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Abelson interacting protein, isoform A (Abelson interacting protein, isoform B) (Abelson interacting protein, isoform F) (Abl tyrosine kinase-interacting protein) (LD37010p)

 Q9Y0S9_DROME            Unreviewed;       473 AA.
Q9Y0S9;
01-NOV-1999, integrated into UniProtKB/TrEMBL.
01-NOV-1999, sequence version 1.
23-MAY-2018, entry version 163.
SubName: Full=Abelson interacting protein, isoform A {ECO:0000313|EMBL:AAF55021.1};
SubName: Full=Abelson interacting protein, isoform B {ECO:0000313|EMBL:ABW08669.1};
SubName: Full=Abelson interacting protein, isoform F {ECO:0000313|EMBL:AGB95941.1};
SubName: Full=Abl tyrosine kinase-interacting protein {ECO:0000313|EMBL:AAD38382.1};
SubName: Full=LD37010p {ECO:0000313|EMBL:AAK93301.1};
Name=Abi {ECO:0000313|EMBL:AAF55021.1,
ECO:0000313|FlyBase:FBgn0020510};
Synonyms=abi {ECO:0000313|EMBL:AAF55021.1},
Abi-1 {ECO:0000313|EMBL:AAF55021.1},
Ablphilin {ECO:0000313|EMBL:AAF55021.1},
dAbi {ECO:0000313|EMBL:AAF55021.1},
Dmel\CG9749 {ECO:0000313|EMBL:AAF55021.1};
ORFNames=CG9749 {ECO:0000313|EMBL:AAF55021.1,
ECO:0000313|FlyBase:FBgn0020510},
Dmel_CG9749 {ECO:0000313|EMBL:AAF55021.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAD38382.1}
NUCLEOTIDE SEQUENCE.
PubMed=10498863; DOI=10.1038/sj.onc.1202911;
Juang J.-L., Hoffmann F.M.;
"Drosophila abelson interacting protein (dAbi) is a positive regulator
of abelson tyrosine kinase activity.";
Oncogene 18:5138-5147(1999).
[2] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000313|EMBL:AAK93301.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Berkeley {ECO:0000313|EMBL:AAK93301.1};
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.,
Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J.,
Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K.,
Yu C., Lewis S.E., Rubin G.M., Celniker S.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[5] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
[7] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[8] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[9] {ECO:0000313|EMBL:AAF55021.1}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AAF55021.1}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[11] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[12] {ECO:0000313|EMBL:AAF55021.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[13] {ECO:0000313|EMBL:AAF55021.1}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
-----------------------------------------------------------------------
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EMBL; AF151115; AAD38382.1; -; mRNA.
EMBL; AE014297; AAF55021.1; -; Genomic_DNA.
EMBL; AY051877; AAK93301.1; -; mRNA.
EMBL; AE014297; ABW08669.1; -; Genomic_DNA.
EMBL; AE014297; AGB95941.1; -; Genomic_DNA.
RefSeq; NP_001097785.1; NM_001104315.2.
RefSeq; NP_001262560.1; NM_001275631.1.
RefSeq; NP_477263.1; NM_057915.5.
UniGene; Dm.3181; -.
SMR; Q9Y0S9; -.
DIP; DIP-35544N; -.
IntAct; Q9Y0S9; 7.
PRIDE; Q9Y0S9; -.
EnsemblMetazoa; FBtr0082910; FBpp0082371; FBgn0020510.
EnsemblMetazoa; FBtr0112896; FBpp0111809; FBgn0020510.
EnsemblMetazoa; FBtr0337097; FBpp0308013; FBgn0020510.
GeneID; 41718; -.
KEGG; dme:Dmel_CG9749; -.
UCSC; CG9749-RA; d. melanogaster.
CTD; 41718; -.
FlyBase; FBgn0020510; Abi.
eggNOG; KOG2546; Eukaryota.
eggNOG; ENOG410Y0MH; LUCA.
GeneTree; ENSGT00390000003756; -.
OrthoDB; EOG091G0AN8; -.
Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
GenomeRNAi; 41718; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0020510; -.
ExpressionAtlas; Q9Y0S9; baseline and differential.
GO; GO:0045178; C:basal part of cell; IDA:FlyBase.
GO; GO:0031258; C:lamellipodium membrane; IDA:FlyBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
GO; GO:0031209; C:SCAR complex; IDA:FlyBase.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
GO; GO:0048846; P:axon extension involved in axon guidance; IMP:FlyBase.
GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:FlyBase.
GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
GO; GO:0030031; P:cell projection assembly; IMP:FlyBase.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:FlyBase.
GO; GO:0022416; P:chaeta development; IMP:FlyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
GO; GO:0030032; P:lamellipodium assembly; IMP:FlyBase.
GO; GO:0016203; P:muscle attachment; IMP:FlyBase.
GO; GO:0007528; P:neuromuscular junction development; IGI:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:FlyBase.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:FlyBase.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
InterPro; IPR028457; ABI.
InterPro; IPR036993; ABI2.
InterPro; IPR012849; Abl-interactor_HHR_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10460; PTHR10460; 1.
PANTHER; PTHR10460:SF0; PTHR10460:SF0; 1.
Pfam; PF07815; Abi_HHR; 1.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Kinase {ECO:0000313|EMBL:AAD38382.1};
Proteomics identification {ECO:0000213|PeptideAtlas:Q9Y0S9};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
SH3 domain {ECO:0000256|PROSITE-ProRule:PRU00192};
Transferase {ECO:0000313|EMBL:AAD38382.1}.
DOMAIN 415 473 SH3. {ECO:0000259|PROSITE:PS50002}.
SEQUENCE 473 AA; 51925 MW; 5C60813E4100252E CRC64;
MLTETPMASE NIMDELASLI RTEIPDGRQS LRDSYTNLER VADYCEDTYY RADNKKAALE
ATKNYTTQSL ASVAYQINTL AYSYMQLLEL QAQQLGEMES QMNHIAQTVH IHKEKVARRE
IGVLTANKVS SRQFKIVAPI NPEKPIKYVR KPIDYSMLDE IGHGINSAQH SQVRQKHRGS
SHGSVQSLLP PSVGPPPTTK PPTPPQMSRA GNTGTLGKSV SNTGTLGKSS REYRTPPVVN
PPQVPSHYAP NYPIGHPKRM STASSTMTTT TTGGGAAGNE RAAGYSALPM PPSQQIATHV
NLPSAGMMQS LPPPPPTTYD DRSSMPPAPP SPLTVSQHEM TEQSHIGMHT LGRNINRNHF
SLNFARPGSQ SPPLPPPPPP EDEHQDFGRP RTSTGPQLAP IVPEDQNLPG WVPKNFIEKV
VAIYDYYADK DDELSFQESS VLYVLKKNDD GWWEGVMDGV TGLFPGNYVE PCV


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