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P32639

- BRR2_YEAST

UniProt

P32639 - BRR2_YEAST

Protein

Pre-mRNA-splicing helicase BRR2

Gene

BRR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi521 – 5288ATPPROSITE-ProRule annotation
    Nucleotide bindingi1370 – 13778ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent RNA helicase activity Source: SGD
    3. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30332-MONOMER.
    ReactomeiREACT_191540. mRNA Splicing - Minor Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-mRNA-splicing helicase BRR2 (EC:3.6.4.13)
    Alternative name(s):
    Protein Snu246
    Gene namesi
    Name:BRR2
    Synonyms:RSS1, SNU246
    Ordered Locus Names:YER172C
    ORF Names:SYGP-ORF66
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER172c.
    SGDiS000000974. BRR2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. spliceosomal complex Source: UniProtKB-KW
    2. U4/U6 x U5 tri-snRNP complex Source: SGD
    3. U5 snRNP Source: SGD

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi858 – 8581G → R: Reduces spliceosomal pre-mRNA splicing. 1 Publication
    Mutagenesisi938 – 9381W → Q: Strongly reduced unwinding of U4/U6 snRNA. 1 Publication
    Mutagenesisi1107 – 11071R → A: Reduced ATP-dependent RNA helicase activity. 1 Publication
    Mutagenesisi1110 – 11101R → N: Abolishes unwinding of U4/U6 snRNA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21632163Pre-mRNA-splicing helicase BRR2PRO_0000102086Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei403 – 4031Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32639.
    PaxDbiP32639.

    Expressioni

    Gene expression databases

    GenevestigatoriP32639.

    Interactioni

    Subunit structurei

    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 YJU2.6 Publications

    Protein-protein interaction databases

    BioGridi36925. 116 interactions.
    DIPiDIP-850N.
    IntActiP32639. 67 interactions.
    MINTiMINT-606933.
    STRINGi4932.YER172C.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi453 – 4564
    Beta strandi458 – 4658
    Helixi480 – 4823
    Helixi487 – 4904
    Beta strandi495 – 4984
    Helixi501 – 51111
    Beta strandi517 – 5215
    Beta strandi523 – 5253
    Helixi527 – 54014
    Beta strandi556 – 5605
    Helixi564 – 57815
    Turni579 – 5824
    Beta strandi585 – 5873
    Helixi594 – 5963
    Turni597 – 6015
    Beta strandi603 – 6075
    Helixi609 – 6179
    Turni619 – 6213
    Helixi622 – 6254
    Beta strandi628 – 6336
    Helixi636 – 6405
    Turni642 – 6443
    Helixi645 – 65612
    Helixi659 – 6613
    Beta strandi666 – 6738
    Helixi677 – 6837
    Helixi688 – 6903
    Beta strandi691 – 6933
    Helixi696 – 6983
    Beta strandi699 – 7013
    Beta strandi703 – 7108
    Helixi715 – 73521
    Beta strandi740 – 7434
    Helixi747 – 76418
    Helixi767 – 7704
    Turni774 – 7774
    Helixi778 – 78710
    Helixi793 – 7986
    Beta strandi801 – 8044
    Beta strandi806 – 8083
    Helixi810 – 82112
    Beta strandi826 – 8305
    Helixi833 – 8375
    Beta strandi842 – 8487
    Beta strandi851 – 8544
    Turni855 – 8584
    Beta strandi859 – 8624
    Helixi865 – 8717
    Beta strandi874 – 8763
    Turni878 – 8803
    Beta strandi884 – 8918
    Helixi892 – 90211
    Turni912 – 9154
    Helixi916 – 92510
    Helixi932 – 9387
    Helixi939 – 9413
    Helixi943 – 9508
    Turni952 – 9565
    Helixi960 – 9634
    Turni964 – 9663
    Helixi967 – 98317
    Beta strandi986 – 9905
    Turni991 – 9944
    Beta strandi995 – 9984
    Helixi1000 – 10078
    Helixi1012 – 102110
    Helixi1028 – 10369
    Helixi1039 – 10413
    Turni1048 – 10503
    Helixi1051 – 10599
    Beta strandi1069 – 10713
    Helixi1072 – 108514
    Helixi1092 – 111928
    Helixi1122 – 113615
    Beta strandi1141 – 11433
    Helixi1145 – 11473
    Helixi1154 – 11629
    Helixi1167 – 11726
    Helixi1176 – 11838
    Helixi1186 – 119712
    Beta strandi1202 – 122423
    Helixi1230 – 12334
    Beta strandi1237 – 12448
    Beta strandi1250 – 125910
    Turni1261 – 12655
    Beta strandi1266 – 127510
    Helixi1278 – 12825
    Beta strandi1286 – 129712
    Beta strandi1301 – 13077
    Helixi1331 – 13333
    Helixi1337 – 13437
    Helixi1350 – 136011
    Beta strandi1366 – 13694
    Helixi1376 – 138813
    Turni1389 – 13913
    Beta strandi1395 – 13984
    Helixi1402 – 141615
    Turni1417 – 14215
    Beta strandi1424 – 14263
    Helixi1432 – 144110
    Beta strandi1443 – 14475
    Helixi1449 – 14568
    Turni1457 – 14615
    Helixi1463 – 14664
    Beta strandi1470 – 14734
    Helixi1476 – 14805
    Helixi1483 – 150220
    Beta strandi1507 – 15137
    Helixi1518 – 15247
    Helixi1529 – 15313
    Beta strandi1532 – 15343
    Helixi1537 – 15393
    Beta strandi1544 – 15496
    Helixi1561 – 157616
    Beta strandi1581 – 15877
    Helixi1588 – 160316
    Turni1614 – 16163
    Helixi1617 – 16215
    Helixi1627 – 16293
    Helixi1630 – 16334
    Turni1634 – 16363
    Beta strandi1637 – 16404
    Helixi1646 – 165813
    Beta strandi1663 – 16675
    Helixi1669 – 16724
    Beta strandi1677 – 16837
    Beta strandi1686 – 16894
    Turni1690 – 16934
    Beta strandi1694 – 16974
    Helixi1700 – 17078
    Beta strandi1718 – 17236
    Helixi1726 – 173510
    Helixi1746 – 17494
    Helixi1750 – 175910
    Helixi1767 – 17748
    Helixi1777 – 17848
    Helixi1786 – 17894
    Helixi1796 – 181621
    Beta strandi1819 – 18235
    Beta strandi1843 – 18464
    Beta strandi1847 – 18493
    Helixi1860 – 186910
    Helixi1876 – 18849
    Helixi1887 – 18915
    Helixi1898 – 19069
    Beta strandi1909 – 19113
    Beta strandi1919 – 19213
    Helixi1922 – 193514
    Helixi1941 – 196727
    Helixi1973 – 198513
    Beta strandi1989 – 19913
    Helixi1993 – 19964
    Helixi2002 – 20109
    Helixi2016 – 20216
    Helixi2024 – 20307
    Helixi2035 – 204713
    Beta strandi2051 – 20577
    Helixi2060 – 20623
    Beta strandi2067 – 207913
    Beta strandi2099 – 21057
    Helixi2106 – 21083
    Beta strandi2110 – 21178
    Beta strandi2121 – 213111
    Beta strandi2135 – 214814
    Beta strandi2154 – 216310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HIBX-ray2.00A1851-2163[»]
    3IM1X-ray1.65A1839-2163[»]
    3IM2X-ray1.99A1839-2163[»]
    4BGDX-ray3.10A442-2163[»]
    ProteinModelPortaliP32639.
    SMRiP32639. Positions 479-1159, 1343-1723, 1839-2163.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32639.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini508 – 692185Helicase ATP-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini718 – 921204Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini998 – 1308311SEC63 1Add
    BLAST
    Domaini1357 – 1533177Helicase ATP-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1846 – 2160315SEC63 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi634 – 6374DEIH box
    Motifi1474 – 14774DDAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1570 – 15756Poly-Ala

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Belongs to the helicase family. SKI2 subfamily.Curated
    Contains 2 helicase ATP-binding domains.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 2 SEC63 domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1204.
    GeneTreeiENSGT00640000091272.
    HOGENOMiHOG000157749.
    KOiK12854.
    OMAiMERINEP.
    OrthoDBiEOG7XDBQ3.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    3.40.50.300. 3 hits.
    InterProiIPR000008. 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]
    PfamiPF00270. DEAD. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF02889. Sec63. 2 hits.
    [Graphical view]
    SMARTiSM00487. DEXDc. 2 hits.
    SM00490. HELICc. 1 hit.
    SM00611. SEC63. 2 hits.
    SM00973. Sec63. 2 hits.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 5 hits.
    SSF81296. SSF81296. 2 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32639-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEHETKDKA KKIREIYRYD EMSNKVLKVD KRFMNTSQNP QRDAEISQPK     50
    SMSGRISAKD MGQGLCNNIN KGLKENDVAV EKTGKSASLK KIQQHNTILN 100
    SSSDFRLHYY PKDPSNVETY EQILQWVTEV LGNDIPHDLI IGTADIFIRQ 150
    LKENEENEDG NIEERKEKIQ HELGINIDSL KFNELVKLMK NITDYETHPD 200
    NSNKQAVAIL ADDEKSDEEE VTEMSNNANV LGGEINDNED DDEEYDYNDV 250
    EVNSKKKNKR ALPNIENDII KLSDSKTSNI ESVPIYSIDE FFLQRKLRSE 300
    LGYKDTSVIQ DLSEKILNDI ETLEHNPVAL EQKLVDLLKF ENISLAEFIL 350
    KNRSTIFWGI RLAKSTENEI PNLIEKMVAK GLNDLVEQYK FRETTHSKRE 400
    LDSGDDQPQS SEAKRTKFSN PAIPPVIDLE KIKFDESSKL MTVTKVSLPE 450
    GSFKRVKPQY DEIHIPAPSK PVIDYELKEI TSLPDWCQEA FPSSETTSLN 500
    PIQSKVFHAA FEGDSNMLIC APTGSGKTNI ALLTVLKALS HHYNPKTKKL 550
    NLSAFKIVYI APLKALVQEQ VREFQRRLAF LGIKVAELTG DSRLSRKQID 600
    ETQVLVSTPE KWDITTRNSN NLAIVELVRL LIIDEIHLLH DDRGPVLESI 650
    VARTFWASKY GQEYPRIIGL SATLPNYEDV GRFLRVPKEG LFYFDSSFRP 700
    CPLSQQFCGI KERNSLKKLK AMNDACYEKV LESINEGNQI IVFVHSRKET 750
    SRTATWLKNK FAEENITHKL TKNDAGSKQI LKTEAANVLD PSLRKLIESG 800
    IGTHHAGLTR SDRSLSEDLF ADGLLQVLVC TATLAWGVNL PAHTVIIKGT 850
    DVYSPEKGSW EQLSPQDVLQ MLGRAGRPRY DTFGEGIIIT DQSNVQYYLS 900
    VLNQQLPIES QFVSKLVDNL NAEVVAGNIK CRNDAVNWLA YTYLYVRMLA 950
    SPMLYKVPDI SSDGQLKKFR ESLVHSALCI LKEQELVLYD AENDVIEATD 1000
    LGNIASSFYI NHASMDVYNR ELDEHTTQID LFRIFSMSEE FKYVSVRYEE 1050
    KRELKQLLEK APIPIREDID DPLAKVNVLL QSYFSQLKFE GFALNSDIVF 1100
    IHQNAGRLLR AMFEICLKRG WGHPTRMLLN LCKSATTKMW PTNCPLRQFK 1150
    TCPVEVIKRL EASTVPWGDY LQLETPAEVG RAIRSEKYGK QVYDLLKRFP 1200
    KMSVTCNAQP ITRSVMRFNI EIIADWIWDM NVHGSLEPFL LMLEDTDGDS 1250
    ILYYDVLFIT PDIVGHEFTL SFTYELKQHN QNNLPPNFFL TLISENWWHS 1300
    EFEIPVSFNG FKLPKKFPPP TPLLENISIS TSELGNDDFS EVFEFKTFNK 1350
    IQSQVFESLY NSNDSVFVGS GKGTGKTAMA ELALLNHWRQ NKGRAVYINP 1400
    SGEKIDFLLS DWNKRFSHLA GGKIINKLGN DPSLNLKLLA KSHVLLATPV 1450
    QFELLSRRWR QRKNIQSLEL MIYDDAHEIS QGVYGAVYET LISRMIFIAT 1500
    QLEKKIRFVC LSNCLANARD FGEWAGMTKS NIYNFSPSER IEPLEINIQS 1550
    FKDVEHISFN FSMLQMAFEA SAAAAGNRNS SSVFLPSRKD CMEVASAFMK 1600
    FSKAIEWDML NVEEEQIVPY IEKLTDGHLR APLKHGVGIL YKGMASNDER 1650
    IVKRLYEYGA VSVLLISKDC SAFACKTDEV IILGTNLYDG AEHKYMPYTI 1700
    NELLEMVGLA SGNDSMAGKV LILTSHNMKA YYKKFLIEPL PTESYLQYII 1750
    HDTLNNEIAN SIIQSKQDCV DWFTYSYFYR RIHVNPSYYG VRDTSPHGIS 1800
    VFLSNLVETC LNDLVESSFI EIDDTEAEVT AEVNGGDDEA TEIISTLSNG 1850
    LIASHYGVSF FTIQSFVSSL SNTSTLKNML YVLSTAVEFE SVPLRKGDRA 1900
    LLVKLSKRLP LRFPEHTSSG SVSFKVFLLL QAYFSRLELP VDFQNDLKDI 1950
    LEKVVPLINV VVDILSANGY LNATTAMDLA QMLIQGVWDV DNPLRQIPHF 2000
    NNKILEKCKE INVETVYDIM ALEDEERDEI LTLTDSQLAQ VAAFVNNYPN 2050
    VELTYSLNNS DSLISGVKQK ITIQLTRDVE PENLQVTSEK YPFDKLESWW 2100
    LVLGEVSKKE LYAIKKVTLN KETQQYELEF DTPTSGKHNL TIWCVCDSYL 2150
    DADKELSFEI NVK 2163
    Length:2,163
    Mass (Da):246,185
    Last modified:February 1, 1995 - v2
    Checksum:iDFAF7E3B7168D944
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18922 Genomic DNA. Translation: AAB64699.1.
    BK006939 Genomic DNA. Translation: DAA07834.1.
    PIRiS50675.
    RefSeqiNP_011099.1. NM_001179062.1.

    Genome annotation databases

    EnsemblFungiiYER172C; YER172C; YER172C.
    GeneIDi856919.
    KEGGisce:YER172C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18922 Genomic DNA. Translation: AAB64699.1 .
    BK006939 Genomic DNA. Translation: DAA07834.1 .
    PIRi S50675.
    RefSeqi NP_011099.1. NM_001179062.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HIB X-ray 2.00 A 1851-2163 [» ]
    3IM1 X-ray 1.65 A 1839-2163 [» ]
    3IM2 X-ray 1.99 A 1839-2163 [» ]
    4BGD X-ray 3.10 A 442-2163 [» ]
    ProteinModelPortali P32639.
    SMRi P32639. Positions 479-1159, 1343-1723, 1839-2163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36925. 116 interactions.
    DIPi DIP-850N.
    IntActi P32639. 67 interactions.
    MINTi MINT-606933.
    STRINGi 4932.YER172C.

    Proteomic databases

    MaxQBi P32639.
    PaxDbi P32639.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER172C ; YER172C ; YER172C .
    GeneIDi 856919.
    KEGGi sce:YER172C.

    Organism-specific databases

    CYGDi YER172c.
    SGDi S000000974. BRR2.

    Phylogenomic databases

    eggNOGi COG1204.
    GeneTreei ENSGT00640000091272.
    HOGENOMi HOG000157749.
    KOi K12854.
    OMAi MERINEP.
    OrthoDBi EOG7XDBQ3.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30332-MONOMER.
    Reactomei REACT_191540. mRNA Splicing - Minor Pathway.

    Miscellaneous databases

    EvolutionaryTracei P32639.
    NextBioi 983377.
    PROi P32639.

    Gene expression databases

    Genevestigatori P32639.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    3.40.50.300. 3 hits.
    InterProi IPR000008. 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 ]
    Pfami PF00270. DEAD. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF02889. Sec63. 2 hits.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 2 hits.
    SM00490. HELICc. 1 hit.
    SM00611. SEC63. 2 hits.
    SM00973. Sec63. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 5 hits.
    SSF81296. SSF81296. 2 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 2 hits.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. 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. 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.

    Entry informationi

    Entry nameiBRR2_YEAST
    AccessioniPrimary (citable) accession number: P32639
    Secondary accession number(s): D3DM80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1440 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3