dbPTM

PI42A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PI42A_HUMAN
UniProt AC	P48426
Protein Name	Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
Gene Name	PIP4K2A
Organism	Homo sapiens (Human).
Sequence Length	406
Subcellular Localization	Cell membrane. Nucleus . Cytoplasm . May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light (By simil
Protein Description	Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size..
Protein Sequence	MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYIIKTITSEDVAEMHNILKKYHQYIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPNIDVYGIKCHENSPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGHILT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATPGNLGS ------CCCCCCCCH	23.62	20068231
3	Phosphorylation	-----MATPGNLGSS -----CCCCCCCCHH	30.36	29255136
9	Phosphorylation	ATPGNLGSSVLASKT CCCCCCCHHHHCCCC	22.05	18691976
10	Phosphorylation	TPGNLGSSVLASKTK CCCCCCHHHHCCCCC	21.25	20164059
14	Phosphorylation	LGSSVLASKTKTKKK CCHHHHCCCCCCCCH	36.38	25159151
15	Acetylation	GSSVLASKTKTKKKH CHHHHCCCCCCCCHH	48.73	25953088
15	Malonylation	GSSVLASKTKTKKKH CHHHHCCCCCCCCHH	48.73	26320211
15	Ubiquitination	GSSVLASKTKTKKKH CHHHHCCCCCCCCHH	48.73	30230243
16	Phosphorylation	SSVLASKTKTKKKHF HHHHCCCCCCCCHHH	41.26	28857561
22	Ubiquitination	KTKTKKKHFVAQKVK CCCCCCHHHHHHHHH	31.15	29967540
27	Ubiquitination	KKHFVAQKVKLFRAS CHHHHHHHHHHHHCC	31.44	29967540
30	Ubiquitination	FVAQKVKLFRASDPL HHHHHHHHHHCCCHH	3.83	29967540
32	Ubiquitination	AQKVKLFRASDPLLS HHHHHHHHCCCHHHH	43.55	-
69	Phosphorylation	MPDDFKAYSKIKVDN CCCCCHHHHCCEECC	15.87	29978859
70	Phosphorylation	PDDFKAYSKIKVDNH CCCCHHHHCCEECCC	32.53	29978859
81	Ubiquitination	VDNHLFNKENMPSHF ECCCCCCCCCCCCCC	43.03	29967540
86	Ubiquitination	FNKENMPSHFKFKEY CCCCCCCCCCCHHHH	30.68	29967540
86	Phosphorylation	FNKENMPSHFKFKEY CCCCCCCCCCCHHHH	30.68	29978859
89	Methylation	ENMPSHFKFKEYCPM CCCCCCCCHHHHHHH	50.53	19608861
89	Acetylation	ENMPSHFKFKEYCPM CCCCCCCCHHHHHHH	50.53	19608861
89	Ubiquitination	ENMPSHFKFKEYCPM CCCCCCCCHHHHHHH	50.53	19608861
91	Methylation	MPSHFKFKEYCPMVF CCCCCCHHHHHHHHH	48.65	54408155
91	Ubiquitination	MPSHFKFKEYCPMVF CCCCCCHHHHHHHHH	48.65	-
93	Phosphorylation	SHFKFKEYCPMVFRN CCCCHHHHHHHHHHH	11.48	22817900
103	Ubiquitination	MVFRNLRERFGIDDQ HHHHHHHHHHCCCCH	56.37	24816145
142	Phosphorylation	HTSYDKRYIIKTITS CCCCCCEEEEEECCH	16.85	26074081
145	Ubiquitination	YDKRYIIKTITSEDV CCCEEEEEECCHHHH	25.06	19608861
145	Acetylation	YDKRYIIKTITSEDV CCCEEEEEECCHHHH	25.06	19608861
146	Phosphorylation	DKRYIIKTITSEDVA CCEEEEEECCHHHHH	21.05	26074081
148	Phosphorylation	RYIIKTITSEDVAEM EEEEEECCHHHHHHH	31.15	26074081
149	Phosphorylation	YIIKTITSEDVAEMH EEEEECCHHHHHHHH	28.13	26074081
154	Ubiquitination	ITSEDVAEMHNILKK CCHHHHHHHHHHHHH	40.60	24816145
154	Ubiquitination	ITSEDVAEMHNILKK CCHHHHHHHHHHHHH	40.60	-
162	Ubiquitination	MHNILKKYHQYIVEC HHHHHHHHHHHHHHH	7.80	24816145
185	Ubiquitination	FLGMYRLNVDGVEIY HHCCEEECCCCEEEE	22.34	29967540
193	Ubiquitination	VDGVEIYVIVTRNVF CCCEEEEEEEECCCH	3.31	-
199	Ubiquitination	YVIVTRNVFSHRLSV EEEEECCCHHCCCEE	4.73	-
201	Ubiquitination	IVTRNVFSHRLSVYR EEECCCHHCCCEEEE	11.92	-
205	Phosphorylation	NVFSHRLSVYRKYDL CCHHCCCEEEEECCC	19.63	28355574
207	Phosphorylation	FSHRLSVYRKYDLKG HHCCCEEEEECCCCC	9.67	23312004
210	Phosphorylation	RLSVYRKYDLKGSTV CCEEEEECCCCCCCC	19.94	28509920
213	Ubiquitination	VYRKYDLKGSTVARE EEEECCCCCCCCCHH	48.17	24816145
215	Phosphorylation	RKYDLKGSTVAREAS EECCCCCCCCCHHHC	20.37	28509920
216	Phosphorylation	KYDLKGSTVAREASD ECCCCCCCCCHHHCC	27.18	28509920
222	Phosphorylation	STVAREASDKEKAKE CCCCHHHCCHHHHHH	44.45	28509920
244	Ubiquitination	DFINEGQKIYIDDNN CCCCCCCEEEECCCC	48.62	29967540
246	Phosphorylation	INEGQKIYIDDNNKK CCCCCEEEECCCCCE	12.82	22817900
252	Ubiquitination	IYIDDNNKKVFLEKL EEECCCCCEEHHHHH	57.48	-
258	Ubiquitination	NKKVFLEKLKKDVEF CCEEHHHHHHHHHHH	68.69	-
260	Ubiquitination	KVFLEKLKKDVEFLA EEHHHHHHHHHHHHH	58.98	-
285	Ubiquitination	VGIHDVERAEQEEVE HCHHCHHHHHHHCCC	43.18	22053931
304	Phosphorylation	DGEEEGESDGTHPVG CCCCCCCCCCCCCCC	52.80	10508590
307	Phosphorylation	EEGESDGTHPVGTPP CCCCCCCCCCCCCCC	28.18	26074081
312	Phosphorylation	DGTHPVGTPPDSPGN CCCCCCCCCCCCCCC	31.70	26074081
316	Ubiquitination	PVGTPPDSPGNTLNS CCCCCCCCCCCCCCC	40.24	30230243
316	Phosphorylation	PVGTPPDSPGNTLNS CCCCCCCCCCCCCCC	40.24	26074081
320	Phosphorylation	PPDSPGNTLNSSPPL CCCCCCCCCCCCCCC	32.98	26074081
323	Phosphorylation	SPGNTLNSSPPLAPG CCCCCCCCCCCCCCC	47.54	26074081
324	Phosphorylation	PGNTLNSSPPLAPGE CCCCCCCCCCCCCCC	29.48	26074081
336	Ubiquitination	PGEFDPNIDVYGIKC CCCCCCCCEEEEEEE	4.63	22053931
336	Ubiquitination	PGEFDPNIDVYGIKC CCCCCCCCEEEEEEE	4.63	-
344	Ubiquitination	DVYGIKCHENSPRKE EEEEEEECCCCCCHH	32.07	22053931
367	Acetylation	ILTHYDAKKKAAHAA HHHHHCHHHHHHHHH	52.49	22361483
375	Ubiquitination	KKAAHAAKTVKHGAG HHHHHHHHHHHCCCC	55.42	30230243
376	Phosphorylation	KAAHAAKTVKHGAGA HHHHHHHHHHCCCCC	30.02	22817900
378	Acetylation	AHAAKTVKHGAGAEI HHHHHHHHCCCCCEE	41.37	25953088
387	Phosphorylation	GAGAEISTVNPEQYS CCCCEEECCCHHHHH	29.93	22210691
395	Ubiquitination	VNPEQYSKRFLDFIG CCHHHHHHHHHHHHH	42.08	21906983

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
304	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
304	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
376	T	Phosphorylation	Kinase	PRKD1	Q15139	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PI42A_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 PI42A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SKP1_HUMAN	SKP1	physical	26344197
PI42B_HUMAN	PIP4K2B	physical	28514442
DIP2C_HUMAN	DIP2C	physical	28514442
UBF1_HUMAN	UBTF	physical	28514442
AFF3_HUMAN	AFF3	physical	28514442
RTF1_HUMAN	RTF1	physical	28514442
AFF4_HUMAN	AFF4	physical	28514442
HDGR2_HUMAN	HDGFRP2	physical	28514442
BRD3_HUMAN	BRD3	physical	28514442
AF9_HUMAN	MLLT3	physical	28514442
PI42C_HUMAN	PIP4K2C	physical	28514442
PNISR_HUMAN	PNISR	physical	28514442
MEX3B_HUMAN	MEX3B	physical	28514442
STRAA_HUMAN	STRADA	physical	28514442
ENL_HUMAN	MLLT1	physical	28514442
AFF1_HUMAN	AFF1	physical	28514442
ELL3_HUMAN	ELL3	physical	28514442
BRD2_HUMAN	BRD2	physical	28514442
GPTC8_HUMAN	GPATCH8	physical	28514442
CHD9_HUMAN	CHD9	physical	28514442
SAHH3_HUMAN	AHCYL2	physical	28514442
STK11_HUMAN	STK11	physical	28514442
BRD4_HUMAN	BRD4	physical	28514442
NAF1_HUMAN	NAF1	physical	28514442
GPAM1_HUMAN	GPALPP1	physical	28514442
MEX3C_HUMAN	MEX3C	physical	28514442
PI51A_HUMAN	PIP5K1A	physical	28514442
EAF2_HUMAN	EAF2	physical	28514442
BRPF1_HUMAN	BRPF1	physical	28514442
GPBL1_HUMAN	GPBP1L1	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
SET1B_HUMAN	SETD1B	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
ELL2_HUMAN	ELL2	physical	28514442
SAHH2_HUMAN	AHCYL1	physical	28514442
KANK1_HUMAN	KANK1	physical	28514442
CWC22_HUMAN	CWC22	physical	28514442
LENG8_HUMAN	LENG8	physical	28514442
RAD18_HUMAN	RAD18	physical	28514442
PPRC1_HUMAN	PPRC1	physical	28514442
STRAB_HUMAN	STRADB	physical	28514442
CL043_HUMAN	C12orf43	physical	28514442
DJC13_HUMAN	DNAJC13	physical	28514442
PLCD3_HUMAN	PLCD3	physical	28514442
IKBL1_HUMAN	NFKBIL1	physical	28514442
CAB39_HUMAN	CAB39	physical	28514442
AP3B1_HUMAN	AP3B1	physical	28514442
NOLC1_HUMAN	NOLC1	physical	28514442
PININ_HUMAN	PNN	physical	28514442
RFWD3_HUMAN	RFWD3	physical	28514442
ELL_HUMAN	ELL	physical	28514442
CLASR_HUMAN	CLASRP	physical	28514442
PPIG_HUMAN	PPIG	physical	28514442
JMJD6_HUMAN	JMJD6	physical	28514442
CXXC1_HUMAN	CXXC1	physical	28514442
MTMR5_HUMAN	SBF1	physical	28514442
CCNT1_HUMAN	CCNT1	physical	28514442
T2FA_HUMAN	GTF2F1	physical	28514442
IWS1_HUMAN	IWS1	physical	28514442
EDC4_HUMAN	EDC4	physical	28514442
SRSF8_HUMAN	SRSF8	physical	28514442
SELH_HUMAN	C11orf31	physical	28514442
TCOF_HUMAN	TCOF1	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
C102A_HUMAN	CCDC102A	physical	28514442
WDR26_HUMAN	WDR26	physical	28514442
AP3M1_HUMAN	AP3M1	physical	28514442
CR025_HUMAN	C18orf25	physical	28514442
SETD2_HUMAN	SETD2	physical	28514442
MINT_HUMAN	SPEN	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
MTMR1_HUMAN	MTMR1	physical	28514442
CHD8_HUMAN	CHD8	physical	28514442
E41L5_HUMAN	EPB41L5	physical	28514442
PIN1_HUMAN	PIN1	physical	28514442
NKAP_HUMAN	NKAP	physical	28514442
CCDC9_HUMAN	CCDC9	physical	28514442
RFIP1_HUMAN	RAB11FIP1	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.

Regulatory Network of PI42A_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]
"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-89 AND LYS-145, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-9; SER-14;SER-304; THR-312; SER-316 AND THR-320, AND MASS SPECTROMETRY.	19369195 [Abstract]
"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 THR-3 AND SER-14, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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-93, AND MASSSPECTROMETRY.	18083107 [Abstract]