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Abl interactor 2 (Abelson interactor 2) (Abi-2) (Abl-binding protein 3) (AblBP3) (Arg-binding protein 1) (ArgBP1)

 ABI2_HUMAN              Reviewed;         513 AA.
Q9NYB9; B4DSN1; Q13147; Q13249; Q13801; Q9BV70;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 155.
RecName: Full=Abl interactor 2;
AltName: Full=Abelson interactor 2;
Short=Abi-2;
AltName: Full=Abl-binding protein 3;
Short=AblBP3;
AltName: Full=Arg-binding protein 1;
Short=ArgBP1;
Name=ABI2; Synonyms=ARGBPIA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION,
PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABL1.
PubMed=7590236; DOI=10.1101/gad.9.21.2569;
Dai Z., Pendergast A.M.;
"Abi-2, a novel SH3-containing protein interacts with the c-Abl
tyrosine kinase and modulates c-Abl transforming activity.";
Genes Dev. 9:2569-2582(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Ren R.;
"Cloning of a binding substrate of the Abl protein tyrosine kinase.";
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
ABL2.
TISSUE=Brain;
PubMed=8649853;
Wang B., Mysliwiec T., Krainc D., Jensen R.A., Sonoda G., Testa J.R.,
Golemis E.A., Kruh G.D.;
"Identification of ArgBP1, an Arg protein tyrosine kinase binding
protein that is the human homologue of a CNS-specific Xenopus gene.";
Oncogene 12:1921-1929(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
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).
[8]
SUBCELLULAR LOCATION.
PubMed=11516653; DOI=10.1016/S0960-9822(01)00239-1;
Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V.,
Pendergast A.M.;
"The Abl interactor proteins localize to sites of actin polymerization
at the tips of lamellipodia and filopodia.";
Curr. Biol. 11:891-895(2001).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-368, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-227 AND
SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135.
PubMed=25121749; DOI=10.1016/j.chom.2014.07.005;
Stanton R.J., Prod'homme V., Purbhoo M.A., Moore M., Aicheler R.J.,
Heinzmann M., Bailer S.M., Haas J., Antrobus R., Weekes M.P.,
Lehner P.J., Vojtesek B., Miners K.L., Man S., Wilkie G.S.,
Davison A.J., Wang E.C., Tomasec P., Wilkinson G.W.;
"HCMV pUL135 remodels the actin cytoskeleton to impair immune
recognition of infected cells.";
Cell Host Microbe 16:201-214(2014).
[15]
STRUCTURE BY NMR OF 444-508.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain of Abl interactor 2 (Abelson
interactor 2).";
Submitted (FEB-2008) to the PDB data bank.
[16]
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-164, AND SUBUNIT.
PubMed=21107423; DOI=10.1038/nature09623;
Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
"Structure and control of the actin regulatory WAVE complex.";
Nature 468:533-538(2010).
-!- FUNCTION: May act in regulation of cell growth and transformation
by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2.
Part of the WAVE complex that regulates lamellipodia formation.
The WAVE complex regulates actin filament reorganization via its
interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated
phosphorylation of MENA. As component of the WAVE1 complex,
required for BDNF-NTRK2 endocytic trafficking and signaling from
early endosomes (By similarity). {ECO:0000250|UniProtKB:P62484,
ECO:0000269|PubMed:10498863, ECO:0000269|PubMed:7590236,
ECO:0000269|PubMed:8649853}.
-!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1
or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a
heterodimer containing NCKAP1 and CYFIP1 interacts with a
heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to
activated RAC1 which causes the complex to dissociate, releasing
activated WASF1. The complex can also be activated by NCK1 (By
similarity). Interacts with ABL1 and ABL2. Interacts with human
cytomegalovirus UL135. {ECO:0000250, ECO:0000269|PubMed:21107423,
ECO:0000269|PubMed:25121749, ECO:0000269|PubMed:7590236,
ECO:0000269|PubMed:8649853}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-743598, EBI-375543;
Q08117:AES; NbExp=3; IntAct=EBI-743598, EBI-717810;
A7KAX9:ARHGAP32; NbExp=3; IntAct=EBI-743598, EBI-308663;
Q9H6L4:ARMC7; NbExp=3; IntAct=EBI-743598, EBI-742909;
Q9NQY0:BIN3; NbExp=4; IntAct=EBI-11096309, EBI-2653038;
Q9UL45:BLOC1S6; NbExp=4; IntAct=EBI-11096309, EBI-465781;
Q2T9L4:C15orf59; NbExp=4; IntAct=EBI-11096309, EBI-4311436;
Q8VHK2:Caskin1 (xeno); NbExp=3; IntAct=EBI-743598, EBI-7049475;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-743598, EBI-10171570;
Q8IYA8:CCDC36; NbExp=4; IntAct=EBI-743598, EBI-8638439;
Q8TD31-3:CCHCR1; NbExp=3; IntAct=EBI-743598, EBI-10175300;
Q9H3R5:CENPH; NbExp=4; IntAct=EBI-11096309, EBI-1003700;
O43186:CRX; NbExp=3; IntAct=EBI-743598, EBI-748171;
Q9Y2H0-1:DLGAP4; NbExp=4; IntAct=EBI-11096309, EBI-12000556;
O60941:DTNB; NbExp=3; IntAct=EBI-743598, EBI-740402;
O43281:EFS; NbExp=3; IntAct=EBI-743598, EBI-718488;
Q9H6Z9:EGLN3; NbExp=3; IntAct=EBI-743598, EBI-1175354;
Q6IB98:EIF3S3; NbExp=3; IntAct=EBI-743598, EBI-10184995;
Q9H0I2:ENKD1; NbExp=4; IntAct=EBI-11096309, EBI-744099;
Q8N4B1-4:FAM109A; NbExp=6; IntAct=EBI-11096309, EBI-14131832;
Q96CN9:GCC1; NbExp=3; IntAct=EBI-743598, EBI-746252;
O95872:GPANK1; NbExp=4; IntAct=EBI-11096309, EBI-751540;
O14964:HGS; NbExp=3; IntAct=EBI-743598, EBI-740220;
P61978:HNRNPK; NbExp=3; IntAct=EBI-743598, EBI-304185;
P61978-2:HNRNPK; NbExp=4; IntAct=EBI-11096309, EBI-7060731;
Q9NSC5:HOMER3; NbExp=5; IntAct=EBI-743598, EBI-748420;
Q8IY31:IFT20; NbExp=4; IntAct=EBI-743598, EBI-744203;
Q5T5P2-6:KIAA1217; NbExp=3; IntAct=EBI-743598, EBI-10188326;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-743598, EBI-2125614;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-743598, EBI-10171552;
P19012:KRT15; NbExp=4; IntAct=EBI-743598, EBI-739566;
Q15323:KRT31; NbExp=3; IntAct=EBI-743598, EBI-948001;
Q14525:KRT33B; NbExp=3; IntAct=EBI-743598, EBI-1049638;
P25800:LMO1; NbExp=4; IntAct=EBI-11096309, EBI-8639312;
P25791:LMO2; NbExp=3; IntAct=EBI-743598, EBI-739696;
P25791-3:LMO2; NbExp=4; IntAct=EBI-11096309, EBI-11959475;
P43355:MAGEA1; NbExp=4; IntAct=EBI-11096309, EBI-740978;
Q96HT8:MRFAP1L1; NbExp=5; IntAct=EBI-743598, EBI-748896;
Q9H9J2:MRPL44; NbExp=3; IntAct=EBI-743598, EBI-713619;
O43639:NCK2; NbExp=4; IntAct=EBI-743598, EBI-713635;
Q5HYW2:NHSL2; NbExp=4; IntAct=EBI-11096309, EBI-2859639;
P37198:NUP62; NbExp=3; IntAct=EBI-743598, EBI-347978;
Q13526:PIN1; NbExp=3; IntAct=EBI-743598, EBI-714158;
P30405:PPIF; NbExp=3; IntAct=EBI-743598, EBI-5544229;
Q96QH2:PRAM1; NbExp=3; IntAct=EBI-743598, EBI-2860740;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-743598, EBI-1181405;
P54646:PRKAA2; NbExp=3; IntAct=EBI-743598, EBI-1383852;
Q569H4:PRR16; NbExp=4; IntAct=EBI-11096309, EBI-5564642;
Q9UHP6:RSPH14; NbExp=4; IntAct=EBI-11096309, EBI-748350;
O00560:SDCBP; NbExp=3; IntAct=EBI-743598, EBI-727004;
O75886:STAM2; NbExp=3; IntAct=EBI-743598, EBI-373258;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-743598, EBI-1105213;
Q13049:TRIM32; NbExp=6; IntAct=EBI-11096309, EBI-742790;
Q15654:TRIP6; NbExp=3; IntAct=EBI-743598, EBI-742327;
O75604:USP2; NbExp=4; IntAct=EBI-11096309, EBI-743272;
Q5ST30-4:VARS2; NbExp=3; IntAct=EBI-743598, EBI-10244997;
P50552:VASP; NbExp=3; IntAct=EBI-743598, EBI-748201;
O43516:WIPF1; NbExp=3; IntAct=EBI-743598, EBI-346356;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell projection, lamellipodium
{ECO:0000250}. Cell projection, filopodium {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Note=Isoform 1 but not
isoform 3 is localized to protruding lamellipodia and filopodia
tips. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Abi-2b;
IsoId=Q9NYB9-1; Sequence=Displayed;
Name=2;
IsoId=Q9NYB9-2; Sequence=VSP_010761, VSP_010762, VSP_010763;
Name=3; Synonyms=Abi-2a;
IsoId=Q9NYB9-3; Sequence=VSP_010759, VSP_010760, VSP_010761,
VSP_010762;
Name=4;
IsoId=Q9NYB9-4; Sequence=VSP_010761;
-!- PTM: Is a substrate for ABL1.
-!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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EMBL; U23435; AAA92289.1; -; mRNA.
EMBL; U31089; AAA75446.1; -; mRNA.
EMBL; AF260261; AAF70308.1; -; mRNA.
EMBL; X95632; CAA64885.1; -; mRNA.
EMBL; BT009920; AAP88922.1; -; mRNA.
EMBL; AK299824; BAG61693.1; -; mRNA.
EMBL; BC001439; AAH01439.1; -; mRNA.
CCDS; CCDS2358.1; -. [Q9NYB9-2]
CCDS; CCDS63093.1; -. [Q9NYB9-1]
CCDS; CCDS63094.1; -. [Q9NYB9-4]
PIR; G01936; G01936.
RefSeq; NP_001269854.1; NM_001282925.1.
RefSeq; NP_001269855.1; NM_001282926.1.
RefSeq; NP_001269856.1; NM_001282927.1. [Q9NYB9-3]
RefSeq; NP_005750.4; NM_005759.5. [Q9NYB9-2]
RefSeq; XP_006712248.1; XM_006712185.1. [Q9NYB9-3]
UniGene; Hs.471156; -.
PDB; 2ED0; NMR; -; A=444-508.
PDB; 3P8C; X-ray; 2.29 A; F=1-164.
PDB; 4N78; X-ray; 2.43 A; F=1-513.
PDBsum; 2ED0; -.
PDBsum; 3P8C; -.
PDBsum; 4N78; -.
ProteinModelPortal; Q9NYB9; -.
SMR; Q9NYB9; -.
BioGrid; 115454; 109.
DIP; DIP-37566N; -.
IntAct; Q9NYB9; 171.
MINT; MINT-252647; -.
iPTMnet; Q9NYB9; -.
PhosphoSitePlus; Q9NYB9; -.
DMDM; 50400673; -.
EPD; Q9NYB9; -.
MaxQB; Q9NYB9; -.
PeptideAtlas; Q9NYB9; -.
PRIDE; Q9NYB9; -.
DNASU; 10152; -.
Ensembl; ENST00000261017; ENSP00000261017; ENSG00000138443. [Q9NYB9-2]
GeneID; 10152; -.
KEGG; hsa:10152; -.
UCSC; uc002uzz.5; human. [Q9NYB9-1]
CTD; 10152; -.
DisGeNET; 10152; -.
EuPathDB; HostDB:ENSG00000138443.15; -.
GeneCards; ABI2; -.
H-InvDB; HIX0002759; -.
HGNC; HGNC:24011; ABI2.
HPA; HPA062433; -.
HPA; HPA070567; -.
MIM; 606442; gene.
neXtProt; NX_Q9NYB9; -.
OpenTargets; ENSG00000138443; -.
PharmGKB; PA134977642; -.
GeneTree; ENSGT00390000003756; -.
HOGENOM; HOG000293213; -.
HOVERGEN; HBG050446; -.
InParanoid; Q9NYB9; -.
KO; K05751; -.
PhylomeDB; Q9NYB9; -.
TreeFam; TF314303; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
SIGNOR; Q9NYB9; -.
ChiTaRS; ABI2; human.
EvolutionaryTrace; Q9NYB9; -.
GeneWiki; ABI2; -.
GenomeRNAi; 10152; -.
PRO; PR:Q9NYB9; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138443; -.
CleanEx; HS_ABI2; -.
ExpressionAtlas; Q9NYB9; baseline and differential.
Genevisible; Q9NYB9; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
GO; GO:0008093; F:cytoskeletal adaptor activity; TAS:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019900; F:kinase binding; NAS:UniProtKB.
GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB.
GO; GO:0016477; P:cell migration; TAS:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
GO; GO:0006928; P:movement of cell or subcellular component; IDA:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd11972; SH3_Abi2; 1.
InterPro; IPR028457; ABI.
InterPro; IPR036993; ABI2.
InterPro; IPR035726; Abi2_SH3.
InterPro; IPR012849; Abl-interactor_HHR_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR000727; T_SNARE_dom.
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.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Host-virus interaction;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 513 Abl interactor 2.
/FTId=PRO_0000191790.
DOMAIN 45 107 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 451 510 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 172 423 Pro-rich.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:P62484}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 361 361 Phosphothreonine.
{ECO:0000250|UniProtKB:P62484}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 45 Missing (in isoform 3).
{ECO:0000303|PubMed:7590236}.
/FTId=VSP_010759.
VAR_SEQ 46 95 ALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRM
ESSINHISQ -> MSCRCWISRHPSYEGWNLQSIIFHKQIR
GVDLESTFVTKFGNNCSLRLNE (in isoform 3).
{ECO:0000303|PubMed:7590236}.
/FTId=VSP_010760.
VAR_SEQ 154 159 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7590236,
ECO:0000303|PubMed:8649853,
ECO:0000303|Ref.2, ECO:0000303|Ref.4}.
/FTId=VSP_010761.
VAR_SEQ 284 344 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7590236,
ECO:0000303|PubMed:8649853,
ECO:0000303|Ref.2, ECO:0000303|Ref.4}.
/FTId=VSP_010762.
VAR_SEQ 399 399 S -> SLAPPPPSILQVTPQLPLMGFVARVQENIS (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8649853,
ECO:0000303|Ref.2, ECO:0000303|Ref.4}.
/FTId=VSP_010763.
CONFLICT 22 22 S -> R (in Ref. 3; CAA64885).
{ECO:0000305}.
CONFLICT 69 69 A -> D (in Ref. 3; CAA64885).
{ECO:0000305}.
CONFLICT 243 243 S -> T (in Ref. 2; AAA75446).
{ECO:0000305}.
CONFLICT 249 249 G -> P (in Ref. 1; AAA92289).
{ECO:0000305}.
CONFLICT 317 317 N -> D (in Ref. 5; BAG61693).
{ECO:0000305}.
CONFLICT 324 325 PN -> QT (in Ref. 5; BAG61693).
{ECO:0000305}.
CONFLICT 432 432 A -> V (in Ref. 2; AAA75446).
{ECO:0000305}.
CONFLICT 500 500 F -> S (in Ref. 2; AAA75446).
{ECO:0000305}.
HELIX 1 9 {ECO:0000244|PDB:4N78}.
HELIX 11 38 {ECO:0000244|PDB:4N78}.
HELIX 43 110 {ECO:0000244|PDB:4N78}.
STRAND 123 125 {ECO:0000244|PDB:4N78}.
TURN 143 151 {ECO:0000244|PDB:4N78}.
STRAND 453 458 {ECO:0000244|PDB:2ED0}.
STRAND 477 483 {ECO:0000244|PDB:2ED0}.
STRAND 485 493 {ECO:0000244|PDB:2ED0}.
STRAND 496 501 {ECO:0000244|PDB:2ED0}.
STRAND 504 507 {ECO:0000244|PDB:2ED0}.
SEQUENCE 513 AA; 55663 MW; 822983A69E5EA512 CRC64;
MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET KAYTTQSLAS
VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK
PPSPPMSGKG TLGRHSPYRT LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT
YSSSGSSGGS HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS
APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF YSMNRPASRH
TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD TPPPPPPVEE PVFDESPPPP
PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV
IKKNDDGWYE GVMNGVTGLF PGNYVESIMH YSE


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