCC	31.68	28270605
26	Phosphorylation	GPGFGFASKTKKKHF CCCCCCCCCCCCHHH	38.30	17192257
27	Acetylation	PGFGFASKTKKKHFV CCCCCCCCCCCHHHH	62.02	7709775
28	Phosphorylation	GFGFASKTKKKHFVQ CCCCCCCCCCHHHHH	45.67	28270605
29	Acetylation	FGFASKTKKKHFVQQ CCCCCCCCCHHHHHH	64.66	7709785
37	Ubiquitination	KKHFVQQKVKVFRAA CHHHHHHHHHHHHHC	27.25	-
83	Ubiquitination	FKASSKIKVNNHLFH CCCCCCEEECCEEEC	42.52	-
96	Phosphorylation	FHRENLPSHFKFKEY ECCCCCCCCCCHHHH	44.73	25690035
99	Methylation	ENLPSHFKFKEYCPQ CCCCCCCCHHHHHHH	50.53	115975033
101	Acetylation	LPSHFKFKEYCPQVF CCCCCCHHHHHHHHH	48.65	27452117
122	Phosphorylation	FGIDDQDYLVSLTRN HCCCCCCEEEEEECC	11.90	-
208	Phosphorylation	LVMRNMFSHRLPVHR EEEHHHHHCCCCCCC	9.27	20068231
217	Phosphorylation	RLPVHRKYDLKGSLV CCCCCCCCCCCCCCC	26.85	20873877
222	Phosphorylation	RKYDLKGSLVSREAS CCCCCCCCCCCCCCC	24.82	28857561
225	Phosphorylation	DLKGSLVSREASDKE CCCCCCCCCCCCCHH	29.69	20873877
239	Phosphorylation	EKVKELPTLKDMDFL HHHHCCCCCCCHHHC	60.09	26074081
241	2-Hydroxyisobutyrylation	VKELPTLKDMDFLNK HHCCCCCCCHHHCCC	54.18	-
248	Ubiquitination	KDMDFLNKNQKVYIG CCHHHCCCCCCEEEC	64.00	-
253	Phosphorylation	LNKNQKVYIGEEEKK CCCCCCEEECHHHHH	15.39	28152594
281	Phosphorylation	VQLKIMDYSLLLGIH HHHHHHCHHHHHCHH	5.48	20068231
282	Phosphorylation	QLKIMDYSLLLGIHD HHHHHCHHHHHCHHH	14.31	20071362
294	Phosphorylation	IHDIIRGSEPEEEAP HHHHHCCCCCCCCCC	39.88	21815630
324	Phosphorylation	GPPALVGSYGTSPEG CCCEEEECCCCCCCC	16.95	24275569
328	Phosphorylation	LVGSYGTSPEGIGGY EEECCCCCCCCCCCC	19.32	18691976
349	Phosphorylation	LGPGEFESFIDVYAI CCCCCCCCEEEEEEH	32.59	17192257
368	Phosphorylation	GAPQKEVYFMGLIDI CCCHHHEEEEHHHHH	6.74	23898821
377	Phosphorylation	MGLIDILTQYDAKKK EHHHHHHHHHHHHHH	25.97	23898821
379	Phosphorylation	LIDILTQYDAKKKAA HHHHHHHHHHHHHHH	16.78	23898821
390	Ubiquitination	KKAAHAAKTVKHGAG HHHHHHHHHHHCCCC	55.42	-
391	Phosphorylation	KAAHAAKTVKHGAGA HHHHHHHHHHCCCCC	30.02	22817900
417	Phosphorylation	KRFLDFITNIFA--- HHHHHHHHHHCC---	23.43	20860994

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
324	S	Phosphorylation	Kinase	MTOR	P42345	PSP
328	S	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PI42C_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PI42C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
PI42C_HUMAN	PIP4K2C	physical	18255255
SKP1_HUMAN	SKP1	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.

Regulatory Network of PI42C_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-349, AND MASSSPECTROMETRY.	18691976 [Abstract]