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Pre-mRNA-splicing factor SPF27 (Breast carcinoma-amplified sequence 2) (DNA amplified in mammary carcinoma 1 protein) (Spliceosome-associated protein SPF 27)

 SPF27_HUMAN             Reviewed;         225 AA.
O75934; Q6FGS0;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
18-JUL-2018, entry version 159.
RecName: Full=Pre-mRNA-splicing factor SPF27;
AltName: Full=Breast carcinoma-amplified sequence 2;
AltName: Full=DNA amplified in mammary carcinoma 1 protein;
AltName: Full=Spliceosome-associated protein SPF 27;
Name=BCAS2; Synonyms=DAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
IDENTIFICATION IN THE SPLICEOSOME COMPLEX.
PubMed=9731529; DOI=10.1038/1700;
Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P.,
Sleeman J., Lamond A.I., Mann M.;
"Mass spectrometry and EST-database searching allows characterization
of the multi-protein spliceosome complex.";
Nat. Genet. 20:46-50(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=10403562; DOI=10.1016/S0304-3835(99)00091-9;
Nagasaki K., Maass N., Manabe T., Hanzawa H., Tsukada T., Kikuchi K.,
Yamaguchi K.;
"Identification of a novel gene, DAM1, amplified at chromosome 1p13.3-
21 region in human breast cancer cell lines.";
Cancer Lett. 140:219-226(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lung;
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).
[7]
PROTEIN SEQUENCE OF 2-42; 77-85; 87-97; 137-151 AND 192-210, CLEAVAGE
OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
SUBCELLULAR LOCATION.
PubMed=12169396; DOI=10.1016/S0304-3835(02)00286-0;
Maass N., Rosel F., Schem C., Hitomi J., Jonat W., Nagasaki K.;
"Amplification of the BCAS2 gene at chromosome 1p13.3-21 in human
primary breast cancer.";
Cancer Lett. 185:219-223(2002).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX,
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INTERACTION WITH CDC5L; PLRG1 AND PRPF19.
PubMed=20176811; DOI=10.1128/MCB.01505-09;
Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
Fischle W., Urlaub H., Luhrmann R.;
"Molecular architecture of the human Prp19/CDC5L complex.";
Mol. Cell. Biol. 30:2105-2119(2010).
[12]
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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, 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).
[15]
FUNCTION.
PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002;
Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D.,
Liu S., Jimenez A.E., Jin J., Zou L.;
"PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and
drives ATR activation via a ubiquitin-mediated circuitry.";
Mol. Cell 53:235-246(2014).
[16]
VARIANT [LARGE SCALE ANALYSIS] SER-139.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Component of the PRP19-CDC5L complex that forms an
integral part of the spliceosome and is required for activating
pre-mRNA splicing. May have a scaffolding role in the spliceosome
assembly as it contacts all other components of the core complex.
The PRP19-CDC5L complex may also play a role in the response to
DNA damage (DDR). {ECO:0000269|PubMed:24332808}.
-!- SUBUNIT: Component of the PRP19-CDC5L splicing complex composed of
a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1
and BCAS2, and at least three less stably associated proteins
CTNNBL1, CWC15 and HSPA8. Interacts directly in the complex with
PRPF19, CDC5L and PLRG1. {ECO:0000269|PubMed:20176811,
ECO:0000269|PubMed:9731529}.
-!- INTERACTION:
Q13155:AIMP2; NbExp=7; IntAct=EBI-1050106, EBI-745226;
Q08379:GOLGA2; NbExp=7; IntAct=EBI-1050106, EBI-618309;
O14964:HGS; NbExp=3; IntAct=EBI-1050106, EBI-740220;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-1050106, EBI-747204;
O76011:KRT34; NbExp=4; IntAct=EBI-1050106, EBI-1047093;
Q6A162:KRT40; NbExp=3; IntAct=EBI-1050106, EBI-10171697;
P25791-3:LMO2; NbExp=4; IntAct=EBI-1050106, EBI-11959475;
P61968:LMO4; NbExp=4; IntAct=EBI-1050106, EBI-2798728;
Q9UMS4:PRPF19; NbExp=2; IntAct=EBI-1050106, EBI-395746;
Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-1050106, EBI-538479;
Q15427:SF3B4; NbExp=2; IntAct=EBI-1050106, EBI-348469;
P15884:TCF4; NbExp=3; IntAct=EBI-1050106, EBI-533224;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12169396, ECO:0000269|PubMed:12429849,
ECO:0000269|PubMed:20176811}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10403562}.
-!- SIMILARITY: Belongs to the SPF27 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF081788; AAC64059.1; -; mRNA.
EMBL; AB020623; BAA34863.1; -; mRNA.
EMBL; CR542037; CAG46834.1; -; mRNA.
EMBL; BT019390; AAV38197.1; -; mRNA.
EMBL; AL390241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005285; AAH05285.1; -; mRNA.
EMBL; BC012623; AAH12623.1; -; mRNA.
EMBL; BC022880; AAH22880.1; -; mRNA.
CCDS; CCDS874.1; -.
RefSeq; NP_005863.1; NM_005872.2.
UniGene; Hs.22960; -.
PDB; 5MQF; EM; 5.90 A; K=1-225.
PDB; 5XJC; EM; 3.60 A; K=1-225.
PDBsum; 5MQF; -.
PDBsum; 5XJC; -.
ProteinModelPortal; O75934; -.
SMR; O75934; -.
BioGrid; 115575; 111.
CORUM; O75934; -.
IntAct; O75934; 76.
MINT; O75934; -.
STRING; 9606.ENSP00000358554; -.
iPTMnet; O75934; -.
PhosphoSitePlus; O75934; -.
BioMuta; BCAS2; -.
SWISS-2DPAGE; O75934; -.
EPD; O75934; -.
MaxQB; O75934; -.
PaxDb; O75934; -.
PeptideAtlas; O75934; -.
PRIDE; O75934; -.
ProteomicsDB; 50297; -.
TopDownProteomics; O75934; -.
DNASU; 10286; -.
Ensembl; ENST00000369541; ENSP00000358554; ENSG00000116752.
GeneID; 10286; -.
KEGG; hsa:10286; -.
UCSC; uc001efa.4; human.
CTD; 10286; -.
DisGeNET; 10286; -.
EuPathDB; HostDB:ENSG00000116752.5; -.
GeneCards; BCAS2; -.
H-InvDB; HIX0077639; -.
HGNC; HGNC:975; BCAS2.
HPA; HPA067881; -.
MIM; 605783; gene.
neXtProt; NX_O75934; -.
OpenTargets; ENSG00000116752; -.
PharmGKB; PA25285; -.
eggNOG; KOG3096; Eukaryota.
eggNOG; ENOG41101IB; LUCA.
GeneTree; ENSGT00390000014494; -.
HOGENOM; HOG000007540; -.
HOVERGEN; HBG050675; -.
InParanoid; O75934; -.
KO; K12861; -.
OMA; LPYIDHG; -.
OrthoDB; EOG091G0NMJ; -.
PhylomeDB; O75934; -.
TreeFam; TF105818; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
ChiTaRS; BCAS2; human.
GeneWiki; BCAS2; -.
GenomeRNAi; 10286; -.
PMAP-CutDB; O75934; -.
PRO; PR:O75934; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116752; -.
CleanEx; HS_BCAS2; -.
ExpressionAtlas; O75934; baseline and differential.
Genevisible; O75934; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
InterPro; IPR008409; SPF27.
PANTHER; PTHR13296; PTHR13296; 1.
Pfam; PF05700; BCAS2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Coiled coil; Complete proteome;
Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Spliceosome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
CHAIN 2 225 Pre-mRNA-splicing factor SPF27.
/FTId=PRO_0000064861.
COILED 138 222 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 139 139 N -> S (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035799.
CONFLICT 24 24 E -> D (in Ref. 3; CAG46834).
{ECO:0000305}.
CONFLICT 89 89 L -> V (in Ref. 3; CAG46834).
{ECO:0000305}.
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


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