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UniProtKB/Swiss-Prot entry P48736


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PK3CG_HUMAN
Primary accession number P48736
Secondary accession numbers Q8IV23 Q9BZC8
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on April 4, 2006 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Synonyms EC 2.7.1.153
PI3-kinase p110 subunit gamma
PtdIns-3-kinase subunit p110
PI3Kgamma
PI3K
p120-PI3K
Gene name
Name: PIK3CG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
PubMed=7624799 [NCBI, ExPASy, EBI, Israel, Japan]
Stoyanov B., Volinia S., Hanck T., Rubio I., Loubtchenkov M., Malek D., Stoyanova S., Vanhaesebroeck B., Dhand R., Nuernberg B., Gierschik P., Seedorf K., Hsuan J.J., Waterfield M.D., Wetzker R.;
"Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase.";
Science 269:690-693(1995).
[2]
SEQUENCE REVISION.
Waterfield M.D.;
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Michalke M., Schaefer M., Stoyanov B., Wetzker R., Nuernberg B.;
"Regulation of a G-protein-activated phosphoinositide-3-kinase.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH PIK3R5.
DOI=10.1016/j.cub.2005.02.020; PubMed=15797027 [NCBI, ExPASy, EBI, Israel, Japan]
Suire S., Coadwell J., Ferguson G.J., Davidson K., Hawkins P., Stephens L.;
"p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma.";
Curr. Biol. 15:566-570(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102.
DOI=10.1038/46319; PubMed=10580505 [NCBI, ExPASy, EBI, Israel, Japan]
Walker E.H., Perisic O., Ried C., Stephens L., Williams R.L.;
"Structural insights into phosphoinositide 3-kinase catalysis and signalling.";
Nature 402:313-320(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X83368; CAA58284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF327656; AAG61115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005018; AAQ96873.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035683; AAH35683.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_002640.2; -.
UniGene Hs.32942
3D structure databases
PDB
1E8Y; X-ray; 2.00 A; A=144-1102.[ExPASy / RCSB / EBI]
1E8Z; X-ray; 2.40 A; A=144-1102.[ExPASy / RCSB / EBI]
1HE8; X-ray; 3.00 A; A=144-1102.[ExPASy / RCSB / EBI]
2A4Z; X-ray; 2.90 A; A=144-1102.[ExPASy / RCSB / EBI]
2A5U; X-ray; 2.70 A; A=144-1102.[ExPASy / RCSB / EBI]
2CHW; X-ray; 2.60 A; A=144-1102.[ExPASy / RCSB / EBI]
2CHX; X-ray; 2.50 A; A=144-1102.[ExPASy / RCSB / EBI]
2CHZ; X-ray; 2.60 A; A=144-1102.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E8Y; -.
1E8Z; -.
1HE8; -.
2A4Z; -.
2A5U; -.
2CHW; -.
2CHX; -.
2CHZ; -.
ModBase P48736.
Protein-protein interaction databases
IntAct P48736; -.
PTM databases
PhosphoSite P48736; -.
Organism-specific databases
H-InvDB HIX0025282; -.
HGNC HGNC:8978; PIK3CG.
GenAtlas PIK3CG.
HPA CAB010283; -.
MIM 601232; gene. [NCBI / EBI]
PharmGKB PA33311; -.
GeneCards P48736.
Gene expression databases
ArrayExpress P48736; -.
CleanEx HS_PIK3CG; -.
GermOnline ENSG00000105851; Homo sapiens.
Ontologies
GO
GO:0016303; Molecular function: 1-phosphatidylinositol-3-kinase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000403; PI3/4_kinase_cat.
IPR002420; PI3K_C2.
IPR000341; PI3K_ras_bd.
IPR001263; PI3Ka.
IPR015433; PI_Kinase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1070.11; PI3/4_kinase_cat; 1.
G3DSA:1.25.40.70; PI3Ka; 1.
PANTHER PTHR10048; PI_Kinase; 1.
Pfam PF00454; PI3_PI4_kinase; 1.
PF00792; PI3K_C2; 1.
PF00794; PI3K_rbd; 1.
PF00613; PI3Ka; 1.
Pfam graphical view of domain structure.
SMART SM00142; PI3K_C2; 1.
SM00144; PI3K_rbd; 1.
SM00145; PI3Ka; 1.
SM00146; PI3Kc; 1.
SMART graphical view of domain structure.
PROSITE PS00915; PI3_4_KINASE_1; 1.
PS00916; PI3_4_KINASE_2; 1.
PS50290; PI3_4_KINASE_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P48736.
Genome annotation databases
Ensembl ENSG00000105851; Homo sapiens. [Contig view]
GeneID 5294; -.
KEGG hsa:5294; -.
Phylogenomic databases
HOGENOM P48736; -.
HOVERGEN P48736; -.
Other
LinkHub P48736; -.
SOURCE PIK3CG; Homo sapiens.
ProtoNet P48736.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1102  1102     Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform. PRO_0000088792
DOMAIN   828   1073  246     PI3K/PI4K. 
COMPBIAS   19     23  5     Poly-Arg. 
CONFLICT   30     30        Missing (in Ref. 1; CAA58284). 
CONFLICT   459    459        Q -> R (in Ref. 1 and 3). 
HELIX   145    158  14      
STRAND   169    171  3      
HELIX   172    179  8      
HELIX   181    190  10      
HELIX   193    198  6      
HELIX   209    212  4      
STRAND   216    218  3      
STRAND   220    226  7      
HELIX   241    243  3      
HELIX   246    252  7      
STRAND   271    274  4      
HELIX   287    289  3      
HELIX   291    298  8      
STRAND   303    308  6      
HELIX   313    316  4      
STRAND   359    369  11      
STRAND   380    391  12      
STRAND   393    398  6      
STRAND   406    419  14      
HELIX   420    422  3      
STRAND   428    434  7      
STRAND   462    469  8      
STRAND   478    483  6      
HELIX   499    502  4      
STRAND   511    513  3      
STRAND   515    520  6      
HELIX   549    560  12      
HELIX   569    577  9      
HELIX   579    582  4      
HELIX   586    588  3      
HELIX   589    593  5      
HELIX   601    612  12      
HELIX   615    618  4      
HELIX   624    630  7      
HELIX   638    648  11      
HELIX   653    666  14      
HELIX   667    669  3      
STRAND   671    674  4      
HELIX   676    687  12      
HELIX   689    705  17      
TURN   707    709  3      
HELIX   710    721  12      
HELIX   726    751  26      
STRAND   755    757  3      
HELIX   761    774  14      
TURN   775    778  4      
STRAND   783    785  3      
STRAND   788    796  9      
HELIX   798    800  3      
STRAND   806    808  3      
STRAND   811    818  8      
STRAND   828    836  9      
HELIX   838    856  19      
TURN   857    859  3      
STRAND   869    873  5      
STRAND   876    880  5      
STRAND   885    887  3      
HELIX   888    895  8      
HELIX   906    914  9      
HELIX   918    941  24      
HELIX   949    951  3      
STRAND   952    955  4      
STRAND   960    962  3      
HELIX   989    994  6      
HELIX   1004   1021  18      
HELIX   1024   1038  15      
STRAND   1039   1041  3      
HELIX   1046   1054  9      
TURN   1055   1058  4      
HELIX   1061   1078  18      
HELIX   1081   1085  5      
Sequence information
Length: 1102 AA [This is the length of the unprocessed precursor] Molecular weight: 126454 Da [This is the MW of the unprocessed precursor] CRC64: EF2B1A0E1CBEF406 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELENYKQPV VLREDNCRRR RRMKPRSAAA SLSSMELIPI EFVLPTSQRK CKSPETALLH 

        70         80         90        100        110        120 
VAGHGNVEQM KAQVWLRALE TSVAADFYHR LGPHHFLLLY QKKGQWYEIY DKYQVVQTLD 

       130        140        150        160        170        180 
CLRYWKATHR SPGQIHLVQR HPPSEESQAF QRQLTALIGY DVTDVSNVHD DELEFTRRGL 

       190        200        210        220        230        240 
VTPRMAEVAS RDPKLYAMHP WVTSKPLPEY LWKKIANNCI FIVIHRSTTS QTIKVSPDDT 

       250        260        270        280        290        300 
PGAILQSFFT KMAKKKSLMD IPESQSEQDF VLRVCGRDEY LVGETPIKNF QWVRHCLKNG 

       310        320        330        340        350        360 
EEIHVVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK 

       370        380        390        400        410        420 
FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS PKPFTEEVLW NVWLEFSIKI 

       430        440        450        460        470        480 
KDLPKGALLN LQIYCGKAPA LSSKASAESP SSESKGKVQL LYYVNLLLID HRFLLRRGEY 

       490        500        510        520        530        540 
VLHMWQISGK GEDQGSFNAD KLTSATNPDK ENSMSISILL DNYCHPIALP KHQPTPDPEG 

       550        560        570        580        590        600 
DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ 

       610        620        630        640        650        660 
QEIVAKTYQL LARREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL 

       670        680        690        700        710        720 
LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY 

       730        740        750        760        770        780 
LRGCGTAMLH DFTQQVQVIE MLQKVTLDIK SLSAEKYDVS SQVISQLKQK LENLQNSQLP 

       790        800        810        820        830        840 
ESFRVPYDPG LKAGALAIEK CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ 

       850        860        870        880        890        900 
DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG 

       910        920        930        940        950        960 
AFKDEVLNHW LKEKSPTEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMITETGNL 

       970        980        990       1000       1010       1020 
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK KTSPHFQKFQ DICVKAYLAL 

      1030       1040       1050       1060       1070       1080 
RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKN EEDAKKYFLD QIEVCRDKGW 

      1090       1100 
TVQFNWFLHL VLGIKQGEKH SA 

P48736 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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