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Protein

Ribosome biogenesis protein BMS1

Gene

BMS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 838ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • GTPase activity Source: SGD
  • GTP binding Source: SGD
  • U3 snoRNA binding Source: SGD

GO - Biological processi

  • endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • rRNA methylation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34106-MONOMER.
ReactomeiR-SCE-6790901. rRNA modification in the nucleus.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome biogenesis protein BMS1
Gene namesi
Name:BMS1
Ordered Locus Names:YPL217C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL217C.
SGDiS000006138. BMS1.

Subcellular locationi

GO - Cellular componenti

  • 90S preribosome Source: GO_Central
  • cytoplasm Source: SGD
  • nucleolus Source: SGD
  • nucleoplasm Source: Reactome
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11831183Ribosome biogenesis protein BMS1PRO_0000195006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei438 – 4381PhosphoserineCombined sources
Modified residuei478 – 4781PhosphoserineCombined sources
Modified residuei492 – 4921PhosphoserineCombined sources
Modified residuei504 – 5041PhosphothreonineCombined sources
Modified residuei516 – 5161PhosphothreonineCombined sources
Modified residuei518 – 5181PhosphoserineCombined sources
Modified residuei523 – 5231PhosphoserineCombined sources
Modified residuei574 – 5741PhosphoserineCombined sources
Modified residuei578 – 5781PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08965.
PRIDEiQ08965.

PTM databases

iPTMnetiQ08965.

Interactioni

Subunit structurei

Associates with RCL1.

Binary interactionsi

WithEntry#Exp.IntActNotes
RCL1Q080964EBI-3683,EBI-14892

Protein-protein interaction databases

BioGridi35968. 162 interactions.
DIPiDIP-6562N.
IntActiQ08965. 19 interactions.
MINTiMINT-647500.

Structurei

Secondary structure

1
1183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi549 – 5535Combined sources
Helixi560 – 5678Combined sources
Helixi618 – 6247Combined sources
Helixi629 – 6346Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CLQX-ray2.02B547-636[»]
ProteinModelPortaliQ08965.
SMRiQ08965. Positions 71-210, 547-636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 234167Bms1-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074774.
HOGENOMiHOG000166882.
InParanoidiQ08965.
KOiK14569.
OMAiWQGMKTV.
OrthoDBiEOG7G7KZ1.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR012948. AARP2CN.
IPR003959. ATPase_AAA_core.
IPR007034. BMS1_TSR1_C.
IPR030387. G_Bms1/Tsr1_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08142. AARP2CN. 1 hit.
PF04950. RIBIOP_C. 1 hit.
[Graphical view]
SMARTiSM00785. AARP2CN. 1 hit.
SM01362. DUF663. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51714. G_BMS1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQSNKQHRK AKEKNTAKKK LHTQGHNAKA FAVAAPGKMA RTMQRSSDVN
60 70 80 90 100
ERKLHVPMVD RTPEDDPPPF IVAVVGPPGT GKTTLIRSLV RRMTKSTLND
110 120 130 140 150
IQGPITVVSG KHRRLTFLEC PADDLNAMID IAKIADLVLL LIDGNFGFEM
160 170 180 190 200
ETMEFLNIAQ HHGMPRVLGV ATHLDLFKSQ STLRASKKRL KHRFWTEVYQ
210 220 230 240 250
GAKLFYLSGV INGRYPDREI LNLSRFISVM KFRPLKWRNE HPYMLADRFT
260 270 280 290 300
DLTHPELIET QGLQIDRKVA IYGYLHGTPL PSAPGTRVHI AGVGDFSVAQ
310 320 330 340 350
IEKLPDPCPT PFYQQKLDDF EREKMKEEAK ANGEITTAST TRRRKRLDDK
360 370 380 390 400
DKLIYAPMSD VGGVLMDKDA VYIDIGKKNE EPSFVPGQER GEGEKLMTGL
410 420 430 440 450
QSVEQSIAEK FDGVGLQLFS NGTELHEVAD HEGMDVESGE ESIEDDEGKS
460 470 480 490 500
KGRTSLRKPR IYGKPVQEED ADIDNLPSDE EPYTNDDDVQ DSEPRMVEID
510 520 530 540 550
FNNTGEQGAE KLALETDSEF EESEDEFSWE RTAANKLKKT ESKKRTWNIG
560 570 580 590 600
KLIYMDNISP EECIRRWRGE DDDSKDESDI EEDVDDDFFR KKDGTVTKEG
610 620 630 640 650
NKDHAVDLEK FVPYFDTFEK LAKKWKSVDA IKERFLGAGI LGNDNKTKSD
660 670 680 690 700
SNEGGEELYG DFEDLEDGNP SEQAEDNSDK ESEDEDENED TNGDDDNSFT
710 720 730 740 750
NFDAEEKKDL TMEQEREMNA AKKEKLRAQF EIEEGENFKE DDENNEYDTW
760 770 780 790 800
YELQKAKISK QLEINNIEYQ EMTPEQRQRI EGFKAGSYVR IVFEKVPMEF
810 820 830 840 850
VKNFNPKFPI VMGGLLPTEI KFGIVKARLR RHRWHKKILK TNDPLVLSLG
860 870 880 890 900
WRRFQTLPIY TTTDSRTRTR MLKYTPEHTY CNAAFYGPLC SPNTPFCGVQ
910 920 930 940 950
IVANSDTGNG FRIAATGIVE EIDVNIEIVK KLKLVGFPYK IFKNTAFIKD
960 970 980 990 1000
MFSSAMEVAR FEGAQIKTVS GIRGEIKRAL SKPEGHYRAA FEDKILMSDI
1010 1020 1030 1040 1050
VILRSWYPVR VKKFYNPVTS LLLKEKTEWK GLRLTGQIRA AMNLETPSNP
1060 1070 1080 1090 1100
DSAYHKIERV ERHFNGLKVP KAVQKELPFK SQIHQMKPQK KKTYMAKRAV
1110 1120 1130 1140 1150
VLGGDEKKAR SFIQKVLTIS KAKDSKRKEQ KASQRKERLK KLAKMEEEKS
1160 1170 1180
QRDKEKKKEY FAQNGKRTTM GGDDESRPRK MRR
Length:1,183
Mass (Da):135,571
Last modified:November 1, 1996 - v1
Checksum:i9A337F1EE0B0F21D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73573 Genomic DNA. Translation: CAA97932.1.
BK006949 Genomic DNA. Translation: DAA11219.1.
PIRiS65236.
RefSeqiNP_015107.1. NM_001184031.1.

Genome annotation databases

EnsemblFungiiYPL217C; YPL217C; YPL217C.
GeneIDi855884.
KEGGisce:YPL217C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73573 Genomic DNA. Translation: CAA97932.1.
BK006949 Genomic DNA. Translation: DAA11219.1.
PIRiS65236.
RefSeqiNP_015107.1. NM_001184031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CLQX-ray2.02B547-636[»]
ProteinModelPortaliQ08965.
SMRiQ08965. Positions 71-210, 547-636.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35968. 162 interactions.
DIPiDIP-6562N.
IntActiQ08965. 19 interactions.
MINTiMINT-647500.

PTM databases

iPTMnetiQ08965.

Proteomic databases

MaxQBiQ08965.
PRIDEiQ08965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL217C; YPL217C; YPL217C.
GeneIDi855884.
KEGGisce:YPL217C.

Organism-specific databases

EuPathDBiFungiDB:YPL217C.
SGDiS000006138. BMS1.

Phylogenomic databases

GeneTreeiENSGT00550000074774.
HOGENOMiHOG000166882.
InParanoidiQ08965.
KOiK14569.
OMAiWQGMKTV.
OrthoDBiEOG7G7KZ1.

Enzyme and pathway databases

BioCyciYEAST:G3O-34106-MONOMER.
ReactomeiR-SCE-6790901. rRNA modification in the nucleus.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

PROiQ08965.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR012948. AARP2CN.
IPR003959. ATPase_AAA_core.
IPR007034. BMS1_TSR1_C.
IPR030387. G_Bms1/Tsr1_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08142. AARP2CN. 1 hit.
PF04950. RIBIOP_C. 1 hit.
[Graphical view]
SMARTiSM00785. AARP2CN. 1 hit.
SM01362. DUF663. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51714. G_BMS1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast."
    Wegierski T., Billy E., Nasr F., Filipowicz W.
    RNA 7:1254-1267(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RCL1.
  4. "Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast."
    Gelperin D., Horton L., Beckman J., Hensold J., Lemmon S.K.
    RNA 7:1268-1283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-438; SER-478; SER-492; THR-504; THR-516; SER-518; SER-523; SER-574 AND SER-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBMS1_YEAST
AccessioniPrimary (citable) accession number: Q08965
Secondary accession number(s): D6W3F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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.