SPF27_MOUSE
ID SPF27_MOUSE Reviewed; 225 AA.
AC Q9D287; Q3TKJ5; Q91YX8; Q9D2U4; Q9DAI0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Pre-mRNA-splicing factor SPF27;
DE AltName: Full=Breast carcinoma-amplified sequence 2 homolog;
DE AltName: Full=DNA amplified in mammary carcinoma 1 protein;
GN Name=Bcas2; Synonyms=Dam1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12406557; DOI=10.1016/s0304-3835(02)00055-1;
RA Lee S., Ha S., Chung M., Kim Y., Choi Y.;
RT "Mouse DAM1 regulates pro-apoptotic activity of BLK in mammary epithelial
RT cells.";
RL Cancer Lett. 188:121-126(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Olfactory bulb, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC spliceosome. Component of the PRP19-CDC5L complex that forms an
CC integral part of the spliceosome and is required for activating pre-
CC mRNA splicing. May have a scaffolding role in the spliceosome assembly
CC as it contacts all other components of the core complex. The PRP19-
CC CDC5L complex may also play a role in the response to DNA damage (DDR).
CC {ECO:0000250|UniProtKB:O75934}.
CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC complexes. Component of the postcatalytic spliceosome P complex.
CC Component of the PRP19-CDC5L splicing complex composed of a core
CC complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2,
CC and at least three less stably associated proteins CTNNBL1, CWC15 and
CC HSPA8. Interacts directly in the complex with PRPF19, CDC5L and PLRG1.
CC {ECO:0000250|UniProtKB:O75934}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75934}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:O75934}.
CC -!- SIMILARITY: Belongs to the SPF27 family. {ECO:0000305}.
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DR EMBL; AY043239; AAK85306.1; -; mRNA.
DR EMBL; AK005825; BAB24258.1; -; mRNA.
DR EMBL; AK018786; BAB31409.1; -; mRNA.
DR EMBL; AK020098; BAB31992.1; -; mRNA.
DR EMBL; AK166967; BAE39150.1; -; mRNA.
DR EMBL; BC037062; AAH37062.1; -; mRNA.
DR CCDS; CCDS17691.1; -.
DR RefSeq; NP_080878.2; NM_026602.3.
DR AlphaFoldDB; Q9D287; -.
DR SMR; Q9D287; -.
DR BioGRID; 212708; 58.
DR ComplexPortal; CPX-5825; PRP19-CDC5L complex.
DR IntAct; Q9D287; 35.
DR MINT; Q9D287; -.
DR STRING; 10090.ENSMUSP00000005830; -.
DR PhosphoSitePlus; Q9D287; -.
DR EPD; Q9D287; -.
DR MaxQB; Q9D287; -.
DR PaxDb; Q9D287; -.
DR PeptideAtlas; Q9D287; -.
DR PRIDE; Q9D287; -.
DR ProteomicsDB; 257309; -.
DR Antibodypedia; 33860; 350 antibodies from 33 providers.
DR DNASU; 68183; -.
DR Ensembl; ENSMUST00000005830; ENSMUSP00000005830; ENSMUSG00000005687.
DR GeneID; 68183; -.
DR KEGG; mmu:68183; -.
DR UCSC; uc008qsu.1; mouse.
DR CTD; 10286; -.
DR MGI; MGI:1915433; Bcas2.
DR VEuPathDB; HostDB:ENSMUSG00000005687; -.
DR eggNOG; KOG3096; Eukaryota.
DR GeneTree; ENSGT00390000014494; -.
DR HOGENOM; CLU_082523_2_1_1; -.
DR InParanoid; Q9D287; -.
DR OMA; SHLSMRH; -.
DR OrthoDB; 1607056at2759; -.
DR PhylomeDB; Q9D287; -.
DR TreeFam; TF105818; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 68183; 18 hits in 71 CRISPR screens.
DR ChiTaRS; Bcas2; mouse.
DR PRO; PR:Q9D287; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D287; protein.
DR Bgee; ENSMUSG00000005687; Expressed in pharyngeal arch 2 and 255 other tissues.
DR ExpressionAtlas; Q9D287; baseline and differential.
DR Genevisible; Q9D287; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005662; C:DNA replication factor A complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR InterPro; IPR008409; SPF27.
DR PANTHER; PTHR13296; PTHR13296; 1.
DR Pfam; PF05700; BCAS2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75934"
FT CHAIN 2..225
FT /note="Pre-mRNA-splicing factor SPF27"
FT /id="PRO_0000064862"
FT COILED 138..222
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75934"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75934"
FT CONFLICT 28
FT /note="V -> A (in Ref. 2; BAB24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="C -> W (in Ref. 2; BAB24258)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="V -> G (in Ref. 2; BAB31409)"
FT /evidence="ECO:0000305"
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
