BCAS3_HUMAN
ID BCAS3_HUMAN Reviewed; 928 AA.
AC Q9H6U6; Q17RM0; Q6KF21; Q8IXI6; Q8NDR8; Q8TDL9; Q8TDM1; Q8WY55; Q9BVF0;
AC Q9H957; Q9H9Y9; Q9NXP4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=BCAS3 microtubule associated cell migration factor {ECO:0000305};
DE AltName: Full=Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470};
DE AltName: Full=GAOB1;
GN Name=BCAS3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHROMOSOMAL
RP TRANSLOCATION WITH BCAS4, AND VARIANT SER-87.
RC TISSUE=Liver;
RX PubMed=12378525; DOI=10.1002/gcc.10121;
RA Baerlund M., Monni O., Weaver J.D., Kauraniemi P., Sauter G., Heiskanen M.,
RA Kallioniemi O.-P., Kallioniemi A.;
RT "Cloning of BCAS3 (17q23) and BCAS4 (20q13) genes that undergo
RT amplification, overexpression, and fusion in breast cancer.";
RL Genes Chromosomes Cancer 35:311-317(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 478-928 (ISOFORM 3), AND VARIANT SER-87.
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-87.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-87.
RC TISSUE=Brain, and Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-433 (ISOFORM 6), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 5).
RA Bauer M.;
RT "Cloning and sequencing of a new isoform similar to FLJ20128 and BCAS3.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-928 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 510-928 (ISOFORMS 1/6).
RA Wu G., Couch F.J.;
RT "Five novel genes from 17q23 amplicon have different amplification and
RT overexpression frequency in breast cancer.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP DOMAIN.
RX PubMed=16099728; DOI=10.1016/j.modgep.2005.06.002;
RA Siva K., Inamdar M.S.;
RT "Rudhira is a cytoplasmic WD40 protein expressed in mouse embryonic stem
RT cells and during embryonic erythropoiesis.";
RL Gene Expr. Patterns 6:225-234(2006).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [11]
RP ERRATUM OF PUBMED:16617102.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [12]
RP FUNCTION, INTERACTION WITH HISTONE H3; ESR1; KAT2B AND PELP1, SUBCELLULAR
RP LOCATION, AND CHROMATIN-BINDING.
RX PubMed=17505058; DOI=10.1210/me.2006-0514;
RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
RT coactivator, through proline-, glutamic acid-, and leucine-rich protein-1
RT (PELP1).";
RL Mol. Endocrinol. 21:1847-1860(2007).
RN [13]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18030336; DOI=10.1371/journal.pone.0001202;
RA Siva K., Venu P., Mahadevan A., Shankar S.K., Inamdar M.S.;
RT "Human BCAS3 expression in embryonic stem cells and vascular precursors
RT suggests a role in human embryogenesis and tumor angiogenesis.";
RL PLoS ONE 2:E1202-E1202(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP INTERACTION WITH BETA-TUBULIN AND VIM.
RX PubMed=22300583; DOI=10.1016/j.yexcr.2012.01.016;
RA Jain M., Bhat G.P., Vijayra havan K., Inamdar M.S.;
RT "Rudhira/BCAS3 is a cytoskeletal protein that controls Cdc42 activation and
RT directional cell migration during angiogenesis.";
RL Exp. Cell Res. 318:753-767(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP FUNCTION, INTERACTION WITH PHAF1, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP HIS-350; ASP-370; LEU-372; HIS-377; HIS-400; ARG-401; ARG-426; THR-428 AND
RP HIS-430, AND PHOSPHOINOSITIDES-BINDING.
RX PubMed=33499712; DOI=10.1080/15548627.2021.1874133;
RA Kojima W., Yamano K., Kosako H., Imai K., Kikuchi R., Tanaka K.,
RA Matsuda N.;
RT "Mammalian BCAS3 and C16orf70 associate with the phagophore assembly site
RT in response to selective and non-selective autophagy.";
RL Autophagy 1:1-26(2021).
RN [24]
RP VARIANTS HEMARS 25-GLN--PRO-928 DEL; 113-GLN--PRO-928 DEL; 192-CYS--PRO-928
RP DEL; 242-TYR--PRO-928 DEL; 486-SER--PRO-928 DEL; LEU-567; ARG-577 AND
RP 743-GLN--PRO-928 DEL, CHARACTERIZATION OF VARIANTS HEMARS LEU-567 AND
RP ARG-577, AND INVOLVEMENT IN HEMARS.
RX PubMed=34022130; DOI=10.1016/j.ajhg.2021.04.024;
RG Care4Rare Canada Consortium;
RG Genomics England Research Consortium;
RA Hengel H., Hannan S.B., Dyack S., MacKay S.B., Schatz U., Fleger M.,
RA Kurringer A., Balousha G., Ghanim Z., Alkuraya F.S., Alzaidan H.,
RA Alsaif H.S., Mitani T., Bozdogan S., Pehlivan D., Lupski J.R.,
RA Gleeson J.J., Dehghani M., Mehrjardi M.Y.V., Sherr E.H., Parks K.C.,
RA Argilli E., Begtrup A., Galehdari H., Balousha O., Shariati G.,
RA Mazaheri N., Malamiri R.A., Pagnamenta A.T., Kingston H., Banka S.,
RA Jackson A., Osmond M., Riess A., Haack T.B., Naegele T., Schuster S.,
RA Hauser S., Admard J., Casadei N., Velic A., Macek B., Ossowski S.,
RA Houlden H., Maroofian R., Schoels L.;
RT "Bi-allelic loss-of-function variants in BCAS3 cause a syndromic
RT neurodevelopmental disorder.";
RL Am. J. Hum. Genet. 108:1069-1082(2021).
CC -!- FUNCTION: Plays a role in angiogenesis. Participates in the regulation
CC of cell polarity and directional endothelial cell migration by
CC mediating both the activation and recruitment of CDC42 and the
CC reorganization of the actin cytoskeleton at the cell leading edge.
CC Promotes filipodia formation (By similarity). Functions synergistically
CC with PELP1 as a transcriptional coactivator of estrogen receptor-
CC responsive genes. Stimulates histone acetyltransferase activity. Binds
CC to chromatin. Plays a regulatory role in autophagic activity. In
CC complex with PHAF1, associates with the preautophagosomal structure
CC during both non-selective and selective autophagy (PubMed:33499712).
CC Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would
CC mediate the recruitment preautophagosomal structures (PubMed:33499712).
CC {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058,
CC ECO:0000269|PubMed:33499712}.
CC -!- SUBUNIT: Interacts with histone H3, ESR1, KAT2B and PELP1; the
CC interactions occur in a estrogen-dependent manner. Interacts with beta-
CC tubulin and VIM. Interacts (via C-terminal) with PHAF1; the interaction
CC is requrired for the association with the phagophore (PubMed:33499712).
CC {ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:22300583,
CC ECO:0000269|PubMed:33499712}.
CC -!- INTERACTION:
CC Q9H6U6; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-6083685, EBI-396137;
CC Q9H6U6; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-6083685, EBI-10171858;
CC Q9H6U6; P56545-3: CTBP2; NbExp=3; IntAct=EBI-6083685, EBI-10171902;
CC Q9H6U6; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6083685, EBI-742388;
CC Q9H6U6; P08670: VIM; NbExp=3; IntAct=EBI-6083685, EBI-353844;
CC Q9H6U6-2; Q9BSU1: PHAF1; NbExp=3; IntAct=EBI-10307911, EBI-946080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617102,
CC ECO:0000269|PubMed:17505058}. Cytoplasm {ECO:0000269|PubMed:16617102,
CC ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:18030336,
CC ECO:0000269|PubMed:33499712}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8CCN5}. Preautophagosomal structure
CC {ECO:0000269|PubMed:33499712}. Note=Localizes in the cytoplasm in
CC stationary cells. Translocates from the cytoplasm to the leading edge
CC in motile cells. Colocalizes with microtubules and intermediate
CC filaments in both stationary and motile cells (By similarity).
CC Associates with chromatin. Recruited to estrogen receptor-induced
CC promoters in a PELP1-dependent manner. The BCAS3:PHAF1 complex is
CC recruited to the preautophagosomal structures adjacent to the damaged
CC mitochondria upon mitophagy in a PRKN-PINK1 dependent manner
CC (PubMed:33499712). {ECO:0000250|UniProtKB:Q8CCN5,
CC ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:33499712}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=2;
CC IsoId=Q9H6U6-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9H6U6-2; Sequence=VSP_007858;
CC Name=3;
CC IsoId=Q9H6U6-3; Sequence=VSP_007858, VSP_007860;
CC Name=4;
CC IsoId=Q9H6U6-8; Sequence=VSP_007860;
CC Name=5; Synonyms=Maaab1;
CC IsoId=Q9H6U6-7; Sequence=VSP_007858, VSP_040113;
CC Name=6; Synonyms=Maaab2;
CC IsoId=Q9H6U6-6; Sequence=VSP_040112, VSP_007858;
CC -!- TISSUE SPECIFICITY: Expressed in stomach, liver, lung, kidney,
CC prostate, testis, thyroid gland, adrenal gland, brain, heart, skeletal
CC muscle, colon, spleen, small intestine, placenta, blood leukocyte and
CC mammary epithelial cells. Expressed in undifferentiated ES cells.
CC Expressed in blood islands and nascent blood vessels derived from
CC differentiated ES cells into embryoid bodies (BD). Expressed in
CC endothelial cells. Not detected in brain. Expressed in brain tumors (at
CC protein level). Expressed in brain. Highly expressed in breast cancers
CC and in glioma cell lines. {ECO:0000269|PubMed:12378525,
CC ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:18030336}.
CC -!- DEVELOPMENTAL STAGE: Fetal.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:16617102}.
CC -!- DOMAIN: Has been proposed to contain 7 WD repeats. This prediction
CC could not be reproduced. {ECO:0000305|PubMed:16099728}.
CC -!- DISEASE: Note=A chromosomal aberration involving BCAS3 has been found
CC in some breast carcinoma cell lines. Translocation t(17;20)(q23;q13)
CC with BCAS4.
CC -!- DISEASE: Hengel-Maroofian-Schols syndrome (HEMARS) [MIM:619641]: An
CC autosomal recessive disorder characterized by severe global
CC developmental delay apparent from infancy or early childhood. Affected
CC individuals have delayed walking or inability to walk, impaired
CC intellectual development with poor or absent speech, lower limb
CC spasticity, poor overall growth, and dysmorphic facial features. Some
CC patients develop seizures. Brain imaging shows thinning of the
CC posterior part of the corpus callosum, delayed myelination, and
CC cerebral and cerebellar atrophy. {ECO:0000269|PubMed:34022130}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the BCAS3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70324.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL99634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA90966.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14078.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 5]:
CC Sequence=AK225757; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD54076.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCAS3ID766.html";
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DR EMBL; AF361219; AAL99632.1; -; mRNA.
DR EMBL; AF361221; AAL99634.1; ALT_INIT; mRNA.
DR EMBL; AK000135; BAA90966.1; ALT_INIT; mRNA.
DR EMBL; AK022526; BAB14078.1; ALT_INIT; mRNA.
DR EMBL; AK023054; BAB14380.1; -; mRNA.
DR EMBL; AK025510; BAB15156.1; -; mRNA.
DR EMBL; AK225757; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC005746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471179; EAW51414.1; -; Genomic_DNA.
DR EMBL; BC001250; AAH01250.2; -; mRNA.
DR EMBL; BC117275; AAI17276.1; -; mRNA.
DR EMBL; BC143386; AAI43387.1; -; mRNA.
DR EMBL; AJ511332; CAD54076.1; ALT_FRAME; mRNA.
DR EMBL; AJ518105; CAD57723.1; -; mRNA.
DR EMBL; AL831895; CAD38568.1; -; mRNA.
DR EMBL; AF260268; AAF70324.1; ALT_FRAME; mRNA.
DR CCDS; CCDS11626.1; -. [Q9H6U6-2]
DR CCDS; CCDS45749.1; -. [Q9H6U6-1]
DR CCDS; CCDS82176.1; -. [Q9H6U6-8]
DR CCDS; CCDS82177.1; -. [Q9H6U6-7]
DR CCDS; CCDS82178.1; -. [Q9H6U6-3]
DR RefSeq; NP_001092902.1; NM_001099432.1. [Q9H6U6-1]
DR RefSeq; NP_001307399.1; NM_001320470.1. [Q9H6U6-7]
DR RefSeq; NP_060149.3; NM_017679.3. [Q9H6U6-2]
DR AlphaFoldDB; Q9H6U6; -.
DR BioGRID; 120182; 66.
DR IntAct; Q9H6U6; 37.
DR MINT; Q9H6U6; -.
DR STRING; 9606.ENSP00000375067; -.
DR iPTMnet; Q9H6U6; -.
DR MetOSite; Q9H6U6; -.
DR PhosphoSitePlus; Q9H6U6; -.
DR BioMuta; BCAS3; -.
DR DMDM; 313104248; -.
DR EPD; Q9H6U6; -.
DR jPOST; Q9H6U6; -.
DR MassIVE; Q9H6U6; -.
DR MaxQB; Q9H6U6; -.
DR PaxDb; Q9H6U6; -.
DR PeptideAtlas; Q9H6U6; -.
DR PRIDE; Q9H6U6; -.
DR ProteomicsDB; 81034; -. [Q9H6U6-1]
DR ProteomicsDB; 81035; -. [Q9H6U6-2]
DR ProteomicsDB; 81036; -. [Q9H6U6-3]
DR ProteomicsDB; 81037; -. [Q9H6U6-6]
DR ProteomicsDB; 81038; -. [Q9H6U6-7]
DR ProteomicsDB; 81039; -. [Q9H6U6-8]
DR Antibodypedia; 9303; 231 antibodies from 36 providers.
DR DNASU; 54828; -.
DR Ensembl; ENST00000390652.9; ENSP00000375067.4; ENSG00000141376.23. [Q9H6U6-1]
DR Ensembl; ENST00000407086.8; ENSP00000385323.2; ENSG00000141376.23. [Q9H6U6-2]
DR Ensembl; ENST00000408905.7; ENSP00000386173.2; ENSG00000141376.23. [Q9H6U6-3]
DR Ensembl; ENST00000588462.5; ENSP00000468592.1; ENSG00000141376.23. [Q9H6U6-8]
DR Ensembl; ENST00000588874.5; ENSP00000464825.1; ENSG00000141376.23. [Q9H6U6-6]
DR Ensembl; ENST00000589222.5; ENSP00000466078.1; ENSG00000141376.23. [Q9H6U6-7]
DR GeneID; 54828; -.
DR KEGG; hsa:54828; -.
DR MANE-Select; ENST00000407086.8; ENSP00000385323.2; NM_017679.5; NP_060149.3. [Q9H6U6-2]
DR UCSC; uc002iyu.5; human. [Q9H6U6-1]
DR CTD; 54828; -.
DR DisGeNET; 54828; -.
DR GeneCards; BCAS3; -.
DR HGNC; HGNC:14347; BCAS3.
DR HPA; ENSG00000141376; Low tissue specificity.
DR MIM; 607470; gene.
DR MIM; 619641; phenotype.
DR neXtProt; NX_Q9H6U6; -.
DR OpenTargets; ENSG00000141376; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA25286; -.
DR VEuPathDB; HostDB:ENSG00000141376; -.
DR eggNOG; KOG2109; Eukaryota.
DR eggNOG; KOG4415; Eukaryota.
DR GeneTree; ENSGT00390000006454; -.
DR InParanoid; Q9H6U6; -.
DR OMA; FHEIHGT; -.
DR OrthoDB; 537714at2759; -.
DR PhylomeDB; Q9H6U6; -.
DR TreeFam; TF105856; -.
DR PathwayCommons; Q9H6U6; -.
DR SignaLink; Q9H6U6; -.
DR BioGRID-ORCS; 54828; 37 hits in 1089 CRISPR screens.
DR ChiTaRS; BCAS3; human.
DR GeneWiki; BCAS3; -.
DR GenomeRNAi; 54828; -.
DR Pharos; Q9H6U6; Tbio.
DR PRO; PR:Q9H6U6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H6U6; protein.
DR Bgee; ENSG00000141376; Expressed in colonic epithelium and 141 other tissues.
DR ExpressionAtlas; Q9H6U6; baseline and differential.
DR Genevisible; Q9H6U6; HS.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022175; BCAS3.
DR InterPro; IPR045142; BCAS3-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13268; PTHR13268; 1.
DR Pfam; PF12490; BCAS3; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Angiogenesis; Chromosomal rearrangement;
KW Cytoplasm; Cytoskeleton; Disease variant; Intellectual disability;
KW Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..928
FT /note="BCAS3 microtubule associated cell migration factor"
FT /id="PRO_0000050883"
FT REPEAT 69..114
FT /note="WD"
FT /evidence="ECO:0000255"
FT REGION 254..312
FT /note="Required for recruitment to preautophagosomal
FT structure in response to mitophagy"
FT /evidence="ECO:0000269|PubMed:33499712"
FT REGION 437..560
FT /note="Required for recruitment to preautophagosomal
FT structure in response to mitophagy"
FT /evidence="ECO:0000269|PubMed:33499712"
FT REGION 472..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 824..825
FT /note="Breakpoint for translocation to form BCAS4-BCAS3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CCN5"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CCN5"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CCN5"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CCN5"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.6"
FT /id="VSP_040112"
FT VAR_SEQ 547..561
FT /note="Missing (in isoform 1, isoform 3, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12378525,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.6"
FT /id="VSP_007858"
FT VAR_SEQ 879
FT /note="T -> TDTALDVAVKTFPPERHVAVKCF (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_007860"
FT VAR_SEQ 880..928
FT /note="ELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP ->
FT DTALDVAVKTFPPERHVAVKCFGKKKGKKKQCQQPSVREQPNSNKACVRDGGRTSARGK
FT HRDSE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040113"
FT VARIANT 25..928
FT /note="Missing (in HEMARS)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086504"
FT VARIANT 87
FT /note="N -> S (in dbSNP:rs2643103)"
FT /evidence="ECO:0000269|PubMed:12378525,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_065093"
FT VARIANT 106
FT /note="I -> V (in dbSNP:rs34712615)"
FT /id="VAR_057583"
FT VARIANT 113..928
FT /note="Missing (in HEMARS)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086505"
FT VARIANT 192..928
FT /note="Missing (in HEMARS)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086506"
FT VARIANT 242..928
FT /note="Missing (in HEMARS)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086507"
FT VARIANT 486..928
FT /note="Missing (in HEMARS)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086508"
FT VARIANT 567
FT /note="P -> L (in HEMARS; no protein detected in patient
FT cells that also carry R-577, suggesting the mutant is
FT unstable)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086509"
FT VARIANT 577
FT /note="G -> R (in HEMARS; no protein detected in patient
FT cells that also carry L-567, suggesting the mutant is
FT unstable)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086510"
FT VARIANT 743..928
FT /note="Missing (in HEMARS)"
FT /evidence="ECO:0000269|PubMed:34022130"
FT /id="VAR_086511"
FT MUTAGEN 350
FT /note="H->A: No effect on recruitment to preautophagosomal
FT structure in response to mitophagy. No effect on
FT interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 370
FT /note="D->A: Decreases recruitment to preautophagosomal
FT structure in response to mitophagy. No effect on
FT interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 372
FT /note="L->A: No effect on recruitment to preautophagosomal
FT structure in response to mitophagy. No effect on
FT interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 377
FT /note="H->A: No effect on recruitment to preautophagosomal
FT structure in response to mitophagy. No effect on
FT interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 400
FT /note="H->A: Decreases recruitment to preautophagosomal
FT structure in response to mitophagy. No effect on
FT interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 401
FT /note="R->A: Almost abolishes recruitment to
FT preautophagosomal structure in response to mitophagy. No
FT effect on interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 426
FT /note="R->A: Decreases recruitment to preautophagosomal
FT structure in response to mitophagy. No effect on
FT interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 428
FT /note="T->A: Almost abolishes recruitment to
FT preautophagosomal structure in response to mitophagy. No
FT effect on interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT MUTAGEN 430
FT /note="H->A: Almost abolishes recruitment to
FT preautophagosomal structure in response to mitophagy. No
FT effect on interaction with PHAF1."
FT /evidence="ECO:0000269|PubMed:33499712"
FT CONFLICT 29
FT /note="E -> K (in Ref. 1; AAL99632)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="R -> K (in Ref. 1; AAL99632)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..200
FT /note="VV -> II (in Ref. 2; BAB15156)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="K -> E (in Ref. 2; BAB14078/BAB14380)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="D -> G (in Ref. 2; BAB15156)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="Q -> R (in Ref. 2; BAB14078)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="S -> P (in Ref. 2; BAB15156)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9H6U6-7:891
FT /note="G -> R (in Ref. 4; CAD54076)"
FT /evidence="ECO:0000305"
SQ 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
