dbPTM

P3C2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P3C2A_HUMAN
UniProt AC	O00443
Protein Name	Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Gene Name	PIK3C2A
Organism	Homo sapiens (Human).
Sequence Length	1686
Subcellular Localization	Cell membrane . Golgi apparatus . Cytoplasmic vesicle, clathrin-coated vesicle . Nucleus . Cytoplasm . Inserts preferentially into membranes containing PtdIns(4,5)P2 (PubMed:17038310). Associated with RNA-containing structures (PubMed:11606566).
Protein Description	Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function..
Protein Sequence	MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSSTRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVTPILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFPSTEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNGKARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLAKDPWDAVLLEERSTANCHLERKVNGKSLSVATVTRSQSLNIRTTQLAKAQGHISQKDPNGTSSLPTGSSLLQEVEVQNEEMAAFCRSITKLKTKFPYTNHRTNPGYLLSPVTAQRNICGENASVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEVLQNNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKPCKEAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESVKKLKRAVNLPRSKTADVTSLFGGEDTSRSSTRGSLNPENPVQVSINQLTAAIYDLLRLHANSGRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDLFKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGILNQSSGSSPDSNKQRKGPEALGKVSLPLFDFKRFLTCGTKLLYLWTSSHTNSVPGTVTKKGYVMERIVLQVDFPSPAFDIIYTTPQVDRSIIQQHNLETLENDIKGKLLDILHKDSSLGLSKEDKAFLWEKRYYCFKHPNCLPKILASAPNWKWVNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAVTWIEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHDVQFSTRYEHVLGALLSVGGKRLREELLKQTKLVQLLGGVAEKVRQASGSARQVVLQRSMERVQSFFQKNKCRLPLKPSLVAKELNIKSCSFFSSNAVPLKVTMVNADPMGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDKHYIYVVRILREGQIEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPTPGQIGGAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQLTAATYL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQISSNSG ------CCCCCCCCC	27.07	19413330
5	Phosphorylation	---MAQISSNSGFKE ---CCCCCCCCCCCC	16.04	-
6	Phosphorylation	--MAQISSNSGFKEC --CCCCCCCCCCCCC	36.32	-
8	Phosphorylation	MAQISSNSGFKECPS CCCCCCCCCCCCCCC	47.78	-
11	Acetylation	ISSNSGFKECPSSHP CCCCCCCCCCCCCCC	63.03	25953088
11	Ubiquitination	ISSNSGFKECPSSHP CCCCCCCCCCCCCCC	63.03	-
41	Ubiquitination	MEAEALAKLQKDRQV HHHHHHHHHHHHHCC	52.91	-
41	Ubiquitination	MEAEALAKLQKDRQV HHHHHHHHHHHHHCC	52.91	-
49	Phosphorylation	LQKDRQVTDNQRGFE HHHHHCCCCCCCCCC	22.39	24719451
58	Phosphorylation	NQRGFELSSSTRKKA CCCCCCCCHHHHHHE	18.29	30266825
59	Phosphorylation	QRGFELSSSTRKKAQ CCCCCCCHHHHHHEE	48.64	30266825
60	Phosphorylation	RGFELSSSTRKKAQV CCCCCCHHHHHHEEE	28.93	30266825
61	Phosphorylation	GFELSSSTRKKAQVY CCCCCHHHHHHEEEE	48.75	30266825
68	Phosphorylation	TRKKAQVYNKQDYDL HHHHEEEECCCCCCE	12.45	21945579
73	Phosphorylation	QVYNKQDYDLMVFPE EEECCCCCCEEEECC	14.42	21945579
81	Phosphorylation	DLMVFPESDSQKRAL CEEEECCCHHHCCHH	42.68	21945579
83	Phosphorylation	MVFPESDSQKRALDI EEECCCHHHCCHHCC	47.05	21945579
94	Ubiquitination	ALDIDVEKLTQAELE HHCCCHHHHHHHHHH	57.60	-
94	Acetylation	ALDIDVEKLTQAELE HHCCCHHHHHHHHHH	57.60	20167786
94	Ubiquitination	ALDIDVEKLTQAELE HHCCCHHHHHHHHHH	57.60	21890473
102	Ubiquitination	LTQAELEKLLLDDSF HHHHHHHHHHCCCCC	57.99	-
108	Phosphorylation	EKLLLDDSFETKKTP HHHHCCCCCCCCCCC	25.34	30266825
111	Phosphorylation	LLDDSFETKKTPVLP HCCCCCCCCCCCCCC	35.51	21815630
112	Ubiquitination	LDDSFETKKTPVLPV CCCCCCCCCCCCCCC	47.67	-
112	Ubiquitination	LDDSFETKKTPVLPV CCCCCCCCCCCCCCC	47.67	21890473
120	Phosphorylation	KTPVLPVTPILSPSF CCCCCCCCCCCCCCC	11.59	-
124	Phosphorylation	LPVTPILSPSFSAQL CCCCCCCCCCCCEEE	21.15	24719451
126	Phosphorylation	VTPILSPSFSAQLYF CCCCCCCCCCEEEEE	28.58	-
139	Dimethylation	YFRPTIQRGQWPPGL EECCCCCCCCCCCCC	35.11	-
139	Methylation	YFRPTIQRGQWPPGL EECCCCCCCCCCCCC	35.11	24377279
175	Methylation	FQNGFNPRMPTFPST HHCCCCCCCCCCCCC	44.83	115487539
229	Ubiquitination	DMAKLFDKIASTSEF HHHHHHHHHHCCHHH	32.60	21890473
229	Ubiquitination	DMAKLFDKIASTSEF HHHHHHHHHHCCHHH	32.60	21890473
232	Phosphorylation	KLFDKIASTSEFLKN HHHHHHHCCHHHHHC	35.62	24670416
233	Phosphorylation	LFDKIASTSEFLKNG HHHHHHCCHHHHHCC	24.21	24670416
234	Phosphorylation	FDKIASTSEFLKNGK HHHHHCCHHHHHCCC	24.69	-
238	Ubiquitination	ASTSEFLKNGKARTD HCCHHHHHCCCCCCC	69.81	-
244	Phosphorylation	LKNGKARTDLEITDS HHCCCCCCCEEECCC	50.20	22617229
251	Phosphorylation	TDLEITDSKVSNLQV CCEEECCCCCCCCEE	26.72	22617229
252	Ubiquitination	DLEITDSKVSNLQVS CEEECCCCCCCCEEC	53.12	-
252	Ubiquitination	DLEITDSKVSNLQVS CEEECCCCCCCCEEC	53.12	21890473
254	Phosphorylation	EITDSKVSNLQVSPK EECCCCCCCCEECCC	35.24	23090842
259	Phosphorylation	KVSNLQVSPKSEDIS CCCCCEECCCCCCCC	17.41	19664994
261	Ubiquitination	SNLQVSPKSEDISKF CCCEECCCCCCCCCC	60.00	-
261	Ubiquitination	SNLQVSPKSEDISKF CCCEECCCCCCCCCC	60.00	21890473
262	Phosphorylation	NLQVSPKSEDISKFD CCEECCCCCCCCCCC	43.83	23090842
266	Phosphorylation	SPKSEDISKFDWLDL CCCCCCCCCCCCCCC	39.32	23090842
267	Ubiquitination	PKSEDISKFDWLDLD CCCCCCCCCCCCCCC	47.91	21890473
267	Ubiquitination	PKSEDISKFDWLDLD CCCCCCCCCCCCCCC	47.91	21890473
277	Phosphorylation	WLDLDPLSKPKVDNV CCCCCCCCCCCCCCE	52.91	26074081
278	Ubiquitination	LDLDPLSKPKVDNVE CCCCCCCCCCCCCEE	57.45	-
278	Ubiquitination	LDLDPLSKPKVDNVE CCCCCCCCCCCCCEE	57.45	21890473
280	Ubiquitination	LDPLSKPKVDNVEVL CCCCCCCCCCCEEEC	66.99	-
280	"N6,N6-dimethyllysine"	LDPLSKPKVDNVEVL CCCCCCCCCCCEEEC	66.99	-
280	Methylation	LDPLSKPKVDNVEVL CCCCCCCCCCCEEEC	66.99	-
280	Ubiquitination	LDPLSKPKVDNVEVL CCCCCCCCCCCEEEC	66.99	-
293	Ubiquitination	VLDHEEEKNVSSLLA ECCHHHHCCHHHHHH	66.96	-
296	Phosphorylation	HEEEKNVSSLLAKDP HHHHCCHHHHHHCCC	25.35	28674419
297	Phosphorylation	EEEKNVSSLLAKDPW HHHCCHHHHHHCCCH	24.10	24275569
301	Ubiquitination	NVSSLLAKDPWDAVL CHHHHHHCCCHHHHH	65.38	-
301	Ubiquitination	NVSSLLAKDPWDAVL CHHHHHHCCCHHHHH	65.38	21890473
327	Phosphorylation	ERKVNGKSLSVATVT EEEECCEEEEEEEEE	27.55	30266825
329	Phosphorylation	KVNGKSLSVATVTRS EECCEEEEEEEEECC	19.45	30266825
332	Phosphorylation	GKSLSVATVTRSQSL CEEEEEEEEECCHHC	21.91	30266825
334	O-linked_Glycosylation	SLSVATVTRSQSLNI EEEEEEEECCHHCCC	21.90	30379171
334	Phosphorylation	SLSVATVTRSQSLNI EEEEEEEECCHHCCC	21.90	20873877
336	Phosphorylation	SVATVTRSQSLNIRT EEEEEECCHHCCCCH	18.11	30266825
338	Phosphorylation	ATVTRSQSLNIRTTQ EEEECCHHCCCCHHH	25.32	26846344
343	Phosphorylation	SQSLNIRTTQLAKAQ CHHCCCCHHHHHHHH	18.33	29514088
344	Phosphorylation	QSLNIRTTQLAKAQG HHCCCCHHHHHHHHC	16.25	29514088
348	Ubiquitination	IRTTQLAKAQGHISQ CCHHHHHHHHCCCCC	50.24	-
361	Phosphorylation	SQKDPNGTSSLPTGS CCCCCCCCCCCCCCC	23.06	28348404
362	Phosphorylation	QKDPNGTSSLPTGSS CCCCCCCCCCCCCCH	31.13	28348404
363	Phosphorylation	KDPNGTSSLPTGSSL CCCCCCCCCCCCCHH	37.90	28348404
366	Phosphorylation	NGTSSLPTGSSLLQE CCCCCCCCCCHHHHE	55.80	28348404
368	Phosphorylation	TSSLPTGSSLLQEVE CCCCCCCCHHHHEEE	21.94	28348404
369	Phosphorylation	SSLPTGSSLLQEVEV CCCCCCCHHHHEEEE	34.15	28348404
390	Ubiquitination	AFCRSITKLKTKFPY HHHHHHHHCCCCCCC	46.44	-
394	Ubiquitination	SITKLKTKFPYTNHR HHHHCCCCCCCCCCC	42.63	-
406	Phosphorylation	NHRTNPGYLLSPVTA CCCCCCCCCCCCHHH	13.01	-
409	Phosphorylation	TNPGYLLSPVTAQRN CCCCCCCCCHHHCCC	18.09	-
412	Phosphorylation	GYLLSPVTAQRNICG CCCCCCHHHCCCCCC	22.06	-
509	Phosphorylation	EIRLQLLTFSAMCQN HHHHHHHHHHHHHHH	24.92	25003641
511	Phosphorylation	RLQLLTFSAMCQNLA HHHHHHHHHHHHHHH	15.17	25003641
520	Phosphorylation	MCQNLARTAEDDETP HHHHHHHCCCCCCCC	28.88	20068231
532	Acetylation	ETPVDLNKHLYQIEK CCCCCHHHHHHHCCH	42.14	66727787
532	Ubiquitination	ETPVDLNKHLYQIEK CCCCCHHHHHHHCCH	42.14	-
539	Ubiquitination	KHLYQIEKPCKEAMT HHHHHCCHHHHHHHH	58.29	-
542	Ubiquitination	YQIEKPCKEAMTRHP HHCCHHHHHHHHHCC	57.97	-
579	Ubiquitination	RAVDQVIKAVRKICS HHHHHHHHHHHHHHH	41.81	21890473
612	Phosphorylation	RAVNLPRSKTADVTS HHHCCCCCCCCCCHH	32.21	23917254
613	Ubiquitination	AVNLPRSKTADVTSL HHCCCCCCCCCCHHH	49.35	21890473
614	Phosphorylation	VNLPRSKTADVTSLF HCCCCCCCCCCHHHC	29.36	28857561
618	Phosphorylation	RSKTADVTSLFGGED CCCCCCCHHHCCCCC	21.91	28348404
619	Phosphorylation	SKTADVTSLFGGEDT CCCCCCHHHCCCCCC	22.88	28348404
626	Phosphorylation	SLFGGEDTSRSSTRG HHCCCCCCCCCCCCC	23.03	23186163
627	Phosphorylation	LFGGEDTSRSSTRGS HCCCCCCCCCCCCCC	42.35	23186163
629	Phosphorylation	GGEDTSRSSTRGSLN CCCCCCCCCCCCCCC	35.51	23186163
630	Phosphorylation	GEDTSRSSTRGSLNP CCCCCCCCCCCCCCC	22.48	23917254
631	Phosphorylation	EDTSRSSTRGSLNPE CCCCCCCCCCCCCCC	40.05	23186163
665	Phosphorylation	LHANSGRSPTDCAQS HHCCCCCCCCHHHHC	35.36	-
667	Phosphorylation	ANSGRSPTDCAQSSK CCCCCCCCHHHHCCC	44.98	-
672	Phosphorylation	SPTDCAQSSKSVKEA CCCHHHHCCCCHHHH	22.62	-
673	Phosphorylation	PTDCAQSSKSVKEAW CCHHHHCCCCHHHHC	19.50	-
674	Ubiquitination	TDCAQSSKSVKEAWT CHHHHCCCCHHHHCC	65.60	-
737	Phosphorylation	GTYKNFFYLIKWDEL CCCCCEEEEEEECEE	11.90	-
771	Phosphorylation	LFGILNQSSGSSPDS HHHHHHCCCCCCCCC	35.28	-
772	Phosphorylation	FGILNQSSGSSPDSN HHHHHCCCCCCCCCC	32.69	-
778	Phosphorylation	SSGSSPDSNKQRKGP CCCCCCCCCCCCCCH	49.68	-
783	Ubiquitination	PDSNKQRKGPEALGK CCCCCCCCCHHHHCC	76.07	-
810	Phosphorylation	TCGTKLLYLWTSSHT CCCCEEEEEECCCCC	15.61	27542207
813	Phosphorylation	TKLLYLWTSSHTNSV CEEEEEECCCCCCCC	20.11	27542207
814	Phosphorylation	KLLYLWTSSHTNSVP EEEEEECCCCCCCCC	14.45	27542207
815	Phosphorylation	LLYLWTSSHTNSVPG EEEEECCCCCCCCCC	27.27	27542207
817	Phosphorylation	YLWTSSHTNSVPGTV EEECCCCCCCCCCCE	31.01	27542207
819	Phosphorylation	WTSSHTNSVPGTVTK ECCCCCCCCCCCEEC	30.74	27542207
823	Phosphorylation	HTNSVPGTVTKKGYV CCCCCCCCEECCCEE	20.94	27542207
825	Phosphorylation	NSVPGTVTKKGYVME CCCCCCEECCCEEEE	27.20	27542207
857	Phosphorylation	TTPQVDRSIIQQHNL ECCCCCHHHHHHCCH	21.41	20873877
866	Phosphorylation	IQQHNLETLENDIKG HHHCCHHHHHHHHHH	42.40	20873877
872	Acetylation	ETLENDIKGKLLDIL HHHHHHHHHHHHHHH	53.51	7430755
872	Ubiquitination	ETLENDIKGKLLDIL HHHHHHHHHHHHHHH	53.51	21890473
874	Ubiquitination	LENDIKGKLLDILHK HHHHHHHHHHHHHCC	40.66	-
881	Acetylation	KLLDILHKDSSLGLS HHHHHHCCCCCCCCC	56.72	7430767
881	Ubiquitination	KLLDILHKDSSLGLS HHHHHHCCCCCCCCC	56.72	21890473
883	Phosphorylation	LDILHKDSSLGLSKE HHHHCCCCCCCCCHH	32.06	20860994
888	Phosphorylation	KDSSLGLSKEDKAFL CCCCCCCCHHHHHHH	32.00	20860994
889	Acetylation	DSSLGLSKEDKAFLW CCCCCCCHHHHHHHH	74.99	7430779
889	Ubiquitination	DSSLGLSKEDKAFLW CCCCCCCHHHHHHHH	74.99	21890473
892	Ubiquitination	LGLSKEDKAFLWEKR CCCCHHHHHHHHHCE	41.97	-
898	Ubiquitination	DKAFLWEKRYYCFKH HHHHHHHCEEECCCC	33.83	-
900	Phosphorylation	AFLWEKRYYCFKHPN HHHHHCEEECCCCCC	18.69	29496907
901	Phosphorylation	FLWEKRYYCFKHPNC HHHHCEEECCCCCCC	8.74	-
920	Ubiquitination	LASAPNWKWVNLAKT HHCCCCCEEEHHHHH	48.15	-
927	Phosphorylation	KWVNLAKTYSLLHQW EEEHHHHHHHHHHHC	16.85	27461979
928	Phosphorylation	WVNLAKTYSLLHQWP EEHHHHHHHHHHHCH	9.16	27461979
929	Phosphorylation	VNLAKTYSLLHQWPA EHHHHHHHHHHHCHH	29.68	27461979
938	Phosphorylation	LHQWPALYPLIALEL HHHCHHHHHHHHHHH	9.71	27461979
948	Phosphorylation	IALELLDSKFADQEV HHHHHHCCCCCCHHH	29.64	27461979
1062	Ubiquitination	LLGGVAEKVRQASGS HHHHHHHHHHHHCCC	32.74	-
1084	Phosphorylation	RSMERVQSFFQKNKC HHHHHHHHHHHCCCC	25.77	27499020
1088	Ubiquitination	RVQSFFQKNKCRLPL HHHHHHHCCCCCCCC	53.90	-
1090	Ubiquitination	QSFFQKNKCRLPLKP HHHHHCCCCCCCCCH	27.97	-
1096	Ubiquitination	NKCRLPLKPSLVAKE CCCCCCCCHHHHHHH	30.53	-
1158	Ubiquitination	QMIKIMDKIWLKEGL HHHHHHHHHHHHCCC	20.57	-
1162	Ubiquitination	IMDKIWLKEGLDLRM HHHHHHHHCCCCCEE	34.44	21890473
1209	Ubiquitination	VTGSFKDKPLAEWLR CCCCCCCCHHHHHHH	42.39	-
1217	Ubiquitination	PLAEWLRKYNPSEEE HHHHHHHHHCCCHHH	47.40	21890473
1218	Phosphorylation	LAEWLRKYNPSEEEY HHHHHHHHCCCHHHH	26.35	29116813
1225	Phosphorylation	YNPSEEEYEKASENF HCCCHHHHHHHHHCH	26.47	29116813
1271	Ubiquitination	MFHIDFGKFLGHAQM EEEEEHHHHHCCHHH	37.09	-
1281	Phosphorylation	GHAQMFGSFKRDRAP CCHHHHCCCCCCCCC	19.14	23403867
1292	Phosphorylation	DRAPFVLTSDMAYVI CCCCEEEECCEEEEC	19.85	28188228
1297	Phosphorylation	VLTSDMAYVINGGEK EEECCEEEECCCCCC	8.67	28188228
1327	O-linked_Glycosylation	YNLIRKQTNLFLNLL HHHHHHHHHHHHHHH	36.60	30379171
1335	O-linked_Glycosylation	NLFLNLLSLMIPSGL HHHHHHHHCCCCCCC	21.03	30379171
1362	Phosphorylation	RDALQPQTTDAEATI HHHHCCCCCCHHHHH	33.07	28387310
1368	Phosphorylation	QTTDAEATIFFTRLI CCCCHHHHHHHHHHH	15.15	28387310
1412	Phosphorylation	DEPILSFSPKTYSFR CCCCEEECCCEEEEC	23.31	24719451
1414	Ubiquitination	PILSFSPKTYSFRQD CCEEECCCEEEECCC	59.92	-
1431	Phosphorylation	IKEVSVFTYHKKYNP EEEEEEEEEECCCCC	23.66	29759185
1432	Phosphorylation	KEVSVFTYHKKYNPD EEEEEEEEECCCCCC	10.52	29759185
1539	Acetylation	HPLLRDEKAEGIARS CHHHCCHHHCCCCCC	56.90	21339330
1546	Phosphorylation	KAEGIARSADAGSFS HHCCCCCCCCCCCCC	22.83	19691289
1551	Phosphorylation	ARSADAGSFSPTPGQ CCCCCCCCCCCCCCC	25.03	30266825
1553	Phosphorylation	SADAGSFSPTPGQIG CCCCCCCCCCCCCCC	29.57	30266825
1555	Phosphorylation	DAGSFSPTPGQIGGA CCCCCCCCCCCCCCE	38.56	30266825
1595	Phosphorylation	DGADPNPYVKTYLLP CCCCCCCCCEEEECC	22.63	-
1597	Ubiquitination	ADPNPYVKTYLLPDN CCCCCCCEEEECCCC	26.13	-
1606	Ubiquitination	YLLPDNHKTSKRKTK EECCCCCCCCCCCCC	61.83	-
1611	Acetylation	NHKTSKRKTKISRKT CCCCCCCCCCCCCCC	58.88	8271313
1632	Phosphorylation	EMLVYSGYSKETLRQ HHHHHCCCCHHHHHH	15.61	-
1633	Phosphorylation	MLVYSGYSKETLRQR HHHHCCCCHHHHHHH	27.78	-
1648	O-linked_Glycosylation	ELQLSVLSAESLREN HHHHHHHCHHHHHHH	28.03	30379171
1648	Phosphorylation	ELQLSVLSAESLREN HHHHHHHCHHHHHHH	28.03	29083192
1651	O-linked_Glycosylation	LSVLSAESLRENFFL HHHHCHHHHHHHCCC	32.23	30379171
1651	Phosphorylation	LSVLSAESLRENFFL HHHHCHHHHHHHCCC	32.23	29083192
1672	Ubiquitination	LKDFNLSKETVKWYQ HHHCCCCHHHHEEEE	61.65	-

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
259	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
259	S	Phosphorylation	12719431
Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation.
259	S	Phosphorylation	12719431
Ser-259 phosphorylation may be mediated by CDK1 or JNK, depending on the physiological state of the cell.

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 P3C2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATG7_HUMAN	ATG7	physical	20562859
ANFY1_HUMAN	ANKFY1	physical	20562859
FKBP4_HUMAN	FKBP4	physical	20562859
SYTC_HUMAN	TARS	physical	20562859
PGK1_HUMAN	PGK1	physical	20562859
MLP3A_HUMAN	MAP1LC3A	physical	20562859
PA2G4_HUMAN	PA2G4	physical	20562859
TKT_HUMAN	TKT	physical	20562859
EIF3A_HUMAN	EIF3A	physical	20562859
TRI27_HUMAN	TRIM27	physical	22128329
CLCA_HUMAN	CLTA	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 P3C2A_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
"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-259, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 SER-108; SER-254; SER-259;SER-338 AND SER-1553, AND MASS SPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-108; SER-259 ANDSER-338, AND MASS SPECTROMETRY.	18669648 [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 SER-108; SER-259 ANDSER-1553, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY.	19007248 [Abstract]
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