AGAP1_HUMAN
ID AGAP1_HUMAN Reviewed; 857 AA.
AC Q9UPQ3; B2RTX7; Q541S5; Q6P9D7; Q9NV93;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1;
DE Short=AGAP-1;
DE AltName: Full=Centaurin-gamma-2;
DE Short=Cnt-g2;
DE AltName: Full=GTP-binding and GTPase-activating protein 1;
DE Short=GGAP1;
GN Name=AGAP1; Synonyms=CENTG2, KIAA1099;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=12640130; DOI=10.1128/mcb.23.7.2476-2488.2003;
RA Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.;
RT "GGAPs, a new family of bifunctional GTP-binding and GTPase-activating
RT proteins.";
RL Mol. Cell. Biol. 23:2476-2488(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ILE-671.
RA Hong W.;
RT "Kiaa1099 as a member (centaurin gamma2) of the centaurin ArfGAP protein
RT family.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-671.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLY-148.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 429-857 (ISOFORM 1), AND VARIANT
RP ILE-671.
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF CYS-647 AND ARG-652.
RX PubMed=12388557; DOI=10.1074/jbc.m202969200;
RA Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J.,
RA Randazzo P.A.;
RT "AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation
RT factor GTPase-activating protein that affects actin cytoskeleton.";
RL J. Biol. Chem. 277:48965-48975(2002).
RN [8]
RP INTERACTION WITH THE AP-3 COMPLEX.
RX PubMed=12967569; DOI=10.1016/s1534-5807(03)00234-x;
RA Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M.,
RA Randazzo P.A.;
RT "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP
RT AGAP1.";
RL Dev. Cell 5:513-521(2003).
RN [9]
RP SUBUNIT, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INTERACTION WITH GUCY1A3
RP AND GUCY1B3.
RX PubMed=15381706; DOI=10.1074/jbc.m410565200;
RA Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.;
RT "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
RT cyclase.";
RL J. Biol. Chem. 279:49346-49354(2004).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=16079295; DOI=10.1242/jcs.02486;
RA Nie Z., Fei J., Premont R.T., Randazzo P.A.;
RT "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein
RT complexes AP-1 and AP-3.";
RL J. Cell Sci. 118:3555-3566(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-605 AND THR-836, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP VARIANTS GLY-82; ILE-671; GLY-798 AND THR-854.
RX PubMed=15892143; DOI=10.1002/ajmg.b.30180;
RA Wassink T.H., Piven J., Vieland V.J., Jenkins L., Frantz R., Bartlett C.W.,
RA Goedken R., Childress D., Spence M.A., Smith M., Sheffield V.C.;
RT "Evaluation of the chromosome 2q37.3 gene CENTG2 as an autism
RT susceptibility gene.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 136:36-44(2005).
CC -!- FUNCTION: GTPase-activating protein for ARF1 and, to a lesser extent,
CC ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-
CC dependent trafficking of proteins in the endosomal-lysosomal system.
CC {ECO:0000269|PubMed:12640130}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 3,4,5-trisphosphate (PIP3) and, to a lesser extent, by
CC phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid
CC potentiates PIP2 stimulation.
CC -!- SUBUNIT: Homodimer. Interacts with several subunits of the AP-3 protein
CC complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3.
CC {ECO:0000269|PubMed:12967569, ECO:0000269|PubMed:15381706}.
CC -!- INTERACTION:
CC Q9UPQ3; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-7159788, EBI-748350;
CC Q9UPQ3; Q76KX8: ZNF534; NbExp=3; IntAct=EBI-7159788, EBI-17208605;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12388557,
CC ECO:0000269|PubMed:12640130}. Note=Associates with the endocytic
CC compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPQ3-2; Sequence=VSP_011183;
CC Name=3;
CC IsoId=Q9UPQ3-3; Sequence=VSP_011181, VSP_011182;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12388557,
CC ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:15381706,
CC ECO:0000269|PubMed:16079295}.
CC -!- DOMAIN: The PH domain mediates AP-3 binding.
CC -!- PTM: Phosphorylated on tyrosines. {ECO:0000269|PubMed:15381706}.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60814.1; Type=Miscellaneous discrepancy; Note=A 4-nucleotides insertion of unknown origin disrupts the reading frame.; Evidence={ECO:0000305};
CC Sequence=BAA83051.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91862.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY033765; AAK56506.1; -; mRNA.
DR EMBL; AF413078; AAL04172.1; -; mRNA.
DR EMBL; AB029022; BAA83051.2; ALT_INIT; mRNA.
DR EMBL; AC012305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC064874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060814; AAH60814.1; ALT_SEQ; mRNA.
DR EMBL; BC140856; AAI40857.1; -; mRNA.
DR EMBL; AK001722; BAA91862.1; ALT_INIT; mRNA.
DR CCDS; CCDS2514.1; -. [Q9UPQ3-2]
DR CCDS; CCDS33408.1; -. [Q9UPQ3-1]
DR CCDS; CCDS58756.1; -. [Q9UPQ3-3]
DR RefSeq; NP_001032208.1; NM_001037131.2. [Q9UPQ3-1]
DR RefSeq; NP_001231817.1; NM_001244888.1. [Q9UPQ3-3]
DR RefSeq; NP_055729.2; NM_014914.4. [Q9UPQ3-2]
DR PDB; 7EB6; X-ray; 3.01 A; A=70-235.
DR PDBsum; 7EB6; -.
DR AlphaFoldDB; Q9UPQ3; -.
DR SMR; Q9UPQ3; -.
DR BioGRID; 125550; 105.
DR IntAct; Q9UPQ3; 9.
DR MINT; Q9UPQ3; -.
DR STRING; 9606.ENSP00000307634; -.
DR iPTMnet; Q9UPQ3; -.
DR PhosphoSitePlus; Q9UPQ3; -.
DR BioMuta; AGAP1; -.
DR DMDM; 160332373; -.
DR EPD; Q9UPQ3; -.
DR jPOST; Q9UPQ3; -.
DR MassIVE; Q9UPQ3; -.
DR MaxQB; Q9UPQ3; -.
DR PaxDb; Q9UPQ3; -.
DR PeptideAtlas; Q9UPQ3; -.
DR PRIDE; Q9UPQ3; -.
DR ProteomicsDB; 85411; -. [Q9UPQ3-1]
DR ProteomicsDB; 85412; -. [Q9UPQ3-2]
DR ProteomicsDB; 85413; -. [Q9UPQ3-3]
DR Antibodypedia; 34463; 150 antibodies from 25 providers.
DR DNASU; 116987; -.
DR Ensembl; ENST00000304032.13; ENSP00000307634.7; ENSG00000157985.19. [Q9UPQ3-1]
DR Ensembl; ENST00000336665.9; ENSP00000338378.5; ENSG00000157985.19. [Q9UPQ3-2]
DR Ensembl; ENST00000409457.5; ENSP00000387174.1; ENSG00000157985.19. [Q9UPQ3-3]
DR GeneID; 116987; -.
DR KEGG; hsa:116987; -.
DR MANE-Select; ENST00000304032.13; ENSP00000307634.7; NM_001037131.3; NP_001032208.1.
DR UCSC; uc002vvs.4; human. [Q9UPQ3-1]
DR CTD; 116987; -.
DR DisGeNET; 116987; -.
DR GeneCards; AGAP1; -.
DR HGNC; HGNC:16922; AGAP1.
DR HPA; ENSG00000157985; Group enriched (brain, retina).
DR MIM; 608651; gene.
DR neXtProt; NX_Q9UPQ3; -.
DR OpenTargets; ENSG00000157985; -.
DR PharmGKB; PA26412; -.
DR VEuPathDB; HostDB:ENSG00000157985; -.
DR eggNOG; KOG0705; Eukaryota.
DR GeneTree; ENSGT00940000154793; -.
DR InParanoid; Q9UPQ3; -.
DR OMA; WYGANIK; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q9UPQ3; -.
DR TreeFam; TF317762; -.
DR PathwayCommons; Q9UPQ3; -.
DR SignaLink; Q9UPQ3; -.
DR BioGRID-ORCS; 116987; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; AGAP1; human.
DR GeneWiki; CENTG2; -.
DR GenomeRNAi; 116987; -.
DR Pharos; Q9UPQ3; Tbio.
DR PRO; PR:Q9UPQ3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UPQ3; protein.
DR Bgee; ENSG00000157985; Expressed in frontal pole and 199 other tissues.
DR ExpressionAtlas; Q9UPQ3; baseline and differential.
DR Genevisible; Q9UPQ3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; Cytoplasm;
KW GTP-binding; GTPase activation; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport;
KW Zinc; Zinc-finger.
FT CHAIN 1..857
FT /note="Arf-GAP with GTPase, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000074218"
FT DOMAIN 346..588
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 609..729
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 768..797
FT /note="ANK 1"
FT REPEAT 801..830
FT /note="ANK 2"
FT ZN_FING 624..647
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 66..276
FT /note="Small GTPase-like"
FT REGION 267..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 122..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXK8"
FT MOD_RES 836
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 352..405
FT /note="MLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTV
FT KV -> LPFFVLALTASTYLRPAGARARQSSPWPGPRGGQTSPHCAEGPQSAQLSGAMM
FT N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011181"
FT VAR_SEQ 406..857
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011182"
FT VAR_SEQ 442..494
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:12640130, ECO:0000303|Ref.2"
FT /id="VSP_011183"
FT VARIANT 82
FT /note="S -> G (in an autistic patient)"
FT /evidence="ECO:0000269|PubMed:15892143"
FT /id="VAR_026446"
FT VARIANT 148
FT /note="D -> G (in dbSNP:rs17855721)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026447"
FT VARIANT 671
FT /note="V -> I (in dbSNP:rs2034648)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15892143, ECO:0000269|Ref.2"
FT /id="VAR_026448"
FT VARIANT 798
FT /note="R -> G (in an autistic patient; dbSNP:rs762355360)"
FT /evidence="ECO:0000269|PubMed:15892143"
FT /id="VAR_026449"
FT VARIANT 829
FT /note="E -> K (in dbSNP:rs15718)"
FT /id="VAR_019550"
FT VARIANT 854
FT /note="P -> T (in a family with an autistic patient;
FT dbSNP:rs368301945)"
FT /evidence="ECO:0000269|PubMed:15892143"
FT /id="VAR_026450"
FT MUTAGEN 647
FT /note="C->S: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:12388557"
FT MUTAGEN 652
FT /note="R->K: Loss of GAP activity. No effect on AP-3-
FT binding."
FT /evidence="ECO:0000269|PubMed:12388557"
FT CONFLICT 288
FT /note="T -> I (in Ref. 1; AAK56506, 2; AAL04172 and 3;
FT BAA83051)"
FT /evidence="ECO:0000305"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:7EB6"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:7EB6"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:7EB6"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:7EB6"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:7EB6"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:7EB6"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:7EB6"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:7EB6"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7EB6"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:7EB6"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:7EB6"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:7EB6"
SQ SEQUENCE 857 AA; 94470 MW; BBFDB8DA0ECD55E8 CRC64;
MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS
QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL
LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD
AISSANPRVI DDARARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI
GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT
ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS
LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI
SSPKTNGLSK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ
WSEATVIANS AISSDTGLGD SVCSSPSISS TTSPKLDPPP SPHANRKKHR RKKSTSNFKA
DGLSGTAEEQ EENFEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK
SRLTSQSEAM ALQSIRNMRG NSHCVDCETQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR
VRSLDLDDWP VELIKVMSSI GNELANSVWE ESSQGRTKPS VDSTREEKER WIRAKYEQKL
FLAPLPCTEL SLGQHLLRAT ADEDLRTAIL LLAHGSRDEV NETCGEGDGR TALHLACRKG
NVVLAQLLIW YGVDVTARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS
RRNNNRNNSS GRVPTII
