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Q99490

- AGAP2_HUMAN

UniProt

Q99490 - AGAP2_HUMAN

Protein

Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2

Gene

AGAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Isoform 1 participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. It aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3 kinase but may protect cells from apoptosis by stimulating Akt. It also regulates the adapter protein 1 (AP-1)-dependent trafficking of proteins in the endosomal system. It seems to be oncogenic. It is overexpressed in cancer cells, prevents apoptosis and promotes cancer cell invasion.4 Publications

    Enzyme regulationi

    GAP activity is stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and, to a lesser extent, by phosphatidylinositol 3,4,5-trisphosphate (PIP3). Phosphatidic acid potentiates PIP2 stimulation.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi413 – 4208GTPSequence Analysis
    Nucleotide bindingi457 – 4615GTPSequence Analysis
    Nucleotide bindingi515 – 5184GTPSequence Analysis
    Zinc fingeri946 – 96924C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ARF GTPase activator activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. negative regulation of neuron apoptotic process Source: MGI
    3. negative regulation of protein catabolic process Source: MGI
    4. protein transport Source: UniProtKB-KW
    5. regulation of ARF GTPase activity Source: InterPro
    6. small GTPase mediated signal transduction Source: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_22237. Netrin-1 signaling.
    SignaLinkiQ99490.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
    Short name:
    AGAP-2
    Alternative name(s):
    Centaurin-gamma-1
    Short name:
    Cnt-g1
    GTP-binding and GTPase-activating protein 2
    Short name:
    GGAP2
    Phosphatidylinositol 3-kinase enhancer
    Short name:
    PIKE
    Gene namesi
    Name:AGAP2
    Synonyms:CENTG1, KIAA0167
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:16921. AGAP2.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. mitochondrion Source: HPA
    3. nucleolus Source: HPA
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA26411.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11921192Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2PRO_0000074217Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei638 – 6381Phosphoserine1 Publication

    Post-translational modificationi

    Isoform PIKE-A is phosphorylated at Tyr-682 and Tyr-774 by FYN, preventing its apoptotic cleavage.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99490.
    PaxDbiQ99490.
    PRIDEiQ99490.

    PTM databases

    PhosphoSiteiQ99490.

    Expressioni

    Tissue specificityi

    Isoform 1 is brain-specific. Isoform 2 is ubiquitously expressed, with highest levels in brain and heart.5 Publications

    Gene expression databases

    ArrayExpressiQ99490.
    BgeeiQ99490.
    CleanExiHS_AGAP2.
    GenevestigatoriQ99490.

    Organism-specific databases

    HPAiHPA023474.

    Interactioni

    Subunit structurei

    Isoform 1 interacts with EPB41L1, PLCG1, NF2, HOMER1 and HOMER2 By similarity. Isoform 2 interacts with activated AKT1 in the presence of guanine nucleotides, and with the AP-1 complex.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    INSRP062132EBI-2361824,EBI-475899
    PrlrQ085012EBI-7737644,EBI-7737664From a different organism.
    STAT5AP422293EBI-7737644,EBI-749537
    Stat5aP422302EBI-7737644,EBI-617434From a different organism.

    Protein-protein interaction databases

    BioGridi125549. 9 interactions.
    IntActiQ99490. 8 interactions.
    MINTiMINT-3037505.
    STRINGi9606.ENSP00000328160.

    Structurei

    Secondary structure

    1
    1192
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi406 – 4127
    Helixi415 – 4173
    Helixi419 – 42810
    Beta strandi438 – 44811
    Beta strandi451 – 4599
    Beta strandi461 – 4633
    Helixi466 – 4716
    Beta strandi473 – 4808
    Helixi484 – 50118
    Beta strandi503 – 5053
    Beta strandi509 – 5157
    Beta strandi521 – 5233
    Helixi529 – 53911
    Beta strandi540 – 5489
    Turni549 – 5524
    Helixi555 – 57420
    Beta strandi677 – 68610
    Beta strandi695 – 7039
    Turni704 – 7063
    Beta strandi707 – 7137
    Helixi714 – 7196
    Beta strandi724 – 7307
    Beta strandi732 – 7343
    Beta strandi878 – 8814
    Beta strandi887 – 8948
    Helixi895 – 91319

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BMJX-ray2.10A402-577[»]
    2IWRX-ray1.50A402-577[»]
    2RLONMR-A674-914[»]
    ProteinModelPortaliQ99490.
    SMRiQ99490. Positions 402-576, 674-752, 846-914, 934-1147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99490.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini676 – 910235PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini931 – 1051121Arf-GAPPROSITE-ProRule annotationAdd
    BLAST
    Repeati1090 – 111930ANK 1Add
    BLAST
    Repeati1123 – 115230ANK 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 2323Interaction with EPB41L1By similarityAdd
    BLAST
    Regioni180 – 22546Interactions with HOMER1 and NF2By similarityAdd
    BLAST
    Regioni267 – 390124Interaction with PLCG1By similarityAdd
    BLAST
    Regioni405 – 572168G domainAdd
    BLAST

    Domaini

    G domain binds GTP and has GTPase activity.
    Arf-GAP domain interacts with G domain and may regulate its GTPase activity.
    Although both PH domains of isoforms 1 and 2 bind phospholipids, they differently regulate subcellular location. PH domain of isoform 1 directs the protein to the nucleus, but PH domain of isoform 2 directs it to the cytosol. PH domain of isoform 2 is required for binding to AP-1.

    Sequence similaritiesi

    Belongs to the centaurin gamma-like family.Curated
    Contains 2 ANK repeats.PROSITE-ProRule annotation
    Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri946 – 96924C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5347.
    HOGENOMiHOG000007233.
    HOVERGENiHBG054045.
    InParanoidiQ99490.
    KOiK17848.
    PhylomeDBiQ99490.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    2.30.29.30. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001164. ArfGAP.
    IPR013684. MIRO-like.
    IPR027417. P-loop_NTPase.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00023. Ank. 1 hit.
    PF01412. ArfGap. 1 hit.
    PF08477. Miro. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    PRINTSiPR00405. REVINTRACTNG.
    SMARTiSM00248. ANK. 2 hits.
    SM00105. ArfGap. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS51419. RAB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99490-1) [UniParc]FASTAAdd to Basket

    Also known as: PIKE-L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSRGAGALQR RTTTYLISLT LVKLESVPPP PPSPSAAAVG APGARGSEPR     50
    DPGSPRGAEE PGKKRHERLF HRQDALWIST SSAGAGGAEP PALSPAPASP 100
    ARPVSPAPGR RLSLWAAPPG PPLSGGLSPD SKPGGAPSSS RRPLLSSPSW 150
    GGPEPEGRTG GGVPGSSSPH PGTGSRRLKV APPPPAPKPC KTVTTSGAKA 200
    GGGKGAGSRL SWPESEGKPR VKGSKSSAGT GASVSAAATA AAAGGGGSTA 250
    STSGGVGAGA GARGKLSPRK GKSKTLDNSD LHPGPPAGSP PPLTLPPTPS 300
    PATAVTAASA QPPGPAPPIT LEPPAPGLKR GREGGRASTR DRKMLKFISG 350
    IFTKSTGGPP GSGPLPGPPS LSSGSGSREL LGAELRASPK AVINSQEWTL 400
    SRSIPELRLG VLGDARSGKS SLIHRFLTGS YQVLEKTESE QYKKEMLVDG 450
    QTHLVLIREE AGAPDAKFSG WADAVIFVFS LEDENSFQAV SRLHGQLSSL 500
    RGEGRGGLAL ALVGTQDRIS ASSPRVVGDA RARALCADMK RCSYYETCAT 550
    YGLNVDRVFQ EVAQKVVTLR KQQQLLAACK SLPSSPSHSA ASTPVAGQAS 600
    NGGHTSDYSS SLPSSPNVGH RELRAEAAAV AGLSTPGSLH RAAKRRTSLF 650
    ANRRGSDSEK RSLDSRGETT GSGRAIPIKQ SFLLKRSGNS LNKEWKKKYV 700
    TLSSNGFLLY HPSINDYIHS THGKEMDLLR TTVKVPGKRP PRAISAFGPS 750
    ASINGLVKDM STVQMGEGLE ATTPMPSPSP SPSSLQPPPD QTSKHLLKPD 800
    RNLARALSTD CTPSGDLSPL SREPPPSPMV KKQRRKKLTT PSKTEGSAGQ 850
    AEAKRKMWKL KSFGSLRNIY KAEENFEFLI VSSTGQTWHF EAASFEERDA 900
    WVQAIESQIL ASLQCCESSK VKLRTDSQSE AVAIQAIRNA KGNSICVDCG 950
    APNPTWASLN LGALICIECS GIHRNLGTHL SRVRSLDLDD WPRELTLVLT 1000
    AIGNDTANRV WESDTRGRAK PSRDSSREER ESWIRAKYEQ LLFLAPLSTS 1050
    EEPLGRQLWA AVQAQDVATV LLLLAHARHG PLDTSVEDPQ LRSPLHLAAE 1100
    LAHVVITQLL LWYGADVAAR DAQGRTALFY ARQAGSQLCA DILLQHGCPG 1150
    EGGSAATTPS AATTPSITAT PSPRRRSSAA SVGRADAPVA LV 1192
    Length:1,192
    Mass (Da):124,674
    Last modified:May 16, 2006 - v2
    Checksum:i8DA53707C0127984
    GO
    Isoform 2 (identifier: Q99490-2) [UniParc]FASTAAdd to Basket

    Also known as: PIKE-A

    The sequence of this isoform differs from the canonical sequence as follows:
         1-336: Missing.
         337-390: ASTRDRKMLK...LGAELRASPK → MHAQRQFVVA...IQASLDSIRE
         853-872: Missing.

    Note: Contains a phosphotyrosine at position 682. Contains a phosphotyrosine at position 774.

    Show »
    Length:836
    Mass (Da):90,537
    Checksum:iB8E42631BC06D5DC
    GO

    Sequence cautioni

    The sequence BAA11484.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1137 – 11371Q → H in AAC39522. (PubMed:9192850)Curated
    Sequence conflicti1147 – 11471G → A in AAC39522. (PubMed:9192850)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti339 – 3391T → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036183
    Natural varianti455 – 4551V → A in a glioblastoma cell line. 1 Publication
    VAR_026438
    Natural varianti507 – 5071G → S.
    Corresponds to variant rs2301553 [ dbSNP | Ensembl ].
    VAR_022046
    Natural varianti518 – 5181R → G in a sarcoma cell line. 1 Publication
    VAR_026439
    Natural varianti568 – 5681T → I in a neuroblastoma cell line. 1 Publication
    VAR_026440
    Natural varianti651 – 6511A → V in a glioblastoma cell line. 1 Publication
    VAR_026441
    Natural varianti767 – 7671E → V in a glioblastoma cell line. 1 Publication
    VAR_026442
    Natural varianti816 – 8161D → Y in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036184
    Natural varianti939 – 9391N → D in a glioblastoma cell line. 1 Publication
    VAR_026443
    Natural varianti947 – 9471V → M in a sarcoma cell line. 1 Publication
    VAR_026444
    Natural varianti1022 – 10221S → P in a glioblastoma cell line. 1 Publication
    VAR_026445
    Natural varianti1124 – 11241G → V.1 Publication
    Corresponds to variant rs238521 [ dbSNP | Ensembl ].
    VAR_055532

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 336336Missing in isoform 2. 5 PublicationsVSP_018531Add
    BLAST
    Alternative sequencei337 – 39054ASTRD…RASPK → MHAQRQFVVAAVRAEVRRHE VAKQALNRLRKLAERVDDPE LQDSIQASLDSIRE in isoform 2. 5 PublicationsVSP_018532Add
    BLAST
    Alternative sequencei853 – 87220Missing in isoform 2. 5 PublicationsVSP_018533Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81031 Genomic DNA. Translation: AAC39522.2.
    AF384128 mRNA. Translation: AAO39848.1.
    AY128689 mRNA. Translation: AAM97540.1.
    D79989 mRNA. Translation: BAA11484.2. Different initiation.
    AF413077 mRNA. Translation: AAL04171.1.
    AK292672 mRNA. Translation: BAF85361.1.
    CH471054 Genomic DNA. Translation: EAW97049.1.
    BC028020 mRNA. Translation: AAH28020.1.
    CCDSiCCDS44932.1. [Q99490-1]
    CCDS8951.1. [Q99490-2]
    RefSeqiNP_001116244.1. NM_001122772.2.
    NP_055585.1. NM_014770.3. [Q99490-2]
    UniGeneiHs.302435.

    Genome annotation databases

    EnsembliENST00000257897; ENSP00000257897; ENSG00000135439. [Q99490-2]
    GeneIDi116986.
    KEGGihsa:116986.
    UCSCiuc001spr.3. human. [Q99490-2]

    Polymorphism databases

    DMDMi97535883.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81031 Genomic DNA. Translation: AAC39522.2 .
    AF384128 mRNA. Translation: AAO39848.1 .
    AY128689 mRNA. Translation: AAM97540.1 .
    D79989 mRNA. Translation: BAA11484.2 . Different initiation.
    AF413077 mRNA. Translation: AAL04171.1 .
    AK292672 mRNA. Translation: BAF85361.1 .
    CH471054 Genomic DNA. Translation: EAW97049.1 .
    BC028020 mRNA. Translation: AAH28020.1 .
    CCDSi CCDS44932.1. [Q99490-1 ]
    CCDS8951.1. [Q99490-2 ]
    RefSeqi NP_001116244.1. NM_001122772.2.
    NP_055585.1. NM_014770.3. [Q99490-2 ]
    UniGenei Hs.302435.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BMJ X-ray 2.10 A 402-577 [» ]
    2IWR X-ray 1.50 A 402-577 [» ]
    2RLO NMR - A 674-914 [» ]
    ProteinModelPortali Q99490.
    SMRi Q99490. Positions 402-576, 674-752, 846-914, 934-1147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125549. 9 interactions.
    IntActi Q99490. 8 interactions.
    MINTi MINT-3037505.
    STRINGi 9606.ENSP00000328160.

    PTM databases

    PhosphoSitei Q99490.

    Polymorphism databases

    DMDMi 97535883.

    Proteomic databases

    MaxQBi Q99490.
    PaxDbi Q99490.
    PRIDEi Q99490.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257897 ; ENSP00000257897 ; ENSG00000135439 . [Q99490-2 ]
    GeneIDi 116986.
    KEGGi hsa:116986.
    UCSCi uc001spr.3. human. [Q99490-2 ]

    Organism-specific databases

    CTDi 116986.
    GeneCardsi GC12M058118.
    H-InvDB HIX0201900.
    HGNCi HGNC:16921. AGAP2.
    HPAi HPA023474.
    MIMi 605476. gene.
    neXtProti NX_Q99490.
    PharmGKBi PA26411.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5347.
    HOGENOMi HOG000007233.
    HOVERGENi HBG054045.
    InParanoidi Q99490.
    KOi K17848.
    PhylomeDBi Q99490.

    Enzyme and pathway databases

    Reactomei REACT_22237. Netrin-1 signaling.
    SignaLinki Q99490.

    Miscellaneous databases

    EvolutionaryTracei Q99490.
    GeneWikii CENTG1.
    GenomeRNAii 116986.
    NextBioi 80070.
    PROi Q99490.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99490.
    Bgeei Q99490.
    CleanExi HS_AGAP2.
    Genevestigatori Q99490.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    2.30.29.30. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001164. ArfGAP.
    IPR013684. MIRO-like.
    IPR027417. P-loop_NTPase.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 1 hit.
    PF01412. ArfGap. 1 hit.
    PF08477. Miro. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    PRINTSi PR00405. REVINTRACTNG.
    SMARTi SM00248. ANK. 2 hits.
    SM00105. ArfGap. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50115. ARFGAP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers."
      Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A., Meltzer P.S.
      Genomics 42:295-301(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), VARIANT VAL-1124.
    2. Roe B.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 389; 768-769; 1124; 1137 AND 1147 (ISOFORM 2).
    3. "GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins."
      Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.
      Mol. Cell. Biol. 23:2476-2488(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
      Tissue: Heart.
    4. "PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis."
      Rong R., Ahn J.-Y., Huang H., Nagata E., Kalman D., Kapp J.A., Tu J., Worley P.F., Snyder S.H., Ye K.
      Nat. Neurosci. 6:1153-1161(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Kiaa0167 as a member (centaurin gamma1) of centaurin ArfGAP family."
      Hong W.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    6. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Thymus.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 2).
      Tissue: Blood.
    10. "PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion."
      Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.
      J. Biol. Chem. 279:16441-16451(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AKT1, FUNCTION.
    11. "PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt."
      Ahn J.-Y., Hu Y., Kroll T.G., Allard P., Ye K.
      Proc. Natl. Acad. Sci. U.S.A. 101:6993-6998(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH AKT1, FUNCTION.
    12. "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3."
      Nie Z., Fei J., Premont R.T., Randazzo P.A.
      J. Cell Sci. 118:3555-3566(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH THE AP-1 COMPLEX, FUNCTION.
    13. "Genetic alteration and expression of the phosphoinositol-3-kinase/Akt pathway genes PIK3CA and PIKE in human glioblastomas."
      Knobbe C.B., Trampe-Kieslich A., Reifenberger G.
      Neuropathol. Appl. Neurobiol. 31:486-490(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-kinase enhancer-activating Akt, preventing its apoptotic cleavage and promoting cell survival."
      Tang X., Feng Y., Ye K.
      Cell Death Differ. 14:368-377(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-682 AND TYR-774 (ISOFORM 2) BY FYN.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "The centaurin gamma-1 GTPase-like domain functions as an NTPase."
      Soundararajan M., Yang X., Elkins J.M., Sobott F., Doyle D.A.
      Biochem. J. 401:679-688(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 402-577.
    17. "Split pleckstrin homology domain-mediated cytoplasmic-nuclear localization of PI3-kinase enhancer GTPase."
      Yan J., Wen W., Chan L.N., Zhang M.
      J. Mol. Biol. 378:425-435(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 674-914.
    18. "Phosphoinositol lipids bind to phosphatidylinositol 3 (PI3)-kinase enhancer GTPase and mediate its stimulatory effect on PI3-kinase and Akt signalings."
      Hu Y., Liu Z., Ye K.
      Proc. Natl. Acad. Sci. U.S.A. 102:16853-16858(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ALA-455; GLY-518; ILE-568; VAL-651; VAL-767; ASP-939; MET-947 AND PRO-1022, SUBCELLULAR LOCATION.
    19. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-339 AND TYR-816.

    Entry informationi

    Entry nameiAGAP2_HUMAN
    AccessioniPrimary (citable) accession number: Q99490
    Secondary accession number(s): A8K9F7
    , O00578, Q548E0, Q8IWU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 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