Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bystin

Gene

BYSL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. cell proliferation Source: Ensembl
  3. female pregnancy Source: ProtInc
  4. maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: Ensembl
  5. trophectodermal cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Bystin
Gene namesi
Name:BYSL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1157. BYSL.

Subcellular locationi

Cytoplasm 1 Publication. Nucleusnucleolus 1 Publication
Note: Associated with 40S ribosomal subunits.

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasm Source: ProtInc
  3. intracellular membrane-bounded organelle Source: HPA
  4. membrane Source: UniProtKB
  5. nucleolus Source: HPA
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437BystinPRO_0000186114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981Phosphoserine7 Publications
Modified residuei167 – 1671Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13895.
PaxDbiQ13895.
PeptideAtlasiQ13895.
PRIDEiQ13895.

2D gel databases

SWISS-2DPAGEQ13895.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ13895.
CleanExiHS_BYSL.
ExpressionAtlasiQ13895. baseline and differential.
GenevestigatoriQ13895.

Organism-specific databases

HPAiHPA031217.
HPA031219.

Interactioni

Subunit structurei

Binds trophinin, tastin and cytokeratins.

Binary interactionsi

WithEntry#Exp.IntActNotes
TROQ128164EBI-358049,EBI-950001
TROAPQ128159EBI-358049,EBI-2349743

Protein-protein interaction databases

BioGridi107167. 106 interactions.
DIPiDIP-50092N.
IntActiQ13895. 12 interactions.
MINTiMINT-1148396.
STRINGi9606.ENSP00000230340.

Structurei

3D structure databases

ProteinModelPortaliQ13895.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the bystin family.Curated

Phylogenomic databases

eggNOGiNOG280148.
GeneTreeiENSGT00390000007241.
HOGENOMiHOG000178028.
HOVERGENiHBG024425.
InParanoidiQ13895.
KOiK14797.
OMAiMTGAGHH.
OrthoDBiEOG7J1804.
PhylomeDBiQ13895.
TreeFamiTF312968.

Family and domain databases

InterProiIPR007955. Bystin.
[Graphical view]
PANTHERiPTHR12821. PTHR12821. 1 hit.
PfamiPF05291. Bystin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKFKAARGV GGQEKHAPLA DQILAGNAVR AGVREKRRGR GTGEAEEEYV
60 70 80 90 100
GPRLSRRILQ QARQQQEELE AEHGTGDKPA APRERTTRLG PRMPQDGSDD
110 120 130 140 150
EDEEWPTLEK AATMTAAGHH AEVVVDPEDE RAIEMFMNKN PPARRTLADI
160 170 180 190 200
IMEKLTEKQT EVETVMSEVS GFPMPQLDPR VLEVYRGVRE VLSKYRSGKL
210 220 230 240 250
PKAFKIIPAL SNWEQILYVT EPEAWTAAAM YQATRIFASN LKERMAQRFY
260 270 280 290 300
NLVLLPRVRD DVAEYKRLNF HLYMALKKAL FKPGAWFKGI LIPLCESGTC
310 320 330 340 350
TLREAIIVGS IITKCSIPVL HSSAAMLKIA EMEYSGANSI FLRLLLDKKY
360 370 380 390 400
ALPYRVLDAL VFHFLGFRTE KRELPVLWHQ CLLTLVQRYK ADLATDQKEA
410 420 430
LLELLRLQPH PQLSPEIRRE LQSAVPRDVE DVPITVE
Length:437
Mass (Da):49,601
Last modified:May 29, 2006 - v3
Checksum:i1A8C5E5EB108DF1A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti214 – 2141E → D in AAH07340 (PubMed:15489334).Curated
Sequence conflicti263 – 2631A → G in AAC16603 (PubMed:9560222).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031E → K.
Corresponds to variant rs2296916 [ dbSNP | Ensembl ].
VAR_033641
Natural varianti426 – 4261P → S.
Corresponds to variant rs3828855 [ dbSNP | Ensembl ].
VAR_048439

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC007340 mRNA. Translation: AAH07340.3.
BC050645 mRNA. Translation: AAH50645.1.
BC062627 mRNA. Translation: AAH62627.2.
L36720 mRNA. Translation: AAC16603.2. Different initiation.
CCDSiCCDS34450.1.
RefSeqiNP_004044.3. NM_004053.3.
UniGeneiHs.106880.

Genome annotation databases

EnsembliENST00000230340; ENSP00000230340; ENSG00000112578.
GeneIDi705.
KEGGihsa:705.
UCSCiuc003orl.3. human.

Polymorphism databases

DMDMi108884834.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC007340 mRNA. Translation: AAH07340.3.
BC050645 mRNA. Translation: AAH50645.1.
BC062627 mRNA. Translation: AAH62627.2.
L36720 mRNA. Translation: AAC16603.2. Different initiation.
CCDSiCCDS34450.1.
RefSeqiNP_004044.3. NM_004053.3.
UniGeneiHs.106880.

3D structure databases

ProteinModelPortaliQ13895.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107167. 106 interactions.
DIPiDIP-50092N.
IntActiQ13895. 12 interactions.
MINTiMINT-1148396.
STRINGi9606.ENSP00000230340.

Polymorphism databases

DMDMi108884834.

2D gel databases

SWISS-2DPAGEQ13895.

Proteomic databases

MaxQBiQ13895.
PaxDbiQ13895.
PeptideAtlasiQ13895.
PRIDEiQ13895.

Protocols and materials databases

DNASUi705.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230340; ENSP00000230340; ENSG00000112578.
GeneIDi705.
KEGGihsa:705.
UCSCiuc003orl.3. human.

Organism-specific databases

CTDi705.
GeneCardsiGC06P041888.
HGNCiHGNC:1157. BYSL.
HPAiHPA031217.
HPA031219.
MIMi603871. gene.
neXtProtiNX_Q13895.
PharmGKBiPA25472.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG280148.
GeneTreeiENSGT00390000007241.
HOGENOMiHOG000178028.
HOVERGENiHBG024425.
InParanoidiQ13895.
KOiK14797.
OMAiMTGAGHH.
OrthoDBiEOG7J1804.
PhylomeDBiQ13895.
TreeFamiTF312968.

Miscellaneous databases

ChiTaRSiBYSL. human.
GeneWikiiBYSL.
GenomeRNAii705.
NextBioi2870.
PROiQ13895.
SOURCEiSearch...

Gene expression databases

BgeeiQ13895.
CleanExiHS_BYSL.
ExpressionAtlasiQ13895. baseline and differential.
GenevestigatoriQ13895.

Family and domain databases

InterProiIPR007955. Bystin.
[Graphical view]
PANTHERiPTHR12821. PTHR12821. 1 hit.
PfamiPF05291. Bystin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-437.
    Tissue: Choriocarcinoma.
  3. Fukuda M.N.
    Submitted (JUN-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(2005) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. 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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. 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(2007) [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(2008) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBYST_HUMAN
AccessioniPrimary (citable) accession number: Q13895
Secondary accession number(s): Q6P5W4, Q86W44, Q96IP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 1998
Last sequence update: May 29, 2006
Last modified: March 3, 2015
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.