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Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)

 ABI1_HUMAN              Reviewed;         508 AA.
Q8IZP0; A9Z1Y6; B3KX62; B4DQ58; H7BXI6; O15147; O76049; O95060;
Q5T2R3; Q5T2R4; Q5T2R6; Q5T2R7; Q5T2R9; Q5W070; Q5W072; Q8TB63;
Q96S81; Q9NXZ9; Q9NYB8;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 170.
RecName: Full=Abl interactor 1;
AltName: Full=Abelson interactor 1;
Short=Abi-1;
AltName: Full=Abl-binding protein 4;
Short=AblBP4;
AltName: Full=Eps8 SH3 domain-binding protein;
Short=Eps8-binding protein;
AltName: Full=Nap1-binding protein;
Short=Nap1BP;
AltName: Full=Spectrin SH3 domain-binding protein 1;
AltName: Full=e3B1;
Name=ABI1 {ECO:0000312|HGNC:HGNC:11320}; Synonyms=SSH3BP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), PHOSPHORYLATION, SUBCELLULAR
LOCATION, AND INTERACTION WITH EPS8 AND ABL1.
PubMed=9010225; DOI=10.1038/sj.onc.1200822;
Biesova Z., Piccoli C., Wong W.T.;
"Isolation and characterization of e3B1, an eps8 binding protein that
regulates cell growth.";
Oncogene 14:233-241(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS
3; 7; 8 AND 9), AND INTERACTION WITH SPTA1.
PubMed=9593709; DOI=10.1074/jbc.273.22.13681;
Ziemnicka-Kotula D., Xu J., Gu H., Potempska A., Kim K.S.,
Jenkins E.C., Trenkner E., Kotula L.;
"Identification of a candidate human spectrin Src homology 3 domain-
binding protein suggests a general mechanism of association of
tyrosine kinases with the spectrin-based membrane skeleton.";
J. Biol. Chem. 273:13681-13692(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
INTERACTION WITH ABL1; NAP1 AND NCK1.
PubMed=11418237; DOI=10.1016/S0378-1119(01)00521-2;
Yamamoto A., Suzuki T., Sakaki Y.;
"Isolation of hNap1BP which interacts with human Nap 1 (NCKAP1) whose
expression is down-regulated in Alzheimer's disease.";
Gene 271:159-169(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH NCF1.
TISSUE=Umbilical vein endothelial cell;
PubMed=12681507; DOI=10.1016/S0014-5793(03)00262-X;
Gu Y., Souza R.F., Wu R.F., Xu Y.C., Terada L.S.;
"Induction of colonic epithelial cell apoptosis by p47-dependent
oxidants(1).";
FEBS Lett. 540:195-200(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=T-cell;
Wilson L.A., Fields D., Cruz L., Friesen J., Siminovitch K.A.;
"A new member of the Abl interactor protein family, AblBP4.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chikri M.M., Boutin M.P., Vaxillaire M.M., Froguel M.P.;
"In silico cloning of the human SSH3BP1/e3B1 gene.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Quackenbush R.C., Pendergast A.M.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 11 AND 12).
TISSUE=Cerebellum;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Muscle;
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).
[12]
PROTEIN SEQUENCE OF 2-17.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[13]
PROTEIN SEQUENCE OF 2-17; 139-154; 229-237 AND 451-477, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[14]
FUNCTION, AND INTERACTION WITH SOS1; SOS2 AND GRB2.
PubMed=11003655; DOI=10.1128/MCB.20.20.7591-7601.2000;
Fan P.-D., Goff S.P.;
"Abl interactor 1 binds to sos and inhibits epidermal growth
factor- and v-Abl-induced activation of extracellular signal-regulated
kinases.";
Mol. Cell. Biol. 20:7591-7601(2000).
[15]
ALTERNATIVE SPLICING (ISOFORMS 2 AND 10), AND CHROMOSOMAL
TRANSLOCATION WITH KMT2A.
PubMed=9694699;
Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F.,
Yanagisawa M., Hayashi Y.;
"ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene
in acute myeloid leukemia with t(10;11)(p11.2;q23).";
Blood 92:1125-1130(1998).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[17]
IDENTIFICATION IN THE WAVE2 COMPLEX.
PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M.,
Yaffe M.B., Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
"Hem-1 complexes are essential for Rac activation, actin
polymerization, and myosin regulation during neutrophil chemotaxis.";
PLoS Biol. 4:E38-E38(2006).
[18]
FUNCTION, AND PHOSPHORYLATION AT TYR-213.
PubMed=18328268; DOI=10.1016/j.bbamcr.2008.01.028;
Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X.,
Debnath A.K., Cowburn D., Kotula L.;
"Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase
by phosphopeptides derived from Abi1/Hssh3bp1.";
Biochim. Biophys. Acta 1783:737-747(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-216, 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).
[22]
INTERACTION WITH FNBP1L; WASF2 AND CDC42.
PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A.,
Malabarba M.G., Disanza A., Stradal T.B., Cassata G., Confalonieri S.,
Hardin J.D., Soto M.C., Grant B.D., Scita G.;
"Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics
and membrane trafficking during Caenorhabditis elegans oocyte growth
and embryonic epidermal morphogenesis.";
PLoS Genet. 5:E1000675-E1000675(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND THR-507, 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).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-225 AND
SER-323, 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).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; TYR-213; SER-225;
SER-319 AND SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[29]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135 (MICROBIAL
INFECTION).
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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; THR-178; SER-183;
SER-187; SER-222 AND SER-225, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: May act in negative regulation of cell growth and
transformation by interacting with nonreceptor tyrosine kinases
ABL1 and/or ABL2. May play a role in regulation of 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:11003655, ECO:0000269|PubMed:18328268}.
-!- SUBUNIT: Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8,
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 (By similarity). Interacts with SOS1, SOS2,
GRB2, SPTA1 and the first SH3 domain of NCK1. Isoform 6 does not
interact with NCK1. Component of the WAVE2 complex composed of
ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic
cells) and WASF2/WAVE2 (PubMed:16417406). 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 (PubMed:19798448). {ECO:0000250,
ECO:0000269|PubMed:11003655, ECO:0000269|PubMed:11418237,
ECO:0000269|PubMed:12681507, ECO:0000269|PubMed:16417406,
ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:9010225,
ECO:0000269|PubMed:9593709}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 protein UL135.
{ECO:0000269|PubMed:25121749}.
-!- INTERACTION:
P00519:ABL1; NbExp=11; IntAct=EBI-375446, EBI-375543;
P00520-4:Abl1 (xeno); NbExp=5; IntAct=EBI-8593095, EBI-8593082;
P42684:ABL2; NbExp=2; IntAct=EBI-375446, EBI-1102694;
O00555:CACNA1A; NbExp=2; IntAct=EBI-375446, EBI-766279;
P22681:CBL; NbExp=3; IntAct=EBI-7358775, EBI-518228;
Q08509:Eps8 (xeno); NbExp=2; IntAct=EBI-375446, EBI-375596;
P13612:ITGA4; NbExp=2; IntAct=EBI-7358775, EBI-703044;
P14598:NCF1; NbExp=5; IntAct=EBI-375446, EBI-395044;
Q9Y2A7:NCKAP1; NbExp=3; IntAct=EBI-375446, EBI-389845;
P27986:PIK3R1; NbExp=8; IntAct=EBI-375446, EBI-79464;
P26450:Pik3r1 (xeno); NbExp=3; IntAct=EBI-375446, EBI-641764;
Q92569:PIK3R3; NbExp=2; IntAct=EBI-375446, EBI-79893;
P20936:RASA1; NbExp=2; IntAct=EBI-375446, EBI-1026476;
O14512:SOCS7; NbExp=2; IntAct=EBI-375446, EBI-1539606;
P02549:SPTA1; NbExp=2; IntAct=EBI-375446, EBI-375617;
P15498:VAV1; NbExp=2; IntAct=EBI-375446, EBI-625518;
P52735:VAV2; NbExp=2; IntAct=EBI-375446, EBI-297549;
-!- 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=12;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q8IZP0-1; Sequence=Displayed;
Name=2; Synonyms=long, B48;
IsoId=Q8IZP0-2; Sequence=VSP_010749, VSP_010750, VSP_010751,
VSP_010752;
Name=3;
IsoId=Q8IZP0-3; Sequence=VSP_010750, VSP_010752;
Name=4;
IsoId=Q8IZP0-4; Sequence=VSP_010750, VSP_010751, VSP_010752;
Name=5;
IsoId=Q8IZP0-5; Sequence=VSP_010749, VSP_010750;
Name=6;
IsoId=Q8IZP0-6; Sequence=VSP_010750, VSP_010751;
Name=7; Synonyms=4;
IsoId=Q8IZP0-7; Sequence=VSP_010750, VSP_010751, VSP_010754,
VSP_010755;
Name=8; Synonyms=5;
IsoId=Q8IZP0-8; Sequence=VSP_010750, VSP_010751, VSP_010754,
VSP_010752;
Name=9; Synonyms=2;
IsoId=Q8IZP0-9; Sequence=VSP_010750;
Name=10; Synonyms=B30;
IsoId=Q8IZP0-10; Sequence=VSP_010749, VSP_010750, VSP_010751,
VSP_010754, VSP_010752, VSP_010753;
Name=11;
IsoId=Q8IZP0-11; Sequence=VSP_043403, VSP_010750, VSP_010751,
VSP_010754, VSP_010752, VSP_010753;
Note=No experimental confirmation available.;
Name=12;
IsoId=Q8IZP0-12; Sequence=VSP_044604, VSP_010752;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
brain. {ECO:0000269|PubMed:11418237}.
-!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
sufficient for interaction with STX1A. {ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:9010225}.
-!- DISEASE: Note=A chromosomal aberration involving ABI1 is a cause
of acute leukemias. Translocation t(10;11)(p11.2;q23) with
KMT2A/MLL1. ABI1 isoform 2 was found to be present in acute
leukemia KMT2A/MLL1-ABI1 fusion transcript.
{ECO:0000269|PubMed:9694699}.
-!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ABI1ID233.html";
-----------------------------------------------------------------------
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EMBL; AF006516; AAB62569.1; -; mRNA.
EMBL; U87166; AAC39757.1; -; mRNA.
EMBL; AB040151; BAB55675.1; -; mRNA.
EMBL; AF540955; AAN28379.1; -; mRNA.
EMBL; AF001628; AAD00897.1; -; mRNA.
EMBL; AJ277065; CAB88006.1; -; Genomic_DNA.
EMBL; AJ277066; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277067; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277068; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277069; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277070; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277071; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277072; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277073; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AJ277074; CAB88006.1; JOINED; Genomic_DNA.
EMBL; AF260262; AAF70309.1; -; mRNA.
EMBL; AK126803; BAG54374.1; -; mRNA.
EMBL; AK298646; BAG60820.1; -; mRNA.
EMBL; AK291823; BAF84512.1; -; mRNA.
EMBL; AL139404; CAH73112.1; -; Genomic_DNA.
EMBL; AL390961; CAH73112.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73113.1; -; Genomic_DNA.
EMBL; AL390961; CAH73113.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73114.1; -; Genomic_DNA.
EMBL; AL390961; CAH73114.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73115.1; -; Genomic_DNA.
EMBL; AL390961; CAH73115.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73116.1; -; Genomic_DNA.
EMBL; AL390961; CAH73116.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73117.1; -; Genomic_DNA.
EMBL; AL390961; CAH73117.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73118.1; -; Genomic_DNA.
EMBL; AL390961; CAH73118.1; JOINED; Genomic_DNA.
EMBL; AL139404; CAH73119.1; -; Genomic_DNA.
EMBL; AL390961; CAH73119.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17272.1; -; Genomic_DNA.
EMBL; AL139404; CAI17272.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17273.1; -; Genomic_DNA.
EMBL; AL139404; CAI17273.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17274.1; -; Genomic_DNA.
EMBL; AL139404; CAI17274.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17275.1; -; Genomic_DNA.
EMBL; AL139404; CAI17275.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17276.1; -; Genomic_DNA.
EMBL; AL139404; CAI17276.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17277.1; -; Genomic_DNA.
EMBL; AL139404; CAI17277.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17278.1; -; Genomic_DNA.
EMBL; AL139404; CAI17278.1; JOINED; Genomic_DNA.
EMBL; AL390961; CAI17279.1; -; Genomic_DNA.
EMBL; AL139404; CAI17279.1; JOINED; Genomic_DNA.
EMBL; CH471072; EAW86079.1; -; Genomic_DNA.
EMBL; CH471072; EAW86080.1; -; Genomic_DNA.
EMBL; BC024254; AAH24254.1; -; mRNA.
CCDS; CCDS31169.1; -. [Q8IZP0-5]
CCDS; CCDS31170.1; -. [Q8IZP0-3]
CCDS; CCDS31171.1; -. [Q8IZP0-9]
CCDS; CCDS53497.1; -. [Q8IZP0-11]
CCDS; CCDS53498.1; -. [Q8IZP0-2]
CCDS; CCDS53499.1; -. [Q8IZP0-4]
CCDS; CCDS53500.1; -. [Q8IZP0-6]
CCDS; CCDS53501.1; -. [Q8IZP0-12]
CCDS; CCDS7150.1; -. [Q8IZP0-1]
CCDS; CCDS73077.1; -. [Q8IZP0-8]
CCDS; CCDS73078.1; -. [Q8IZP0-7]
RefSeq; NP_001012768.1; NM_001012750.2. [Q8IZP0-9]
RefSeq; NP_001012769.1; NM_001012751.2. [Q8IZP0-3]
RefSeq; NP_001012770.1; NM_001012752.2. [Q8IZP0-5]
RefSeq; NP_001171587.1; NM_001178116.1. [Q8IZP0-12]
RefSeq; NP_001171590.1; NM_001178119.1. [Q8IZP0-6]
RefSeq; NP_001171591.1; NM_001178120.1. [Q8IZP0-4]
RefSeq; NP_001171592.1; NM_001178121.1. [Q8IZP0-2]
RefSeq; NP_001171593.1; NM_001178122.1. [Q8IZP0-7]
RefSeq; NP_001171594.1; NM_001178123.1.
RefSeq; NP_001171595.1; NM_001178124.1. [Q8IZP0-10]
RefSeq; NP_001171596.1; NM_001178125.1. [Q8IZP0-11]
RefSeq; NP_005461.2; NM_005470.3. [Q8IZP0-1]
UniGene; Hs.508148; -.
ProteinModelPortal; Q8IZP0; -.
SMR; Q8IZP0; -.
BioGrid; 115324; 67.
CORUM; Q8IZP0; -.
DIP; DIP-31118N; -.
ELM; Q8IZP0; -.
IntAct; Q8IZP0; 111.
MINT; Q8IZP0; -.
STRING; 9606.ENSP00000365312; -.
iPTMnet; Q8IZP0; -.
PhosphoSitePlus; Q8IZP0; -.
BioMuta; ABI1; -.
DMDM; 50400546; -.
EPD; Q8IZP0; -.
MaxQB; Q8IZP0; -.
PaxDb; Q8IZP0; -.
PeptideAtlas; Q8IZP0; -.
PRIDE; Q8IZP0; -.
ProteomicsDB; 71380; -.
ProteomicsDB; 71381; -. [Q8IZP0-10]
ProteomicsDB; 71382; -. [Q8IZP0-11]
ProteomicsDB; 71383; -. [Q8IZP0-2]
ProteomicsDB; 71384; -. [Q8IZP0-3]
ProteomicsDB; 71385; -. [Q8IZP0-4]
ProteomicsDB; 71386; -. [Q8IZP0-5]
ProteomicsDB; 71387; -. [Q8IZP0-6]
ProteomicsDB; 71388; -. [Q8IZP0-7]
ProteomicsDB; 71389; -. [Q8IZP0-8]
ProteomicsDB; 71390; -. [Q8IZP0-9]
Ensembl; ENST00000346832; ENSP00000279599; ENSG00000136754. [Q8IZP0-12]
Ensembl; ENST00000359188; ENSP00000352114; ENSG00000136754. [Q8IZP0-6]
Ensembl; ENST00000376137; ENSP00000365307; ENSG00000136754. [Q8IZP0-7]
Ensembl; ENST00000376138; ENSP00000365308; ENSG00000136754. [Q8IZP0-3]
Ensembl; ENST00000376139; ENSP00000365309; ENSG00000136754. [Q8IZP0-5]
Ensembl; ENST00000376140; ENSP00000365310; ENSG00000136754. [Q8IZP0-9]
Ensembl; ENST00000376142; ENSP00000365312; ENSG00000136754. [Q8IZP0-1]
Ensembl; ENST00000376166; ENSP00000365336; ENSG00000136754. [Q8IZP0-2]
Ensembl; ENST00000376170; ENSP00000365340; ENSG00000136754. [Q8IZP0-4]
Ensembl; ENST00000490841; ENSP00000440101; ENSG00000136754. [Q8IZP0-11]
GeneID; 10006; -.
KEGG; hsa:10006; -.
UCSC; uc001isx.4; human. [Q8IZP0-1]
CTD; 10006; -.
DisGeNET; 10006; -.
EuPathDB; HostDB:ENSG00000136754.16; -.
GeneCards; ABI1; -.
HGNC; HGNC:11320; ABI1.
HPA; CAB008375; -.
HPA; HPA029973; -.
HPA; HPA068407; -.
MIM; 603050; gene.
neXtProt; NX_Q8IZP0; -.
OpenTargets; ENSG00000136754; -.
PharmGKB; PA36144; -.
eggNOG; ENOG410IPCV; Eukaryota.
eggNOG; ENOG410XQ3Y; LUCA.
GeneTree; ENSGT00390000003756; -.
HOGENOM; HOG000293213; -.
HOVERGEN; HBG050446; -.
InParanoid; Q8IZP0; -.
OMA; VGHGVKE; -.
OrthoDB; EOG091G0AN8; -.
PhylomeDB; Q8IZP0; -.
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.
SignaLink; Q8IZP0; -.
SIGNOR; Q8IZP0; -.
ChiTaRS; ABI1; human.
GeneWiki; ABI1; -.
GenomeRNAi; 10006; -.
PRO; PR:Q8IZP0; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000136754; Expressed in 232 organ(s), highest expression level in mouth mucosa.
ExpressionAtlas; Q8IZP0; baseline and differential.
Genevisible; Q8IZP0; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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; Chromosomal rearrangement; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Host-virus interaction; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Postsynaptic cell membrane; Reference proteome;
SH3 domain; Synapse.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.13}.
CHAIN 2 508 Abl interactor 1.
/FTId=PRO_0000191787.
DOMAIN 45 107 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 446 505 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 18 79 Required for binding to WASF1.
{ECO:0000250}.
COMPBIAS 260 418 Pro-rich.
SITE 95 96 Breakpoint for translocation to form
KMT2A/MLL1-ABI1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.13}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QZM5}.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 213 213 Phosphotyrosine; by ABL1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18328268}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8CBW3}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 455 455 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8CBW3}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZM5}.
MOD_RES 507 507 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 38 38 I -> IQRHGFAVLLCLLSNSWP (in isoform 12).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044604.
VAR_SEQ 96 159 Missing (in isoform 11).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043403.
VAR_SEQ 154 158 Missing (in isoform 2, isoform 5 and
isoform 10).
{ECO:0000303|PubMed:12681507,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.7}.
/FTId=VSP_010749.
VAR_SEQ 274 300 Missing (in isoform 2, isoform 3, isoform
4, isoform 5, isoform 6, isoform 7,
isoform 8, isoform 9, isoform 10 and
isoform 11).
{ECO:0000303|PubMed:11418237,
ECO:0000303|PubMed:12681507,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9010225,
ECO:0000303|Ref.5, ECO:0000303|Ref.7}.
/FTId=VSP_010750.
VAR_SEQ 301 301 Missing (in isoform 2, isoform 4, isoform
6, isoform 7, isoform 8, isoform 10 and
isoform 11).
{ECO:0000303|PubMed:12681507,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9010225,
ECO:0000303|Ref.5, ECO:0000303|Ref.7}.
/FTId=VSP_010751.
VAR_SEQ 302 359 Missing (in isoform 7, isoform 8, isoform
10 and isoform 11).
{ECO:0000303|PubMed:12681507,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_010754.
VAR_SEQ 360 388 Missing (in isoform 2, isoform 3, isoform
4, isoform 8, isoform 10, isoform 11 and
isoform 12).
{ECO:0000303|PubMed:11418237,
ECO:0000303|PubMed:12681507,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5, ECO:0000303|Ref.7}.
/FTId=VSP_010752.
VAR_SEQ 360 360 I -> V (in isoform 7).
{ECO:0000303|Ref.5}.
/FTId=VSP_010755.
VAR_SEQ 389 389 I -> V (in isoform 10 and isoform 11).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010753.
VARIANT 331 331 G -> A (in dbSNP:rs2306236).
/FTId=VAR_048159.
CONFLICT 177 177 P -> L (in Ref. 2; AAC39757).
{ECO:0000305}.
CONFLICT 410 410 S -> F (in Ref. 2; AAC39757 and 4;
AAN28379). {ECO:0000305}.
CONFLICT 437 437 D -> G (in Ref. 8; BAG54374).
{ECO:0000305}.
SEQUENCE 508 AA; 55081 MW; 2D76F305934127CB CRC64;
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK
PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS
GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPENISVPP PSGAPPAPPL APLLPVSTVI
AAPGSAPGSQ YGTMTRQISR HNSTTSSTSS GGYRRTPSVT AQFSAQPHVN GGPLYSQNSI
SIAPPPPPMP QLTPQIPLTG FVARVQENIA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD
YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFMEG AIIYVIKKND
DGWYEGVCNR VTGLFPGNYV ESIMHYTD


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18-003-42687 Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP Polyclonal 0.1 mg Protein A
10-288-22014F Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP 0.1 mg
10-288-22014F Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP 0.05 mg
EIAAB12528 CAP-binding protein complex-interacting protein 1,DJ-1-binding protein,DJBP,DJBP,EFCAB6,EF-hand calcium-binding domain-containing protein 6,Homo sapiens,Human,KIAA1672
EIAAB46106 Formin-binding protein 21,Rat,Rattus norvegicus,Wbp4,WBP-4,WW domain-binding protein 4,WW domain-containing-binding protein 4
EIAAB12809 ELMO domain-containing protein 3,ELMOD3,Homo sapiens,Human,PP4068,RBED1,RBM29,RNA-binding motif and ELMO domain-containing protein 1,RNA-binding motif protein 29,RNA-binding protein 29
EIAAB26845 Amyloid beta A4 protein-binding family A member 2-binding protein,APBA2BP,Bos taurus,Bovine,NECAB3,N-terminal EF-hand calcium-binding protein 3,X11L-binding protein 51,XB51
EIAAB46099 Homo sapiens,Human,Npw38-binding protein,NpwBP,NPWBP,SH3 domain-binding protein SNP70,SIPP1,SNP70,Splicing factor that interacts with PQBP-1 and PP1,WBP11,WBP-11,WW domain-binding protein 11
EIAAB26846 Amyloid beta A4 protein-binding family A member 2-binding protein,Apba2bp,Mouse,Mus musculus,mXB51,Necab3,N-terminal EF-hand calcium-binding protein 3,X11L-binding protein 51,Xb51
18-003-44214 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
18-003-43630 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
U1772m CLIA Gbp3,GBP-3,Gbp4,GBP-4,GTP-binding protein 3,GTP-binding protein 4,Guanine nucleotide-binding protein 4,Guanylate-binding protein 3,Guanylate-binding protein 4,Mouse,Mus musculus 96T
E1772m ELISA kit Gbp3,GBP-3,Gbp4,GBP-4,GTP-binding protein 3,GTP-binding protein 4,Guanine nucleotide-binding protein 4,Guanylate-binding protein 3,Guanylate-binding protein 4,Mouse,Mus musculus 96T
E1772m ELISA Gbp3,GBP-3,Gbp4,GBP-4,GTP-binding protein 3,GTP-binding protein 4,Guanine nucleotide-binding protein 4,Guanylate-binding protein 3,Guanylate-binding protein 4,Mouse,Mus musculus 96T
31-225 Human DNA-binding protein (dbpA) is a member of a Y-box binding protein family containing a cold shock domain. The increased expression of Y box binding proteins in somatic cells is associated with ce 0.1 mg
31-224 Human DNA-binding protein (dbpA) is a member of a Y-box binding protein family containing a cold shock domain. The increased expression of Y box binding proteins in somatic cells is associated with ce 0.1 mg


 

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