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P32639

- BRR2_YEAST

UniProt

P32639 - BRR2_YEAST

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Protein
Pre-mRNA-splicing helicase BRR2
Gene
BRR2, RSS1, SNU246, YER172C, SYGP-ORF66
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 5288ATP Reviewed prediction
Nucleotide bindingi1370 – 13778ATP Reviewed prediction

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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

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

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 BRR2
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP32639.

Family & Domainsi

Domains and Repeats

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

Contains 2 SEC63 domains.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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.

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

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