ASAP1_HUMAN
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 03-AUG-2022, entry version 199.
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; 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 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 [16]
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 [17]
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 [18]
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 (By similarity). Plays a role in
CC ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:20393563}.
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). {ECO:0000250,
CC ECO:0000269|PubMed:12149250, ECO:0000269|PubMed:16636290,
CC ECO:0000269|PubMed:20509626}.
CC -!- INTERACTION:
CC Q9ULH1; Q13191: CBLB; NbExp=2; IntAct=EBI-346622, EBI-744027;
CC Q9ULH1; P46108: CRK; NbExp=5; 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; P07947: YES1; NbExp=2; IntAct=EBI-346622, EBI-515331;
CC Q9ULH1; P70039: apc; Xeno; NbExp=5; IntAct=EBI-346622, EBI-8069633;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Predominantly cytoplasmic. Partially membrane-associated.
CC {ECO:0000250}.
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="http://atlasgeneticsoncology.org/Genes/ASAP1ID44351ch8q24.html";
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; 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. [Q9ULH1-2]
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; 44.
DR CORUM; Q9ULH1; -.
DR IntAct; Q9ULH1; 38.
DR MINT; Q9ULH1; -.
DR STRING; 9606.ENSP00000429900; -.
DR BindingDB; Q9ULH1; -.
DR ChEMBL; CHEMBL2146311; -.
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; Q9ULH1; -.
DR PeptideAtlas; Q9ULH1; -.
DR PRIDE; Q9ULH1; -.
DR ProteomicsDB; 85025; -. [Q9ULH1-1]
DR ProteomicsDB; 85026; -. [Q9ULH1-2]
DR ABCD; Q9ULH1; 7 sequenced antibodies.
DR Antibodypedia; 27290; 244 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 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; 751525at2759; -.
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; 14 hits in 1073 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 195 other tissues.
DR ExpressionAtlas; Q9ULH1; baseline and differential.
DR Genevisible; Q9ULH1; HS.
DR GO; GO:0031253; C:cell projection membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IBA:GO_Central.
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:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; IBA:GO_Central.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IBA:GO_Central.
DR CDD; cd07641; BAR_ASAP1; 1.
DR CDD; cd13251; PH_ASAP; 1.
DR CDD; cd11965; SH3_ASAP1; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 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; 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; PTHR45854; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 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; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 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; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat;
KW Cilium biogenesis/degradation; Cytoplasm; GTPase activation; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW 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
