Atlas of Genetics and Cytogenetics in Oncology and Haematology

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BYSL (Bystin-Like)

Written2013-09Michiko N Fukuda, Kazuhiro Sugihara
Tumor Microenvironment Program, Cancer Center, Sanford-Burnham Medical Research Institute, La Jolla, CA, USA (MNF); Department of Gynecology, Obstetrics, Hamamatsu University School of Medicine, Hamamatsu City, Shizuoka, Japan (KS)

(Note : for Links provided by Atlas : click)


HGNC Alias symbEnp1
HGNC Previous namebystin-like
LocusID (NCBI) 705
Atlas_Id 857
Location 6p21.1  [Link to chromosome band 6p21]
Location_base_pair Starts at 41921499 and ends at 41933046 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping BYSL.png]
Local_order In human chromosome, BYSL gene localizes in chromosome 6, between TRFP encoding a transcription mediator, and CCND3 encoding cyclin D3 (Figure 1).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
BYSL (6p21.1)::BYSL (6p21.1)


  Figure 1. Genomic organization of BYSL.
Description BYSL locates on 6 chromosome 6p21.1 (Pack et al., 1998). It contains 8 exons spanning 10.7 kb of genomic DNA.


Description Human bystin is a 49.6 kDa cytoplasmic protein composed of 437 amino acid residues. Bystin is a basic protein with isoelectric point 8.10. Bystin protein contains many potential protein kinase phosphorylation sites, suggesting an active role of bystin in signal transduction. However, no known structural motif is found in bystin protein.
Expression BYSL is expressed in trophectoderm cells and endometrial epithelial cells during embryo implantation in human (Aoki and Fukuda, 2000; Nakayama et al., 2003; Suzuki et al., 1999; Suzuki et al., 1998). The expression pattern of mouse bystin at peri-implantation (Aoki et al., 2006) is similar to that of mouse trophinin (Nadano et al., 2002).
In the mouse, bystin protein was found in the blastocyst embryo and endometrial epithelial cells during peri-implantation period (Aoki et al., 2006). Bystin is expressed in mouse endometrial luminal and glandular epithelial cells throughout hormonal cycles (Aoki et al., 2006). Bystin in the luminal epithelia showed a distinct blastocyst-dependent pattern: in the presence of blastocysts, bystin proteins localized to the apical side of the epithelia, whereas in their absence bystin protein was localized to the abluminal or basal side of the epithelia (Figure 2). This observation suggests the existence of an embryonic factor affecting in a way determining the localization of bystin in the maternal epithelia. The molecular basis underlying apical or basal localization of bystin is presently unknown.
Bysl is strongly expressed in the adult rat brain after injury (Ma et al., 2006; Sheng et al., 2004). Bystin is expressed after optic nerve injury in zebra fish (Neve et al., 2012).
Bystin protein was found in mature sperm, of which function is implicated to sperm motility (Hatakeyama et al., 2008). Bystin is overexpressed in hepatocellular carcinoma, suggesting its function in cell proliferation in liver cancer (Wang et al., 2009).
In the Drosophila embryo, bys expression is ubiquitous but relatively weak at early stages, but at later stages bys expression is strong and specifically localized to larval imaginal discs, suggesting a role of bys in cell adhesion. In particular, bys expression is strong in the region of the wing pouch giving rise to two epithelial sheets of the adult wing that adhere to one another after the disc everts (Stewart and Nordquist, 2005).
  Figure 2. Blastocyst-dependent localization of bystin protein in the mouse endometrial epithelia. Above: mouse endometrium with implanting blastocyst (Bl) shows bystin protein (red) on the apical side of epithelia. below: mouse endometrium from pseudopregnant female shows bystin at abluminal side of epithelia. Glandular epithelia (ge); luminal epithelia (le).
Localisation In 6 weeks human placenta, bystin protein was found in the cytoplasm of the syncytiotrophoblast and cytotrophoblast in the chorionic villi, and in endometrial decidual cells at the utero placental interface. In 10 weeks placenta, bystin was exclusively in the nucli of cytotrophoblast (Suzuki et al., 1999). In cultured cells, bystin localizes to both the nucleus and cytoplasm (Aoki et al., 2006; Miyoshi et al., 2007). In the nucleus, bystin was often found in the nucleoli.
Function Bystin function in human embryo implantation: Bystin was originally identified as a cytoplasmic protein that forms a complex with trophinin and tastin in human trophoblastic embryonal carcinoma HT-H cells (Fukuda and Nozawa, 1999; Suzuki et al., 1998). While genes encoding trophinin and tastin are only found in mammals, the bystin gene is conserved across a wide range of eukaryotes, including yeast, nematodes, insects, snakes, and mammals (Roos et al., 1997; Stewart and Denell, 1993; Stewart and Nordquist, 2005; Trachtulec and Forejt, 2001). Trophinin is an intrinsic membrane protein that mediates cell adhesion by homophilic trophinin-trophinin binding (Fukuda et al., 1995). Tastin and bystin are cytoplasmic proteins required for trophinin to function efficiently as a cell adhesion molecule. In humans, trophinin, tastin and bystin are expressed at the utero-placental interface or at implantation sites (Suzuki et al., 1999). These proteins are expressed in human placenta at early stages of pregnancy but disappear from the placenta after 10 weeks of pregnancy (Aoki and Fukuda, 2000; Fukuda and Nozawa, 1999; Suzuki et al., 1999).
In trophoblastic HT-H cells, bystin protein associates with trophinin and ErbB4 in the cytoplasm (Sugihara et al., 2007). When trophinin-mediated cell adhesion takes place on the cell surface, bystin dissociates from trophinin and tyrosine phosphorylation of ErbB4 takes place, suggesting the mechanism underlying the trophectoderm cell activation upon human embryo implantation (Figure 3). Bystin functions as molecular switch in trophinin-mediated signal transduction in trophoblastic cells (Fukuda and Sugihara, 2007; Fukuda and Sugihara,2008; Fukuda and Sugihara,2012).
Bystin function in mouse embryo: Bystin null mouse embryos implanted successfully but died soon after implantation (Aoki et al., 2006), suggesting that bystin is essential for mouse embryo survival after implantation. However, as described below, Bysl gene knockdown experiments show that bystin is also required for survival of pre-implantation stage mouse embryos (Adachi et al., 2007). In the knockout mouse, it is likely that maternally derived Bysl mRNA masks loss of Bysl at pre-implantation stages.
When Bysl siRNAs were microinjected into fertilized eggs, compaction at the eight-cell stage occurred normally in vitro (Adachi et al., 2007). Bysl siRNA-injected embryos showed slightly reduced expression of cytokeratin 8 (EndoA), an early trophectoderm marker (Oshima et al., 1983). While control blastocysts showed assembled cytokeratin structures in the trophectoderm layer, no organized structures were detected in Bysl siRNA-injected embryos. Consequently, blastocyst formation was completely inhibited. These embryos failed to hatch from the zona pellucida and could not outgrow in culture, suggesting that the bystin functions in trophectoderm differentiation. Bysl knockdown also inhibited embryonic stem cell proliferation (Adachi et al., 2007).
Bystin function in stem cells: Mouse bystin gene Bysl has been identified as the stem cell marker commonly expressed in embryonal, neuronal and hematopoietic stem cells (Ramalho-Santos et al., 2002). BYSL is also identified as the major target of MYC in B-cells (Basso et al., 2005). Since MYC is one of essential genes for converting somatic cells into induced pluripotent stem cell (iPS) (Takahashi and Yamanaka, 2006), these observations suggest strongly an essential role of bystin in pluripotent stem cells. Bysl is included in a gene cluster of stem cell markers found on mouse chromosome 16 (Ramalho-Santos et al., 2002).
Bystin function in human sperm motility: Bystin regulates sperm motility (Hatakeyama et al., 2008). Trophinin plays multiple roles in each cell type under different conditions.
Bystin function in ribosomal biogenesis: The yeast bystin homologue ENP1 is essential for budding yeast to survive (Roos et al., 1997). A temperature-sensitive ENP1-null mutant showed defective processing of ribosomal RNA (rRNA) (Chen et al., 2003). Studies of ribosomal biogenesis in yeast indicate that Enp1 is required to synthesize 40S ribosomal subunits by functioning in their nuclear export (Schafer et al., 2003).
Eukaryotic ribosome formation occurs predominantly in nucleoli, but late maturation steps occur in both the nucleoplasm and cytoplasm. Location of bystin in the cytoplasm during G1 and its nuclear localization prior to mitosis suggest that bystin plays dual roles in cell growth and proliferation in mammalian cells.
Although bystin exhibits activities similar to Enp1, human bystin cannot rescue the lethal phenotype of Enp1-null yeast mutant, suggesting that ribosomal RNA processing pathways in multicellular organisms differ from those in yeast and that bystin's activities may have been modified during evolution. Recent studies reveal that maturation of the 40S ribosomal subunit precursors in mammals includes an additional step during processing of the internal transcribed spacer 1 (ITS1), and that coordination between maturation and nuclear export of pre-40S particles has evolved differently in yeast and mammalian cells (Carron et al., 2011). In higher organisms, it was long believed that rRNA processing is completed within the nucleus. However, maturation of the 40S subunit, including final processing of 18S rRNA, occurs in the cytoplasm in human cells (Zemp and Kutay, 2007). Since part of cytoplasmic bystin is associated with the 40S subunit before translation in human cells (Miyoshi et al., 2007), bystin may also function in the final step of 40S subunit synthesis in the cytoplasm.
Bystin associates with undefined nuclear particles following actinomycin D treatment of HeLa cells (Miyoshi et al., 2007). Soluble proteins involved in ribosome biogenesis may shuttle between the nucleolus and nucleoplasm (Dez and Tollervey, 2004). Given the dependence of cell proliferation on ribosome biogenesis, when biogenesis is halted by nucleolar stress this system may allow rapid ribosome re-synthesis following relief from stress (Phipps et al., 2011).
  Figure 3. Role of bystin protein in signal transduction. Prior to trophinin-mediated cell adhesion or in silent trophectoderm cells, ErbB4 is arrested by trophinin-bystin complex. When trophinin-mediated cell adhesion occurs or trophinin-binding GWRQ peptide mimics trophinin-mediated cell adhesion, bystin dissociates from trophinin leading into tyrosine phosphorylation of ErbB4 (Sugihara et al., 2007). Figure 4. Ribosomal biogenesis and rRNA processing in eukaryotic cells. The initial pre-rRNA transcript is first transcribed from repetitive ribosomal DNA genes by RNA polymerase I in the nucleolus. rRNA precursors are then processed, chemically modified, and folded in the nucleolus, and ribosomal proteins, which are translated in the cytoplasm and imported into this organelle, concomitantly assemble with pre-rRNAs. There are two alternative pathways for rRNA processing in human HeLa cells. Bystin is likely involved in processing of a 21S intermediate, of which the final product, 18S rRNA, is included in the 40S small subunit. Bystin is involved in 18S rRNA processing.
Homology None.

Implicated in

Entity Various cancers
Note Cancer progression depends on cell growth and cell cycle progression. Upregulation of BYSL is implicated to following cancers.
Entity Gastric cancer
Note Genome-wide genomic copy aberration analysis of gastric cancer revealed several genes and BYSL was identified as one of them along with CDC6, SEC61G, ANP32E, BYSL and FDFT1 (Tsukamoto et al., 2008).
Entity Hepatocellular carcinoma (HCC)
Note Expression levels of BYSL mRNA and protein in human HCC specimens were markedly increased compared with those seen in adjacent non-cancerous tissue (Wang et al., 2009). BYSL shRNA decreased HCC cell proliferation in vitro, induced apoptosis and partially arrested the cell cycle in the G2/M phase. In vivo, HCC cells treated with BYSL siRNA failed to form tumors in nude mice after subcutaneous implantation. BYSL was found at multiple stages during nucleologenesis, including in nucleolus-derived foci (NDF), perichromosomal regions and the prenucleolar body (PNB) during mitosis. BYSL depletion remarkably suppressed NDF and PNB formation, and disrupted nucleoli assembly after mitosis, resulting in increased apoptosis and reduced tolerance of HCC cells to serum starvation.
Entity Prostate cancers
Note In prostate cancer cells, which adhere to neurons, bystin protein is expressed in a manner suggesting a role in cell-cell contact and cell growth (Ayala et al., 2006).
Entity B cell lymphoma
Note Indeed BYSL and CCND3 are both elevated in B cell lymphoma (Bea, 2010; Kasugai et al., 2005), which is consistent with close proximity of BYSL and CCND3 encoding cyclin D3 (Figure 1) suggesting their co-ordinated role in normal and malignant cells.


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. 2007 Mar;27(6):2202-14. Epub 2007 Jan 22.
PMID 17242206
Recent molecular approaches to elucidate the mechanism of embryo implantation: trophinin, bystin, and tastin as molecules involved in the initial attachment of blastocysts to the uterus in humans.
Aoki R, Fukuda MN.
Semin Reprod Med. 2000;18(3):265-71. (REVIEW)
PMID 11299965
The Bysl gene product, bystin, is essential for survival of mouse embryos.
Aoki R, Suzuki N, Paria BC, Sugihara K, Akama TO, Raab G, Miyoshi M, Nadano D, Fukuda MN.
FEBS Lett. 2006 Nov 13;580(26):6062-8. Epub 2006 Oct 16.
PMID 17055491
Bystin in perineural invasion of prostate cancer.
Ayala GE, Dai H, Li R, Ittmann M, Thompson TC, Rowley D, Wheeler TM.
Prostate. 2006 Feb 15;66(3):266-72.
PMID 16245277
Reverse engineering of regulatory networks in human B cells.
Basso K, Margolin AA, Stolovitzky G, Klein U, Dalla-Favera R, Califano A.
Nat Genet. 2005 Apr;37(4):382-90. Epub 2005 Mar 20.
PMID 15778709
Amplifications and target genes in diffuse large B-cell lymphoma: real targets or consequences of structural features of the genome?
Bea S.
Leuk Lymphoma. 2010 May;51(5):743-4. doi: 10.3109/10428191003699894.
PMID 20233055
Analysis of two human pre-ribosomal factors, bystin and hTsr1, highlights differences in evolution of ribosome biogenesis between yeast and mammals.
Carron C, O'Donohue MF, Choesmel V, Faubladier M, Gleizes PE.
Nucleic Acids Res. 2011 Jan;39(1):280-91. doi: 10.1093/nar/gkq734. Epub 2010 Aug 30.
PMID 20805244
Enp1, a yeast protein associated with U3 and U14 snoRNAs, is required for pre-rRNA processing and 40S subunit synthesis.
Chen W, Bucaria J, Band DA, Sutton A, Sternglanz R.
Nucleic Acids Res. 2003 Jan 15;31(2):690-9.
PMID 12527778
Ribosome synthesis meets the cell cycle.
Dez C, Tollervey D.
Curr Opin Microbiol. 2004 Dec;7(6):631-7. (REVIEW)
PMID 15556036
Trophinin, tastin, and bystin: a complex mediating unique attachment between trophoblastic and endometrial epithelial cells at their respective apical cell membranes.
Fukuda MN, Nozawa S.
emin Reprod Endocrinol. 1999;17(3):229-34. (REVIEW)
PMID 10797941
Trophinin and tastin, a novel cell adhesion molecule complex with potential involvement in embryo implantation.
Fukuda MN, Sato T, Nakayama J, Klier G, Mikami M, Aoki D, Nozawa S.
Genes Dev. 1995 May 15;9(10):1199-210.
PMID 7758945
Enhancement of human sperm motility by trophinin binding peptide.
Hatakeyama S, Sugihara K, Lee SH, Nadano D, Nakayama J, Ohyama C, Fukuda MN.
J Urol. 2008 Aug;180(2):767-71. doi: 10.1016/j.juro.2008.03.185. Epub 2008 Jun 13.
PMID 18554632
Identification of CCND3 and BYSL as candidate targets for the 6p21 amplification in diffuse large B-cell lymphoma.
Kasugai Y, Tagawa H, Kameoka Y, Morishima Y, Nakamura S, Seto M.
Clin Cancer Res. 2005 Dec 1;11(23):8265-72.
PMID 16322284
Expression of trophinin and bystin identifies distinct cell types in the germinal zones of adult rat brain.
Ma L, Yin M, Wu X, Wu C, Yang S, Sheng J, Ni H, Fukuda MN, Zhou J.
Eur J Neurosci. 2006 May;23(9):2265-76.
PMID 16706835
Bystin in human cancer cells: intracellular localization and function in ribosome biogenesis.
Miyoshi M, Okajima T, Matsuda T, Fukuda MN, Nadano D.
Biochem J. 2007 Jun 15;404(3):373-81.
PMID 17381424
Significant differences between mouse and human trophinins are revealed by their expression patterns and targeted disruption of mouse trophinin gene.
Nadano D, Sugihara K, Paria BC, Saburi S, Copeland NG, Gilbert DJ, Jenkins NA, Nakayama J, Fukuda MN.
Biol Reprod. 2002 Feb;66(2):313-21.
PMID 11804944
Implantation-dependent expression of trophinin by maternal fallopian tube epithelia during tubal pregnancies: possible role of human chorionic gonadotrophin on ectopic pregnancy.
Nakayama J, Aoki D, Suga T, Akama TO, Ishizone S, Yamaguchi H, Imakawa K, Nadano D, Fazleabas AT, Katsuyama T, Nozawa S, Fukuda MN.
Am J Pathol. 2003 Dec;163(6):2211-9.
PMID 14633596
Activating transcription factor 3 and reactive astrocytes following optic nerve injury in zebrafish.
Neve LD, Savage AA, Koke JR, Garcia DM.
Comp Biochem Physiol C Toxicol Pharmacol. 2012 Mar;155(2):213-8. doi: 10.1016/j.cbpc.2011.08.006. Epub 2011 Aug 24.
PMID 21889613
Intermediate filament protein synthesis in preimplantation murine embryos.
Oshima RG, Howe WE, Klier FG, Adamson ED, Shevinsky LH.
Dev Biol. 1983 Oct;99(2):447-55.
PMID 6352374
Assignment1 of the bystin gene BYSL to human chromosome band 6p21.1 by in situ hybridization.
Pack SD, Pak E, Tanigami A, Ledbetter DH, Fukuda MN.
Cytogenet Cell Genet. 1998;83(1-2):76-7.
PMID 9925933
The small subunit processome in ribosome biogenesis - progress and prospects.
Phipps KR, Charette J, Baserga SJ.
Wiley Interdiscip Rev RNA. 2011 Jan-Feb;2(1):1-21. doi: 10.1002/wrna.57. (REVIEW)
PMID 21318072
"Stemness": transcriptional profiling of embryonic and adult stem cells.
Ramalho-Santos M, Yoon S, Matsuzaki Y, Mulligan RC, Melton DA.
Science. 2002 Oct 18;298(5593):597-600. Epub 2002 Sep 12.
PMID 12228720
ENP1, an essential gene encoding a nuclear protein that is highly conserved from yeast to humans.
Roos J, Luz JM, Centoducati S, Sternglanz R, Lennarz WJ.
Gene. 1997 Jan 31;185(1):137-46.
PMID 9034325
The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.
Schafer T, Strauss D, Petfalski E, Tollervey D, Hurt E.
EMBO J. 2003 Mar 17;22(6):1370-80.
PMID 12628929
Bystin as a novel marker for reactive astrocytes in the adult rat brain following injury.
Sheng J, Yang S, Xu L, Wu C, Wu X, Li A, Yu Y, Ni H, Fukuda M, Zhou J.
Eur J Neurosci. 2004 Aug;20(4):873-84.
PMID 15305856
Drosophila Bys is nuclear and shows dynamic tissue-specific expression during development.
Stewart MJ, Nordquist EK.
Dev Genes Evol. 2005 Feb;215(2):97-102. Epub 2004 Dec 3.
PMID 15580530
Trophoblast cell activation by trophinin ligation is implicated in human embryo implantation.
Sugihara K, Sugiyama D, Byrne J, Wolf DP, Lowitz KP, Kobayashi Y, Kabir-Salmani M, Nadano D, Aoki D, Nozawa S, Nakayama J, Mustelin T, Ruoslahti E, Yamaguchi N, Fukuda MN.
Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3799-804. Epub 2007 Feb 26.
PMID 17360433
Expression of trophinin, tastin, and bystin by trophoblast and endometrial cells in human placenta.
Suzuki N, Nakayama J, Shih IM, Aoki D, Nozawa S, Fukuda MN.
Biol Reprod. 1999 Mar;60(3):621-7.
PMID 10026108
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 RG, Watson KL, Fukuda MN.
Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):5027-32.
PMID 9560222
Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors.
Takahashi K, Yamanaka S.
Cell. 2006 Aug 25;126(4):663-76. Epub 2006 Aug 10.
PMID 16904174
Synteny of orthologous genes conserved in mammals, snake, fly, nematode, and fission yeast.
Trachtulec Z, Forejt J.
Mamm Genome. 2001 Mar;12(3):227-31.
PMID 11252172
Genome-wide analysis of DNA copy number alterations and gene expression in gastric cancer.
Tsukamoto Y, Uchida T, Karnan S, Noguchi T, Nguyen LT, Tanigawa M, Takeuchi I, Matsuura K, Hijiya N, Nakada C, Kishida T, Kawahara K, Ito H, Murakami K, Fujioka T, Seto M, Moriyama M.
J Pathol. 2008 Dec;216(4):471-82. doi: 10.1002/path.2424.
PMID 18798223
Bystin-like protein is upregulated in hepatocellular carcinoma and required for nucleologenesis in cancer cell proliferation.
Wang H, Xiao W, Zhou Q, Chen Y, Yang S, Sheng J, Yin Y, Fan J, Zhou J.
Cell Res. 2009 Oct;19(10):1150-64. doi: 10.1038/cr.2009.99. Epub 2009 Aug 18.
PMID 19687802
Nuclear export and cytoplasmic maturation of ribosomal subunits.
Zemp I, Kutay U.
FEBS Lett. 2007 Jun 19;581(15):2783-93. Epub 2007 May 11. (REVIEW)
PMID 17509569


This paper should be referenced as such :
Fukuda, MN ; Sugihara, K
BYSL (Bystin-Like)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(5):293-298.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)BYSL   1157
Entrez_Gene (NCBI)BYSL    bystin like
AliasesBYSTIN; Enp1
GeneCards (Weizmann)BYSL
Ensembl hg19 (Hinxton)ENSG00000112578 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000112578 [Gene_View]  ENSG00000112578 [Sequence]  chr6:41921499-41933046 [Contig_View]  BYSL [Vega]
ICGC DataPortalENSG00000112578
Genatlas (Paris)BYSL
SOURCE (Princeton)BYSL
Genetics Home Reference (NIH)BYSL
Genomic and cartography
GoldenPath hg38 (UCSC)BYSL  -     chr6:41921499-41933046 +  6p21.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)BYSL  -     6p21.1   [Description]    (hg19-Feb_2009)
GoldenPathBYSL - 6p21.1 [CytoView hg19]  BYSL - 6p21.1 [CytoView hg38]
Genome Data Viewer NCBIBYSL [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AK095253 AK314147 BC007340 BC050645 BC062627
RefSeq transcript (Entrez)NM_004053
Consensus coding sequences : CCDS (NCBI)BYSL
Gene ExpressionBYSL [ NCBI-GEO ]   BYSL [ EBI - ARRAY_EXPRESS ]   BYSL [ SEEK ]   BYSL [ MEM ]
Gene Expression Viewer (FireBrowse)BYSL [ Firebrowse - Broad ]
GenevisibleExpression of BYSL in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)705
GTEX Portal (Tissue expression)BYSL
Human Protein AtlasENSG00000112578-BYSL [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13895   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13895  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13895
Domains : Interpro (EBI)Bystin   
Domain families : Pfam (Sanger)Bystin (PF05291)   
Domain families : Pfam (NCBI)pfam05291   
Conserved Domain (NCBI)BYSL
PDB (RSDB)6G18    6G4S    6G4W   
PDB Europe6G18    6G4S    6G4W   
PDB (PDBSum)6G18    6G4S    6G4W   
PDB (IMB)6G18    6G4S    6G4W   
Structural Biology KnowledgeBase6G18    6G4S    6G4W   
SCOP (Structural Classification of Proteins)6G18    6G4S    6G4W   
CATH (Classification of proteins structures)6G18    6G4S    6G4W   
AlphaFold pdb e-kbQ13895   
Human Protein Atlas [tissue]ENSG00000112578-BYSL [tissue]
Protein Interaction databases
IntAct (EBI)Q13895
Ontologies - Pathways
Ontology : AmiGOmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)  trophectodermal cell differentiation  RNA binding  protein binding  nucleoplasm  nucleoplasm  chromosome  nucleolus  nucleolus  cytoplasm  cytosol  rRNA processing  cell population proliferation  membrane  snoRNA binding  preribosome, small subunit precursor  ribosome biogenesis  intracellular membrane-bounded organelle  apical part of cell  regulation of protein localization to nucleolus  
Ontology : EGO-EBImaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)  trophectodermal cell differentiation  RNA binding  protein binding  nucleoplasm  nucleoplasm  chromosome  nucleolus  nucleolus  cytoplasm  cytosol  rRNA processing  cell population proliferation  membrane  snoRNA binding  preribosome, small subunit precursor  ribosome biogenesis  intracellular membrane-bounded organelle  apical part of cell  regulation of protein localization to nucleolus  
REACTOMEQ13895 [protein]
REACTOME PathwaysR-HSA-6791226 [pathway]   
NDEx NetworkBYSL
Atlas of Cancer Signalling NetworkBYSL
Wikipedia pathwaysBYSL
Orthology - Evolution
GeneTree (enSembl)ENSG00000112578
Phylogenetic Trees/Animal Genes : TreeFamBYSL
Homologs : HomoloGeneBYSL
Homology/Alignments : Family Browser (UCSC)BYSL
Gene fusions - Rearrangements
Fusion : QuiverBYSL
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerBYSL [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)BYSL
Exome Variant ServerBYSL
GNOMAD BrowserENSG00000112578
Varsome BrowserBYSL
ACMGBYSL variants
Genomic Variants (DGV)BYSL [DGVbeta]
DECIPHERBYSL [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisBYSL 
ICGC Data PortalBYSL 
TCGA Data PortalBYSL 
Broad Tumor PortalBYSL
OASIS PortalBYSL [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICBYSL  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DBYSL
Mutations and Diseases : HGMDBYSL
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)BYSL
DoCM (Curated mutations)BYSL
CIViC (Clinical Interpretations of Variants in Cancer)BYSL
NCG (London)BYSL
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry BYSL
NextProtQ13895 [Medical]
Target ValidationBYSL
Huge Navigator BYSL [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDBYSL
Pharm GKB GenePA25472
Clinical trialBYSL
DataMed IndexBYSL
PubMed85 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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