ID   ASAP1_HUMAN             Reviewed;        1129 AA.
AC   Q9ULH1; B2RNV3;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1;
DE   AltName: Full=130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein;
DE   AltName: Full=ADP-ribosylation factor-directed GTPase-activating protein 1;
DE            Short=ARF GTPase-activating protein 1;
DE   AltName: Full=Development and differentiation-enhancing factor 1;
DE            Short=DEF-1;
DE            Short=Differentiation-enhancing factor 1;
DE   AltName: Full=PIP2-dependent ARF1 GAP;
GN   Name=ASAP1;
GN   Synonyms=DDEF1, KIAA1249, PAG2 {ECO:0000303|PubMed:12149250};
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-1129 (ISOFORM 2).
RC   TISSUE=Bone marrow;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-1129 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9819391; DOI=10.1128/mcb.18.12.7038;
RA   Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA   Randazzo P.A.;
RT   "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT   associates with and is phosphorylated by Src.";
RL   Mol. Cell. Biol. 18:7038-7051(1998).
RN   [7]
RP   INTERACTION WITH REPS2.
RX   PubMed=12149250; DOI=10.1074/jbc.m203453200;
RA   Oshiro T., Koyama S., Sugiyama S., Kondo A., Onodera Y., Asahara T.,
RA   Sabe H., Kikuchi A.;
RT   "Interaction of POB1, a downstream molecule of small G protein Ral, with
RT   PAG2, a paxillin-binding protein, is involved in cell migration.";
RL   J. Biol. Chem. 277:38618-38626(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1027, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   FUNCTION.
RX   PubMed=20393563; DOI=10.1038/nature08895;
RA   Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T.,
RA   Aza-Blanc P., Gleeson J.G.;
RT   "Functional genomic screen for modulators of ciliogenesis and cilium
RT   length.";
RL   Nature 464:1048-1051(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717; SER-839; SER-843;
RP   SER-1027 AND SER-1041, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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-717 AND SER-839, AND
RP   IDENTIFICATION BY 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   FUNCTION, INTERACTION WITH RAB11A; RAB3IP; RAB11FIP3; ARF4 AND RHO, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=25673879; DOI=10.1242/jcs.162925;
RA   Wang J., Deretic D.;
RT   "The Arf and Rab11 effector FIP3 acts synergistically with ASAP1 to direct
RT   Rabin8 in ciliary receptor targeting.";
RL   J. Cell Sci. 128:1375-1385(2015).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 823-837 IN COMPLEX WITH CTTN.
RX   PubMed=16636290; DOI=10.1073/pnas.0509166103;
RA   Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H.,
RA   Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H.,
RA   Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.;
RT   "Targeting AMAP1 and cortactin binding bearing an atypical src homology
RT   3/proline interface for prevention of breast cancer invasion and
RT   metastasis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006).
RN   [17]
RP   STRUCTURE BY NMR OF 319-428.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-
RT   activating protein from human.";
RL   Submitted (JUN-2006) to the PDB data bank.
RN   [18]
RP   STRUCTURE BY NMR OF 1067-1129.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3 domain of 130 kDA phosphatidylinositol 4,5-
RT   biphosphate-dependent ARF1 GTPase-activating protein.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [19]
RP   STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, AND INTERACTION WITH
RP   APC.
RX   PubMed=20509626; DOI=10.1021/bi100563z;
RA   Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T.;
RT   "Structural basis of the recognition of the SAMP motif of adenomatous
RT   polyposis coli by the Src-homology 3 domain.";
RL   Biochemistry 49:5143-5153(2010).
CC   -!- FUNCTION: Possesses phosphatidylinositol 4,5-bisphosphate-dependent
CC       GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1)
CC       and ARF5 and a lesser activity towards ARF6. May coordinate membrane
CC       trafficking with cell growth or actin cytoskeleton remodeling by
CC       binding to both SRC and PIP2. May function as a signal transduction
CC       protein involved in the differentiation of fibroblasts into adipocytes
CC       and possibly other cell types. Part of the ciliary targeting complex
CC       containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which
CC       direct preciliary vesicle trafficking to mother centriole and
CC       ciliogenesis initiation (PubMed:25673879). {ECO:0000250,
CC       ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:25673879}.
CC   -!- ACTIVITY REGULATION: Activity stimulated by phosphatidylinositol 4,5-
CC       bisphosphate (PIP2). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with
CC       RAB11FIP3. Interacts with PTK2B/PYK2 (By similarity). Interacts with
CC       CTTN. Interacts (via SH3 domain) with APC. Interacts with REPS2; the
CC       interaction is direct (PubMed:12149250). Forms a complex containing
CC       RAB11A, ASAP1, RAB3IP, RAP11FIP3 and ARF4; the complex promotes
CC       preciliary trafficking; the complex binds to RHO in photoreceptor cells
CC       and promotes RHO ciliary transport (PubMed:25673879). {ECO:0000250,
CC       ECO:0000269|PubMed:12149250, ECO:0000269|PubMed:16636290,
CC       ECO:0000269|PubMed:20509626, ECO:0000269|PubMed:25673879}.
CC   -!- INTERACTION:
CC       Q9ULH1; Q13191: CBLB; NbExp=2; IntAct=EBI-346622, EBI-744027;
CC       Q9ULH1; P46108: CRK; NbExp=4; IntAct=EBI-346622, EBI-886;
CC       Q9ULH1; Q14247: CTTN; NbExp=7; IntAct=EBI-346622, EBI-351886;
CC       Q9ULH1; P06241: FYN; NbExp=3; IntAct=EBI-346622, EBI-515315;
CC       Q9ULH1; P62993: GRB2; NbExp=10; IntAct=EBI-346622, EBI-401755;
CC       Q9ULH1; P08631: HCK; NbExp=2; IntAct=EBI-346622, EBI-346340;
CC       Q9ULH1; P16333: NCK1; NbExp=6; IntAct=EBI-346622, EBI-389883;
CC       Q9ULH1; P19174: PLCG1; NbExp=3; IntAct=EBI-346622, EBI-79387;
CC       Q9ULH1; Q96B97: SH3KBP1; NbExp=11; IntAct=EBI-346622, EBI-346595;
CC       Q9ULH1; P12931: SRC; NbExp=3; IntAct=EBI-346622, EBI-621482;
CC       Q9ULH1; P0CG48: UBC; NbExp=2; IntAct=EBI-346622, EBI-3390054;
CC       Q9ULH1; P70039: apc; Xeno; NbExp=5; IntAct=EBI-346622, EBI-8069633;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC       Golgi apparatus {ECO:0000269|PubMed:25673879}. Golgi apparatus, trans-
CC       Golgi network {ECO:0000269|PubMed:25673879}. Note=Predominantly
CC       cytoplasmic. Partially membrane-associated. Localized to the Golgi, TGN
CC       and rhodopsin transport carriers (RTC) when interacting with RHO in
CC       photoreceptors (PubMed:25673879). Localized to RTC when interacting
CC       with RAB11A and RAB11FIP3 in photoreceptors (PubMed:25673879).
CC       {ECO:0000250, ECO:0000269|PubMed:25673879}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=Q9ULH1-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q9ULH1-2; Sequence=VSP_008365;
CC   -!- DOMAIN: The PH domain most probably contributes to the
CC       phosphoinositide-dependent regulation of ADP ribosylation factors.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000250}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44351/ASAP1";
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DR   EMBL; AC009682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471060; EAW92130.1; -; Genomic_DNA.
DR   EMBL; BC137135; AAI37136.1; -; mRNA.
DR   EMBL; BX537768; CAD97831.1; -; mRNA.
DR   EMBL; AB033075; BAA86563.1; -; mRNA.
DR   CCDS; CCDS6362.1; -. [Q9ULH1-1]
DR   RefSeq; NP_001234925.1; NM_001247996.1.
DR   RefSeq; NP_060952.2; NM_018482.3. [Q9ULH1-1]
DR   RefSeq; XP_005250982.1; XM_005250925.1.
DR   RefSeq; XP_006716626.1; XM_006716563.3.
DR   RefSeq; XP_011515354.1; XM_011517052.2. [Q9ULH1-2]
DR   PDB; 2D1X; X-ray; 1.90 A; P/Q=823-837.
DR   PDB; 2DA0; NMR; -; A=323-423.
DR   PDB; 2ED1; NMR; -; A=1067-1129.
DR   PDB; 2RQT; NMR; -; A=1069-1129.
DR   PDB; 2RQU; NMR; -; A=1069-1129.
DR   PDBsum; 2D1X; -.
DR   PDBsum; 2DA0; -.
DR   PDBsum; 2ED1; -.
DR   PDBsum; 2RQT; -.
DR   PDBsum; 2RQU; -.
DR   AlphaFoldDB; Q9ULH1; -.
DR   BMRB; Q9ULH1; -.
DR   SMR; Q9ULH1; -.
DR   BioGRID; 119126; 64.
DR   CORUM; Q9ULH1; -.
DR   IntAct; Q9ULH1; 41.
DR   MINT; Q9ULH1; -.
DR   STRING; 9606.ENSP00000429900; -.
DR   BindingDB; Q9ULH1; -.
DR   ChEMBL; CHEMBL2146311; -.
DR   GlyGen; Q9ULH1; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9ULH1; -.
DR   PhosphoSitePlus; Q9ULH1; -.
DR   BioMuta; ASAP1; -.
DR   DMDM; 296439459; -.
DR   EPD; Q9ULH1; -.
DR   jPOST; Q9ULH1; -.
DR   MassIVE; Q9ULH1; -.
DR   MaxQB; Q9ULH1; -.
DR   PaxDb; 9606-ENSP00000429900; -.
DR   PeptideAtlas; Q9ULH1; -.
DR   ProteomicsDB; 85025; -. [Q9ULH1-1]
DR   ProteomicsDB; 85026; -. [Q9ULH1-2]
DR   Pumba; Q9ULH1; -.
DR   ABCD; Q9ULH1; 7 sequenced antibodies.
DR   Antibodypedia; 27290; 275 antibodies from 30 providers.
DR   CPTC; Q9ULH1; 3 antibodies.
DR   DNASU; 50807; -.
DR   Ensembl; ENST00000518721.6; ENSP00000429900.1; ENSG00000153317.15. [Q9ULH1-1]
DR   GeneID; 50807; -.
DR   KEGG; hsa:50807; -.
DR   MANE-Select; ENST00000518721.6; ENSP00000429900.1; NM_018482.4; NP_060952.2.
DR   UCSC; uc003yta.3; human. [Q9ULH1-1]
DR   AGR; HGNC:2720; -.
DR   CTD; 50807; -.
DR   DisGeNET; 50807; -.
DR   GeneCards; ASAP1; -.
DR   HGNC; HGNC:2720; ASAP1.
DR   HPA; ENSG00000153317; Low tissue specificity.
DR   MIM; 605953; gene.
DR   neXtProt; NX_Q9ULH1; -.
DR   OpenTargets; ENSG00000153317; -.
DR   PharmGKB; PA164716055; -.
DR   VEuPathDB; HostDB:ENSG00000153317; -.
DR   eggNOG; KOG0521; Eukaryota.
DR   GeneTree; ENSGT00940000158547; -.
DR   HOGENOM; CLU_006942_0_0_1; -.
DR   InParanoid; Q9ULH1; -.
DR   OMA; CAVKNGM; -.
DR   OrthoDB; 1449795at2759; -.
DR   PhylomeDB; Q9ULH1; -.
DR   TreeFam; TF325156; -.
DR   PathwayCommons; Q9ULH1; -.
DR   Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR   SignaLink; Q9ULH1; -.
DR   SIGNOR; Q9ULH1; -.
DR   BioGRID-ORCS; 50807; 16 hits in 1154 CRISPR screens.
DR   ChiTaRS; ASAP1; human.
DR   EvolutionaryTrace; Q9ULH1; -.
DR   GeneWiki; DDEF1; -.
DR   GenomeRNAi; 50807; -.
DR   Pharos; Q9ULH1; Tbio.
DR   PRO; PR:Q9ULH1; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9ULH1; Protein.
DR   Bgee; ENSG00000153317; Expressed in endothelial cell and 197 other cell types or tissues.
DR   ExpressionAtlas; Q9ULH1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0002102; C:podosome; IBA:GO_Central.
DR   GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0061000; P:negative regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:1903527; P:positive regulation of membrane tubulation; IBA:GO_Central.
DR   GO; GO:0061512; P:protein localization to cilium; IDA:UniProtKB.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR   CDD; cd08848; ArfGap_ASAP1; 1.
DR   CDD; cd07641; BAR_ASAP1; 1.
DR   CDD; cd13251; PH_ASAP; 1.
DR   CDD; cd11965; SH3_ASAP1; 1.
DR   Gene3D; 1.25.40.950; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   IDEAL; IID00333; -.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
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; IPR043593; ASAP.
DR   InterPro; IPR037928; ASAP1_BAR.
DR   InterPro; IPR038016; ASAP1_SH3.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR037844; PH_ASAP.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR45854:SF2; ARF-GAP WITH SH3 DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45854; ASAP FAMILY MEMBER; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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; PS50002; SH3; 1.
DR   Genevisible; Q9ULH1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat;
KW   Cilium biogenesis/degradation; Cytoplasm; Golgi apparatus;
KW   GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
FT   CHAIN           1..1129
FT                   /note="Arf-GAP with SH3 domain, ANK repeat and PH domain-
FT                   containing protein 1"
FT                   /id="PRO_0000074196"
FT   DOMAIN          324..416
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          439..560
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REPEAT          600..632
FT                   /note="ANK 1"
FT   REPEAT          636..665
FT                   /note="ANK 2"
FT   DOMAIN          1067..1129
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   ZN_FING         454..477
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          713..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..801
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..851
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..989
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1005..1051
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         717
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         726
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q1AAU6"
FT   MOD_RES         839
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         843
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1008
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087"
FT   MOD_RES         1027
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1041
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1048
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QWY8"
FT   MOD_RES         1128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QWY8"
FT   VAR_SEQ         303
FT                   /note="E -> ESRR (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:10574462"
FT                   /id="VSP_008365"
FT   VARIANT         728
FT                   /note="I -> V (in dbSNP:rs966185)"
FT                   /id="VAR_055528"
FT   STRAND          327..334
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          342..350
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          353..356
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          366..369
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   TURN            370..372
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          373..377
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          379..383
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          385..389
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          392..397
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   HELIX           401..419
FT                   /evidence="ECO:0007829|PDB:2DA0"
FT   STRAND          1070..1076
FT                   /evidence="ECO:0007829|PDB:2ED1"
FT   STRAND          1081..1085
FT                   /evidence="ECO:0007829|PDB:2ED1"
FT   STRAND          1093..1098
FT                   /evidence="ECO:0007829|PDB:2ED1"
FT   STRAND          1101..1109
FT                   /evidence="ECO:0007829|PDB:2ED1"
FT   STRAND          1116..1120
FT                   /evidence="ECO:0007829|PDB:2ED1"
FT   HELIX           1121..1123
FT                   /evidence="ECO:0007829|PDB:2ED1"
FT   STRAND          1124..1126
FT                   /evidence="ECO:0007829|PDB:2ED1"
SQ   SEQUENCE   1129 AA;  125498 MW;  7F54B22015638D55 CRC64;
     MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL
     EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK
     FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI
     EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL
     IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD
     QKEDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK VWQRRKCSVK NGILTISHAT
     SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED EQDYVAWISV LTNSKEEALT
     MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG NDICCDCGSS EPTWLSTNLG ILTCIECSGI
     HREMGVHISR IQSLELDKLG TSELLLAKNV GNNSFNDIME ANLPSPSPKP TPSSDMTVRK
     EYITAKYVDH RFSRKTCSTS SAKLNELLEA IKSRDLLALI QVYAEGVELM EPLLEPGQEL
     GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTV LHYCSMYSKP ECLKLLLRSK
     PTVDIVNQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH VHVEYEWNLR QEEIDESDDD
     LDDKPSPIKK ERSPRPQSFC HSSSISPQDK LALPGFSTPR DKQRLSYGAF TNQIFVSTST
     DSPTSPTTEA PPLPPRNAGK GPTGPPSTLP LSTQTSSGSS TLSKKRPPPP PPGHKRTLSD
     PPSPLPHGPP NKGAVPWGND GGPSSSSKTT NKFEGLSQQS STSSAKTALG PRVLPKLPQK
     VALRKTDHLS LDKATIPPEI FQKSSQLAEL PQKPPPGDLP PKPTELAPKP QIGDLPPKPG
     ELPPKPQLGD LPPKPQLSDL PPKPQMKDLP PKPQLGDLLA KSQTGDVSPK AQQPSEVTLK
     SHPLDLSPNV QSRDAIQKQA SEDSNDLTPT LPETPVPLPR KINTGKNKVR RVKTIYDCQA
     DNDDELTFIE GEVIIVTGEE DQEWWIGHIE GQPERKGVFP VSFVHILSD
//