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Protein

Pre-mRNA-splicing factor SPF27

Gene

BCAS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

GO - Biological processi

  • mRNA splicing, via spliceosome Source: GO_Central
  • RNA splicing Source: UniProtKB
  • RNA splicing, via transesterification reactions Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor SPF27
Alternative name(s):
Breast carcinoma-amplified sequence 2
DNA amplified in mammary carcinoma 1 protein
Spliceosome-associated protein SPF 27
Gene namesi
Name:BCAS2
Synonyms:DAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:975. BCAS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25285.

Polymorphism and mutation databases

BioMutaiBCAS2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 225224Pre-mRNA-splicing factor SPF27PRO_0000064861Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei94 – 941PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75934.
MaxQBiO75934.
PaxDbiO75934.
PeptideAtlasiO75934.
PRIDEiO75934.
TopDownProteomicsiO75934.

2D gel databases

SWISS-2DPAGEO75934.

PTM databases

iPTMnetiO75934.
PhosphoSiteiO75934.

Miscellaneous databases

PMAP-CutDBO75934.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiO75934.
CleanExiHS_BCAS2.
ExpressionAtlasiO75934. baseline and differential.
GenevisibleiO75934. HS.

Interactioni

Subunit structurei

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 PLRG1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131553EBI-1050106,EBI-745226
GOLGA2Q083793EBI-1050106,EBI-618309
HGSO149643EBI-1050106,EBI-740220
IKZF3Q9UKT93EBI-1050106,EBI-747204
KRT40Q6A1623EBI-1050106,EBI-10171697
PRPF19Q9UMS42EBI-1050106,EBI-395746
PRPF8Q6P2Q92EBI-1050106,EBI-538479
SF3B4Q154272EBI-1050106,EBI-348469
TCF4P158843EBI-1050106,EBI-533224

Protein-protein interaction databases

BioGridi115575. 81 interactions.
IntActiO75934. 29 interactions.
MINTiMINT-3002049.
STRINGi9606.ENSP00000358554.

Structurei

3D structure databases

ProteinModelPortaliO75934.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili138 – 22285Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SPF27 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3096. Eukaryota.
ENOG41101IB. LUCA.
GeneTreeiENSGT00390000014494.
HOGENOMiHOG000007540.
HOVERGENiHBG050675.
InParanoidiO75934.
KOiK12861.
OMAiQNRLPME.
OrthoDBiEOG7RBZ99.
PhylomeDBiO75934.
TreeFamiTF105818.

Family and domain databases

InterProiIPR008409. SPF27.
[Graphical view]
PANTHERiPTHR13296:SF0. PTHR13296:SF0. 1 hit.
PfamiPF05700. BCAS2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTGLVAGE VVVDALPYFD QGYEAPGVRE AAAALVEEET RRYRPTKNYL
60 70 80 90 100
SYLTAPDYSA FETDIMRNEF ERLAARQPIE LLSMKRYELP APSSGQKNDI
110 120 130 140 150
TAWQECVNNS MAQLEHQAVR IENLELMSQH GCNAWKVYNE NLVHMIEHAQ
160 170 180 190 200
KELQKLRKHI QDLNWQRKNM QLTAGSKLRE MESNWVSLVS KNYEIERTIV
210 220
QLENEIYQIK QQHGEANKEN IRQDF
Length:225
Mass (Da):26,131
Last modified:November 1, 1998 - v1
Checksum:i9112718EEFD96890
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241E → D in CAG46834 (Ref. 3) Curated
Sequence conflicti89 – 891L → V in CAG46834 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391N → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035799

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081788 mRNA. Translation: AAC64059.1.
AB020623 mRNA. Translation: BAA34863.1.
CR542037 mRNA. Translation: CAG46834.1.
BT019390 mRNA. Translation: AAV38197.1.
AL390241 Genomic DNA. Translation: CAI13553.1.
BC005285 mRNA. Translation: AAH05285.1.
BC012623 mRNA. Translation: AAH12623.1.
BC022880 mRNA. Translation: AAH22880.1.
CCDSiCCDS874.1.
RefSeqiNP_005863.1. NM_005872.2.
UniGeneiHs.22960.

Genome annotation databases

EnsembliENST00000369541; ENSP00000358554; ENSG00000116752.
GeneIDi10286.
KEGGihsa:10286.
UCSCiuc001efa.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081788 mRNA. Translation: AAC64059.1.
AB020623 mRNA. Translation: BAA34863.1.
CR542037 mRNA. Translation: CAG46834.1.
BT019390 mRNA. Translation: AAV38197.1.
AL390241 Genomic DNA. Translation: CAI13553.1.
BC005285 mRNA. Translation: AAH05285.1.
BC012623 mRNA. Translation: AAH12623.1.
BC022880 mRNA. Translation: AAH22880.1.
CCDSiCCDS874.1.
RefSeqiNP_005863.1. NM_005872.2.
UniGeneiHs.22960.

3D structure databases

ProteinModelPortaliO75934.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115575. 81 interactions.
IntActiO75934. 29 interactions.
MINTiMINT-3002049.
STRINGi9606.ENSP00000358554.

PTM databases

iPTMnetiO75934.
PhosphoSiteiO75934.

Polymorphism and mutation databases

BioMutaiBCAS2.

2D gel databases

SWISS-2DPAGEO75934.

Proteomic databases

EPDiO75934.
MaxQBiO75934.
PaxDbiO75934.
PeptideAtlasiO75934.
PRIDEiO75934.
TopDownProteomicsiO75934.

Protocols and materials databases

DNASUi10286.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369541; ENSP00000358554; ENSG00000116752.
GeneIDi10286.
KEGGihsa:10286.
UCSCiuc001efa.4. human.

Organism-specific databases

CTDi10286.
GeneCardsiBCAS2.
H-InvDBHIX0077639.
HGNCiHGNC:975. BCAS2.
MIMi605783. gene.
neXtProtiNX_O75934.
PharmGKBiPA25285.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3096. Eukaryota.
ENOG41101IB. LUCA.
GeneTreeiENSGT00390000014494.
HOGENOMiHOG000007540.
HOVERGENiHBG050675.
InParanoidiO75934.
KOiK12861.
OMAiQNRLPME.
OrthoDBiEOG7RBZ99.
PhylomeDBiO75934.
TreeFamiTF105818.

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

GeneWikiiBCAS2.
GenomeRNAii10286.
PMAP-CutDBO75934.
PROiO75934.
SOURCEiSearch...

Gene expression databases

BgeeiO75934.
CleanExiHS_BCAS2.
ExpressionAtlasiO75934. baseline and differential.
GenevisibleiO75934. HS.

Family and domain databases

InterProiIPR008409. SPF27.
[Graphical view]
PANTHERiPTHR13296:SF0. PTHR13296:SF0. 1 hit.
PfamiPF05700. BCAS2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex."
    Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.
    Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOME COMPLEX.
  2. "Identification of a novel gene, DAM1, amplified at chromosome 1p13.3-21 region in human breast cancer cell lines."
    Nagasaki K., Maass N., Manabe T., Hanzawa H., Tsukada T., Kikuchi K., Yamaguchi K.
    Cancer Lett. 140:219-226(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Lung.
  7. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-42; 77-85; 87-97; 137-151 AND 192-210, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  8. "Amplification of the BCAS2 gene at chromosome 1p13.3-21 in human primary breast cancer."
    Maass N., Rosel F., Schem C., Hitomi J., Jonat W., Nagasaki K.
    Cancer Lett. 185:219-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH CDC5L; PLRG1 AND PRPF19.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry."
    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.
    Mol. Cell 53:235-246(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-139.

Entry informationi

Entry nameiSPF27_HUMAN
AccessioniPrimary (citable) accession number: O75934
Secondary accession number(s): Q6FGS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.