dbPTM

PI3R4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PI3R4_HUMAN
UniProt AC	Q99570
Protein Name	Phosphoinositide 3-kinase regulatory subunit 4
Gene Name	PIK3R4
Organism	Homo sapiens (Human).
Sequence Length	1358
Subcellular Localization	Late endosome . Cytoplasmic vesicle, autophagosome . Membrane Lipid-anchor . As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes. Localizes also to d
Protein Description	Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2. [PubMed: 20643123]
Protein Sequence	MGNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDPTLPLTSYKQELEELKIRLNSAQNCLPFQKASEKASEKAAMLFRQYVRDNLYDRISTRPFLNNIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNPADFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRTRGELKRAMDIFSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDHSIRELVTQMIHREPDKRLEAEDYLKQQRGNAFPEIFYTFLQPYMAQFAKETFLSADERILVIRKDLGNIIHNLCGHDLPEKAEGEPKENGLVILVSVITSCLQTLKYCDSKLAALELILHLAPRLSVEILLDRITPYLLHFSNDSVPRVRAEALRTLTKVLALVKEVPRNDINIYPEYILPGIAHLAQDDATIVRLAYAENIALLAETALRFLELVQLKNLNMENDPNNEEIDEVTHPNGNYDTELQALHEMVQQKVVTLLSDPENIVKQTLMENGITRLCVFFGRQKANDVLLSHMITFLNDKNDWHLRGAFFDSIVGVAAYVGWQSSSILKPLLQQGLSDAEEFVIVKALYALTCMCQLGLLQKPHVYEFASDIAPFLCHPNLWIRYGAVGFITVVARQISTADVYCKLMPYLDPYITQPIIQIERKLVLLSVLKEPVSRSIFDYALRSKDITSLFRHLHMRQKKRNGSLPDCPPPEDPAIAQLLKKLLSQGMTEEEEDKLLALKDFMMKSNKAKANIVDQSHLHDSSQKGVIDLAALGITGRQVDLVKTKQEPDDKRARKHVKQDSNVNEEWKSMFGSLDPPNMPQALPKGSDQEVIQTGKPPRSESSAGICVPLSTSSQVPEVTTVQNKKPVIPVLSSTILPSTYQIRITTCKTELQQLIQQKREQCNAERIAKQMMENAEWESKPPPPGWRPKGLLVAHLHEHKSAVNRIRVSDEHSLFATCSNDGTVKIWNSQKMEGKTTTTRSILTYSRIGGRVKTLTFCQGSHYLAIASDNGAVQLLGIEASKLPKSPKIHPLQSRILDQKEDGCVVDMHHFNSGAQSVLAYATVNGSLVGWDLRSSSNAWTLKHDLKSGLITSFAVDIHQCWLCIGTSSGTMACWDMRFQLPISSHCHPSRARIRRLSMHPLYQSWVIAAVQGNNEVSMWDMETGDRRFTLWASSAPPLSELQPSPHSVHGIYCSPADGNPILLTAGSDMKIRFWDLAYPERSYVVAGSTSSPSVSYYRKIIEGTEVVQEIQNKQKVGPSDDTPRRGPESLPVGHHDIITDVATFQTTQGFIVTASRDGIVKVWK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGNQLAGIA ------CCCCCCCCC	41.73	-
2	Myristoylation	------MGNQLAGIA ------CCCCCCCCC	41.73	8999962
39	Ubiquitination	LGSTRFFKVARAKHR CCCCCHHHHHHHHCC	32.07	27667366
61	Phosphorylation	VFAIQDPTLPLTSYK EEEECCCCCCCCCHH	49.66	21406692
65	Phosphorylation	QDPTLPLTSYKQELE CCCCCCCCCHHHHHH	28.24	21406692
66	Phosphorylation	DPTLPLTSYKQELEE CCCCCCCCHHHHHHH	37.71	21406692
67	Phosphorylation	PTLPLTSYKQELEEL CCCCCCCHHHHHHHH	16.08	21406692
68	Ubiquitination	TLPLTSYKQELEELK CCCCCCHHHHHHHHH	36.74	21906983
75	Ubiquitination	KQELEELKIRLNSAQ HHHHHHHHHHHHHHC	29.12	27667366
89	Ubiquitination	QNCLPFQKASEKASE CCCCCHHHHHHHHHH	55.01	21963094
93	Ubiquitination	PFQKASEKASEKAAM CHHHHHHHHHHHHHH	55.51	22817900
97	Ubiquitination	ASEKASEKAAMLFRQ HHHHHHHHHHHHHHH	38.66	21906983
111	Phosphorylation	QYVRDNLYDRISTRP HHHHHHHHHHHCCCH	14.94	24043423
115	Phosphorylation	DNLYDRISTRPFLNN HHHHHHHCCCHHHHH	21.18	24043423
116	Phosphorylation	NLYDRISTRPFLNNI HHHHHHCCCHHHHHH	39.73	24043423
169	Phosphorylation	VLLTDFASFKPTYLP EEEECHHHCCCCCCC	33.52	24719451
210	Phosphorylation	VDGGMFATELEYMRD CCCCCCEEHHHCCCC	29.82	28796482
214	Phosphorylation	MFATELEYMRDPSTP CCEEHHHCCCCCCCC	15.29	28796482
219	Phosphorylation	LEYMRDPSTPLVDLN HHCCCCCCCCCCCCC	47.12	28796482
220	Phosphorylation	EYMRDPSTPLVDLNS HCCCCCCCCCCCCCC	26.48	28796482
280	Ubiquitination	FPEQVLNKIEDHSIR CHHHHHHHHCCCCHH	43.22	21906983
300	Ubiquitination	MIHREPDKRLEAEDY HHHCCCCHHHCHHHH	70.38	29967540
309	Ubiquitination	LEAEDYLKQQRGNAF HCHHHHHHHHHCCCC	37.85	21906983
338	Phosphorylation	FAKETFLSADERILV HHHHHHCCCCCEEEE	29.50	-
348	Ubiquitination	ERILVIRKDLGNIIH CEEEEEECHHHHHHH	46.29	29967540
419	Phosphorylation	EILLDRITPYLLHFS HHHHHHHHHHHHHCC	13.53	29209046
421	Phosphorylation	LLDRITPYLLHFSND HHHHHHHHHHHCCCC	17.16	29209046
426	Phosphorylation	TPYLLHFSNDSVPRV HHHHHHCCCCCCHHH	29.04	29209046
429	Phosphorylation	LLHFSNDSVPRVRAE HHHCCCCCCHHHHHH	37.97	29209046
443	Ubiquitination	EALRTLTKVLALVKE HHHHHHHHHHHHHHC	38.06	21963094
449	Ubiquitination	TKVLALVKEVPRNDI HHHHHHHHCCCCCCC	54.57	21906983
459	Phosphorylation	PRNDINIYPEYILPG CCCCCCCCHHHHCCC	5.87	24043423
462	Phosphorylation	DINIYPEYILPGIAH CCCCCHHHHCCCHHH	11.85	24043423
476	Phosphorylation	HLAQDDATIVRLAYA HHHCCCCHHHHHHHH	27.31	24043423
482	Phosphorylation	ATIVRLAYAENIALL CHHHHHHHHHHHHHH	21.02	24043423
492	Phosphorylation	NIALLAETALRFLEL HHHHHHHHHHHHHHH	25.94	24043423
543	Phosphorylation	MVQQKVVTLLSDPEN HHHHHHHHHHCCHHH	25.60	20068231
546	Phosphorylation	QKVVTLLSDPENIVK HHHHHHHCCHHHHHH	54.99	20068231
553	Ubiquitination	SDPENIVKQTLMENG CCHHHHHHHHHHHCC	33.49	21906983
579	Phosphorylation	KANDVLLSHMITFLN HHHHHHHHHHHHHHC	13.57	26270265
583	Phosphorylation	VLLSHMITFLNDKND HHHHHHHHHHCCCCC	17.94	26270265
614	Phosphorylation	YVGWQSSSILKPLLQ HHCCCCHHHHHHHHH	36.87	24719451
673	Phosphorylation	HPNLWIRYGAVGFIT CCCEEEECCCHHHHE	10.58	19664994
680	Phosphorylation	YGAVGFITVVARQIS CCCHHHHEEEEECCC	13.48	-
698	Phosphorylation	VYCKLMPYLDPYITQ HHHHHHHHCCCCCCC	15.12	20071362
713	Ubiquitination	PIIQIERKLVLLSVL CHHHHHHHHHHHHHH	30.11	-
731	Phosphorylation	VSRSIFDYALRSKDI CCHHHHHHHHHCCCH	9.22	28152594
736	Ubiquitination	FDYALRSKDITSLFR HHHHHHCCCHHHHHH	46.87	-
740	Phosphorylation	LRSKDITSLFRHLHM HHCCCHHHHHHHHHH	26.33	24719451
772	Ubiquitination	PAIAQLLKKLLSQGM HHHHHHHHHHHHCCC	50.39	22817900
773	Malonylation	AIAQLLKKLLSQGMT HHHHHHHHHHHCCCC	55.41	26320211
773	Ubiquitination	AIAQLLKKLLSQGMT HHHHHHHHHHHCCCC	55.41	21906983
776	Phosphorylation	QLLKKLLSQGMTEEE HHHHHHHHCCCCHHH	34.81	23401153
780	Phosphorylation	KLLSQGMTEEEEDKL HHHHCCCCHHHHHHH	47.25	-
786	Ubiquitination	MTEEEEDKLLALKDF CCHHHHHHHHHHHHH	48.99	22817900
791	Ubiquitination	EDKLLALKDFMMKSN HHHHHHHHHHHHHCC	43.23	21906983
796	Ubiquitination	ALKDFMMKSNKAKAN HHHHHHHHCCHHHCC	38.80	22817900
797	Phosphorylation	LKDFMMKSNKAKANI HHHHHHHCCHHHCCC	26.18	29255136
801	Ubiquitination	MMKSNKAKANIVDQS HHHCCHHHCCCCCHH	43.50	29967540
808	Phosphorylation	KANIVDQSHLHDSSQ HCCCCCHHHCCCCCC	24.45	30266825
813	Phosphorylation	DQSHLHDSSQKGVID CHHHCCCCCCCCCCH	24.74	30266825
814	Phosphorylation	QSHLHDSSQKGVIDL HHHCCCCCCCCCCHH	41.80	30266825
816	Acetylation	HLHDSSQKGVIDLAA HCCCCCCCCCCHHHH	58.03	25953088
816	Ubiquitination	HLHDSSQKGVIDLAA HCCCCCCCCCCHHHH	58.03	29967540
835	Ubiquitination	GRQVDLVKTKQEPDD CCEEEEEECCCCCCH	58.25	27667366
836	Phosphorylation	RQVDLVKTKQEPDDK CEEEEEECCCCCCHH	30.40	28857561
837	Ubiquitination	QVDLVKTKQEPDDKR EEEEEECCCCCCHHH	47.12	24816145
843	Acetylation	TKQEPDDKRARKHVK CCCCCCHHHHHHHHH	56.17	26051181
847	Ubiquitination	PDDKRARKHVKQDSN CCHHHHHHHHHCCCC	52.33	22817900
850	Ubiquitination	KRARKHVKQDSNVNE HHHHHHHHCCCCCCH	48.37	21906983
853	Phosphorylation	RKHVKQDSNVNEEWK HHHHHCCCCCCHHHH	39.94	22167270
861	Phosphorylation	NVNEEWKSMFGSLDP CCCHHHHHHHCCCCC	22.03	21082442
865	Phosphorylation	EWKSMFGSLDPPNMP HHHHHHCCCCCCCCC	20.52	25159151
886	Phosphorylation	SDQEVIQTGKPPRSE CCHHHHHCCCCCCCC	35.73	26074081
888	Ubiquitination	QEVIQTGKPPRSESS HHHHHCCCCCCCCCC	56.06	21906983
892	Phosphorylation	QTGKPPRSESSAGIC HCCCCCCCCCCCCEE	47.83	30278072
894	Phosphorylation	GKPPRSESSAGICVP CCCCCCCCCCCEEEE	27.08	30278072
895	Phosphorylation	KPPRSESSAGICVPL CCCCCCCCCCEEEEC	26.85	30576142
903	Phosphorylation	AGICVPLSTSSQVPE CCEEEECCCCCCCCC	21.85	26074081
904	Phosphorylation	GICVPLSTSSQVPEV CEEEECCCCCCCCCE	39.83	26074081
905	Phosphorylation	ICVPLSTSSQVPEVT EEEECCCCCCCCCEE	18.52	26074081
906	Phosphorylation	CVPLSTSSQVPEVTT EEECCCCCCCCCEEE	34.97	26074081
912	Phosphorylation	SSQVPEVTTVQNKKP CCCCCCEEEECCCCC	21.42	20068231
913	Phosphorylation	SQVPEVTTVQNKKPV CCCCCEEEECCCCCC	25.85	20068231
918	Ubiquitination	VTTVQNKKPVIPVLS EEEECCCCCCEEEEC	52.66	-
925	Phosphorylation	KPVIPVLSSTILPST CCCEEEECCCCCCCC	26.18	30266825
926	Phosphorylation	PVIPVLSSTILPSTY CCEEEECCCCCCCCE	18.46	30266825
927	Phosphorylation	VIPVLSSTILPSTYQ CEEEECCCCCCCCEE	24.13	30266825
931	Phosphorylation	LSSTILPSTYQIRIT ECCCCCCCCEEEEEE	35.98	20068231
932	Phosphorylation	SSTILPSTYQIRITT CCCCCCCCEEEEEEE	19.94	27251275
933	Phosphorylation	STILPSTYQIRITTC CCCCCCCEEEEEEEC	13.28	27642862
938	Phosphorylation	STYQIRITTCKTELQ CCEEEEEEECHHHHH	19.12	20068231
939	Phosphorylation	TYQIRITTCKTELQQ CEEEEEEECHHHHHH	15.05	20068231
941	Ubiquitination	QIRITTCKTELQQLI EEEEEECHHHHHHHH	42.83	-
942	Phosphorylation	IRITTCKTELQQLIQ EEEEECHHHHHHHHH	44.04	-
951	Acetylation	LQQLIQQKREQCNAE HHHHHHHHHHHHCHH	41.34	25953088
951	Malonylation	LQQLIQQKREQCNAE HHHHHHHHHHHHCHH	41.34	26320211
951	Ubiquitination	LQQLIQQKREQCNAE HHHHHHHHHHHHCHH	41.34	22817900
962	Ubiquitination	CNAERIAKQMMENAE HCHHHHHHHHHHHCC	36.03	29967540
973	Ubiquitination	ENAEWESKPPPPGWR HHCCCCCCCCCCCCC	50.45	29967540
993	Ubiquitination	VAHLHEHKSAVNRIR EEEHHHCCCHHCEEE	36.81	29967540
1018	Ubiquitination	CSNDGTVKIWNSQKM ECCCCCEEEEECCCC	41.67	29967540
1024	Acetylation	VKIWNSQKMEGKTTT EEEEECCCCCCCCCC	38.45	26051181
1034	Phosphorylation	GKTTTTRSILTYSRI CCCCCCHHHHEEEEE	21.62	20068231
1037	Phosphorylation	TTTRSILTYSRIGGR CCCHHHHEEEEECCE	20.13	20068231
1038	Phosphorylation	TTRSILTYSRIGGRV CCHHHHEEEEECCEE	7.78	20068231
1039	Phosphorylation	TRSILTYSRIGGRVK CHHHHEEEEECCEEE	16.52	20068231
1074	Phosphorylation	QLLGIEASKLPKSPK EEEEEEHHHCCCCCC	23.18	-
1079	Phosphorylation	EASKLPKSPKIHPLQ EHHHCCCCCCCCCCH	29.50	19369195
1081	Ubiquitination	SKLPKSPKIHPLQSR HHCCCCCCCCCCHHH	61.82	29967540
1272	Phosphorylation	IRFWDLAYPERSYVV EEEEECCCCCCEEEE	16.96	-
1276	Phosphorylation	DLAYPERSYVVAGST ECCCCCCEEEEECCC	22.18	23663014
1277	Phosphorylation	LAYPERSYVVAGSTS CCCCCCEEEEECCCC	12.74	23663014
1282	Phosphorylation	RSYVVAGSTSSPSVS CEEEEECCCCCCCHH	18.51	23663014
1283	Phosphorylation	SYVVAGSTSSPSVSY EEEEECCCCCCCHHH	32.10	23663014
1284	Phosphorylation	YVVAGSTSSPSVSYY EEEECCCCCCCHHHH	41.78	23663014
1285	Phosphorylation	VVAGSTSSPSVSYYR EEECCCCCCCHHHHH	22.68	23663014
1287	Phosphorylation	AGSTSSPSVSYYRKI ECCCCCCCHHHHHHH	26.16	23663014
1289	Phosphorylation	STSSPSVSYYRKIIE CCCCCCHHHHHHHHC	22.30	23663014
1290	Phosphorylation	TSSPSVSYYRKIIEG CCCCCHHHHHHHHCC	12.72	23663014
1291	Phosphorylation	SSPSVSYYRKIIEGT CCCCHHHHHHHHCCC	9.64	23663014
1293	Ubiquitination	PSVSYYRKIIEGTEV CCHHHHHHHHCCCHH	31.73	22817900
1307	Ubiquitination	VVQEIQNKQKVGPSD HHHHHHHCCCCCCCC	34.81	21906983
1309	Ubiquitination	QEIQNKQKVGPSDDT HHHHHCCCCCCCCCC	51.25	22817900
1316	Phosphorylation	KVGPSDDTPRRGPES CCCCCCCCCCCCCCC	24.56	21082442

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
Oops, there are no upstream regulatory protein records of PI3R4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PI3R4_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 PI3R4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PI3R4_HUMAN !!

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 PI3R4_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Characterization of p150, an adaptor protein for the humanphosphatidylinositol (PtdIns) 3-kinase. Substrate presentation byphosphatidylinositol transfer protein to the p150.PtdIns 3-kinasecomplex."; Panaretou C., Domin J., Cockcroft S., Waterfield M.D.; J. Biol. Chem. 272:2477-2485(1997). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-63; 333-343;540-554 AND 786-791, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION,COFACTOR, TISSUE SPECIFICITY, AND INTERACTION WITH PIK3C3.	8999962 [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 SER-808; SER-813; SER-814;SER-853; SER-861; SER-865; SER-892; SER-925 AND SER-1079, AND MASSSPECTROMETRY.	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 SER-853; SER-865 ANDTHR-1316, AND MASS SPECTROMETRY.	18691976 [Abstract]