Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99490 (AGAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

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

Names and origin

Protein namesRecommended 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 names
Name:AGAP2
Synonyms:CENTG1, KIAA0167
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.10 Ref.11 Ref.12

Enzyme regulation

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.

Subunit structure

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. Ref.10 Ref.11 Ref.12

Subcellular location

Isoform 1: Cytoplasm. Nucleus Ref.3 Ref.10 Ref.18.

Isoform 2: Cytoplasm Ref.3 Ref.10 Ref.18.

Tissue specificity

Isoform 1 is brain-specific. Isoform 2 is ubiquitously expressed, with highest levels in brain and heart. Ref.3 Ref.10 Ref.11 Ref.12 Ref.13

Domain

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.

Post-translational modification

Isoform PIKE-Ais phosphorylated at Tyr-682 and Tyr-774 by FYN, preventing its apoptotic cleavage. Ref.14

Sequence similarities

Belongs to the centaurin gamma-like family.

Contains 2 ANK repeats.

Contains 1 Arf-GAP domain.

Contains 1 PH domain.

Sequence caution

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

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainANK repeat
Repeat
Zinc-finger
   LigandGTP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 18374643. Source: MGI

negative regulation of protein catabolic process

Inferred from direct assay PubMed 18374643. Source: MGI

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of ARF GTPase activity

Inferred from electronic annotation. Source: InterPro

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from sequence or structural similarity PubMed 11136977. Source: UniProtKB

   Molecular_functionARF GTPase activator activity

Inferred from electronic annotation. Source: InterPro

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 21720388PubMed 20075866. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99490-1)

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.
Isoform 2 (identifier: Q99490-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11921192Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
PRO_0000074217

Regions

Domain676 – 910235PH
Domain931 – 1051121Arf-GAP
Repeat1090 – 111930ANK 1
Repeat1123 – 115230ANK 2
Nucleotide binding413 – 4208GTP Potential
Nucleotide binding457 – 4615GTP Potential
Nucleotide binding515 – 5184GTP Potential
Zinc finger946 – 96924C4-type
Region1 – 2323Interaction with EPB41L1 By similarity
Region180 – 22546Interactions with HOMER1 and NF2 By similarity
Region267 – 390124Interaction with PLCG1 By similarity
Region405 – 572168G domain

Amino acid modifications

Modified residue6381Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 336336Missing in isoform 2.
VSP_018531
Alternative sequence337 – 39054ASTRD…RASPK → MHAQRQFVVAAVRAEVRRHE VAKQALNRLRKLAERVDDPE LQDSIQASLDSIRE in isoform 2.
VSP_018532
Alternative sequence853 – 87220Missing in isoform 2.
VSP_018533
Natural variant3391T → A in a breast cancer sample; somatic mutation. Ref.19
VAR_036183
Natural variant4551V → A in a glioblastoma cell line. Ref.18
VAR_026438
Natural variant5071G → S.
Corresponds to variant rs2301553 [ dbSNP | Ensembl ].
VAR_022046
Natural variant5181R → G in a sarcoma cell line. Ref.18
VAR_026439
Natural variant5681T → I in a neuroblastoma cell line. Ref.18
VAR_026440
Natural variant6511A → V in a glioblastoma cell line. Ref.18
VAR_026441
Natural variant7671E → V in a glioblastoma cell line. Ref.18
VAR_026442
Natural variant8161D → Y in a breast cancer sample; somatic mutation. Ref.19
VAR_036184
Natural variant9391N → D in a glioblastoma cell line. Ref.18
VAR_026443
Natural variant9471V → M in a sarcoma cell line. Ref.18
VAR_026444
Natural variant10221S → P in a glioblastoma cell line. Ref.18
VAR_026445
Natural variant11241G → V. Ref.1
Corresponds to variant rs238521 [ dbSNP | Ensembl ].
VAR_055532

Experimental info

Sequence conflict11371Q → H in AAC39522. Ref.1
Sequence conflict11471G → A in AAC39522. Ref.1

Secondary structure

............................................... 1192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PIKE-L) [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 8DA53707C0127984

FASTA1,192124,674
        10         20         30         40         50         60 
MSRGAGALQR RTTTYLISLT LVKLESVPPP PPSPSAAAVG APGARGSEPR DPGSPRGAEE 

        70         80         90        100        110        120 
PGKKRHERLF HRQDALWIST SSAGAGGAEP PALSPAPASP ARPVSPAPGR RLSLWAAPPG 

       130        140        150        160        170        180 
PPLSGGLSPD SKPGGAPSSS RRPLLSSPSW GGPEPEGRTG GGVPGSSSPH PGTGSRRLKV 

       190        200        210        220        230        240 
APPPPAPKPC KTVTTSGAKA GGGKGAGSRL SWPESEGKPR VKGSKSSAGT GASVSAAATA 

       250        260        270        280        290        300 
AAAGGGGSTA STSGGVGAGA GARGKLSPRK GKSKTLDNSD LHPGPPAGSP PPLTLPPTPS 

       310        320        330        340        350        360 
PATAVTAASA QPPGPAPPIT LEPPAPGLKR GREGGRASTR DRKMLKFISG IFTKSTGGPP 

       370        380        390        400        410        420 
GSGPLPGPPS LSSGSGSREL LGAELRASPK AVINSQEWTL SRSIPELRLG VLGDARSGKS 

       430        440        450        460        470        480 
SLIHRFLTGS YQVLEKTESE QYKKEMLVDG QTHLVLIREE AGAPDAKFSG WADAVIFVFS 

       490        500        510        520        530        540 
LEDENSFQAV SRLHGQLSSL RGEGRGGLAL ALVGTQDRIS ASSPRVVGDA RARALCADMK 

       550        560        570        580        590        600 
RCSYYETCAT YGLNVDRVFQ EVAQKVVTLR KQQQLLAACK SLPSSPSHSA ASTPVAGQAS 

       610        620        630        640        650        660 
NGGHTSDYSS SLPSSPNVGH RELRAEAAAV AGLSTPGSLH RAAKRRTSLF ANRRGSDSEK 

       670        680        690        700        710        720 
RSLDSRGETT GSGRAIPIKQ SFLLKRSGNS LNKEWKKKYV TLSSNGFLLY HPSINDYIHS 

       730        740        750        760        770        780 
THGKEMDLLR TTVKVPGKRP PRAISAFGPS ASINGLVKDM STVQMGEGLE ATTPMPSPSP 

       790        800        810        820        830        840 
SPSSLQPPPD QTSKHLLKPD RNLARALSTD CTPSGDLSPL SREPPPSPMV KKQRRKKLTT 

       850        860        870        880        890        900 
PSKTEGSAGQ AEAKRKMWKL KSFGSLRNIY KAEENFEFLI VSSTGQTWHF EAASFEERDA 

       910        920        930        940        950        960 
WVQAIESQIL ASLQCCESSK VKLRTDSQSE AVAIQAIRNA KGNSICVDCG APNPTWASLN 

       970        980        990       1000       1010       1020 
LGALICIECS GIHRNLGTHL SRVRSLDLDD WPRELTLVLT AIGNDTANRV WESDTRGRAK 

      1030       1040       1050       1060       1070       1080 
PSRDSSREER ESWIRAKYEQ LLFLAPLSTS EEPLGRQLWA AVQAQDVATV LLLLAHARHG 

      1090       1100       1110       1120       1130       1140 
PLDTSVEDPQ LRSPLHLAAE LAHVVITQLL LWYGADVAAR DAQGRTALFY ARQAGSQLCA 

      1150       1160       1170       1180       1190 
DILLQHGCPG EGGSAATTPS AATTPSITAT PSPRRRSSAA SVGRADAPVA LV 

« Hide

Isoform 2 (PIKE-A) [UniParc].

Checksum: B8E42631BC06D5DC
Show »

FASTA83690,537

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-339 AND TYR-816.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44932.1. [Q99490-1]
CCDS8951.1. [Q99490-2]
RefSeqNP_001116244.1. NM_001122772.2.
NP_055585.1. NM_014770.3. [Q99490-2]
UniGeneHs.302435.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BMJX-ray2.10A402-577[»]
2IWRX-ray1.50A402-577[»]
2RLONMR-A674-914[»]
ProteinModelPortalQ99490.
SMRQ99490. Positions 402-576, 674-752, 846-914, 934-1147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125549. 9 interactions.
IntActQ99490. 8 interactions.
MINTMINT-3037505.
STRING9606.ENSP00000328160.

PTM databases

PhosphoSiteQ99490.

Polymorphism databases

DMDM97535883.

Proteomic databases

MaxQBQ99490.
PaxDbQ99490.
PRIDEQ99490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257897; ENSP00000257897; ENSG00000135439. [Q99490-2]
GeneID116986.
KEGGhsa:116986.
UCSCuc001spr.3. human. [Q99490-2]

Organism-specific databases

CTD116986.
GeneCardsGC12M058118.
H-InvDBHIX0201900.
HGNCHGNC:16921. AGAP2.
HPAHPA023474.
MIM605476. gene.
neXtProtNX_Q99490.
PharmGKBPA26411.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000007233.
HOVERGENHBG054045.
InParanoidQ99490.
KOK17848.
PhylomeDBQ99490.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkQ99490.

Gene expression databases

ArrayExpressQ99490.
BgeeQ99490.
CleanExHS_AGAP2.
GenevestigatorQ99490.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
2.30.29.30. 2 hits.
3.40.50.300. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00023. Ank. 1 hit.
PF01412. ArfGap. 1 hit.
PF08477. Miro. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50297. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ99490.
GeneWikiCENTG1.
GenomeRNAi116986.
NextBio80070.
PROQ99490.
SOURCESearch...

Entry information

Entry nameAGAP2_HUMAN
AccessionPrimary (citable) accession number: Q99490
Secondary accession number(s): A8K9F7 expand/collapse secondary AC list , O00578, Q548E0, Q8IWU3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 16, 2006
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

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