Skip Header

Contribute Send feedback
Read comments (?) or add your own

O54825 (BYST_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Bystin
Gene names
Name:Bysl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. Ref.4 Ref.5

Subunit structure

Binds trophinin, tastin and cytokeratins By similarity.

Subcellular location

Cytoplasm. Nucleusnucleolus. Note: Associated with 40S ribosomal subunits. Ref.5

Tissue specificity

High levels in preimplantation embryos, bone marrow, brain, testis and ovary. Ref.5

Developmental stage

High levels of maternal transcript in unfertilized eggs. High levels up to blastocyst stage. Ref.5

Disruption phenotype

Mice show embryonic lethality around stage E6.5 shortly after implantation. Mice lacking maternal Bysl transcript upon injection of siRNA into fertilized eggs are arrested at the 16-cell stage, fail to induce trophectoderm, and show altered morphology of developing nucleoli. Embryonic stem cells lacking Bysl show accumulation of pre-20S rRNA precursors and a reduction of 40S ribosomal subunits in the cytoplasm. Ref.4

Sequence similarities

Belongs to the bystin family.

Sequence caution

The sequence AAH17530.3 differs from that shown. Reason: Erroneous initiation.

The sequence BAB31619.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAC38736.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Bystin
PRO_0000186115

Amino acid modifications

Modified residue971Phosphoserine Ref.6 Ref.7 Ref.8
Modified residue1661Phosphoserine By similarity

Experimental info

Sequence conflict2841A → V in BAE40242. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54825 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: EFA148BED2072B72

FASTA43649,784
        10         20         30         40         50         60 
MPKFKVTRGA SNREKHAPLA EQILAGNAVR AGTREKRRGR EVEEEEEYVG PRLSRRILQQ 

        70         80         90        100        110        120 
ARQQQEELET DHGAGDRSAP PRERATRLGP GLPQDGSDEE DEEWPTLEKA AKMAGVDHQA 

       130        140        150        160        170        180 
EVIVDPEDER AIEMFMNKNP PVRRTLADII MEKLTEKQTE VETVMSEVSG FPMPQLDPRV 

       190        200        210        220        230        240 
LEVYRGVREV LCKYRSGKLP KAFKVIPALS NWEQILYVTE PEAWTAAAMY QATRIFASNL 

       250        260        270        280        290        300 
KERMAQRFYN LVLLPRVRDD IAEYKRLNFH LYMALKKALF KPGAWFKGIL IPLCESGTCT 

       310        320        330        340        350        360 
LREAIIVGSI ITKCSIPVLH SSAAMLKIAE MEYSGANSIF LRLLLDKKYA LPYRVLDALV 

       370        380        390        400        410        420 
FHFLAFRTEK RQLPVLWHQC LLTLAQRYKA DLATEQKEAL LELLRLQPHP QLSPEIRREL 

       430 
QSAVPRDVED GGVTME 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c and C57BL/6J.
Tissue: Embryo, Embryonic spinal cord and Lung.
[2]"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: Salivary gland.
[3]"Characterization of mouse bystin."
Suzuki N., Fukuda M.N.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 151-436.
[4]"The Bysl gene product, bystin, is essential for survival of mouse embryos."
Aoki R., Suzuki N., Paria B.C., Sugihara K., Akama T.O., Raab G., Miyoshi M., Nadano D., Fukuda M.N.
FEBS Lett. 580:6062-6068(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Crucial role of Bysl in mammalian preimplantation development as an integral factor for 40S ribosome biogenesis."
Adachi K., Soeta-Saneyoshi C., Sagara H., Iwakura Y.
Mol. Cell. Biol. 27:2202-2214(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, MASS SPECTROMETRY.
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, MASS SPECTROMETRY.
Tissue: Macrophage.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK019239 mRNA. Translation: BAB31619.2. Different initiation.
AK083033 mRNA. Translation: BAC38736.1. Different initiation.
AK143027 mRNA. Translation: BAE25255.1.
AK168301 mRNA. Translation: BAE40242.1.
BC017530 mRNA. Translation: AAH17530.3. Different initiation.
AF007802 mRNA. Translation: AAB94491.1.
IPIIPI00118762.
RefSeqNP_058555.3. NM_016859.3.
UniGeneMm.472101.

3D structure databases

ProteinModelPortalO54825.
ModBaseSearch...

Protein-protein interaction databases

IntActO54825. 1 interaction.

PTM databases

PhosphoSiteO54825.

Proteomic databases

PaxDbO54825.
PRIDEO54825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024783; ENSMUSP00000024783; ENSMUSG00000023988.
GeneID53414.
KEGGmmu:53414.
UCSCuc008cvq.2. mouse.

Organism-specific databases

CTD705.
MGIMGI:1858419. Bysl.

Phylogenomic databases

eggNOGNOG280148.
GeneTreeENSGT00390000007241.
HOGENOMHOG000178028.
HOVERGENHBG024425.
InParanoidO54825.
KOK14797.
OMALNFHLYQ.
OrthoDBEOG4VHK6H.

Gene expression databases

ArrayExpressO54825.
BgeeO54825.
CleanExMM_BYSL.
GenevestigatorO54825.
GermOnlineENSMUSG00000023988. Mus musculus.

Family and domain databases

InterProIPR007955. Bystin.
[Graphical view]
PANTHERPTHR12821. PTHR12821. 1 hit.
PfamPF05291. Bystin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBYSL. mouse.
NextBio310229.
SOURCESearch...

Entry information

Entry nameBYST_MOUSE
AccessionPrimary (citable) accession number: O54825
Secondary accession number(s): Q3THF4, Q3UPY9, Q8VD68
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2006
Last modified: April 3, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families