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Abl interactor 1 (Abelson interactor 1) (Abi-1) (Ablphilin-1) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Spectrin SH3 domain-binding protein 1) (e3B1)

 ABI1_MOUSE              Reviewed;         481 AA.
Q8CBW3; Q3U8V0; Q60747; Q91ZM5; Q923I9; Q99KH4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 152.
RecName: Full=Abl interactor 1;
AltName: Full=Abelson interactor 1;
Short=Abi-1;
AltName: Full=Ablphilin-1;
AltName: Full=Eps8 SH3 domain-binding protein;
Short=Eps8-binding protein;
AltName: Full=Spectrin SH3 domain-binding protein 1;
AltName: Full=e3B1;
Name=Abi1 {ECO:0000312|MGI:MGI:104913}; Synonyms=Ssh3bp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORM
2), AND FUNCTION.
STRAIN=BALB/cJ;
PubMed=11526477; DOI=10.1038/sj.onc.1204502;
Ikeguchi A., Yang H.-Y., Gao G., Goff S.P.;
"Inhibition of v-Abl transformation in 3T3 cells overexpressing
different forms of the Abelson interactor protein Abi-1.";
Oncogene 20:4926-4934(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11477655; DOI=10.1002/gcc.1160;
Shibuya N., Taki T., Mugishima H., Chin M., Tsuchida M., Sako M.,
Kawa K., Ishii E., Miura I., Yanagisawa M., Hayashi Y.;
"t(10;11)-acute leukemias with MLL-AF10 and MLL-ABI1 chimeric
transcripts: specific expression patterns of ABI1 gene in leukemia and
solid tumor cell lines.";
Genes Chromosomes Cancer 32:1-10(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Diencephalon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 70-360 (ISOFORM 4), FUNCTION,
PHOSPHORYLATION, TISSUE SPECIFICITY, AND INTERACTION WITH ABL1 AND
V-ABL.
PubMed=7590237; DOI=10.1101/gad.9.21.2583;
Shi Y., Alin K., Goff S.P.;
"Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal
portion of the Abl protein, suppresses v-abl transforming activity.";
Genes Dev. 9:2583-2597(1995).
[6]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH EPS8 AND SOS1.
PubMed=10499589; DOI=10.1038/45822;
Scita G., Nordstrom J., Carbone R., Tenca P., Giardina G., Gutkind S.,
Bjarnegard M., Betsholtz C., Di Fiore P.P.;
"EPS8 and E3B1 transduce signals from Ras to Rac.";
Nature 401:290-293(1999).
[7]
FUNCTION, AND INTERACTION WITH ENAH.
PubMed=12672821; DOI=10.1074/jbc.M301447200;
Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,
Shishido T.;
"Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
enabled (Mena) by c-Abl kinase.";
J. Biol. Chem. 278:21685-21692(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STX1A; SNAP25;
VAMP2 AND WASF1.
PubMed=15143189; DOI=10.1128/MCB.24.11.4979-4993.2004;
Echarri A., Lai M.J., Robinson M.R., Pendergast A.M.;
"Abl interactor 1 (Abi-1) wave-binding and SNARE domains regulate its
nucleocytoplasmic shuttling, lamellipodium localization, and wave-1
levels.";
Mol. Cell. Biol. 24:4979-4993(2004).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10995551; DOI=10.1006/mcne.2000.0865;
Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S.,
Pendergast A.M.;
"Localization and phosphorylation of Abl-interactor proteins, Abi-1
and Abi-2, in the developing nervous system.";
Mol. Cell. Neurosci. 16:244-257(2000).
[10]
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).
[11]
COMPONENT OF WAVE2 COMPLEX.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=14765121; DOI=10.1038/sj.emboj.7600084;
Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G.,
Wehland J., Stradal T.E.B.;
"Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia
formation.";
EMBO J. 23:749-759(2004).
[12]
FUNCTION, AND INTERACTION WITH EPS8.
PubMed=15558031; DOI=10.1038/ncb1199;
Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E.,
Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G.;
"Eps8 controls actin-based motility by capping the barbed ends of
actin filaments.";
Nat. Cell Biol. 6:1180-1188(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND TYR-213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May act in negative regulation of cell growth and
transformation by interacting with nonreceptor tyrosine kinases
ABL1 and/or ABL2. In vitro, at least isoform 2 and isoform 4
suppress the transforming activity of Abelson murine leukemia
virus (v-Abl) after overexpression in fibroblasts. May play a role
in regulation EGF-induced Erk pathway activation. Involved in
cytoskeletal reorganization and EGFR signaling. Together with EPS8
participates in transduction of signals from Ras to Rac. In vitro,
a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific
guanine nucleotide exchange factor (GEF) activity and ABI1 seems
to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated
phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there
seems to regulate WASF1 protein level. In brain, seems to regulate
the dendritic outgrowth and branching as well as to determine the
shape and number of synaptic contacts of developing neurons.
{ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11526477,
ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15143189,
ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:7590237}.
-!- SUBUNIT: Interacts with ENAH, Abelson murine leukemia virus V-ABL,
ABL1, STX1A, SNAP25, VAMP2, and through its N-terminus with WASF1.
Part of a complex consisting of ABI1, STX1A and SNAP25. Part of a
complex consisting of ABI1, EPS8 and SOS1. Interacts with EPS8,
SOS1, SOS2, GRB2, SPTA1, and the first SH3 domain of NCK1 (By
similarity). Component of the WAVE2 complex composed of ABI1,
CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and
WASF2/WAVE2. Interacts (via SH3 domain) with SHANK2 and SHANK3,
but not SHANK1; the interaction is direct. Interacts with the
heterodimer MYC:MAX; the interaction may enhance MYC:MAX
transcriptional activity. Interacts with FNBP1L (via the SH3
domain), WASF2, and CDC42, but only in the presence of FNBP1L (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8IZP0,
ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:12672821,
ECO:0000269|PubMed:15143189, ECO:0000269|PubMed:15558031,
ECO:0000269|PubMed:7590237}.
-!- INTERACTION:
Q9Z207:Diaph3; NbExp=2; IntAct=EBI-375511, EBI-6550123;
Q08509:Eps8; NbExp=3; IntAct=EBI-375511, EBI-375596;
Q02384:Sos2; NbExp=2; IntAct=EBI-375511, EBI-395573;
Q8BH43:Wasf2; NbExp=2; IntAct=EBI-375511, EBI-643162;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
projection, filopodium {ECO:0000250}. Cell projection, growth cone
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density {ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000250}. Note=Localized to protruding lamellipodia and
filopodia tips. Also localized to neuronal growth cones and
synaptosomes. May shuttle from the postsynaptic densities to the
nucleus (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8CBW3-1; Sequence=Displayed;
Name=2; Synonyms=short;
IsoId=Q8CBW3-2; Sequence=VSP_010756, VSP_010757, VSP_010758;
Name=3;
IsoId=Q8CBW3-3; Sequence=VSP_010756;
Name=4; Synonyms=long;
IsoId=Q8CBW3-4; Sequence=VSP_010756, VSP_010757;
Name=5;
IsoId=Q8CBW3-5; Sequence=VSP_010756, VSP_022636;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in bone
marrow, spleen, brain, testes, and embryonic brain. In adult brain
prominently expressed in the neocortex, hippocampus and dentate
gyrus. {ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:7590237}.
-!- DEVELOPMENTAL STAGE: Detected at E10 and E12 in developing brain,
but does not appear more prominent in the neuroepithelium compared
to the surrounding tissue. {ECO:0000269|PubMed:10995551}.
-!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
sufficient for interaction with STX1A.
-!- PTM: Phosphorylated on tyrosine residues after serum stimulation
or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by
ABL1, required for nuclear but not for synaptic localization (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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EMBL; AF420251; AAL16036.1; -; mRNA.
EMBL; AY033645; AAK59381.1; -; mRNA.
EMBL; AK034476; BAC28722.1; -; mRNA.
EMBL; AK152061; BAE30917.1; -; mRNA.
EMBL; AK152184; BAE31015.1; -; mRNA.
EMBL; AK151026; BAE30044.1; -; mRNA.
EMBL; BC004657; AAH04657.1; -; mRNA.
EMBL; U17698; AAB00373.1; ALT_SEQ; mRNA.
CCDS; CCDS38058.1; -. [Q8CBW3-5]
CCDS; CCDS38059.1; -. [Q8CBW3-3]
CCDS; CCDS38060.1; -. [Q8CBW3-2]
CCDS; CCDS38061.1; -. [Q8CBW3-1]
CCDS; CCDS50513.1; -. [Q8CBW3-4]
RefSeq; NP_001070658.1; NM_001077190.3. [Q8CBW3-1]
RefSeq; NP_001070660.1; NM_001077192.3. [Q8CBW3-2]
RefSeq; NP_001070661.1; NM_001077193.3. [Q8CBW3-5]
RefSeq; NP_031406.2; NM_007380.4. [Q8CBW3-4]
UniGene; Mm.205647; -.
UniGene; Mm.249752; -.
ProteinModelPortal; Q8CBW3; -.
SMR; Q8CBW3; -.
BioGrid; 197905; 12.
CORUM; Q8CBW3; -.
DIP; DIP-29534N; -.
IntAct; Q8CBW3; 31.
MINT; MINT-128698; -.
STRING; 10090.ENSMUSP00000118491; -.
iPTMnet; Q8CBW3; -.
PhosphoSitePlus; Q8CBW3; -.
PaxDb; Q8CBW3; -.
PRIDE; Q8CBW3; -.
DNASU; 11308; -.
Ensembl; ENSMUST00000114544; ENSMUSP00000110191; ENSMUSG00000058835. [Q8CBW3-5]
Ensembl; ENSMUST00000123948; ENSMUSP00000118491; ENSMUSG00000058835. [Q8CBW3-1]
Ensembl; ENSMUST00000126112; ENSMUSP00000117335; ENSMUSG00000058835. [Q8CBW3-3]
Ensembl; ENSMUST00000140164; ENSMUSP00000120462; ENSMUSG00000058835. [Q8CBW3-4]
Ensembl; ENSMUST00000149719; ENSMUSP00000120621; ENSMUSG00000058835. [Q8CBW3-2]
GeneID; 11308; -.
KEGG; mmu:11308; -.
UCSC; uc008ins.2; mouse. [Q8CBW3-1]
UCSC; uc008inw.2; mouse. [Q8CBW3-5]
CTD; 10006; -.
MGI; MGI:104913; Abi1.
eggNOG; KOG2546; Eukaryota.
eggNOG; ENOG410Y0MH; LUCA.
GeneTree; ENSGT00390000003756; -.
HOGENOM; HOG000293213; -.
HOVERGEN; HBG050446; -.
InParanoid; Q8CBW3; -.
OMA; VGHGVKE; -.
PhylomeDB; Q8CBW3; -.
TreeFam; TF314303; -.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
ChiTaRS; Abi1; mouse.
PRO; PR:Q8CBW3; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000058835; -.
CleanEx; MM_ABI1; -.
ExpressionAtlas; Q8CBW3; baseline and differential.
Genevisible; Q8CBW3; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0031209; C:SCAR complex; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; ISO:MGI.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
GO; GO:0048813; P:dendrite morphogenesis; IDA:MGI.
GO; GO:0072673; P:lamellipodium morphogenesis; IMP:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0001756; P:somitogenesis; IMP:MGI.
CDD; cd11971; SH3_Abi1; 1.
InterPro; IPR028457; ABI.
InterPro; IPR028456; ABI1.
InterPro; IPR035725; Abi1_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:SF2; PTHR10460:SF2; 1.
Pfam; PF07815; Abi_HHR; 1.
Pfam; PF00018; SH3_1; 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;
Acetylation; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Membrane; Nucleus; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; SH3 domain; Synapse.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8IZP0}.
CHAIN 2 481 Abl interactor 1.
/FTId=PRO_0000191788.
DOMAIN 45 107 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 419 478 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 18 79 Required for binding to WASF1.
COMPBIAS 337 391 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QZM5}.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 213 213 Phosphotyrosine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 428 428 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZM5}.
MOD_RES 480 480 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZP0}.
VAR_SEQ 154 158 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000303|PubMed:11477655,
ECO:0000303|PubMed:11526477,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:7590237}.
/FTId=VSP_010756.
VAR_SEQ 274 362 AAPGAAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVAA
QFSAQPHVNGGPLYSQNSISVAPPPPPMPQLTPQIPLTGFV
ARVQENI -> V (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022636.
VAR_SEQ 274 274 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11477655,
ECO:0000303|PubMed:11526477,
ECO:0000303|PubMed:7590237}.
/FTId=VSP_010757.
VAR_SEQ 333 361 Missing (in isoform 2).
{ECO:0000303|PubMed:11477655}.
/FTId=VSP_010758.
CONFLICT 313 313 A -> T (in Ref. 4; AAH04657).
{ECO:0000305}.
SEQUENCE 481 AA; 52288 MW; 1654A1E89438BC1D CRC64;
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK
PPSPPVSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS
GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT AGPAAPGAAP GSQYGTMTRQ ISRHNSTTSS
TSSGGYRRTP SVAAQFSAQP HVNGGPLYSQ NSISVAPPPP PMPQLTPQIP LTGFVARVQE
NIADSPTPPP PPPPDDIPMF DDSPPPPPPP PVDYEDEEAA VVQYSDPYAD GDPAWAPKNY
IEKVVAIYDY TKDKDDELSF KEGAIIYVIK KNDDGWFEGV CNRVTGLFPG NYVESIMHYT
D


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