Full text data of ASAP1
ASAP1
(DDEF1, KIAA1249)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein; ADP-ribosylation factor-directed GTPase-activating protein 1; ARF GTPase-activating protein 1; Development and differentiation-enhancing factor 1; DEF-1; Differentiation-enhancing factor 1; PIP2-dependent ARF1 GAP)
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein; ADP-ribosylation factor-directed GTPase-activating protein 1; ARF GTPase-activating protein 1; Development and differentiation-enhancing factor 1; DEF-1; Differentiation-enhancing factor 1; PIP2-dependent ARF1 GAP)
UniProt
Q9ULH1
ID ASAP1_HUMAN Reviewed; 1129 AA.
AC Q9ULH1; B2RNV3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 4.
DT 22-JAN-2014, entry version 129.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA 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.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9819391;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, AND
RP MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1027, AND
RP MASS SPECTROMETRY.
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 [10]
RP FUNCTION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K.,
RA Ideker T., 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M.,
RA Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.;
RT "Targeting AMAP1 and cortactin binding bearing an atypical src
RT homology 3/proline interface for prevention of breast cancer invasion
RT and metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006).
RN [13]
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 [14]
RP STRUCTURE BY NMR OF 1067-1129.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of 130 kDA phosphatidylinositol
RT 4,5-biphosphate-dependent ARF1 GTPase-activating protein.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, AND INTERACTION
RP WITH 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-
CC dependent GTPase-activating protein activity for ARF1 (ADP
CC ribosylation factor 1) and ARF5 and a lesser activity towards
CC ARF6. May coordinate membrane trafficking with cell growth or
CC actin cytoskeleton remodeling by binding to both SRC and PIP2. May
CC function as a signal transduction protein involved in the
CC differentiation of fibroblasts into adipocytes and possibly other
CC cell types (By similarity). Plays a role in ciliogenesis.
CC -!- ENZYME REGULATION: Activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) (By similarity).
CC -!- SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with
CC RAB11FIP3. Interacts with PTK2B/PYK2 (By similarity). Interacts
CC with CTTN. Interacts (via SH3 domain) with APC.
CC -!- INTERACTION:
CC P70039:apc (xeno); NbExp=5; IntAct=EBI-346622, EBI-8069633;
CC Q13191:CBLB; NbExp=2; IntAct=EBI-346622, EBI-744027;
CC P46108:CRK; NbExp=2; IntAct=EBI-346622, EBI-886;
CC Q14247:CTTN; NbExp=7; IntAct=EBI-346622, EBI-351886;
CC P06241:FYN; NbExp=3; IntAct=EBI-346622, EBI-515315;
CC P62993:GRB2; NbExp=7; IntAct=EBI-346622, EBI-401755;
CC P08631:HCK; NbExp=2; IntAct=EBI-346622, EBI-346340;
CC P16333:NCK1; NbExp=6; IntAct=EBI-346622, EBI-389883;
CC P19174:PLCG1; NbExp=3; IntAct=EBI-346622, EBI-79387;
CC Q96B97:SH3KBP1; NbExp=8; IntAct=EBI-346622, EBI-346595;
CC P12931:SRC; NbExp=3; IntAct=EBI-346622, EBI-621482;
CC P0CG48:UBC; NbExp=2; IntAct=EBI-346622, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC similarity). Note=Predominantly cytoplasmic (By similarity).
CC Partially membrane-associated (By similarity).
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 (By similarity).
CC -!- PTM: Phosphorylated on tyrosine residues by SRC (By similarity).
CC -!- SIMILARITY: Contains 2 ANK repeats.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ASAP1ID44351ch8q24.html";
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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 RefSeq; NP_001234925.1; NM_001247996.1.
DR RefSeq; NP_060952.2; NM_018482.3.
DR RefSeq; XP_005250982.1; XM_005250925.1.
DR UniGene; Hs.655552; -.
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 ProteinModelPortal; Q9ULH1; -.
DR SMR; Q9ULH1; 31-429, 437-709, 1069-1129.
DR IntAct; Q9ULH1; 29.
DR MINT; MINT-243352; -.
DR STRING; 9606.ENSP00000350297; -.
DR ChEMBL; CHEMBL2146311; -.
DR PhosphoSite; Q9ULH1; -.
DR DMDM; 296439459; -.
DR PaxDb; Q9ULH1; -.
DR PRIDE; Q9ULH1; -.
DR DNASU; 50807; -.
DR Ensembl; ENST00000357668; ENSP00000350297; ENSG00000153317.
DR Ensembl; ENST00000518721; ENSP00000429900; ENSG00000153317.
DR GeneID; 50807; -.
DR KEGG; hsa:50807; -.
DR UCSC; uc003yta.2; human.
DR CTD; 50807; -.
DR GeneCards; GC08M131064; -.
DR H-InvDB; HIX0007806; -.
DR HGNC; HGNC:2720; ASAP1.
DR HPA; CAB037292; -.
DR MIM; 605953; gene.
DR neXtProt; NX_Q9ULH1; -.
DR PharmGKB; PA164716055; -.
DR eggNOG; COG5347; -.
DR HOGENOM; HOG000230570; -.
DR HOVERGEN; HBG051327; -.
DR KO; K12488; -.
DR OMA; DFLVQNC; -.
DR PhylomeDB; Q9ULH1; -.
DR ChiTaRS; ASAP1; human.
DR EvolutionaryTrace; Q9ULH1; -.
DR GeneWiki; DDEF1; -.
DR GenomeRNAi; 50807; -.
DR NextBio; 53242; -.
DR PRO; PR:Q9ULH1; -.
DR ArrayExpress; Q9ULH1; -.
DR Bgee; Q9ULH1; -.
DR CleanEx; HS_ASAP1; -.
DR Genevestigator; Q9ULH1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR001164; ArfGAP.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00018; SH3_1; 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; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 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; Complete proteome; Cytoplasm;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1 1129 Arf-GAP with SH3 domain, ANK repeat and
FT PH domain-containing protein 1.
FT /FTId=PRO_0000074196.
FT DOMAIN 324 416 PH.
FT DOMAIN 439 560 Arf-GAP.
FT REPEAT 600 632 ANK 1.
FT REPEAT 636 665 ANK 2.
FT DOMAIN 1067 1129 SH3.
FT ZN_FING 454 477 C4-type.
FT COMPBIAS 783 993 Pro-rich.
FT MOD_RES 717 717 Phosphoserine (By similarity).
FT MOD_RES 843 843 Phosphoserine.
FT MOD_RES 1008 1008 Phosphoserine.
FT MOD_RES 1027 1027 Phosphoserine.
FT VAR_SEQ 303 303 E -> ESRR (in isoform 1).
FT /FTId=VSP_008365.
FT VARIANT 728 728 I -> V (in dbSNP:rs966185).
FT /FTId=VAR_055528.
FT STRAND 327 334
FT STRAND 336 338
FT STRAND 342 350
FT STRAND 353 356
FT STRAND 366 369
FT TURN 370 372
FT STRAND 373 377
FT STRAND 379 383
FT STRAND 385 389
FT STRAND 392 397
FT HELIX 401 419
FT STRAND 1070 1076
FT STRAND 1081 1085
FT STRAND 1093 1098
FT STRAND 1101 1109
FT STRAND 1116 1120
FT HELIX 1121 1123
FT STRAND 1124 1126
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
//
ID ASAP1_HUMAN Reviewed; 1129 AA.
AC Q9ULH1; B2RNV3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 4.
DT 22-JAN-2014, entry version 129.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA 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.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9819391;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, AND
RP MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1027, AND
RP MASS SPECTROMETRY.
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 [10]
RP FUNCTION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K.,
RA Ideker T., 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M.,
RA Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.;
RT "Targeting AMAP1 and cortactin binding bearing an atypical src
RT homology 3/proline interface for prevention of breast cancer invasion
RT and metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006).
RN [13]
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 [14]
RP STRUCTURE BY NMR OF 1067-1129.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of 130 kDA phosphatidylinositol
RT 4,5-biphosphate-dependent ARF1 GTPase-activating protein.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, AND INTERACTION
RP WITH 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-
CC dependent GTPase-activating protein activity for ARF1 (ADP
CC ribosylation factor 1) and ARF5 and a lesser activity towards
CC ARF6. May coordinate membrane trafficking with cell growth or
CC actin cytoskeleton remodeling by binding to both SRC and PIP2. May
CC function as a signal transduction protein involved in the
CC differentiation of fibroblasts into adipocytes and possibly other
CC cell types (By similarity). Plays a role in ciliogenesis.
CC -!- ENZYME REGULATION: Activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) (By similarity).
CC -!- SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with
CC RAB11FIP3. Interacts with PTK2B/PYK2 (By similarity). Interacts
CC with CTTN. Interacts (via SH3 domain) with APC.
CC -!- INTERACTION:
CC P70039:apc (xeno); NbExp=5; IntAct=EBI-346622, EBI-8069633;
CC Q13191:CBLB; NbExp=2; IntAct=EBI-346622, EBI-744027;
CC P46108:CRK; NbExp=2; IntAct=EBI-346622, EBI-886;
CC Q14247:CTTN; NbExp=7; IntAct=EBI-346622, EBI-351886;
CC P06241:FYN; NbExp=3; IntAct=EBI-346622, EBI-515315;
CC P62993:GRB2; NbExp=7; IntAct=EBI-346622, EBI-401755;
CC P08631:HCK; NbExp=2; IntAct=EBI-346622, EBI-346340;
CC P16333:NCK1; NbExp=6; IntAct=EBI-346622, EBI-389883;
CC P19174:PLCG1; NbExp=3; IntAct=EBI-346622, EBI-79387;
CC Q96B97:SH3KBP1; NbExp=8; IntAct=EBI-346622, EBI-346595;
CC P12931:SRC; NbExp=3; IntAct=EBI-346622, EBI-621482;
CC P0CG48:UBC; NbExp=2; IntAct=EBI-346622, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC similarity). Note=Predominantly cytoplasmic (By similarity).
CC Partially membrane-associated (By similarity).
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 (By similarity).
CC -!- PTM: Phosphorylated on tyrosine residues by SRC (By similarity).
CC -!- SIMILARITY: Contains 2 ANK repeats.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ASAP1ID44351ch8q24.html";
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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 RefSeq; NP_001234925.1; NM_001247996.1.
DR RefSeq; NP_060952.2; NM_018482.3.
DR RefSeq; XP_005250982.1; XM_005250925.1.
DR UniGene; Hs.655552; -.
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 ProteinModelPortal; Q9ULH1; -.
DR SMR; Q9ULH1; 31-429, 437-709, 1069-1129.
DR IntAct; Q9ULH1; 29.
DR MINT; MINT-243352; -.
DR STRING; 9606.ENSP00000350297; -.
DR ChEMBL; CHEMBL2146311; -.
DR PhosphoSite; Q9ULH1; -.
DR DMDM; 296439459; -.
DR PaxDb; Q9ULH1; -.
DR PRIDE; Q9ULH1; -.
DR DNASU; 50807; -.
DR Ensembl; ENST00000357668; ENSP00000350297; ENSG00000153317.
DR Ensembl; ENST00000518721; ENSP00000429900; ENSG00000153317.
DR GeneID; 50807; -.
DR KEGG; hsa:50807; -.
DR UCSC; uc003yta.2; human.
DR CTD; 50807; -.
DR GeneCards; GC08M131064; -.
DR H-InvDB; HIX0007806; -.
DR HGNC; HGNC:2720; ASAP1.
DR HPA; CAB037292; -.
DR MIM; 605953; gene.
DR neXtProt; NX_Q9ULH1; -.
DR PharmGKB; PA164716055; -.
DR eggNOG; COG5347; -.
DR HOGENOM; HOG000230570; -.
DR HOVERGEN; HBG051327; -.
DR KO; K12488; -.
DR OMA; DFLVQNC; -.
DR PhylomeDB; Q9ULH1; -.
DR ChiTaRS; ASAP1; human.
DR EvolutionaryTrace; Q9ULH1; -.
DR GeneWiki; DDEF1; -.
DR GenomeRNAi; 50807; -.
DR NextBio; 53242; -.
DR PRO; PR:Q9ULH1; -.
DR ArrayExpress; Q9ULH1; -.
DR Bgee; Q9ULH1; -.
DR CleanEx; HS_ASAP1; -.
DR Genevestigator; Q9ULH1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR001164; ArfGAP.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00018; SH3_1; 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; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 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; Complete proteome; Cytoplasm;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1 1129 Arf-GAP with SH3 domain, ANK repeat and
FT PH domain-containing protein 1.
FT /FTId=PRO_0000074196.
FT DOMAIN 324 416 PH.
FT DOMAIN 439 560 Arf-GAP.
FT REPEAT 600 632 ANK 1.
FT REPEAT 636 665 ANK 2.
FT DOMAIN 1067 1129 SH3.
FT ZN_FING 454 477 C4-type.
FT COMPBIAS 783 993 Pro-rich.
FT MOD_RES 717 717 Phosphoserine (By similarity).
FT MOD_RES 843 843 Phosphoserine.
FT MOD_RES 1008 1008 Phosphoserine.
FT MOD_RES 1027 1027 Phosphoserine.
FT VAR_SEQ 303 303 E -> ESRR (in isoform 1).
FT /FTId=VSP_008365.
FT VARIANT 728 728 I -> V (in dbSNP:rs966185).
FT /FTId=VAR_055528.
FT STRAND 327 334
FT STRAND 336 338
FT STRAND 342 350
FT STRAND 353 356
FT STRAND 366 369
FT TURN 370 372
FT STRAND 373 377
FT STRAND 379 383
FT STRAND 385 389
FT STRAND 392 397
FT HELIX 401 419
FT STRAND 1070 1076
FT STRAND 1081 1085
FT STRAND 1093 1098
FT STRAND 1101 1109
FT STRAND 1116 1120
FT HELIX 1121 1123
FT STRAND 1124 1126
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
//
MIM
605953
*RECORD*
*FIELD* NO
605953
*FIELD* TI
*605953 DEVELOPMENT- AND DIFFERENTIATION-ENHANCING FACTOR 1; DDEF1
;;ADP-RIBOSYLATION FACTOR-DIRECTED GTPase-ACTIVATING PROTEIN;;
read moreARF GTPase-ACTIVATING PROTEIN 1; ASAP1
*FIELD* TX
CLONING
Membrane trafficking is regulated in part by small GTP-binding proteins
of the ADP-ribosylation factor (ARF) family (see 600464). ARF function
depends on the controlled exchange and hydrolysis of GTP. Brown et al.
(1998) purified a 130-kD phosphatidylinositol 4,5-bisphosphate
(PIP2)-dependent ARF GTPase-associated protein (GAP), termed ASAP1, from
bovine brain. Using peptide sequences, the authors cloned the
corresponding mouse gene. They found 2 alternatively spliced forms of
the cDNA, termed ASAP1a and ASAP1b, encoding 1,147-amino acid and
1,090-amino acid polypeptides, respectively. The protein sequence
contains a pleckstrin homology (PH) domain, a zinc finger motif, 3
ankyrin repeats, a proline-rich region containing several SH3 ligand
motifs, and an SH3 domain. Northern blot analysis of mouse tissues
revealed expression in a variety of tissues. Western blot analysis
detected crossreacting proteins, suggesting that ASAP1 is part of a gene
family. Studies of the expressed ASAP1 protein showed that it has GAP
activity on ARF1 (103180) and ARF5 (103188) substrates. ASAP1 binds to
SH3 domains, including those of SRC (190090) and CRK (164762). Both
isoforms of ASAP1 became tyrosine phosphorylated by active SRC.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DDEF1
gene to chromosome 8q24.1-q24.2 (TMAP WI-8901).
*FIELD* RF
1. Brown, M. T.; Andrade, J.; Radhakrishna, H.; Donaldson, J. G.;
Cooper, J. A.; Randazzo, P. A.: ASAP1, a phospholipid-dependent Arf
GTPase-activating protein that associates with and is phosphorylated
by Src. Molec. Cell. Biol. 18: 7038-7051, 1998.
*FIELD* CN
Carol A. Bocchini - updated: 5/22/2001
*FIELD* CD
Jennifer P. Macke: 5/19/1999
*FIELD* ED
alopez: 05/14/2009
mcapotos: 5/23/2001
carol: 5/22/2001
alopez: 9/13/1999
alopez: 7/20/1999
alopez: 5/19/1999
*RECORD*
*FIELD* NO
605953
*FIELD* TI
*605953 DEVELOPMENT- AND DIFFERENTIATION-ENHANCING FACTOR 1; DDEF1
;;ADP-RIBOSYLATION FACTOR-DIRECTED GTPase-ACTIVATING PROTEIN;;
read moreARF GTPase-ACTIVATING PROTEIN 1; ASAP1
*FIELD* TX
CLONING
Membrane trafficking is regulated in part by small GTP-binding proteins
of the ADP-ribosylation factor (ARF) family (see 600464). ARF function
depends on the controlled exchange and hydrolysis of GTP. Brown et al.
(1998) purified a 130-kD phosphatidylinositol 4,5-bisphosphate
(PIP2)-dependent ARF GTPase-associated protein (GAP), termed ASAP1, from
bovine brain. Using peptide sequences, the authors cloned the
corresponding mouse gene. They found 2 alternatively spliced forms of
the cDNA, termed ASAP1a and ASAP1b, encoding 1,147-amino acid and
1,090-amino acid polypeptides, respectively. The protein sequence
contains a pleckstrin homology (PH) domain, a zinc finger motif, 3
ankyrin repeats, a proline-rich region containing several SH3 ligand
motifs, and an SH3 domain. Northern blot analysis of mouse tissues
revealed expression in a variety of tissues. Western blot analysis
detected crossreacting proteins, suggesting that ASAP1 is part of a gene
family. Studies of the expressed ASAP1 protein showed that it has GAP
activity on ARF1 (103180) and ARF5 (103188) substrates. ASAP1 binds to
SH3 domains, including those of SRC (190090) and CRK (164762). Both
isoforms of ASAP1 became tyrosine phosphorylated by active SRC.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DDEF1
gene to chromosome 8q24.1-q24.2 (TMAP WI-8901).
*FIELD* RF
1. Brown, M. T.; Andrade, J.; Radhakrishna, H.; Donaldson, J. G.;
Cooper, J. A.; Randazzo, P. A.: ASAP1, a phospholipid-dependent Arf
GTPase-activating protein that associates with and is phosphorylated
by Src. Molec. Cell. Biol. 18: 7038-7051, 1998.
*FIELD* CN
Carol A. Bocchini - updated: 5/22/2001
*FIELD* CD
Jennifer P. Macke: 5/19/1999
*FIELD* ED
alopez: 05/14/2009
mcapotos: 5/23/2001
carol: 5/22/2001
alopez: 9/13/1999
alopez: 7/20/1999
alopez: 5/19/1999