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Q13895 (BYST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bystin
Gene names
Name:BYSL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 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. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos. Ref.5 Ref.6

Subunit structure

Binds trophinin, tastin and cytokeratins.

Subcellular location

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

Tissue specificity

Found in the placenta from the sixth week of pregnancy. Was localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the level decreased and then disappeared from placental villi.

Miscellaneous

HeLa cells lacking BYSL show a delay in the processing of the 18S rRNA component of the 40S ribosomal subunit. HT-H cells lacking BYSL show trophinin-independent signaling through ERBB4.

Sequence similarities

Belongs to the bystin family.

Sequence caution

The sequence AAC16603.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Bystin
PRO_0000186114

Amino acid modifications

Modified residue981Phosphoserine Ref.4 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue1671Phosphoserine Ref.11

Natural variations

Natural variant1031E → K.
Corresponds to variant rs2296916 [ dbSNP | Ensembl ].
VAR_033641
Natural variant4261P → S.
Corresponds to variant rs3828855 [ dbSNP | Ensembl ].
VAR_048439

Experimental info

Sequence conflict2141E → D in AAH07340. Ref.1
Sequence conflict2631A → G in AAC16603. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q13895 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: 1A8C5E5EB108DF1A

FASTA43749,601
        10         20         30         40         50         60 
MPKFKAARGV GGQEKHAPLA DQILAGNAVR AGVREKRRGR GTGEAEEEYV GPRLSRRILQ 

        70         80         90        100        110        120 
QARQQQEELE AEHGTGDKPA APRERTTRLG PRMPQDGSDD EDEEWPTLEK AATMTAAGHH 

       130        140        150        160        170        180 
AEVVVDPEDE RAIEMFMNKN PPARRTLADI IMEKLTEKQT EVETVMSEVS GFPMPQLDPR 

       190        200        210        220        230        240 
VLEVYRGVRE VLSKYRSGKL PKAFKIIPAL SNWEQILYVT EPEAWTAAAM YQATRIFASN 

       250        260        270        280        290        300 
LKERMAQRFY NLVLLPRVRD DVAEYKRLNF HLYMALKKAL FKPGAWFKGI LIPLCESGTC 

       310        320        330        340        350        360 
TLREAIIVGS IITKCSIPVL HSSAAMLKIA EMEYSGANSI FLRLLLDKKY ALPYRVLDAL 

       370        380        390        400        410        420 
VFHFLGFRTE KRELPVLWHQ CLLTLVQRYK ADLATDQKEA LLELLRLQPH PQLSPEIRRE 

       430 
LQSAVPRDVE DVPITVE 

« Hide

References

« Hide 'large scale' references
[1]"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: Lung, Ovary and Pancreas.
[2]"A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin-mediated cell adhesion between trophoblast and endometrial epithelial cells."
Suzuki N., Zara J., Sato T., Ong E., Bakhiet N., Oshima R.G., Watson K.L., Fukuda M.N.
Proc. Natl. Acad. Sci. U.S.A. 95:5027-5032(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-437.
Tissue: Choriocarcinoma.
[3]Fukuda M.N.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Bystin in human cancer cells: intracellular localization and function in ribosome biogenesis."
Miyoshi M., Okajima T., Matsuda T., Fukuda M.N., Nadano D.
Biochem. J. 404:373-381(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Trophoblast cell activation by trophinin ligation is implicated in human embryo implantation."
Sugihara K., Sugiyama D., Byrne J., Wolf D.P., Lowitz K.P., Kobayashi Y., Kabir-Salmani M., Nadano D., Aoki D., Nozawa S., Nakayama J., Mustelin T., Ruoslahti E., Yamaguchi N., Fukuda M.N.
Proc. Natl. Acad. Sci. U.S.A. 104:3799-3804(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC007340 mRNA. Translation: AAH07340.3.
BC050645 mRNA. Translation: AAH50645.1.
BC062627 mRNA. Translation: AAH62627.2.
L36720 mRNA. Translation: AAC16603.2. Different initiation.
RefSeqNP_004044.3. NM_004053.3.
UniGeneHs.106880.

3D structure databases

ProteinModelPortalQ13895.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107167. 30 interactions.
IntActQ13895. 12 interactions.
MINTMINT-1148396.
STRING9606.ENSP00000230340.

Polymorphism databases

DMDM108884834.

2D gel databases

SWISS-2DPAGEQ13895.

Proteomic databases

PaxDbQ13895.
PeptideAtlasQ13895.
PRIDEQ13895.

Protocols and materials databases

DNASU705.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230340; ENSP00000230340; ENSG00000112578.
GeneID705.
KEGGhsa:705.
UCSCuc003orl.3. human.

Organism-specific databases

CTD705.
GeneCardsGC06P041888.
HGNCHGNC:1157. BYSL.
HPAHPA031217.
HPA031219.
MIM603871. gene.
neXtProtNX_Q13895.
PharmGKBPA25472.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280148.
HOGENOMHOG000178028.
HOVERGENHBG024425.
InParanoidQ13895.
KOK14797.
OMACHAATRI.
OrthoDBEOG7J1804.
PhylomeDBQ13895.
TreeFamTF312968.

Gene expression databases

ArrayExpressQ13895.
BgeeQ13895.
CleanExHS_BYSL.
GenevestigatorQ13895.

Family and domain databases

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

Other

GeneWikiBYSL.
GenomeRNAi705.
NextBio2870.
PROQ13895.
SOURCESearch...

Entry information

Entry nameBYST_HUMAN
AccessionPrimary (citable) accession number: Q13895
Secondary accession number(s): Q6P5W4, Q86W44, Q96IP8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM