PK3CG_HUMAN - dbPTM
PK3CG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PK3CG_HUMAN
UniProt AC P48736
Protein Name Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Gene Name PIK3CG
Organism Homo sapiens (Human).
Sequence Length 1102
Subcellular Localization Cytoplasm . Cell membrane .
Protein Description Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis..
Protein Sequence MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLHVAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA
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 Orthologous
Protein Cluster
7Ubiquitination-MELENYKQPVVLRE
-CCCCCCCCCEEECC		60.76-
31PhosphorylationKPRSAAASLSSMELI
CCHHHHHHHHCCCEE		24.8627251275
33PhosphorylationRSAAASLSSMELIPI
HHHHHHHHCCCEEEE		25.7427251275
34PhosphorylationSAAASLSSMELIPIE
HHHHHHHCCCEEEEE		22.9027251275
103UbiquitinationFLLLYQKKGQWYEIY
EEEEEEECCCEEEEE		40.59-
113PhosphorylationWYEIYDKYQVVQTLD
EEEEECHHHHHHHHH		12.0224043423
118PhosphorylationDKYQVVQTLDCLRYW
CHHHHHHHHHHHHHH		16.9824043423
182PhosphorylationFTRRGLVTPRMAEVA
EECCCCCCHHHHHHH		15.3724719451
196PhosphorylationASRDPKLYAMHPWVT
HCCCCCCCEECCCCC		14.1720049867
204PhosphorylationAMHPWVTSKPLPEYL
EECCCCCCCCCCHHH		23.7424719451
227PhosphorylationIFIVIHRSTTSQTIK
EEEEEECCCCCCEEE		23.1322817900
228PhosphorylationFIVIHRSTTSQTIKV
EEEEECCCCCCEEEE		30.35-
229PhosphorylationIVIHRSTTSQTIKVS
EEEECCCCCCEEEEC		21.78-
230PhosphorylationVIHRSTTSQTIKVSP
EEECCCCCCEEEECC		25.97-
232PhosphorylationHRSTTSQTIKVSPDD
ECCCCCCEEEECCCC		23.64-
250PhosphorylationAILQSFFTKMAKKKS
HHHHHHHHHHHHCCC		20.2122817900
255UbiquitinationFFTKMAKKKSLMDIP
HHHHHHHCCCCCCCC		37.75-
256UbiquitinationFTKMAKKKSLMDIPE
HHHHHHCCCCCCCCC		48.38-
288UbiquitinationLVGETPIKNFQWVRH
EECCCCCCCCHHHHH		53.57-
417PhosphorylationWNVWLEFSIKIKDLP
HHHHHEEEEECCCCC		17.3824719451
444UbiquitinationKAPALSSKASAESPS
CCCHHCCCCCCCCCC		42.88-
449PhosphorylationSSKASAESPSSESKG
CCCCCCCCCCCCCCC		29.7829052541
451PhosphorylationKASAESPSSESKGKV
CCCCCCCCCCCCCHH		56.8929052541
452PhosphorylationASAESPSSESKGKVQ
CCCCCCCCCCCCHHH		49.6429052541
496PhosphorylationGKGEDQGSFNADKLT
CCCCCCCCCCHHHHH		15.0822468782
501UbiquitinationQGSFNADKLTSATNP
CCCCCHHHHHCCCCC		51.78-
503PhosphorylationSFNADKLTSATNPDK
CCCHHHHHCCCCCCC		23.2722468782
506PhosphorylationADKLTSATNPDKENS
HHHHHCCCCCCCCCC		47.2322468782
553UbiquitinationEMPNQLRKQLEAIIA
HCCHHHHHHHHHHHH		68.76-
582PhosphorylationLWHFRYESLKHPKAY
HHHHHHHHCCCCCCC		33.51-
597UbiquitinationPKLFSSVKWGQQEIV
HHHHHCCCCCHHHHH		47.78-
606UbiquitinationGQQEIVAKTYQLLAR
CHHHHHHHHHHHHHH		36.55-
607PhosphorylationQQEIVAKTYQLLARR
HHHHHHHHHHHHHHH		13.53-
620PhosphorylationRREVWDQSALDVGLT
HHCCCCHHHHHHCHH		28.46-
627PhosphorylationSALDVGLTMQLLDCN
HHHHHCHHEEHHCCC		9.28-
636PhosphorylationQLLDCNFSDENVRAI
EHHCCCCCCHHHHHH		29.98-
650PhosphorylationIAVQKLESLEDDDVL
HEEEEHHHCCCHHHH		47.7124719451
746PhosphorylationIEMLQKVTLDIKSLS
HHHHHHHCEEHHHCC		26.25-
750UbiquitinationQKVTLDIKSLSAEKY
HHHCEEHHHCCCCCC		45.04-
753PhosphorylationTLDIKSLSAEKYDVS
CEEHHHCCCCCCCHH		41.2826091039
756UbiquitinationIKSLSAEKYDVSSQV
HHHCCCCCCCHHHHH		46.60-
757PhosphorylationKSLSAEKYDVSSQVI
HHCCCCCCCHHHHHH		17.0622817900
760PhosphorylationSAEKYDVSSQVISQL
CCCCCCHHHHHHHHH		16.5028122231
761PhosphorylationAEKYDVSSQVISQLK
CCCCCHHHHHHHHHH		28.4528122231
765PhosphorylationDVSSQVISQLKQKLE
CHHHHHHHHHHHHHH		30.5124719451
768UbiquitinationSQVISQLKQKLENLQ
HHHHHHHHHHHHHHC		37.44-
770UbiquitinationVISQLKQKLENLQNS
HHHHHHHHHHHHCCC		57.06-
792UbiquitinationVPYDPGLKAGALAIE
CCCCCCCCHHCHHHH		51.17-
853PhosphorylationQILRIMESIWETESL
HHHHHHHHHHCCCCC		18.6724275569
903UbiquitinationVGNTGAFKDEVLNHW
CCCCCCHHHHHHHHH		53.06-
912UbiquitinationEVLNHWLKEKSPTEE
HHHHHHHHCCCCCHH		58.88-
974PhosphorylationHILGNYKSFLGINKE
HHHCCCHHHHCCCCC		18.4926657352
1000AcetylationFVMGTSGKKTSPHFQ
EEECCCCCCCCCCHH		53.2830591325
1024PhosphorylationYLALRHHTNLLIILF
HHHHHHHHHHHHHHH		22.8021474070
1101PhosphorylationIKQGEKHSA------
CCCCCCCCC------		46.9012661022
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
582SPhosphorylationKinasePRKCBP05771
GPS
1024TPhosphorylationKinasePKACAP17612
PSP
1024TPhosphorylationKinasePKA-Uniprot
1101SPhosphorylationKinasePK3CGP48736
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:15308747
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PK3CG_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 PK3CG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASK_HUMANKRASphysical
10542052
UTRO_HUMANUTRNphysical
20562859
ANM7_HUMANPRMT7physical
20562859
ZN282_HUMANZNF282physical
21900206
SET_HUMANSETphysical
21419339
LYN_HUMANLYNphysical
7721825
GBB1_HUMANGNB1genetic
12507995
GBG2_HUMANGNG2genetic
12507995
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
D10189 Pictilisib (USAN); Pictrelisib
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PK3CG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Identification and characterization of the autophosphorylation sitesof phosphoinositide 3-kinase isoforms beta and gamma.";
Czupalla C., Culo M., Muller E.C., Brock C., Reusch H.P., Spicher K.,Krause E., Nurnberg B.;
J. Biol. Chem. 278:11536-11545(2003).
Cited for: AUTOPHOSPHORYLATION AT SER-1101.

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