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O75747

- P3C2G_HUMAN

UniProt

O75747 - P3C2G_HUMAN

Protein

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma

Gene

PIK3C2G

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. 1-phosphatidylinositol-3-kinase activity Source: UniProtKB
    2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
    3. ATP binding Source: UniProtKB-KW
    4. phosphatidylinositol binding Source: InterPro
    5. phosphatidylinositol phosphate kinase activity Source: UniProtKB

    GO - Biological processi

    1. chemotaxis Source: UniProtKB-KW
    2. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    3. phosphatidylinositol biosynthetic process Source: Reactome
    4. phosphatidylinositol-mediated signaling Source: InterPro
    5. phospholipid metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06583-MONOMER.
    BRENDAi2.7.1.137. 2681.
    ReactomeiREACT_120836. Synthesis of PIPs at the Golgi membrane.
    REACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma (EC:2.7.1.154)
    Short name:
    PI3K-C2-gamma
    Short name:
    PtdIns-3-kinase C2 subunit gamma
    Alternative name(s):
    Phosphoinositide 3-kinase-C2-gamma
    Gene namesi
    Name:PIK3C2G
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8973. PIK3C2G.

    Subcellular locationi

    Membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. phosphatidylinositol 3-kinase complex Source: RefGenome
    3. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33306.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14451445Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gammaPRO_0000088799Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei419 – 4191Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO75747.
    PRIDEiO75747.

    PTM databases

    PhosphoSiteiO75747.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO75747.
    BgeeiO75747.
    CleanExiHS_PIK3C2G.
    GenevestigatoriO75747.

    Interactioni

    Protein-protein interaction databases

    BioGridi111306. 1 interaction.
    STRINGi9606.ENSP00000404845.

    Structurei

    Secondary structure

    1
    1445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1204 – 121411
    Beta strandi1217 – 122711
    Beta strandi1232 – 12376
    Helixi1239 – 125214
    Turni1253 – 12553
    Helixi1267 – 12715
    Helixi1273 – 128715
    Helixi1292 – 12954
    Helixi1298 – 13058

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WWEX-ray1.25A1204-1307[»]
    ProteinModelPortaliO75747.
    SMRiO75747. Positions 539-1162, 1204-1307, 1332-1440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75747.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini285 – 37187PI3K-RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini453 – 628176C2 PI3K-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini643 – 819177PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini916 – 1180265PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini1199 – 1311113PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini1328 – 142497C2Add
    BLAST

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
    Contains 1 C2 domain.Curated
    Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
    Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
    Contains 1 PIK helical domain.PROSITE-ProRule annotation
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5032.
    HOGENOMiHOG000168239.
    HOVERGENiHBG053398.
    InParanoidiO75747.
    KOiK00923.
    PhylomeDBiO75747.
    TreeFamiTF102031.

    Family and domain databases

    Gene3Di1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 2 hits.
    3.30.1520.10. 1 hit.
    InterProiIPR016024. 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10048. PTHR10048. 1 hit.
    PfamiPF00454. 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]
    SMARTiSM00239. 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]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 2 hits.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS00915. 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]

    Sequencei

    Sequence statusi: Complete.

    O75747-1 [UniParc]FASTAAdd to Basket

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    MAYSWQTDPN PNESHEKQYE HQEFLFVNQP HSSSQVSLGF DQIVDEISGK     50
    IPHYESEIDE NTFFVPTAPK WDSTGHSLNE AHQISLNEFT SKSRELSWHQ 100
    VSKAPAIGFS PSVLPKPQNT NKECSWGSPI GKHHGADDSR FSILAPSFTS 150
    LDKINLEKEL ENENHNYHIG FESSIPPTNS SFSSDFMPKE ENKRSGHVNI 200
    VEPSLMLLKG SLQPGMWEST WQKNIESIGC SIQLVEVPQS SNTSLASFCN 250
    KVKKIRERYH AADVNFNSGK IWSTTTAFPY QLFSKTKFNI HIFIDNSTQP 300
    LHFMPCANYL VKDLIAEILH FCTNDQLLPK DHILSVCGSE EFLQNDHCLG 350
    SHKMFQKDKS VIQLHLQKSR EAPGKLSRKH EEDHSQFYLN QLLEFMHIWK 400
    VSRQCLLTLI RKYDFHLKYL LKTQENVYNI IEEVKKICSV LGCVETKQIT 450
    DAVNELSLIL QRKGENFYQS SETSAKGLIE KVTTELSTSI YQLINVYCNS 500
    FYADFQPVNV PRCTSYLNPG LPSHLSFTVY AAHNIPETWV HRINFPLEIK 550
    SLPRESMLTV KLFGIACATN NANLLAWTCL PLFPKEKSIL GSMLFSMTLQ 600
    SEPPVEMITP GVWDVSQPSP VTLQIDFPAT GWEYMKPDSE ENRSNLEEPL 650
    KECIKHIARL SQKQTPLLLS EEKKRYLWFY RFYCNNENCS LPLVLGSAPG 700
    WDERTVSEMH TILRRWTFSQ PLEALGLLTS SFPDQEIRKV AVQQLDNLLN 750
    DELLEYLPQL VQAVKFEWNL ESPLVQLLLH RSLQSIQVAH RLYWLLKNAE 800
    NEAYFKSWYQ KLLAALQFCA GKALNDEFSK EQKLIKILGD IGERVKSASD 850
    HQRQEVLKKE IGRLEEFFQD VNTCHLPLNP ALCIKGIDHD ACSYFTSNAL 900
    PLKITFINAN PMGKNISIIF KAGDDLRQDM LVLQLIQVMD NIWLQEGLDM 950
    QMIIYRCLST GKDQGLVQMV PDAVTLAKIH RHSGLIGPLK ENTIKKWFSQ 1000
    HNHLKADYEK ALRNFFYSCA GWCVVTFILG VCDRHNDNIM LTKSGHMFHI 1050
    DFGKFLGHAQ TFGGIKRDRA PFIFTSEMEY FITEGGKNPQ HFQDFVELCC 1100
    RAYNIIRKHS QLLLNLLEMM LYAGLPELSG IQDLKYVYNN LRPQDTDLEA 1150
    TSHFTKKIKE SLECFPVKLN NLIHTLAQMS AISPAKSTSQ TFPQESCLLS 1200
    TTRSIERATI LGFSKKSSNL YLIQVTHSNN ETSLTEKSFE QFSKLHSQLQ 1250
    KQFASLTLPE FPHWWHLPFT NSDHRRFRDL NHYMEQILNV SHEVTNSDCV 1300
    LSFFLSEAVQ QTVEESSPVY LGEKFPDKKP KVQLVISYED VKLTILVKHM 1350
    KNIHLPDGSA PSAHVEFYLL PYPSEVRRRK TKSVPKCTDP TYNEIVVYDE 1400
    VTELQGHVLM LIVKSKTVFV GAINIRLCSV PLDKEKWYPL GNSII 1445
    Length:1,445
    Mass (Da):165,715
    Last modified:November 30, 2010 - v3
    Checksum:i8D02A3620AE4318D
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291Missing in EAW96387. 1 PublicationCurated
    Sequence conflicti129 – 1291Missing in AAI30278. (PubMed:15489334)Curated
    Sequence conflicti965 – 9651G → R in CAA03853. (PubMed:9878262)Curated
    Sequence conflicti1209 – 12091Missing in CAA03853. (PubMed:9878262)Curated
    Sequence conflicti1314 – 13141Missing in CAA03853. (PubMed:9878262)Curated
    Sequence conflicti1323 – 13231E → EK in CAA03853. (PubMed:9878262)Curated
    Sequence conflicti1377 – 13771R → L in CAA03853. (PubMed:9878262)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti146 – 1461P → L.3 Publications
    Corresponds to variant rs11044004 [ dbSNP | Ensembl ].
    VAR_056676
    Natural varianti261 – 2611A → E.
    Corresponds to variant rs7133666 [ dbSNP | Ensembl ].
    VAR_056677
    Natural varianti911 – 9111P → L.3 Publications
    Corresponds to variant rs12312266 [ dbSNP | Ensembl ].
    VAR_060323
    Natural varianti1290 – 12901V → G.
    Corresponds to variant rs12099555 [ dbSNP | Ensembl ].
    VAR_060324
    Natural varianti1442 – 14421N → T.
    Corresponds to variant rs12816860 [ dbSNP | Ensembl ].
    VAR_060325

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS44839.1.
    PIRiPC4347.
    RefSeqiNP_001275701.1. NM_001288772.1.
    NP_001275703.1. NM_001288774.1.
    NP_004561.3. NM_004570.5.
    UniGeneiHs.22500.

    Genome annotation databases

    EnsembliENST00000266497; ENSP00000266497; ENSG00000139144.
    ENST00000433979; ENSP00000404845; ENSG00000139144.
    GeneIDi5288.
    KEGGihsa:5288.
    UCSCiuc001rdt.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS44839.1.
    PIRi PC4347.
    RefSeqi NP_001275701.1. NM_001288772.1.
    NP_001275703.1. NM_001288774.1.
    NP_004561.3. NM_004570.5.
    UniGenei Hs.22500.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WWE X-ray 1.25 A 1204-1307 [» ]
    ProteinModelPortali O75747.
    SMRi O75747. Positions 539-1162, 1204-1307, 1332-1440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111306. 1 interaction.
    STRINGi 9606.ENSP00000404845.

    Chemistry

    BindingDBi O75747.
    ChEMBLi CHEMBL1163120.
    GuidetoPHARMACOLOGYi 2288.

    PTM databases

    PhosphoSitei O75747.

    Proteomic databases

    PaxDbi O75747.
    PRIDEi O75747.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266497 ; ENSP00000266497 ; ENSG00000139144 .
    ENST00000433979 ; ENSP00000404845 ; ENSG00000139144 .
    GeneIDi 5288.
    KEGGi hsa:5288.
    UCSCi uc001rdt.3. human.

    Organism-specific databases

    CTDi 5288.
    GeneCardsi GC12P018414.
    H-InvDB HIX0036732.
    HGNCi HGNC:8973. PIK3C2G.
    MIMi 609001. gene.
    neXtProti NX_O75747.
    PharmGKBi PA33306.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5032.
    HOGENOMi HOG000168239.
    HOVERGENi HBG053398.
    InParanoidi O75747.
    KOi K00923.
    PhylomeDBi O75747.
    TreeFami TF102031.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06583-MONOMER.
    BRENDAi 2.7.1.137. 2681.
    Reactomei REACT_120836. Synthesis of PIPs at the Golgi membrane.
    REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    EvolutionaryTracei O75747.
    GeneWikii PIK3C2G.
    GenomeRNAii 5288.
    NextBioi 20434.
    PROi O75747.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75747.
    Bgeei O75747.
    CleanExi HS_PIK3C2G.
    Genevestigatori O75747.

    Family and domain databases

    Gene3Di 1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 2 hits.
    3.30.1520.10. 1 hit.
    InterProi IPR016024. 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10048. PTHR10048. 1 hit.
    Pfami PF00454. 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 ]
    SMARTi SM00239. 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 ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 2 hits.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS00915. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiP3C2G_HUMAN
    AccessioniPrimary (citable) accession number: O75747
    Secondary accession number(s): A1L3U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [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

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3