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Q99490

- AGAP2_HUMAN

UniProt

Q99490 - AGAP2_HUMAN

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Protein
Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
Gene
AGAP2, CENTG1, KIAA0167
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 4208GTP Reviewed prediction
Nucleotide bindingi457 – 4615GTP Reviewed prediction
Nucleotide bindingi515 – 5184GTP Reviewed prediction
Zinc fingeri946 – 96924C4-type
Add
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
Complete GO annotation...

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
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: Chromosome 12

Organism-specific databases

HGNCiHGNC:16921. AGAP2.

Subcellular locationi

Isoform 1 : Cytoplasm. Nucleus 3 Publications
Isoform 2 : Cytoplasm 3 Publications

GO - Cellular componenti

  1. mitochondrion Source: HPA
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

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 2
PRO_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.3 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

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.

Miscellaneous databases

EvolutionaryTraceiQ99490.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2323Interaction with EPB41L1 By similarity
Add
BLAST
Regioni180 – 22546Interactions with HOMER1 and NF2 By similarity
Add
BLAST
Regioni267 – 390124Interaction with PLCG1 By similarity
Add
BLAST
Regioni405 – 572168G domain
Add
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

Contains 2 ANK repeats.
Contains 1 Arf-GAP domain.
Contains 1 PH domain.

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.

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.
VSP_018531Add
BLAST
Alternative sequencei337 – 39054ASTRD…RASPK → MHAQRQFVVAAVRAEVRRHE VAKQALNRLRKLAERVDDPE LQDSIQASLDSIRE in isoform 2.
VSP_018532Add
BLAST
Alternative sequencei853 – 87220Missing in isoform 2.
VSP_018533Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1137 – 11371Q → H in AAC39522. 1 Publication
Sequence conflicti1147 – 11471G → A in AAC39522. 1 Publication

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...

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

« 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: September 3, 2014
This is version 161 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

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