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Breast carcinoma-amplified sequence 3 (GAOB1)

 BCAS3_HUMAN             Reviewed;         928 AA.
Q9H6U6; Q17RM0; Q6KF21; Q8IXI6; Q8NDR8; Q8TDL9; Q8TDM1; Q8WY55;
Q9BVF0; Q9H957; Q9H9Y9; Q9NXP4;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
22-NOV-2017, entry version 148.
RecName: Full=Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470};
AltName: Full=GAOB1;
Name=BCAS3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470};
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 1), TISSUE SPECIFICITY,
CHROMOSOMAL TRANSLOCATION WITH BCAS4, AND VARIANT SER-87.
TISSUE=Liver;
PubMed=12378525; DOI=10.1002/gcc.10121;
Baerlund M., Monni O., Weaver J.D., Kauraniemi P., Sauter G.,
Heiskanen M., Kallioniemi O.-P., Kallioniemi A.;
"Cloning of BCAS3 (17q23) and BCAS4 (20q13) genes that undergo
amplification, overexpression, and fusion in breast cancer.";
Genes Chromosomes Cancer 35:311-317(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6),
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 478-928 (ISOFORM 3), AND
VARIANT SER-87.
TISSUE=Colon;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-87.
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-87.
TISSUE=Brain, and Cervix;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-433 (ISOFORM 6), AND PARTIAL
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Bauer M.;
"Cloning and sequencing of a new isoform similar to FLJ20128 and
BCAS3.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-928 (ISOFORM 4).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 510-928 (ISOFORMS 1/6).
Wu G., Couch F.J.;
"Five novel genes from 17q23 amplicon have different amplification and
overexpression frequency in breast cancer.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
DOMAIN.
PubMed=16099728; DOI=10.1016/j.modgep.2005.06.002;
Siva K., Inamdar M.S.;
"Rudhira is a cytoplasmic WD40 protein expressed in mouse embryonic
stem cells and during embryonic erythropoiesis.";
Gene Expr. Patterns 6:225-234(2006).
[10]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16617102; DOI=10.1073/pnas.0601989103;
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
"MTA1, a transcriptional activator of breast cancer amplified sequence
3.";
Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
[11]
ERRATUM.
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
[12]
FUNCTION, INTERACTION WITH HISTONE H3; ESR1; KAT2B AND PELP1,
SUBCELLULAR LOCATION, AND CHROMATIN-BINDING.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich
protein-1 (PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18030336; DOI=10.1371/journal.pone.0001202;
Siva K., Venu P., Mahadevan A., Shankar S.K., Inamdar M.S.;
"Human BCAS3 expression in embryonic stem cells and vascular
precursors suggests a role in human embryogenesis and tumor
angiogenesis.";
PLoS ONE 2:E1202-E1202(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
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).
[17]
INTERACTION WITH BETA-TUBULIN AND VIM.
PubMed=22300583; DOI=10.1016/j.yexcr.2012.01.016;
Jain M., Bhat G.P., Vijayra havan K., Inamdar M.S.;
"Rudhira/BCAS3 is a cytoskeletal protein that controls Cdc42
activation and directional cell migration during angiogenesis.";
Exp. Cell Res. 318:753-767(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, 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).
[20]
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).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Plays a role in angiogenesis. Participates in the
regulation of cell polarity and directional endothelial cell
migration by mediating both the activation and recruitment of
CDC42 and the reorganization of the actin cytoskeleton at the cell
leading edge. Promotes filipodia formation (By similarity).
Functions synergistically with PELP1 as a transcriptional
coactivator of estrogen receptor-responsive genes. Stimulates
histone acetyltransferase activity. Binds to chromatin.
{ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.
-!- SUBUNIT: Interacts with histone H3, ESR1, KAT2B and PELP1; the
interactions occur in a estrogen-dependent manner. Interacts with
beta-tubulin and VIM. {ECO:0000269|PubMed:17505058,
ECO:0000269|PubMed:22300583}.
-!- INTERACTION:
Q9BSU1:C16orf70; NbExp=3; IntAct=EBI-10307911, EBI-946080;
Q9UJX2:CDC23; NbExp=3; IntAct=EBI-6083685, EBI-396137;
Q13363-2:CTBP1; NbExp=3; IntAct=EBI-6083685, EBI-10171858;
P56545-3:CTBP2; NbExp=3; IntAct=EBI-6083685, EBI-10171902;
P08670:VIM; NbExp=3; IntAct=EBI-6083685, EBI-353844;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617102,
ECO:0000269|PubMed:17505058}. Cytoplasm
{ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058,
ECO:0000269|PubMed:18030336}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q8CCN5}. Note=Localizes in the cytoplasm in
stationary cells. Translocates from the cytoplasm to the leading
edge in motile cells. Colocalizes with microtubules and
intermediate filaments in both stationary and motile cells (By
similarity). Associates with chromatin. Recruited to estrogen
receptor-induced promoters in a PELP1-dependent manner.
{ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=2;
IsoId=Q9H6U6-1; Sequence=Displayed;
Name=1;
IsoId=Q9H6U6-2; Sequence=VSP_007858;
Name=3;
IsoId=Q9H6U6-3; Sequence=VSP_007858, VSP_007860;
Name=4;
IsoId=Q9H6U6-8; Sequence=VSP_007860;
Name=5; Synonyms=Maaab1;
IsoId=Q9H6U6-7; Sequence=VSP_007858, VSP_040113;
Note=No experimental confirmation available. Ref.2 (AK225757)
sequence differs from that shown due to a frameshift in position
895. Ref.4 (CAD54076) sequence differs from that shown due to a
frameshift in position 894. Ref.4 (CAD54076) sequence is in
conflict in position: 891:G->R. {ECO:0000305};
Name=6; Synonyms=Maaab2;
IsoId=Q9H6U6-6; Sequence=VSP_040112, VSP_007858;
-!- TISSUE SPECIFICITY: Expressed in stomach, liver, lung, kidney,
prostate, testis, thyroid gland, adrenal gland, brain, heart,
skeletal muscle, colon, spleen, small intestine, placenta, blood
leukocyte and mammary epithelial cells. Expressed in
undifferentiated ES cells. Expressed in blood islands and nascent
blood vessels derived from differentiated ES cells into embryoid
bodies (BD). Expressed in endothelial cells. Not detected in
brain. Expressed in brain tumors (at protein level). Expressed in
brain. Highly expressed in breast cancers and in glioma cell
lines. {ECO:0000269|PubMed:12378525, ECO:0000269|PubMed:16617102,
ECO:0000269|PubMed:18030336}.
-!- DEVELOPMENTAL STAGE: Fetal.
-!- INDUCTION: By estrogen. {ECO:0000269|PubMed:16617102}.
-!- DOMAIN: Has been proposed to contain 7 WD repeats. This prediction
could not be reproduced. {ECO:0000305|PubMed:16099728}.
-!- DISEASE: Note=A chromosomal aberration involving BCAS3 has been
found in some breast carcinoma cell lines. Translocation
t(17;20)(q23;q13) with BCAS4.
-!- SIMILARITY: Belongs to the BCAS3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF70324.1; Type=Frameshift; Positions=693; Evidence={ECO:0000305};
Sequence=AAL99634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA90966.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14078.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCAS3ID766.html";
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EMBL; AF361219; AAL99632.1; -; mRNA.
EMBL; AF361221; AAL99634.1; ALT_INIT; mRNA.
EMBL; AK000135; BAA90966.1; ALT_INIT; mRNA.
EMBL; AK022526; BAB14078.1; ALT_INIT; mRNA.
EMBL; AK023054; BAB14380.1; -; mRNA.
EMBL; AK025510; BAB15156.1; -; mRNA.
EMBL; AK225757; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC005746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC015876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471179; EAW51414.1; -; Genomic_DNA.
EMBL; BC001250; AAH01250.2; -; mRNA.
EMBL; BC117275; AAI17276.1; -; mRNA.
EMBL; BC143386; AAI43387.1; -; mRNA.
EMBL; AJ511332; CAD54076.1; ALT_FRAME; mRNA.
EMBL; AJ518105; CAD57723.1; -; mRNA.
EMBL; AL831895; CAD38568.1; -; mRNA.
EMBL; AF260268; AAF70324.1; ALT_FRAME; mRNA.
CCDS; CCDS11626.1; -. [Q9H6U6-2]
CCDS; CCDS45749.1; -. [Q9H6U6-1]
CCDS; CCDS82176.1; -. [Q9H6U6-8]
CCDS; CCDS82177.1; -. [Q9H6U6-7]
CCDS; CCDS82178.1; -. [Q9H6U6-3]
RefSeq; NP_001092902.1; NM_001099432.1. [Q9H6U6-1]
RefSeq; NP_001307399.1; NM_001320470.1. [Q9H6U6-7]
RefSeq; NP_060149.3; NM_017679.3. [Q9H6U6-2]
UniGene; Hs.655028; -.
ProteinModelPortal; Q9H6U6; -.
BioGrid; 120182; 40.
IntAct; Q9H6U6; 29.
STRING; 9606.ENSP00000375067; -.
iPTMnet; Q9H6U6; -.
PhosphoSitePlus; Q9H6U6; -.
BioMuta; BCAS3; -.
DMDM; 313104248; -.
EPD; Q9H6U6; -.
MaxQB; Q9H6U6; -.
PaxDb; Q9H6U6; -.
PeptideAtlas; Q9H6U6; -.
PRIDE; Q9H6U6; -.
Ensembl; ENST00000390652; ENSP00000375067; ENSG00000141376. [Q9H6U6-1]
Ensembl; ENST00000407086; ENSP00000385323; ENSG00000141376. [Q9H6U6-2]
Ensembl; ENST00000408905; ENSP00000386173; ENSG00000141376. [Q9H6U6-3]
Ensembl; ENST00000588462; ENSP00000468592; ENSG00000141376. [Q9H6U6-8]
Ensembl; ENST00000588874; ENSP00000464825; ENSG00000141376. [Q9H6U6-6]
Ensembl; ENST00000589222; ENSP00000466078; ENSG00000141376. [Q9H6U6-7]
GeneID; 54828; -.
KEGG; hsa:54828; -.
UCSC; uc002iyu.5; human. [Q9H6U6-1]
CTD; 54828; -.
DisGeNET; 54828; -.
EuPathDB; HostDB:ENSG00000141376.20; -.
GeneCards; BCAS3; -.
H-InvDB; HIX0021877; -.
HGNC; HGNC:14347; BCAS3.
HPA; HPA052409; -.
HPA; HPA057289; -.
MIM; 607470; gene.
neXtProt; NX_Q9H6U6; -.
OpenTargets; ENSG00000141376; -.
PharmGKB; PA25286; -.
eggNOG; KOG2109; Eukaryota.
eggNOG; KOG4415; Eukaryota.
eggNOG; ENOG410XSW7; LUCA.
GeneTree; ENSGT00390000006454; -.
HOVERGEN; HBG050676; -.
InParanoid; Q9H6U6; -.
OMA; TPLEMVT; -.
OrthoDB; EOG091G038X; -.
PhylomeDB; Q9H6U6; -.
TreeFam; TF105856; -.
SignaLink; Q9H6U6; -.
ChiTaRS; BCAS3; human.
GeneWiki; BCAS3; -.
GenomeRNAi; 54828; -.
PRO; PR:Q9H6U6; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141376; -.
ExpressionAtlas; Q9H6U6; baseline and differential.
Genevisible; Q9H6U6; HS.
GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:0042594; P:response to starvation; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035148; P:tube formation; ISS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR022175; BCAS3.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12490; BCAS3; 1.
SUPFAM; SSF50978; SSF50978; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Angiogenesis;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 928 Breast carcinoma-amplified sequence 3.
/FTId=PRO_0000050883.
SITE 824 825 Breakpoint for translocation to form
BCAS4-BCAS3.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CCN5}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CCN5}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CCN5}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CCN5}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 229 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_040112.
VAR_SEQ 547 561 Missing (in isoform 1, isoform 3, isoform
5 and isoform 6).
{ECO:0000303|PubMed:12378525,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.6}.
/FTId=VSP_007858.
VAR_SEQ 879 879 T -> TDTALDVAVKTFPPERHVAVKCF (in isoform
3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_007860.
VAR_SEQ 880 928 ELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPL
SLFPTGFP -> DTALDVAVKTFPPERHVAVKCFGKKKGKK
KQCQQPSVREQPNSNKACVRDGGRTSARGKHRDSE (in
isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040113.
VARIANT 87 87 N -> S (in dbSNP:rs2643103).
{ECO:0000269|PubMed:12378525,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_065093.
VARIANT 106 106 I -> V (in dbSNP:rs34712615).
/FTId=VAR_057583.
CONFLICT 29 29 E -> K (in Ref. 1; AAL99632).
{ECO:0000305}.
CONFLICT 127 127 R -> K (in Ref. 1; AAL99632).
{ECO:0000305}.
CONFLICT 199 200 VV -> II (in Ref. 2; BAB15156).
{ECO:0000305}.
CONFLICT 533 533 K -> E (in Ref. 2; BAB14078/BAB14380).
{ECO:0000305}.
CONFLICT 640 640 D -> G (in Ref. 2; BAB15156).
{ECO:0000305}.
CONFLICT 666 666 Q -> R (in Ref. 2; BAB14078).
{ECO:0000305}.
CONFLICT 806 806 S -> P (in Ref. 2; BAB15156).
{ECO:0000305}.
SEQUENCE 928 AA; 101237 MW; 00D82E2EDCD1E8D7 CRC64;
MNEAMATDSP RRPSRCTGGV VVRPQAVTEQ SYMESVVTFL QDVVPQAYSG TPLTEEKEKI
VWVRFENADL NDTSRNLEFH EIHSTGNEPP LLIMIGYSDG MQVWSIPISG EAQELFSVRH
GPIRAARILP APQFGAQKCD NFAEKRPLLG VCKSIGSSGT SPPYCCVDLY SLRTGEMVKS
IQFKTPIYDL HCNKRILVVV LQEKIAAFDS CTFTKKFFVT SCYPCPGPNM NPIALGSRWL
AYAENKLIRC HQSRGGACGD NIQSYTATVI SAAKTLKSGL TMVGKVVTQL TGTLPSGVTE
DDVAIHSNSR RSPLVPGIIT VIDTETVGEG QVLVSEDSDS DGIVAHFPAH EKPVCCMAFN
TSGMLLVTTD TLGHDFHVFQ ILTHPWSSSQ CAVHHLYTLH RGETEAKVQD ICFSHDCRWV
VVSTLRGTSH VFPINPYGGQ PCVRTHMSPR VVNRMSRFQK SAGLEEIEQE LTSKQGGRCS
PVPGLSSSPS GSPLHGKLNS QDSYNNFTNN NPGNPRLSPL PSLMVVMPLA QIKQPMTLGT
ITKRTGPYLF GAGCFSIKAP CKVKPPPQIS PSKSMGGEFC VAAIFGTSRS WFANNAGLKR
EKDQSKQVVV ESLYIISCYG TLVEHMMEPR PLSTAPKISD DTPLEMMTSP RASWTLVRTP
QWNELQPPFN ANHPLLLAAD AVQYYQFLLA GLVPPGSPGP ITRHGSYDSL ASDHSGQEDE
EWLSQVEIVT HTGPHRRLWM GPQFQFKTIH PSGQTTVISS SSSVLQSHGP SDTPQPLLDF
DTDDLDLNSL RIQPVRSDPV SMPGSSRPVS DRRGVSTVID AASGTFDRSV TLLEVCGSWP
EGFGLRHMSS MEHTEEGLRE RLADAMAESP SRDVVGSGTE LQREGSIETL SNSSGSTSGS
IPRNFDGYRS PLPTNESQPL SLFPTGFP


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