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Protein

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

Gene

AGAP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • axon guidance Source: Reactome
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of protein catabolic process Source: MGI
  • protein transport Source: UniProtKB-KW
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16921. AGAP2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: HPA
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA26411.

Polymorphism and mutation databases

BioMutaiAGAP2.
DMDMi97535883.

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
Isoform 2 (identifier: Q99490-2)
Modified residuei682 – 6821Phosphotyrosine
Modified residuei774 – 7741Phosphotyrosine

Post-translational modificationi

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

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

BgeeiQ99490.
CleanExiHS_AGAP2.
ExpressionAtlasiQ99490. baseline and differential.
GenevisibleiQ99490. HS.

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. 8 interactions.
IntActiQ99490. 8 interactions.
MINTiMINT-3037505.
STRINGi9606.ENSP00000449241.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
[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. AlignAdd to basket

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

        10         20         30         40         50
MSRGAGALQR RTTTYLISLT LVKLESVPPP PPSPSAAAVG APGARGSEPR
60 70 80 90 100
DPGSPRGAEE PGKKRHERLF HRQDALWIST SSAGAGGAEP PALSPAPASP
110 120 130 140 150
ARPVSPAPGR RLSLWAAPPG PPLSGGLSPD SKPGGAPSSS RRPLLSSPSW
160 170 180 190 200
GGPEPEGRTG GGVPGSSSPH PGTGSRRLKV APPPPAPKPC KTVTTSGAKA
210 220 230 240 250
GGGKGAGSRL SWPESEGKPR VKGSKSSAGT GASVSAAATA AAAGGGGSTA
260 270 280 290 300
STSGGVGAGA GARGKLSPRK GKSKTLDNSD LHPGPPAGSP PPLTLPPTPS
310 320 330 340 350
PATAVTAASA QPPGPAPPIT LEPPAPGLKR GREGGRASTR DRKMLKFISG
360 370 380 390 400
IFTKSTGGPP GSGPLPGPPS LSSGSGSREL LGAELRASPK AVINSQEWTL
410 420 430 440 450
SRSIPELRLG VLGDARSGKS SLIHRFLTGS YQVLEKTESE QYKKEMLVDG
460 470 480 490 500
QTHLVLIREE AGAPDAKFSG WADAVIFVFS LEDENSFQAV SRLHGQLSSL
510 520 530 540 550
RGEGRGGLAL ALVGTQDRIS ASSPRVVGDA RARALCADMK RCSYYETCAT
560 570 580 590 600
YGLNVDRVFQ EVAQKVVTLR KQQQLLAACK SLPSSPSHSA ASTPVAGQAS
610 620 630 640 650
NGGHTSDYSS SLPSSPNVGH RELRAEAAAV AGLSTPGSLH RAAKRRTSLF
660 670 680 690 700
ANRRGSDSEK RSLDSRGETT GSGRAIPIKQ SFLLKRSGNS LNKEWKKKYV
710 720 730 740 750
TLSSNGFLLY HPSINDYIHS THGKEMDLLR TTVKVPGKRP PRAISAFGPS
760 770 780 790 800
ASINGLVKDM STVQMGEGLE ATTPMPSPSP SPSSLQPPPD QTSKHLLKPD
810 820 830 840 850
RNLARALSTD CTPSGDLSPL SREPPPSPMV KKQRRKKLTT PSKTEGSAGQ
860 870 880 890 900
AEAKRKMWKL KSFGSLRNIY KAEENFEFLI VSSTGQTWHF EAASFEERDA
910 920 930 940 950
WVQAIESQIL ASLQCCESSK VKLRTDSQSE AVAIQAIRNA KGNSICVDCG
960 970 980 990 1000
APNPTWASLN LGALICIECS GIHRNLGTHL SRVRSLDLDD WPRELTLVLT
1010 1020 1030 1040 1050
AIGNDTANRV WESDTRGRAK PSRDSSREER ESWIRAKYEQ LLFLAPLSTS
1060 1070 1080 1090 1100
EEPLGRQLWA AVQAQDVATV LLLLAHARHG PLDTSVEDPQ LRSPLHLAAE
1110 1120 1130 1140 1150
LAHVVITQLL LWYGADVAAR DAQGRTALFY ARQAGSQLCA DILLQHGCPG
1160 1170 1180 1190
EGGSAATTPS AATTPSITAT PSPRRRSSAA SVGRADAPVA LV
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.

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

Sequence cautioni

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

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:
EMBLi
GenBanki
DDBJi
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.
GeneIDi116986.
KEGGihsa:116986.
UCSCiuc001spr.3. human. [Q99490-2]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125549. 8 interactions.
IntActiQ99490. 8 interactions.
MINTiMINT-3037505.
STRINGi9606.ENSP00000449241.

PTM databases

PhosphoSiteiQ99490.

Polymorphism and mutation databases

BioMutaiAGAP2.
DMDMi97535883.

Proteomic databases

MaxQBiQ99490.
PaxDbiQ99490.
PRIDEiQ99490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi116986.
GeneCardsiGC12M058118.
H-InvDBHIX0201900.
HGNCiHGNC:16921. AGAP2.
HPAiHPA023474.
MIMi605476. gene.
neXtProtiNX_Q99490.
PharmGKBiPA26411.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_22237. Netrin-1 signaling.
SignaLinkiQ99490.

Miscellaneous databases

ChiTaRSiAGAP2. human.
EvolutionaryTraceiQ99490.
GeneWikiiCENTG1.
GenomeRNAii116986.
NextBioi80070.
PROiQ99490.
SOURCEiSearch...

Gene expression databases

BgeeiQ99490.
CleanExiHS_AGAP2.
ExpressionAtlasiQ99490. baseline and differential.
GenevisibleiQ99490. HS.

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.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 170 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.