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O75747 (P3C2G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma

Short name=PI3K-C2-gamma
Short name=PtdIns-3-kinase C2 subunit gamma
EC=2.7.1.154
Alternative name(s):
Phosphoinositide 3-kinase-C2-gamma
Gene names
Name:PIK3C2G
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis By similarity.

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.

Subcellular location

Membrane; Peripheral membrane protein By similarity.

Tissue specificity

Highly expressed in liver, prostate and testis. Lower levels in small intestine, kidney and pancreas. Ref.1

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 domain.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K-RBD domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Contains 1 PX (phox homology) domain.

Sequence caution

The sequence CAA03853.1 differs from that shown. Reason: Erroneous termination at position 1446. Translated as stop.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol-3-phosphate biosynthetic process

Non-traceable author statement Ref.1. Source: GOC

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

phosphatidylinositol 3-kinase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_function1-phosphatidylinositol-3-kinase activity

Non-traceable author statement Ref.1. Source: UniProtKB

1-phosphatidylinositol-4-phosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol phosphate kinase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14451445Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma
PRO_0000088799

Regions

Domain285 – 37187PI3K-RBD
Domain453 – 628176C2 PI3K-type
Domain643 – 819177PIK helical
Domain916 – 1180265PI3K/PI4K
Domain1199 – 1311113PX
Domain1328 – 142497C2

Amino acid modifications

Modified residue4191Phosphotyrosine Ref.5

Natural variations

Natural variant1461P → L. Ref.3 Ref.4 Ref.6
Corresponds to variant rs11044004 [ dbSNP | Ensembl ].
VAR_056676
Natural variant2611A → E.
Corresponds to variant rs7133666 [ dbSNP | Ensembl ].
VAR_056677
Natural variant9111P → L. Ref.1 Ref.3 Ref.4
Corresponds to variant rs12312266 [ dbSNP | Ensembl ].
VAR_060323
Natural variant12901V → G.
Corresponds to variant rs12099555 [ dbSNP | Ensembl ].
VAR_060324
Natural variant14421N → T.
Corresponds to variant rs12816860 [ dbSNP | Ensembl ].
VAR_060325

Experimental info

Sequence conflict1291Missing in EAW96387. Ref.3
Sequence conflict1291Missing in AAI30278. Ref.4
Sequence conflict9651G → R in CAA03853. Ref.1
Sequence conflict12091Missing in CAA03853. Ref.1
Sequence conflict13141Missing in CAA03853. Ref.1
Sequence conflict13231E → EK in CAA03853. Ref.1
Sequence conflict13771R → L in CAA03853. Ref.1

Secondary structure

.................. 1445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75747 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 8D02A3620AE4318D

FASTA1,445165,715
        10         20         30         40         50         60 
MAYSWQTDPN PNESHEKQYE HQEFLFVNQP HSSSQVSLGF DQIVDEISGK IPHYESEIDE 

        70         80         90        100        110        120 
NTFFVPTAPK WDSTGHSLNE AHQISLNEFT SKSRELSWHQ VSKAPAIGFS PSVLPKPQNT 

       130        140        150        160        170        180 
NKECSWGSPI GKHHGADDSR FSILAPSFTS LDKINLEKEL ENENHNYHIG FESSIPPTNS 

       190        200        210        220        230        240 
SFSSDFMPKE ENKRSGHVNI VEPSLMLLKG SLQPGMWEST WQKNIESIGC SIQLVEVPQS 

       250        260        270        280        290        300 
SNTSLASFCN KVKKIRERYH AADVNFNSGK IWSTTTAFPY QLFSKTKFNI HIFIDNSTQP 

       310        320        330        340        350        360 
LHFMPCANYL VKDLIAEILH FCTNDQLLPK DHILSVCGSE EFLQNDHCLG SHKMFQKDKS 

       370        380        390        400        410        420 
VIQLHLQKSR EAPGKLSRKH EEDHSQFYLN QLLEFMHIWK VSRQCLLTLI RKYDFHLKYL 

       430        440        450        460        470        480 
LKTQENVYNI IEEVKKICSV LGCVETKQIT DAVNELSLIL QRKGENFYQS SETSAKGLIE 

       490        500        510        520        530        540 
KVTTELSTSI YQLINVYCNS FYADFQPVNV PRCTSYLNPG LPSHLSFTVY AAHNIPETWV 

       550        560        570        580        590        600 
HRINFPLEIK SLPRESMLTV KLFGIACATN NANLLAWTCL PLFPKEKSIL GSMLFSMTLQ 

       610        620        630        640        650        660 
SEPPVEMITP GVWDVSQPSP VTLQIDFPAT GWEYMKPDSE ENRSNLEEPL KECIKHIARL 

       670        680        690        700        710        720 
SQKQTPLLLS EEKKRYLWFY RFYCNNENCS LPLVLGSAPG WDERTVSEMH TILRRWTFSQ 

       730        740        750        760        770        780 
PLEALGLLTS SFPDQEIRKV AVQQLDNLLN DELLEYLPQL VQAVKFEWNL ESPLVQLLLH 

       790        800        810        820        830        840 
RSLQSIQVAH RLYWLLKNAE NEAYFKSWYQ KLLAALQFCA GKALNDEFSK EQKLIKILGD 

       850        860        870        880        890        900 
IGERVKSASD HQRQEVLKKE IGRLEEFFQD VNTCHLPLNP ALCIKGIDHD ACSYFTSNAL 

       910        920        930        940        950        960 
PLKITFINAN PMGKNISIIF KAGDDLRQDM LVLQLIQVMD NIWLQEGLDM QMIIYRCLST 

       970        980        990       1000       1010       1020 
GKDQGLVQMV PDAVTLAKIH RHSGLIGPLK ENTIKKWFSQ HNHLKADYEK ALRNFFYSCA 

      1030       1040       1050       1060       1070       1080 
GWCVVTFILG VCDRHNDNIM LTKSGHMFHI DFGKFLGHAQ TFGGIKRDRA PFIFTSEMEY 

      1090       1100       1110       1120       1130       1140 
FITEGGKNPQ HFQDFVELCC RAYNIIRKHS QLLLNLLEMM LYAGLPELSG IQDLKYVYNN 

      1150       1160       1170       1180       1190       1200 
LRPQDTDLEA TSHFTKKIKE SLECFPVKLN NLIHTLAQMS AISPAKSTSQ TFPQESCLLS 

      1210       1220       1230       1240       1250       1260 
TTRSIERATI LGFSKKSSNL YLIQVTHSNN ETSLTEKSFE QFSKLHSQLQ KQFASLTLPE 

      1270       1280       1290       1300       1310       1320 
FPHWWHLPFT NSDHRRFRDL NHYMEQILNV SHEVTNSDCV LSFFLSEAVQ QTVEESSPVY 

      1330       1340       1350       1360       1370       1380 
LGEKFPDKKP KVQLVISYED VKLTILVKHM KNIHLPDGSA PSAHVEFYLL PYPSEVRRRK 

      1390       1400       1410       1420       1430       1440 
TKSVPKCTDP TYNEIVVYDE VTELQGHVLM LIVKSKTVFV GAINIRLCSV PLDKEKWYPL 


GNSII 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of a third human C2-domain-containing class II phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this gene (PIK3C2G) to 12p12."
Rozycka M., Lu Y.-J., Brown R.A., Lau M.R., Shipley J.M., Fry M.J.
Genomics 54:569-574(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT LEU-911.
Tissue: Liver, Mammary gland and Prostate.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LEU-146 AND LEU-911.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-146 AND LEU-911.
[5]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[6]"Association of the PIK3C2G gene polymorphisms with type 2 DM in a Japanese population."
Daimon M., Sato H., Oizumi T., Toriyama S., Saito T., Karasawa S., Jimbu Y., Wada K., Kameda W., Susa S., Yamaguchi H., Emi M., Muramatsu M., Kubota I., Kawata S., Kato T.
Biochem. Biophys. Res. Commun. 365:466-471(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-146.
[7]"Crystal structure of the phox homology domain of human phosphoinositide-3-kinase-C2-gamma."
Structural genomics consortium (SGC)
Submitted (NOV-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1204-1307.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000008 mRNA. Translation: CAA03853.1. Sequence problems.
AC087236 Genomic DNA. No translation available.
AC087240 Genomic DNA. No translation available.
AC091815 Genomic DNA. No translation available.
AC092851 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96387.1.
BC130277 mRNA. Translation: AAI30278.1.
PIRPC4347.
RefSeqNP_001275701.1. NM_001288772.1.
NP_001275703.1. NM_001288774.1.
NP_004561.3. NM_004570.5.
UniGeneHs.22500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WWEX-ray1.25A1204-1307[»]
ProteinModelPortalO75747.
SMRO75747. Positions 227-1162, 1204-1307, 1332-1440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111306. 1 interaction.
STRING9606.ENSP00000404845.

Chemistry

BindingDBO75747.
ChEMBLCHEMBL1163120.
GuidetoPHARMACOLOGY2288.

PTM databases

PhosphoSiteO75747.

Proteomic databases

PaxDbO75747.
PRIDEO75747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266497; ENSP00000266497; ENSG00000139144.
ENST00000433979; ENSP00000404845; ENSG00000139144.
GeneID5288.
KEGGhsa:5288.
UCSCuc001rdt.3. human.

Organism-specific databases

CTD5288.
GeneCardsGC12P018414.
H-InvDBHIX0036732.
HGNCHGNC:8973. PIK3C2G.
MIM609001. gene.
neXtProtNX_O75747.
PharmGKBPA33306.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000168239.
HOVERGENHBG053398.
InParanoidO75747.
KOK00923.
PhylomeDBO75747.
TreeFamTF102031.

Enzyme and pathway databases

BioCycMetaCyc:HS06583-MONOMER.
BRENDA2.7.1.137. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO75747.
BgeeO75747.
CleanExHS_PIK3C2G.
GenevestigatorO75747.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75747.
GeneWikiPIK3C2G.
GenomeRNAi5288.
NextBio20434.
PROO75747.
SOURCESearch...

Entry information

Entry nameP3C2G_HUMAN
AccessionPrimary (citable) accession number: O75747
Secondary accession number(s): A1L3U0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM