SPF27_HUMAN
ID SPF27_HUMAN Reviewed; 225 AA.
AC O75934; Q6FGS0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Pre-mRNA-splicing factor SPF27;
DE AltName: Full=Breast carcinoma-amplified sequence 2;
DE AltName: Full=DNA amplified in mammary carcinoma 1 protein;
DE AltName: Full=Spliceosome-associated protein SPF 27;
GN Name=BCAS2; Synonyms=DAM1 {ECO:0000303|PubMed:10403562};
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE SPLICEOSOME COMPLEX.
RX PubMed=9731529; DOI=10.1038/1700;
RA Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P.,
RA Sleeman J., Lamond A.I., Mann M.;
RT "Mass spectrometry and EST-database searching allows characterization of
RT the multi-protein spliceosome complex.";
RL Nat. Genet. 20:46-50(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10403562; DOI=10.1016/s0304-3835(99)00091-9;
RA Nagasaki K., Maass N., Manabe T., Hanzawa H., Tsukada T., Kikuchi K.,
RA Yamaguchi K.;
RT "Identification of a novel gene, DAM1, amplified at chromosome 1p13.3-21
RT region in human breast cancer cell lines.";
RL Cancer Lett. 140:219-226(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [7]
RP PROTEIN SEQUENCE OF 2-42; 77-85; 87-97; 137-151 AND 192-210, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12169396; DOI=10.1016/s0304-3835(02)00286-0;
RA Maass N., Rosel F., Schem C., Hitomi J., Jonat W., Nagasaki K.;
RT "Amplification of the BCAS2 gene at chromosome 1p13.3-21 in human primary
RT breast cancer.";
RL Cancer Lett. 185:219-223(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH CDC5L; PLRG1 AND PRPF19.
RX PubMed=20176811; DOI=10.1128/mcb.01505-09;
RA Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
RA Fischle W., Urlaub H., Luhrmann R.;
RT "Molecular architecture of the human Prp19/CDC5L complex.";
RL Mol. Cell. Biol. 30:2105-2119(2010).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, 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 [15]
RP FUNCTION.
RX PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002;
RA Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S.,
RA Jimenez A.E., Jin J., Zou L.;
RT "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives
RT ATR activation via a ubiquitin-mediated circuitry.";
RL Mol. Cell 53:235-246(2014).
RN [16] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [17] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
RN [18] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29360106; DOI=10.1038/cr.2018.14;
RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT "Structure of the human activated spliceosome in three conformational
RT states.";
RL Cell Res. 28:307-322(2018).
RN [19] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
RN [20] {ECO:0007744|PDB:6QDV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=30705154; DOI=10.1126/science.aaw5569;
RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT "A human postcatalytic spliceosome structure reveals essential roles of
RT metazoan factors for exon ligation.";
RL Science 363:710-714(2019).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] SER-139.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC spliceosome (PubMed:28502770, PubMed:28076346, PubMed:29360106,
CC PubMed:29301961, PubMed:30705154). Component of the PRP19-CDC5L complex
CC that forms an integral part of the spliceosome and is required for
CC activating pre-mRNA splicing. May have a scaffolding role in the
CC spliceosome assembly as it contacts all other components of the core
CC complex. The PRP19-CDC5L complex may also play a role in the response
CC to DNA damage (DDR). {ECO:0000269|PubMed:20176811,
CC ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154}.
CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC complexes (PubMed:9731529, PubMed:28502770, PubMed:28076346,
CC PubMed:29360106, PubMed:29301961). Component of the postcatalytic
CC spliceosome P complex (PubMed:30705154). Component of the PRP19-CDC5L
CC splicing complex composed of a core complex comprising a homotetramer
CC of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably
CC associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly in the
CC complex with PRPF19, CDC5L and PLRG1 (PubMed:20176811).
CC {ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154,
CC ECO:0000269|PubMed:9731529}.
CC -!- INTERACTION:
CC O75934; Q03154: ACY1; NbExp=3; IntAct=EBI-1050106, EBI-742064;
CC O75934; Q13155: AIMP2; NbExp=12; IntAct=EBI-1050106, EBI-745226;
CC O75934; Q8WW14-2: C10orf82; NbExp=3; IntAct=EBI-1050106, EBI-12831628;
CC O75934; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-1050106, EBI-744556;
CC O75934; Q96LX7-5: CCDC17; NbExp=3; IntAct=EBI-1050106, EBI-12165781;
CC O75934; Q99459: CDC5L; NbExp=13; IntAct=EBI-1050106, EBI-374880;
CC O75934; Q16610: ECM1; NbExp=3; IntAct=EBI-1050106, EBI-947964;
CC O75934; Q9NT22: EMILIN3; NbExp=3; IntAct=EBI-1050106, EBI-3197883;
CC O75934; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-1050106, EBI-744099;
CC O75934; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-1050106, EBI-12845222;
CC O75934; P14136: GFAP; NbExp=3; IntAct=EBI-1050106, EBI-744302;
CC O75934; Q08379: GOLGA2; NbExp=9; IntAct=EBI-1050106, EBI-618309;
CC O75934; O14964: HGS; NbExp=4; IntAct=EBI-1050106, EBI-740220;
CC O75934; O75031: HSF2BP; NbExp=3; IntAct=EBI-1050106, EBI-7116203;
CC O75934; P80217-2: IFI35; NbExp=3; IntAct=EBI-1050106, EBI-12823003;
CC O75934; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-1050106, EBI-747204;
CC O75934; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1050106, EBI-1055254;
CC O75934; O14901: KLF11; NbExp=3; IntAct=EBI-1050106, EBI-948266;
CC O75934; P35900: KRT20; NbExp=3; IntAct=EBI-1050106, EBI-742094;
CC O75934; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1050106, EBI-3044087;
CC O75934; Q15323: KRT31; NbExp=3; IntAct=EBI-1050106, EBI-948001;
CC O75934; O76011: KRT34; NbExp=5; IntAct=EBI-1050106, EBI-1047093;
CC O75934; Q92764: KRT35; NbExp=3; IntAct=EBI-1050106, EBI-1058674;
CC O75934; O76013-2: KRT36; NbExp=3; IntAct=EBI-1050106, EBI-11958506;
CC O75934; O76014: KRT37; NbExp=3; IntAct=EBI-1050106, EBI-1045716;
CC O75934; Q6A162: KRT40; NbExp=3; IntAct=EBI-1050106, EBI-10171697;
CC O75934; O95678: KRT75; NbExp=3; IntAct=EBI-1050106, EBI-2949715;
CC O75934; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-1050106, EBI-12805508;
CC O75934; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-1050106, EBI-10261141;
CC O75934; P25800: LMO1; NbExp=3; IntAct=EBI-1050106, EBI-8639312;
CC O75934; P25791-3: LMO2; NbExp=3; IntAct=EBI-1050106, EBI-11959475;
CC O75934; Q8TAP4-4: LMO3; NbExp=5; IntAct=EBI-1050106, EBI-11742507;
CC O75934; P61968: LMO4; NbExp=3; IntAct=EBI-1050106, EBI-2798728;
CC O75934; Q9NX70: MED29; NbExp=3; IntAct=EBI-1050106, EBI-394656;
CC O75934; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-1050106, EBI-2801965;
CC O75934; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-1050106, EBI-5662487;
CC O75934; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1050106, EBI-2811583;
CC O75934; O43482: OIP5; NbExp=3; IntAct=EBI-1050106, EBI-536879;
CC O75934; Q02548: PAX5; NbExp=3; IntAct=EBI-1050106, EBI-296331;
CC O75934; Q9H0N5: PCBD2; NbExp=3; IntAct=EBI-1050106, EBI-634289;
CC O75934; Q99471: PFDN5; NbExp=3; IntAct=EBI-1050106, EBI-357275;
CC O75934; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-1050106, EBI-2876622;
CC O75934; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1050106, EBI-742388;
CC O75934; O43660: PLRG1; NbExp=2; IntAct=EBI-1050106, EBI-1051504;
CC O75934; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-1050106, EBI-12000762;
CC O75934; Q9UMS4: PRPF19; NbExp=7; IntAct=EBI-1050106, EBI-395746;
CC O75934; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-1050106, EBI-538479;
CC O75934; Q15427: SF3B4; NbExp=2; IntAct=EBI-1050106, EBI-348469;
CC O75934; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-1050106, EBI-358489;
CC O75934; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-1050106, EBI-10269322;
CC O75934; P09234: SNRPC; NbExp=3; IntAct=EBI-1050106, EBI-766589;
CC O75934; P15884: TCF4; NbExp=4; IntAct=EBI-1050106, EBI-533224;
CC O75934; Q9BT92: TCHP; NbExp=3; IntAct=EBI-1050106, EBI-740781;
CC O75934; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-1050106, EBI-11952721;
CC O75934; Q99757: TXN2; NbExp=3; IntAct=EBI-1050106, EBI-2932492;
CC O75934; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1050106, EBI-739895;
CC O75934; O95229: ZWINT; NbExp=3; IntAct=EBI-1050106, EBI-1001132;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12169396,
CC ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10403562}.
CC -!- SIMILARITY: Belongs to the SPF27 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF081788; AAC64059.1; -; mRNA.
DR EMBL; AB020623; BAA34863.1; -; mRNA.
DR EMBL; CR542037; CAG46834.1; -; mRNA.
DR EMBL; BT019390; AAV38197.1; -; mRNA.
DR EMBL; AL390241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005285; AAH05285.1; -; mRNA.
DR EMBL; BC012623; AAH12623.1; -; mRNA.
DR EMBL; BC022880; AAH22880.1; -; mRNA.
DR CCDS; CCDS874.1; -.
DR RefSeq; NP_005863.1; NM_005872.2.
DR PDB; 5MQF; EM; 5.90 A; K=1-225.
DR PDB; 5XJC; EM; 3.60 A; K=1-225.
DR PDB; 5YZG; EM; 4.10 A; K=1-225.
DR PDB; 5Z56; EM; 5.10 A; K=1-225.
DR PDB; 5Z57; EM; 6.50 A; K=1-225.
DR PDB; 6FF7; EM; 4.50 A; K=1-225.
DR PDB; 6ICZ; EM; 3.00 A; K=1-225.
DR PDB; 6ID0; EM; 2.90 A; K=1-225.
DR PDB; 6ID1; EM; 2.86 A; K=1-225.
DR PDB; 6QDV; EM; 3.30 A; s=1-225.
DR PDB; 7A5P; EM; 5.00 A; K=1-225.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; O75934; -.
DR SMR; O75934; -.
DR BioGRID; 115575; 257.
DR ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR CORUM; O75934; -.
DR IntAct; O75934; 108.
DR MINT; O75934; -.
DR STRING; 9606.ENSP00000358554; -.
DR GlyGen; O75934; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75934; -.
DR PhosphoSitePlus; O75934; -.
DR BioMuta; BCAS2; -.
DR SWISS-2DPAGE; O75934; -.
DR EPD; O75934; -.
DR jPOST; O75934; -.
DR MassIVE; O75934; -.
DR MaxQB; O75934; -.
DR PaxDb; O75934; -.
DR PeptideAtlas; O75934; -.
DR PRIDE; O75934; -.
DR ProteomicsDB; 50297; -.
DR TopDownProteomics; O75934; -.
DR Antibodypedia; 33860; 350 antibodies from 33 providers.
DR DNASU; 10286; -.
DR Ensembl; ENST00000369541.4; ENSP00000358554.3; ENSG00000116752.6.
DR GeneID; 10286; -.
DR KEGG; hsa:10286; -.
DR MANE-Select; ENST00000369541.4; ENSP00000358554.3; NM_005872.3; NP_005863.1.
DR UCSC; uc001efa.4; human.
DR CTD; 10286; -.
DR DisGeNET; 10286; -.
DR GeneCards; BCAS2; -.
DR HGNC; HGNC:975; BCAS2.
DR HPA; ENSG00000116752; Low tissue specificity.
DR MIM; 605783; gene.
DR neXtProt; NX_O75934; -.
DR OpenTargets; ENSG00000116752; -.
DR PharmGKB; PA25285; -.
DR VEuPathDB; HostDB:ENSG00000116752; -.
DR eggNOG; KOG3096; Eukaryota.
DR GeneTree; ENSGT00390000014494; -.
DR HOGENOM; CLU_082523_2_1_1; -.
DR InParanoid; O75934; -.
DR OMA; SHLSMRH; -.
DR OrthoDB; 1607056at2759; -.
DR PhylomeDB; O75934; -.
DR TreeFam; TF105818; -.
DR PathwayCommons; O75934; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O75934; -.
DR BioGRID-ORCS; 10286; 633 hits in 1084 CRISPR screens.
DR ChiTaRS; BCAS2; human.
DR GeneWiki; BCAS2; -.
DR GenomeRNAi; 10286; -.
DR Pharos; O75934; Tbio.
DR PRO; PR:O75934; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75934; protein.
DR Bgee; ENSG00000116752; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; O75934; baseline and differential.
DR Genevisible; O75934; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; IPI:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR InterPro; IPR008409; SPF27.
DR PANTHER; PTHR13296; PTHR13296; 1.
DR Pfam; PF05700; BCAS2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..225
FT /note="Pre-mRNA-splicing factor SPF27"
FT /id="PRO_0000064861"
FT COILED 138..222
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 139
FT /note="N -> S (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1197668726)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035799"
FT CONFLICT 24
FT /note="E -> D (in Ref. 3; CAG46834)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="L -> V (in Ref. 3; CAG46834)"
FT /evidence="ECO:0000305"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 106..134
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 137..198
FT /evidence="ECO:0007829|PDB:6ID1"
SQ SEQUENCE 225 AA; 26131 MW; 9112718EEFD96890 CRC64;
MAGTGLVAGE VVVDALPYFD QGYEAPGVRE AAAALVEEET RRYRPTKNYL SYLTAPDYSA
FETDIMRNEF ERLAARQPIE LLSMKRYELP APSSGQKNDI TAWQECVNNS MAQLEHQAVR
IENLELMSQH GCNAWKVYNE NLVHMIEHAQ KELQKLRKHI QDLNWQRKNM QLTAGSKLRE
MESNWVSLVS KNYEIERTIV QLENEIYQIK QQHGEANKEN IRQDF
