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P32639 (BRR2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-splicing helicase BRR2

EC=3.6.4.13
Alternative name(s):
Protein Snu246
Gene names
Name:BRR2
Synonyms:RSS1, SNU246
Ordered Locus Names:YER172C
ORF Names:SYGP-ORF66
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length2163 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome. Ref.10 Ref.12 Ref.13 Ref.14

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.10 Ref.13 Ref.14

Subunit structure

Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interaction with PRP8 is important for recruitment to the U4/U6-U5 tri-snRNP complex. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Ref.5 Ref.6 Ref.9 Ref.10 Ref.12 Ref.14

Subcellular location

Nucleus Probable.

Domain

Contains two helicase domains. The N-terminal helicase domain has catalytic activity by itself, contrary to the C-terminal helicase domain that may have a regulatory role and enhance the activity of the first helicase domain. Ref.14

Miscellaneous

Present with 1440 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the helicase family. SKI2 subfamily.

Contains 2 helicase ATP-binding domains.

Contains 1 helicase C-terminal domain.

Contains 2 SEC63 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21632163Pre-mRNA-splicing helicase BRR2
PRO_0000102086

Regions

Domain508 – 692185Helicase ATP-binding 1
Domain718 – 921204Helicase C-terminal
Domain998 – 1308311SEC63 1
Domain1357 – 1533177Helicase ATP-binding 2
Domain1846 – 2160315SEC63 2
Nucleotide binding521 – 5288ATP Potential
Nucleotide binding1370 – 13778ATP Potential
Motif634 – 6374DEIH box
Motif1474 – 14774DDAH box
Compositional bias1570 – 15756Poly-Ala

Amino acid modifications

Modified residue4031Phosphoserine Ref.8 Ref.11

Experimental info

Mutagenesis8581G → R: Reduces spliceosomal pre-mRNA splicing. Ref.12
Mutagenesis9381W → Q: Strongly reduced unwinding of U4/U6 snRNA. Ref.13
Mutagenesis11071R → A: Reduced ATP-dependent RNA helicase activity. Ref.14
Mutagenesis11101R → N: Abolishes unwinding of U4/U6 snRNA. Ref.13

Secondary structure

........................................................................................................................................................................................................................................................................................................ 2163
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32639 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: DFAF7E3B7168D944

FASTA2,163246,185
        10         20         30         40         50         60 
MTEHETKDKA KKIREIYRYD EMSNKVLKVD KRFMNTSQNP QRDAEISQPK SMSGRISAKD 

        70         80         90        100        110        120 
MGQGLCNNIN KGLKENDVAV EKTGKSASLK KIQQHNTILN SSSDFRLHYY PKDPSNVETY 

       130        140        150        160        170        180 
EQILQWVTEV LGNDIPHDLI IGTADIFIRQ LKENEENEDG NIEERKEKIQ HELGINIDSL 

       190        200        210        220        230        240 
KFNELVKLMK NITDYETHPD NSNKQAVAIL ADDEKSDEEE VTEMSNNANV LGGEINDNED 

       250        260        270        280        290        300 
DDEEYDYNDV EVNSKKKNKR ALPNIENDII KLSDSKTSNI ESVPIYSIDE FFLQRKLRSE 

       310        320        330        340        350        360 
LGYKDTSVIQ DLSEKILNDI ETLEHNPVAL EQKLVDLLKF ENISLAEFIL KNRSTIFWGI 

       370        380        390        400        410        420 
RLAKSTENEI PNLIEKMVAK GLNDLVEQYK FRETTHSKRE LDSGDDQPQS SEAKRTKFSN 

       430        440        450        460        470        480 
PAIPPVIDLE KIKFDESSKL MTVTKVSLPE GSFKRVKPQY DEIHIPAPSK PVIDYELKEI 

       490        500        510        520        530        540 
TSLPDWCQEA FPSSETTSLN PIQSKVFHAA FEGDSNMLIC APTGSGKTNI ALLTVLKALS 

       550        560        570        580        590        600 
HHYNPKTKKL NLSAFKIVYI APLKALVQEQ VREFQRRLAF LGIKVAELTG DSRLSRKQID 

       610        620        630        640        650        660 
ETQVLVSTPE KWDITTRNSN NLAIVELVRL LIIDEIHLLH DDRGPVLESI VARTFWASKY 

       670        680        690        700        710        720 
GQEYPRIIGL SATLPNYEDV GRFLRVPKEG LFYFDSSFRP CPLSQQFCGI KERNSLKKLK 

       730        740        750        760        770        780 
AMNDACYEKV LESINEGNQI IVFVHSRKET SRTATWLKNK FAEENITHKL TKNDAGSKQI 

       790        800        810        820        830        840 
LKTEAANVLD PSLRKLIESG IGTHHAGLTR SDRSLSEDLF ADGLLQVLVC TATLAWGVNL 

       850        860        870        880        890        900 
PAHTVIIKGT DVYSPEKGSW EQLSPQDVLQ MLGRAGRPRY DTFGEGIIIT DQSNVQYYLS 

       910        920        930        940        950        960 
VLNQQLPIES QFVSKLVDNL NAEVVAGNIK CRNDAVNWLA YTYLYVRMLA SPMLYKVPDI 

       970        980        990       1000       1010       1020 
SSDGQLKKFR ESLVHSALCI LKEQELVLYD AENDVIEATD LGNIASSFYI NHASMDVYNR 

      1030       1040       1050       1060       1070       1080 
ELDEHTTQID LFRIFSMSEE FKYVSVRYEE KRELKQLLEK APIPIREDID DPLAKVNVLL 

      1090       1100       1110       1120       1130       1140 
QSYFSQLKFE GFALNSDIVF IHQNAGRLLR AMFEICLKRG WGHPTRMLLN LCKSATTKMW 

      1150       1160       1170       1180       1190       1200 
PTNCPLRQFK TCPVEVIKRL EASTVPWGDY LQLETPAEVG RAIRSEKYGK QVYDLLKRFP 

      1210       1220       1230       1240       1250       1260 
KMSVTCNAQP ITRSVMRFNI EIIADWIWDM NVHGSLEPFL LMLEDTDGDS ILYYDVLFIT 

      1270       1280       1290       1300       1310       1320 
PDIVGHEFTL SFTYELKQHN QNNLPPNFFL TLISENWWHS EFEIPVSFNG FKLPKKFPPP 

      1330       1340       1350       1360       1370       1380 
TPLLENISIS TSELGNDDFS EVFEFKTFNK IQSQVFESLY NSNDSVFVGS GKGTGKTAMA 

      1390       1400       1410       1420       1430       1440 
ELALLNHWRQ NKGRAVYINP SGEKIDFLLS DWNKRFSHLA GGKIINKLGN DPSLNLKLLA 

      1450       1460       1470       1480       1490       1500 
KSHVLLATPV QFELLSRRWR QRKNIQSLEL MIYDDAHEIS QGVYGAVYET LISRMIFIAT 

      1510       1520       1530       1540       1550       1560 
QLEKKIRFVC LSNCLANARD FGEWAGMTKS NIYNFSPSER IEPLEINIQS FKDVEHISFN 

      1570       1580       1590       1600       1610       1620 
FSMLQMAFEA SAAAAGNRNS SSVFLPSRKD CMEVASAFMK FSKAIEWDML NVEEEQIVPY 

      1630       1640       1650       1660       1670       1680 
IEKLTDGHLR APLKHGVGIL YKGMASNDER IVKRLYEYGA VSVLLISKDC SAFACKTDEV 

      1690       1700       1710       1720       1730       1740 
IILGTNLYDG AEHKYMPYTI NELLEMVGLA SGNDSMAGKV LILTSHNMKA YYKKFLIEPL 

      1750       1760       1770       1780       1790       1800 
PTESYLQYII HDTLNNEIAN SIIQSKQDCV DWFTYSYFYR RIHVNPSYYG VRDTSPHGIS 

      1810       1820       1830       1840       1850       1860 
VFLSNLVETC LNDLVESSFI EIDDTEAEVT AEVNGGDDEA TEIISTLSNG LIASHYGVSF 

      1870       1880       1890       1900       1910       1920 
FTIQSFVSSL SNTSTLKNML YVLSTAVEFE SVPLRKGDRA LLVKLSKRLP LRFPEHTSSG 

      1930       1940       1950       1960       1970       1980 
SVSFKVFLLL QAYFSRLELP VDFQNDLKDI LEKVVPLINV VVDILSANGY LNATTAMDLA 

      1990       2000       2010       2020       2030       2040 
QMLIQGVWDV DNPLRQIPHF NNKILEKCKE INVETVYDIM ALEDEERDEI LTLTDSQLAQ 

      2050       2060       2070       2080       2090       2100 
VAAFVNNYPN VELTYSLNNS DSLISGVKQK ITIQLTRDVE PENLQVTSEK YPFDKLESWW 

      2110       2120       2130       2140       2150       2160 
LVLGEVSKKE LYAIKKVTLN KETQQYELEF DTPTSGKHNL TIWCVCDSYL DADKELSFEI 


NVK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations."
Noble S.M., Guthrie C.
Genetics 143:67-80(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: DBY473.
[4]"The HeLa 200 kDa U5 snRNP-specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH-box protein family of putative RNA helicases."
Lauber J., Fabrizio P., Teigelkamp S., Lane W.S., Hartmann E., Luehrmann R.
EMBO J. 15:4001-4015(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6.U5] tri-snRNP."
Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R., Fabrizio P.
EMBO J. 18:4535-4548(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CWC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy."
Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B., Stark H., Fabrizio P., Luhrmann R.
Nat. Struct. Mol. Biol. 15:1206-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, ELECTRON MICROSCOPY.
[10]"ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8."
Maeder C., Kutach A.K., Guthrie C.
Nat. Struct. Mol. Biol. 16:42-48(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH PRP8.
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Brr2p-mediated conformational rearrangements in the spliceosome during activation and substrate repositioning."
Hahn D., Kudla G., Tollervey D., Beggs J.D.
Genes Dev. 26:2408-2421(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF GLY-858.
[13]"Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase."
Pena V., Jovin S.M., Fabrizio P., Orlowski J., Bujnicki J.M., Luhrmann R., Wahl M.C.
Mol. Cell 35:454-466(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1839-2163, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TRP-938 AND ARG-1110.
[14]"Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2."
Zhang L., Xu T., Maeder C., Bud L.O., Shanks J., Nix J., Guthrie C., Pleiss J.A., Zhao R.
Nat. Struct. Mol. Biol. 16:731-739(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1851-2163, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-1107, INTERACTION WITH PRP8 AND SNU114.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18922 Genomic DNA. Translation: AAB64699.1.
BK006939 Genomic DNA. Translation: DAA07834.1.
PIRS50675.
RefSeqNP_011099.1. NM_001179062.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HIBX-ray2.00A1851-2163[»]
3IM1X-ray1.65A1839-2163[»]
3IM2X-ray1.99A1839-2163[»]
4BGDX-ray3.10A442-2163[»]
ProteinModelPortalP32639.
SMRP32639. Positions 479-1159, 1343-1723, 1839-2163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36925. 116 interactions.
DIPDIP-850N.
IntActP32639. 67 interactions.
MINTMINT-606933.
STRING4932.YER172C.

Proteomic databases

MaxQBP32639.
PaxDbP32639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER172C; YER172C; YER172C.
GeneID856919.
KEGGsce:YER172C.

Organism-specific databases

CYGDYER172c.
SGDS000000974. BRR2.

Phylogenomic databases

eggNOGCOG1204.
GeneTreeENSGT00640000091272.
HOGENOMHOG000157749.
KOK12854.
OMAMERINEP.
OrthoDBEOG7XDBQ3.

Enzyme and pathway databases

BioCycYEAST:G3O-30332-MONOMER.

Gene expression databases

GenevestigatorP32639.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
3.40.50.300. 3 hits.
InterProIPR000008. C2_dom.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
[Graphical view]
PfamPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 1 hit.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTSM00487. DEXDc. 2 hits.
SM00490. HELICc. 1 hit.
SM00611. SEC63. 2 hits.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 5 hits.
SSF81296. SSF81296. 2 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32639.
NextBio983377.
PROP32639.

Entry information

Entry nameBRR2_YEAST
AccessionPrimary (citable) accession number: P32639
Secondary accession number(s): D3DM80
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references