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Protein

Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform

Gene

PIK3CG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.5 Publications

Miscellaneous

Candidate target in therapy for inflammatory diseases. Selective inhibitors and protein ablation are anti-inflammatory in multiple disease models such as asthma, rheumatoid arthritis, allergy, systemic lupus erythematosus, airway inflammation, lung injury and pancreatitis (PubMed:18278175).1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.
ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by both the alpha and the beta-gamma G proteins following stimulation of G protein-coupled receptors (GPCRs). Activation by GPCRs is assisted by the regulatory subunits (PIK3R5 or PIK3R6) leading to the translocation from the cytosol to the plasma membrane and to kinase activation. Inhibited by AS-604850 and AS-605240.2 Publications

Pathwayi: phosphatidylinositol phosphate biosynthesis

This protein is involved in the pathway phosphatidylinositol phosphate biosynthesis, which is part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol phosphate biosynthesis and in Phospholipid metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi829 – 838ATPBy similarity10
Nucleotide bindingi864 – 872ATPBy similarity9
Nucleotide bindingi961 – 969ATPBy similarity9

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: GO_Central
  • 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • ephrin receptor binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • kinase activity Source: MGI
  • phosphatidylinositol 3-kinase activity Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: GO_Central
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • adaptive immune response Source: UniProtKB
  • angiogenesis Source: UniProtKB-KW
  • cellular response to cAMP Source: Ensembl
  • cytokine production Source: UniProtKB
  • dendritic cell chemotaxis Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • hepatocyte apoptotic process Source: Ensembl
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • natural killer cell chemotaxis Source: UniProtKB
  • negative regulation of cardiac muscle contraction Source: UniProtKB
  • negative regulation of fibroblast apoptotic process Source: Ensembl
  • negative regulation of triglyceride catabolic process Source: Ensembl
  • neutrophil chemotaxis Source: UniProtKB
  • neutrophil extravasation Source: UniProtKB
  • phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • phosphatidylinositol biosynthetic process Source: Reactome
  • phosphorylation Source: MGI
  • platelet activation Source: Reactome
  • platelet aggregation Source: UniProtKB
  • positive regulation of acute inflammatory response Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • regulation of calcium ion transmembrane transport Source: Ensembl
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
  • respiratory burst involved in defense response Source: UniProtKB
  • secretory granule localization Source: Ensembl
  • T cell activation Source: UniProtKB
  • T cell chemotaxis Source: UniProtKB
  • T cell proliferation Source: UniProtKB

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processAngiogenesis, Chemotaxis, Endocytosis, Immunity, Inflammatory response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02818-MONOMER
BRENDAi2.7.1.137 2681
2.7.1.153 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
SignaLinkiP48736
SIGNORiP48736
UniPathwayiUPA00220

Chemistry databases

SwissLipidsiSLP:000000909

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC:2.7.1.153)
Short name:
PI3-kinase subunit gamma
Short name:
PI3K-gamma
Short name:
PI3Kgamma
Short name:
PtdIns-3-kinase subunit gamma
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma
Short name:
PtdIns-3-kinase subunit p110-gamma
Short name:
p110gamma
Phosphoinositide-3-kinase catalytic gamma polypeptide
Serine/threonine protein kinase PIK3CG (EC:2.7.11.1)
p120-PI3K
Gene namesi
Name:PIK3CG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000105851.10
HGNCiHGNC:8978 PIK3CG
MIMi601232 gene
neXtProtiNX_P48736

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi833K → R: Reduced inflammatory reactions but no alterations in cardiac contractility. 1 Publication1
Mutagenesisi947R → P: Abolishes protein and lipid kinase activity. Does not abolishes interaction with GRK2. 1 Publication1

Organism-specific databases

DisGeNETi5294
OpenTargetsiENSG00000105851
PharmGKBiPA33311

Chemistry databases

ChEMBLiCHEMBL3267
DrugBankiDB06831 2-((9H-PURIN-6-YLTHIO)METHYL)-5-CHLORO-3-(2-METHOXYPHENYL)QUINAZOLIN-4(3H)-ONE
DB02656 2-(4-Morpholinyl)-8-Phenyl-4h-1-Benzopyran-4-One
DB02375 Myricetin
DB06836 N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE
DB04216 Quercetin
DB02010 Staurosporine
DB05241 XL765
GuidetoPHARMACOLOGYi2156

Polymorphism and mutation databases

BioMutaiPIK3CG
DMDMi92090623

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000887921 – 1102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoformAdd BLAST1102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1024Phosphothreonine; by PKABy similarity1
Modified residuei1101Phosphoserine; by autocatalysis1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP48736
MaxQBiP48736
PaxDbiP48736
PeptideAtlasiP48736
PRIDEiP48736

PTM databases

iPTMnetiP48736
PhosphoSitePlusiP48736

Expressioni

Tissue specificityi

Pancreas, skeletal muscle, liver and heart.1 Publication

Gene expression databases

BgeeiENSG00000105851
CleanExiHS_PIK3CG
ExpressionAtlasiP48736 baseline and differential
GenevisibleiP48736 HS

Organism-specific databases

HPAiHPA069976

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK helical domain. Interaction with GRK2 is required for targeting to agonist-occupied receptor. Interacts with PDE3B (By similarity). Interacts with TPM2. Interacts with EPHA8; regulates integrin-mediated cell adhesion to substrate. Interacts with HRAS; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi111312, 22 interactors
DIPiDIP-37781N
IntActiP48736, 19 interactors
MINTiP48736
STRINGi9606.ENSP00000352121

Chemistry databases

BindingDBiP48736

Structurei

Secondary structure

11102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi145 – 158Combined sources14
Helixi165 – 167Combined sources3
Beta strandi169 – 171Combined sources3
Helixi172 – 179Combined sources8
Helixi181 – 190Combined sources10
Helixi193 – 198Combined sources6
Helixi209 – 212Combined sources4
Helixi213 – 215Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi220 – 226Combined sources7
Beta strandi229 – 235Combined sources7
Helixi241 – 243Combined sources3
Helixi246 – 252Combined sources7
Helixi256 – 259Combined sources4
Beta strandi263 – 265Combined sources3
Beta strandi271 – 274Combined sources4
Beta strandi283 – 285Combined sources3
Helixi287 – 289Combined sources3
Helixi291 – 298Combined sources8
Beta strandi303 – 308Combined sources6
Helixi313 – 316Combined sources4
Helixi354 – 356Combined sources3
Beta strandi359 – 369Combined sources11
Beta strandi375 – 377Combined sources3
Beta strandi380 – 391Combined sources12
Beta strandi393 – 398Combined sources6
Beta strandi406 – 419Combined sources14
Helixi420 – 422Combined sources3
Beta strandi428 – 434Combined sources7
Beta strandi462 – 469Combined sources8
Beta strandi473 – 475Combined sources3
Beta strandi478 – 483Combined sources6
Beta strandi484 – 486Combined sources3
Helixi499 – 502Combined sources4
Beta strandi511 – 513Combined sources3
Beta strandi515 – 520Combined sources6
Helixi549 – 560Combined sources12
Beta strandi563 – 565Combined sources3
Helixi569 – 577Combined sources9
Helixi579 – 582Combined sources4
Helixi586 – 588Combined sources3
Helixi589 – 593Combined sources5
Helixi601 – 612Combined sources12
Helixi615 – 618Combined sources4
Helixi624 – 630Combined sources7
Beta strandi632 – 634Combined sources3
Helixi638 – 648Combined sources11
Helixi653 – 666Combined sources14
Helixi667 – 669Combined sources3
Beta strandi671 – 674Combined sources4
Helixi676 – 687Combined sources12
Helixi689 – 705Combined sources17
Turni707 – 709Combined sources3
Helixi710 – 721Combined sources12
Turni722 – 724Combined sources3
Helixi726 – 751Combined sources26
Beta strandi755 – 757Combined sources3
Helixi761 – 774Combined sources14
Turni775 – 778Combined sources4
Beta strandi783 – 785Combined sources3
Beta strandi788 – 796Combined sources9
Helixi798 – 800Combined sources3
Beta strandi806 – 808Combined sources3
Beta strandi811 – 818Combined sources8
Beta strandi828 – 836Combined sources9
Helixi838 – 856Combined sources19
Turni857 – 859Combined sources3
Beta strandi869 – 873Combined sources5
Beta strandi876 – 880Combined sources5
Beta strandi885 – 887Combined sources3
Helixi888 – 895Combined sources8
Beta strandi898 – 900Combined sources3
Helixi906 – 914Combined sources9
Beta strandi915 – 917Combined sources3
Helixi918 – 941Combined sources24
Helixi949 – 951Combined sources3
Beta strandi952 – 955Combined sources4
Turni956 – 958Combined sources3
Beta strandi960 – 962Combined sources3
Helixi965 – 970Combined sources6
Helixi989 – 994Combined sources6
Turni998 – 1000Combined sources3
Helixi1004 – 1021Combined sources18
Helixi1024 – 1038Combined sources15
Beta strandi1039 – 1041Combined sources3
Turni1042 – 1045Combined sources4
Helixi1046 – 1054Combined sources9
Turni1055 – 1058Combined sources4
Helixi1061 – 1078Combined sources18
Helixi1081 – 1085Combined sources5
Turni1090 – 1092Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E8YX-ray2.00A144-1102[»]
1E8ZX-ray2.40A144-1102[»]
1HE8X-ray3.00A144-1102[»]
2A4ZX-ray2.90A144-1102[»]
2A5UX-ray2.70A144-1102[»]
2CHWX-ray2.60A144-1102[»]
2CHXX-ray2.50A144-1102[»]
2CHZX-ray2.60A144-1102[»]
2V4LX-ray2.50A144-1102[»]
3APCX-ray2.54A144-1102[»]
3APDX-ray2.55A144-1102[»]
3APFX-ray2.82A144-1102[»]
3CSFX-ray2.80A144-1102[»]
3CSTX-ray3.20A144-1102[»]
3DBSX-ray2.80A144-1102[»]
3DPDX-ray2.85A144-1102[»]
3ENEX-ray2.40A144-1102[»]
3IBEX-ray2.80A144-1102[»]
3L08X-ray2.70A144-1102[»]
3L13X-ray3.00A144-1102[»]
3L16X-ray2.90A144-1102[»]
3L17X-ray3.00A144-1102[»]
3L54X-ray2.30A144-1102[»]
3LJ3X-ray2.43A144-1102[»]
3MJWX-ray2.87A144-1102[»]
3ML8X-ray2.70A144-1102[»]
3ML9X-ray2.55A144-1102[»]
3NZSX-ray2.75A147-1094[»]
3NZUX-ray2.60A147-1094[»]
3OAWX-ray2.75A144-1102[»]
3P2BX-ray3.20A144-1102[»]
3PREX-ray2.91A144-1102[»]
3PRZX-ray2.60A144-1102[»]
3PS6X-ray2.60A144-1102[»]
3QAQX-ray2.90A144-1102[»]
3QARX-ray2.65A144-1102[»]
3QJZX-ray2.90A144-1102[»]
3QK0X-ray2.85A144-1102[»]
3R7QX-ray2.50A144-1102[»]
3R7RX-ray2.90A144-1102[»]
3S2AX-ray2.55A144-1102[»]
3SD5X-ray3.20A144-1102[»]
3T8MX-ray2.50A144-1102[»]
3TJPX-ray2.70A144-1102[»]
3TL5X-ray2.79A144-1102[»]
3ZVVX-ray2.50A144-1102[»]
3ZW3X-ray2.80A144-1102[»]
4ANUX-ray2.81A144-1102[»]
4ANVX-ray2.13A144-1102[»]
4ANWX-ray2.31A144-1102[»]
4ANXX-ray2.73A144-1102[»]
4AOFX-ray3.30A144-1102[»]
4DK5X-ray2.95A144-1102[»]
4EZJX-ray2.67A144-1102[»]
4EZKX-ray2.80A144-1102[»]
4EZLX-ray2.94A144-1102[»]
4F1SX-ray3.00A144-1102[»]
4FA6X-ray2.70A144-1102[»]
4FADX-ray2.70A144-1102[»]
4FHJX-ray2.60A144-1102[»]
4FHKX-ray3.00A144-1102[»]
4FJYX-ray2.90A144-1102[»]
4FJZX-ray3.00A144-1102[»]
4FLHX-ray2.60A144-1102[»]
4FULX-ray2.47A144-1102[»]
4G11X-ray3.40A144-1102[»]
4GB9X-ray2.44A144-1102[»]
4HLEX-ray2.78A144-1102[»]
4HVBX-ray2.35A144-1102[»]
4J6IX-ray2.90A144-1102[»]
4KZ0X-ray2.87A144-1102[»]
4KZCX-ray3.25A144-1102[»]
4PS3X-ray2.90A144-1102[»]
4PS7X-ray2.69A144-1102[»]
4PS8X-ray2.99A144-1102[»]
4URKX-ray2.90A144-1102[»]
4WWNX-ray2.70A144-1102[»]
4WWOX-ray2.30A144-1102[»]
4WWPX-ray2.40A144-1102[»]
4XX5X-ray2.76A144-1102[»]
4XZ4X-ray2.60A144-1102[»]
5EDSX-ray2.80A144-1102[»]
5G2NX-ray2.68A144-1102[»]
5G55X-ray2.45A144-1102[»]
5JHAX-ray2.51A144-1102[»]
5JHBX-ray2.48A144-1102[»]
5KAEX-ray2.65A144-1102[»]
5OQ4X-ray2.70A144-1102[»]
5T23X-ray2.78A144-1102[»]
6AUDX-ray2.02A144-1102[»]
ProteinModelPortaliP48736
SMRiP48736
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48736

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 141PI3K-ABDPROSITE-ProRule annotationAdd BLAST108
Domaini217 – 309PI3K-RBDPROSITE-ProRule annotationAdd BLAST93
Domaini357 – 521C2 PI3K-typePROSITE-ProRule annotationAdd BLAST165
Domaini541 – 723PIK helicalPROSITE-ProRule annotationAdd BLAST183
Domaini828 – 1073PI3K/PI4KPROSITE-ProRule annotationAdd BLAST246

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi19 – 23Poly-Arg5

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0904 Eukaryota
COG5032 LUCA
GeneTreeiENSGT00760000119110
HOGENOMiHOG000252912
HOVERGENiHBG101026
InParanoidiP48736
KOiK21289
OMAiFTEEVLW
OrthoDBiEOG091G027R
PhylomeDBiP48736
TreeFamiTF102031

Family and domain databases

Gene3Di1.10.1070.11, 1 hit
2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR035892 C2_domain_sf
IPR011009 Kinase-like_dom_sf
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR003113 PI3K_adapt-bd_dom
IPR002420 PI3K_C2_dom
IPR000341 PI3K_Ras-bd_dom
IPR008290 PI3K_Vps34
IPR015433 PI_Kinase
IPR001263 PInositide-3_kin_accessory_dom
IPR029071 Ubiquitin-like_domsf
PANTHERiPTHR10048 PTHR10048, 1 hit
PfamiView protein in Pfam
PF00454 PI3_PI4_kinase, 1 hit
PF00792 PI3K_C2, 1 hit
PF00794 PI3K_rbd, 1 hit
PF00613 PI3Ka, 1 hit
PIRSFiPIRSF000587 PI3K_Vps34, 1 hit
SMARTiView protein in SMART
SM00142 PI3K_C2, 1 hit
SM00144 PI3K_rbd, 1 hit
SM00145 PI3Ka, 1 hit
SM00146 PI3Kc, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
SSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00915 PI3_4_KINASE_1, 1 hit
PS00916 PI3_4_KINASE_2, 1 hit
PS50290 PI3_4_KINASE_3, 1 hit
PS51544 PI3K_ABD, 1 hit
PS51547 PI3K_C2, 1 hit
PS51546 PI3K_RBD, 1 hit
PS51545 PIK_HELICAL, 1 hit

Sequencei

Sequence statusi: Complete.

P48736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELENYKQPV VLREDNCRRR RRMKPRSAAA SLSSMELIPI EFVLPTSQRK
60 70 80 90 100
CKSPETALLH VAGHGNVEQM KAQVWLRALE TSVAADFYHR LGPHHFLLLY
110 120 130 140 150
QKKGQWYEIY DKYQVVQTLD CLRYWKATHR SPGQIHLVQR HPPSEESQAF
160 170 180 190 200
QRQLTALIGY DVTDVSNVHD DELEFTRRGL VTPRMAEVAS RDPKLYAMHP
210 220 230 240 250
WVTSKPLPEY LWKKIANNCI FIVIHRSTTS QTIKVSPDDT PGAILQSFFT
260 270 280 290 300
KMAKKKSLMD IPESQSEQDF VLRVCGRDEY LVGETPIKNF QWVRHCLKNG
310 320 330 340 350
EEIHVVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF
360 370 380 390 400
TVSLWDCDRK FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS
410 420 430 440 450
PKPFTEEVLW NVWLEFSIKI KDLPKGALLN LQIYCGKAPA LSSKASAESP
460 470 480 490 500
SSESKGKVQL LYYVNLLLID HRFLLRRGEY VLHMWQISGK GEDQGSFNAD
510 520 530 540 550
KLTSATNPDK ENSMSISILL DNYCHPIALP KHQPTPDPEG DRVRAEMPNQ
560 570 580 590 600
LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ
610 620 630 640 650
QEIVAKTYQL LARREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES
660 670 680 690 700
LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR
710 720 730 740 750
SEIAQSRHYQ QRFAVILEAY LRGCGTAMLH DFTQQVQVIE MLQKVTLDIK
760 770 780 790 800
SLSAEKYDVS SQVISQLKQK LENLQNSQLP ESFRVPYDPG LKAGALAIEK
810 820 830 840 850
CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ DMLILQILRI
860 870 880 890 900
MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG
910 920 930 940 950
AFKDEVLNHW LKEKSPTEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND
960 970 980 990 1000
NIMITETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK
1010 1020 1030 1040 1050
KTSPHFQKFQ DICVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY
1060 1070 1080 1090 1100
IRDALTVGKN EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH

SA
Length:1,102
Mass (Da):126,454
Last modified:April 4, 2006 - v3
Checksum:iEF2B1A0E1CBEF406
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30Missing in CAA58284 (PubMed:7624799).Curated1
Sequence conflicti459Q → R in CAA58284 (PubMed:7624799).Curated1
Sequence conflicti459Q → R in AAG61115 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83368 mRNA Translation: CAA58284.1
AF327656 mRNA Translation: AAG61115.1
AC005018 Genomic DNA Translation: AAQ96873.1
CH236947 Genomic DNA Translation: EAL24396.1
CH471070 Genomic DNA Translation: EAW83387.1
BC035683 mRNA Translation: AAH35683.1
CCDSiCCDS5739.1
RefSeqiNP_001269355.1, NM_001282426.1
NP_001269356.1, NM_001282427.1
NP_002640.2, NM_002649.3
XP_005250500.1, XM_005250443.3
UniGeneiHs.32942
Hs.561747

Genome annotation databases

EnsembliENST00000359195; ENSP00000352121; ENSG00000105851
ENST00000440650; ENSP00000392258; ENSG00000105851
ENST00000496166; ENSP00000419260; ENSG00000105851
GeneIDi5294
KEGGihsa:5294
UCSCiuc003vdu.5 human

Similar proteinsi

Entry informationi

Entry nameiPK3CG_HUMAN
AccessioniPrimary (citable) accession number: P48736
Secondary accession number(s): A4D0Q6, Q8IV23, Q9BZC8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 4, 2006
Last modified: March 28, 2018
This is version 187 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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