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FAU (Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed)

Written2011-07Mark Pickard
Institute for Science, Technology in Medicine, Huxley Building, Keele University, Keele, ST5 5BG, UK

(Note : for Links provided by Atlas : click)


Alias (NCBI)FAU1
HGNC Alias symbRPS30
HGNC Alias nameribosomal protein S30
 Monoclonal nonspecific suppressor factor beta
HGNC Previous nameFinkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed (fox derived)
 Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed
 FAU, ubiquitin like and ribosomal protein S30 fusion
LocusID (NCBI) 2197
Atlas_Id 40538
Location 11q13.1  [Link to chromosome band 11q13]
Location_base_pair Starts at 65120630 and ends at 65122134 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping FAU.png]
Local_order FAU is flanked by SYVN1 and ZNHIT2 on the negative strand.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ANKRD11 (16q24.3) / FAU (11q13.1)APOL6 (22q12.3) / FAU (11q13.1)FAU (11q13.1) / BAD (11q13.1)
FAU (11q13.1) / CALR (19p13.2)FAU (11q13.1) / CNOT2 (12q15)FAU (11q13.1) / MIR5095 (1p32.3)
FAU (11q13.1) / MRPL16 (11q12.1)FAU (11q13.1) / PLIN3 (19p13.3)PRKDC (8q11.21) / FAU (11q13.1)
PTPRD (9p24.1) / FAU (11q13.1)
Note FAU was originally identified as the cellular homologue of the fox gene of the retrovirus Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV); fox is antisense to FAU, and has been shown to increase the tumorigenicity of FBR-MuSV. FAU encodes a ubiquitin-like protein fused to ribosomal protein S30 as a carboxy-terminal extension; the two products are thought to be cleaved post-translationally. The S30 protein is a member of the S30E family of ribosomal proteins and is a constituent of the 40S subunit of the ribosome; additionally it is secreted and has anti-microbial activity ('ubiquicidin'). The function of the ubiquitin-like protein, termed FUBI, is unclear; in murine cells, it has been reported to covalently modify inter alia a T-cell receptor alpha-like protein and Bcl-G, suggestive of roles in immunomodulation and apoptosis regulation, respectively. In human cells, ectopic FAU expression enhances basal apoptosis, whereas siRNA-mediated silencing of FAU gene expression induces resistance to apoptosis induction in response to a range of stimuli. FAU gene expression is down-regulated in a number of human cancers, including breast, prostate and ovarian cancers.


  FAU comprises 5 exons - the coding sequence for FUBI is located within exons 2 and 3, whereas the coding sequence for S30 is located within exons 4 and 5.
Description Gene is located on the negative strand at -64889908: -64887863 (2046 bases). The promoter contains a number of regulatory elements, including binding sites for transcription factors such as AP-1, IRF-1, Max, c-Myc, glucocorticoid receptor isoforms and ATF.
Transcription Comprises 5 exons spanning -64888099: -64889672. The mRNA product length is 579 bases.
Pseudogene A retropseudogene, FAU1P, has been described in the human genome and is located on chromosome 18. Retropseudogenes of FAU have also been described in the mouse genome.


  A. Protein products of FAU - FAU encodes a ubiquitin-like protein (FUBI) with ribosomal protein S30 as a C-terminal extension protein (CEP). These are cleaved post-translationally. B. FUBI has 37/57% sequence identity/similarity to ubiquitin (Ub; latter is fused to CEP80/S27a ribosomal protein). The C-terminal G-G dipeptide (shown in orange), which is required for cleavage from the CEP and for isopeptide bond formation to lysine of targets, is conserved. Note however, that lysine residues (shown in green) which serve as sites for polyubiquitin chain formation are absent. Consequently, FUBI is unlikely to have an analogous role to ubiquitin in protein degradation.
Description The protein product comprises a ubiquitin-like protein, FUBI, with ribosomal protein S30 as a carboxy-terminal extension protein (CEP); other ribosomal proteins are produced as CEPs fused to ubiquitin. FUBI and S30 are thought to be cleaved post-translationally, but the enzyme catalyzing this step has not been identified. Whilst FUBI shows a high degree of sequence similarity to ubiquitin, notably retaining the C-terminal G-G dipeptide motif that is required for isopeptide bond formation between ubiquitin and lysines of target proteins, it lacks internal lysine residues (especially lysine-48) which serve as sites of polyubiquitin chain formation and usually facilitate proteasomal degradation of target molecules. Rather, modification of proteins with monomers of ubiquitin or ubiquitin-like proteins may influence the activity, intracellular localisation or inter-molecular interactions of target proteins. Little information exists regarding target proteins for FUBI in human cells. In mouse, four target proteins have been identified. Covalent modification occurs for: (i) a T-cell receptor alpha-like protein (resulting in the production of murine monoclonal non-specific suppressor factor, which exhibits immunomodulatory activity); (ii) Bcl-G (a pro-apoptotic member of the Bcl-2 family; and (iii) endophilin II (regulates phagocytosis in mouse macrophages). Non-covalent modification of histone 2A has also been reported.
Expression Steady state FAU mRNA levels are highly abundant and largely invariant in normal tissues indicative of a house-keeping gene role. However, physiological variations occur in FAU expression, notably in endometrium. FAU transcript levels have been reported to be reduced in a number of human cancers, including those affecting the breast, the prostate and the ovary.
Localisation Cytosolic, ribosomal and nuclear localisations have been reported for FAU products. In addition, secretion of FUBI (in association with a T-cell receptor-alpha-like molecule) has been reported for some immune system cell types.
Function FAU regulates apoptosis in human epithelial and T-cell lines. It also possesses immunomodulatory and anti-microbial activities, and encodes a constituent of the ribosome.
Regulation of apoptosis
Functional expression cloning in mouse leukemic cell lines, with selection (dexamethasone and gamma-irradiation) for suppression of cell death, led to the isolation of a sequence which was antisense to FAU (Mourtada-Maarabouni et al., 2004). Subcloning experiments confirmed that this antisense sequence produced resistance to apoptosis induced by dexamethasone and, additionally, by cisplatin and by ultraviolet-C irradiation. The antisense sequence reduced endogenous FAU expression. Conversely, overexpression of FAU promoted cell death, and this effect could be prevented by co-transfection with a plasmid encoding Bcl-2 (an anti-apoptotic factor) or by inhibition of caspases. Further work in human T-cell lines and the epithelial cell line, 293T/17, has confirmed that ectopic FAU expression increases basal apoptosis, and that siRNA-mediated silencing of FAU attenuates apoptosis in response to ultraviolet-C irradiation (Pickard et al., 2011). FAU also regulates apoptosis in other human epithelial cell lines derived from breast (Pickard et al., 2009), ovarian (Moss et al., 2010) and prostate (Pickard et al., 2010) tumours (see 'Implicated in'). FUBI has been shown to covalently modify Bcl-G (a pro-apoptotic member of the Bcl-2 family) in mouse cells (Nakamura and Tanigawa, 2003), and it is feasible therefore, that FAU regulates apoptosis via Bcl-G. Indeed, prior knockdown of Bcl-G ablated the stimulation of basal apoptosis by FAU in human cells (Pickard et al., 2011). This pro-apoptotic activity may underlie the putative tumour suppressor role of FAU, since failure of apoptosis is known to play a central role in the development of many cancers.
Monoclonal non-specific suppressor factor (MNSF) was first isolated from mouse cells in 1986 (Nakamura et al., 1988) and subsequently, from ascites fluid of a patient with systemic lupus erythematosus (Xavier et al., 1994); most studies of MNSF to-date have focussed on murine cells. This lymphokine-like molecule, which comprises alpha- and beta-chains, is secreted by CD8+ T-cells (Xavier et al., 1995). cDNA encoding MNSF-beta was first isolated from the mouse in 1995, and it was shown to be identical to FAU (Nakamura et al., 1995). MNSF inhibits, inter alia, proliferation of mitogen-stimulated T- and B-cells, immunoglobulin secretion by B-cells in an isotype-specific manner (IgE and IgG3 are especially affected), TNFalpha production by activated macrophages and interleukin-4 secretion by bone marrow-derived mast cells and by a type-2 helper T-cell clone (Nakamura et al., 1988; Nakamura et al., 1994; Xavier et al., 1994; Nakamura et al., 1995; Xavier et al., 1995; Nakamura et al., 1996; Suzuki et al., 1996). Inhibitory effects on T- and B-cell proliferation are subject to negative regulation by interleukin-2 (Nakamura et al., 1988). Many of these immunosuppresive effects of MNSF can be ascribed to the MNSFbeta subunit, and specifically to FUBI (aka Ubi-L) (Nakamura et al., 1996). Cell surface receptors for MNSF have been described in target cells (Nakamura et al., 1992), and these exhibit similarities to cytokine receptors (Nakamura and Tanigawa, 1999), with tyrosine phosphorylation being implicated in transmembrane signalling (Nakamura and Tanigawa, 2000; Nakamura et al., 2002). Both the expression of cell surface receptors on target cells and the secretion of MNSFbeta/FUBI by splenocytes are stimulated by interferon-gamma (Nakamura et al., 1992; Nakamura et al., 1996). In splenocytes, FUBI conjugates to a range of intracellular proteins, including a T-cell receptor-alpha-like molecule; the resulting complex, which comprises intact MNSF, is secreted by cells (Nakamura et al., 1998; Nakamura et al., 2002). FUBI also covalently modifies Bcl-G in spleen but not in testis, despite high levels of Bcl-G expression in the latter tissue (Nakamura and Tanigawa, 2003). In macrophages, the FUBI/Bcl-G adduct binds to ERKs and inhibits ERK activation by MEK1 (Nakamura and Yamaguchi, 2006). In liver and macrophages, FUBI also forms an adduct with endophilin II and inhibits phagocytosis by macrophages (Nakamura and Shimosaki, 2009; Nakamura and Watanabe, 2010).
Host defence
An anti-microbial protein, termed ubiquicidin, has been isolated from the cytosol of a mouse macrophage cell line treated with interferon-gamma; the protein is active against Listeria monocytogenes, Salmonella typhimurium, Escherichia coli, Staphylococcus aureus and Yersinia enterocolitica (Hiemstra et al., 1999). Ubiquicidin is identical to FAU-encoded ribosomal protein S30 (Hiemstra et al., 1999). Ubiquicidin is also produced by human colonic mucosa (Tollin et al., 2003) and rainbow trout skin (Fernandes and Smith, 2002). It is also active against methicillin-resistant Staphylococcus aureus and accumulates at sites of infection in mice (Brouwer et al., 2006). Radiolabelled ubiquicidin has applications in clinical imaging for microbial infections (Brouwer et al., 2008).
Homology At the amino acid level, FUBI has 37/57% sequence identity/similarity to ubiquitin.

Implicated in

Entity Various cancers
Note Tumor suppression: The retrovirus, FBR-MuSV, which contains the transduced genes v-fos and fox, can induce osteosarcomas in mice. In vitro experiments have shown that fox increases the transforming capacity of FBR-MuSV approximately two-fold (Michiels et al., 1993). Fox is an antisense sequence to the cellular gene FAU, indicative of a tumour suppressor role for FAU. Retropseudogenes of FAU have been identified in human (Kas et al., 1995) and mouse (Casteels et al., 1995) genomes, suggesting a possible source for the viral fox gene (which is antisense to FAU). Further evidence for a tumour suppressor role for FAU has come from studies of the human carcinogen arsenite. Thus, functional cloning approaches in Chinese hamster V79 cells with selection for arsenite resistance, resulted in the isolation of the asr1 gene, which is homologous to FAU (Rossman and Wang, 1999). Subsequent work by this group using human osteogenic sarcoma cells, indicated that the ability to confer arsenite resistance resided in the S30 domain of FAU (Rossman et al., 2003).
Oncogenesis Expression of the FUBI domain of FAU has been shown to transform human osteogenic sarcoma cells to anchorage-independent growth (Rossman et al., 2003).
Entity Breast cancer
Note Serial analysis of gene expression (SAGE) identified FAU as an underexpressed gene in ductal carcinoma in situ when compared with normal breast epithelium (Abba et al., 2004). This was subsequently confirmed using quantitative RT-PCR analysis of matched (same patient) samples of breast cancer tissue and adjacent breast epithelial tissue (Pickard et al., 2009). Furthermore, in a separate group of breast cancer patients, expression levels of FAU (determined by cDNA microarray analysis) were shown to be related to patient survival in Kaplan-Meier analyses (Pickard et al., 2009). This analysis indicated that higher expression of Fau has a protective effect, consistent with its candidate tumour suppressor role. Whilst Bcl-G expression was also shown to be down-regulated in breast cancer, Bcl-G expression was not related to patient survival (Pickard et al., 2009), suggesting that the regulation of Bcl-G activity by post-translational modification is more important than Bcl-G expression per se in determining breast cancer patient survival. Functional studies in the T-47D breast cancer cell line demonstrated that down-regulation of either FAU or Bcl-G expression by siRNA-mediated silencing attenuated apoptosis induction by ultraviolet-C irradiation (Pickard et al., 2009). Notably, no additional effect was observed when the two genes were simultaneously silenced, consistent with a role for Bcl-G in mediating the pro-apoptotic activity of FAU.
Entity Ovarian cancer
Note A reduction in FAU gene expression has been reported for malignant versus normal ovarian tissue, and for Type I ovarian tumours (typically include mucinous, endometrioid, clear cell, and low-grade serous cancers), in particular (Moss et al., 2010). Over-expression of FAU in a cisplatin-resistant ovarian cancer cell sub-line, A2780cis, resulted in increased sensitivity to carboplatin-induced apoptosis (Moss et al., 2010). Conversely, down-regulation of FAU in the A2780 parental cell line resulted in increased resistance to carboplatin-induced apoptosis (Moss et al., 2010). These in vitro findings suggest a role for FAU in the regulation of platinum-based drug resistance in ovarian cancer.
Entity Prostate cancer
Note Steady state FAU mRNA levels are down-regulated in prostate cancer when compared with normal tissue and tissue from patients with benign prostate hyperplasia; a similar trend was found for Bcl-G (Pickard et al., 2010). siRNA-mediated silencing of FAU or Bcl-G expression in the prostate cell line, 22Rv1, attenuated apoptosis induction consequent upon ultraviolet-C irradiation. A similar degree of apoptosis resistance was observed when the two genes were simultaneously down-regulated, consistent with FAU and Bcl-G acting in the same pathway.
Entity Reproduction (implantation)
Note FAU is expressed in endometrial stromal cells in non-pregnant mouse uterus (Salamonsen et al., 2002) and it is also expressed in human endometrium (Nie et al., 2005). In the mouse uterus, differential expression of FAU occurs during blastocyst implantation, with low expression levels noted in implantation versus interimplantation sites (Nie et al., 2000). Expression levels remain low as implantation advances (Nie et al., 2000). Administration of antisera to FAU into the mouse uterine lumen inhibits implantation in a dose-dependent manner (Wang et al., 2007), suggesting an essential role for secreted products in implantation. Trophoblast-derived interferons have been shown to induce endometrial FAU expression in pigs (Chwetzoff and d'Andrea, 1997), also supporting an important role for FAU in early pregnancy.


Note A t(11;14)(q13;q21)-positive B-cell non-Hodgkin's lymphoma patient has been described with an additional translocation of t(11;17)(q13;q21). The chromosome 11 breakpoint in the latter translocation was reported as a 40 kbp region around FAU.


Transcriptomic changes in human breast cancer progression as determined by serial analysis of gene expression.
Abba MC, Drake JA, Hawkins KA, Hu Y, Sun H, Notcovich C, Gaddis S, Sahin A, Baggerly K, Aldaz CM.
Breast Cancer Res. 2004;6(5):R499-513. Epub 2004 Jul 6.
PMID 15318932
The pharmacology of radiolabeled cationic antimicrobial peptides.
Brouwer CP, Wulferink M, Welling MM.
J Pharm Sci. 2008 May;97(5):1633-51. (REVIEW)
PMID 17786940
The mouse Fau gene: genomic structure, chromosomal localization, and characterization of two retropseudogenes.
Casteels D, Poirier C, Guenet JL, Merregaert J.
Genomics. 1995 Jan 1;25(1):291-4.
PMID 7774934
Ubiquitin is physiologically induced by interferons in luminal epithelium of porcine uterine endometrium in early pregnancy: global RT-PCR cDNA in place of RNA for differential display screening.
Chwetzoff S, d'Andrea S.
FEBS Lett. 1997 Mar 24;405(2):148-52.
PMID 9089280
A novel antimicrobial function for a ribosomal peptide from rainbow trout skin.
Fernandes JM, Smith VJ.
Biochem Biophys Res Commun. 2002 Aug 9;296(1):167-71.
PMID 12147245
Ubiquicidin, a novel murine microbicidal protein present in the cytosolic fraction of macrophages.
Hiemstra PS, van den Barselaar MT, Roest M, Nibbering PH, van Furth R.
J Leukoc Biol. 1999 Sep;66(3):423-8.
PMID 10496312
Genomic structure and expression of the human fau gene: encoding the ribosomal protein S30 fused to a ubiquitin-like protein.
Kas K, Michiels L, Merregaert J.
Biochem Biophys Res Commun. 1992 Sep 16;187(2):927-33.
PMID 1326960
Assignment of the human FAU gene to a subregion of chromosome 11q13.
Kas K, Schoenmakers E, van de Ven W, Weber G, Nordenskjold M, Michiels L, Merregaert J, Larsson C.
Genomics. 1993 Aug;17(2):387-92.
PMID 8406491
Characterization of a processed pseudogene of human FAU1 on chromosome 18.
Kas K, Stickens D, Merregaert J.
Gene. 1995 Jul 28;160(2):273-6.
PMID 7642109
Ubiquitin-like polypeptide inhibits the proliferative response of T cells in vivo.
Kondoh T, Nakamura M, Nabika T, Yoshimura Y, Tanigawa Y.
Immunobiology. 1999 Feb;200(1):140-9.
PMID 10084702
fau cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus.
Michiels L, Van der Rauwelaert E, Van Hasselt F, Kas K, Merregaert J.
Oncogene. 1993 Sep;8(9):2537-46.
PMID 8395683
FAU regulates carboplatin resistance in ovarian cancer.
Moss EL, Mourtada-Maarabouni M, Pickard MR, Redman CW, Williams GT.
Genes Chromosomes Cancer. 2010 Jan;49(1):70-7.
PMID 19830698
Regulation of apoptosis by fau revealed by functional expression cloning and antisense expression.
Mourtada-Maarabouni M, Kirkham L, Farzaneh F, Williams GT.
Oncogene. 2004 Dec 16;23(58):9419-26.
PMID 15543234
Conjugation of ubiquitin-like polypeptide to intracellular acceptor proteins.
Nagata T, Nakamura M, Kawauchi H, Tanigawa Y.
Biochim Biophys Acta. 1998 Mar 5;1401(3):319-28.
PMID 9540822
Ubiquitin-like protein MNSFbeta/endophilin II complex regulates Dectin-1-mediated phagocytosis and inflammatory responses in macrophages.
Nakamura M, Watanabe N.
Biochem Biophys Res Commun. 2010 Oct 15;401(2):257-61. Epub 2010 Sep 16.
PMID 20849826
Identification of novel endometrial targets for contraception.
Nie G, Findlay JK, Salamonsen LA.
Contraception. 2005 Apr;71(4):272-81. (REVIEW)
PMID 15792646
Identification of monoclonal nonspecific suppressor factor beta (mNSFbeta) as one of the genes differentially expressed at implantation sites compared to interimplantation sites in the mouse uterus.
Nie GY, Li Y, Hampton AL, Salamonsen LA, Clements JA, Findlay JK.
Mol Reprod Dev. 2000 Apr;55(4):351-63.
PMID 10694741
The carboxyl extension of a ubiquitin-like protein is rat ribosomal protein S30.
Olvera J, Wool IG.
J Biol Chem. 1993 Aug 25;268(24):17967-74.
PMID 8394356
Candidate tumour suppressor Fau regulates apoptosis in human cells: An essential role for Bcl-G.
Pickard MR, Mourtada-Maarabouni M, Williams GT.
Biochim Biophys Acta. 2011 Sep;1812(9):1146-53. Epub 2011 Apr 29.
PMID 21550398
fau and its ubiquitin-like domain (FUBI) transforms human osteogenic sarcoma (HOS) cells to anchorage-independence.
Rossman TG, Visalli MA, Komissarova EV.
Oncogene. 2003 Mar 27;22(12):1817-21.
PMID 12660817
Complex regulation of decidualization: a role for cytokines and proteases--a review.
Salamonsen LA, Dimitriadis E, Jones RL, Nie G.
Placenta. 2003 Apr;24 Suppl A:S76-85. (REVIEW)
PMID 12842418
Monoclonal nonspecific suppressor factor beta (MNSF beta) inhibits the production of TNF-alpha by lipopolysaccharide-activated macrophages.
Suzuki K, Nakamura M, Nariai Y, Dekio S, Tanigawa Y.
Immunobiology. 1996 Jul;195(2):187-98.
PMID 8877395
Antimicrobial peptides in the first line defence of human colon mucosa.
Tollin M, Bergman P, Svenberg T, Jornvall H, Gudmundsson GH, Agerberth B.
Peptides. 2003 Apr;24(4):523-30.
PMID 12860195
Immunoneutralization of endometrial monoclonal nonspecific suppressor factor beta (MNSFbeta) inhibits mouse embryo implantation in vivo.
Wang J, Huang ZP, Nie GY, Salamonsen LA, Shen QX.
Mol Reprod Dev. 2007 Nov;74(11):1419-27.
PMID 17393421
Molecular mapping of the chromosome 11 breakpoint of t(11;17)(q13;q21) in a t(11;14)(q13;q32)-positive B non-Hodgkin's lymphoma.
Wlodarska I, Schoenmakers E, Kas K, Merregaert J, Lemahieu V, Weier U, Van den Berghe H, Van de Ven WJ.
Genes Chromosomes Cancer. 1993 Dec;8(4):224-9.
PMID 7512365
Human nonspecific suppressor factor (hNSF): cell source and effects on T and B lymphocytes.
Xavier R, Nakamura M, Kobayashi S, Ishikura H, Tanigawa Y.
Immunobiology. 1995 Feb;192(3-4):262-71.
PMID 7782099
Isolation and characterization of a human nonspecific suppressor factor from ascitic fluid of systemic lupus erythematosus. Evidence for a human counterpart of the monoclonal nonspecific suppressor factor and relationship to the T cell receptor alpha-chain.
Xavier RM, Nakamura M, Tsunematsu T.
J Immunol. 1994 Mar 1;152(5):2624-32.
PMID 8133068


This paper should be referenced as such :
Pickard, M
FAU (Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(1):12-17.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)FAU   3597
Entrez_Gene (NCBI)FAU    FAU ubiquitin like and ribosomal protein S30 fusion
AliasesFAU1; Fub1; Fubi; MNSFbeta; 
RPS30; S30; asr1
GeneCards (Weizmann)FAU
Ensembl hg19 (Hinxton)ENSG00000149806 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000149806 [Gene_View]  ENSG00000149806 [Sequence]  chr11:65120630-65122134 [Contig_View]  FAU [Vega]
ICGC DataPortalENSG00000149806
TCGA cBioPortalFAU
Genatlas (Paris)FAU
SOURCE (Princeton)FAU
Genetics Home Reference (NIH)FAU
Genomic and cartography
GoldenPath hg38 (UCSC)FAU  -     chr11:65120630-65122134 -  11q13.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FAU  -     11q13.1   [Description]    (hg19-Feb_2009)
GoldenPathFAU - 11q13.1 [CytoView hg19]  FAU - 11q13.1 [CytoView hg38]
genome Data Viewer NCBIFAU [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AA449261 AK026639 BC033877 BC051834 BP296770
RefSeq transcript (Entrez)NM_001997
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)FAU
Alternative Splicing GalleryENSG00000149806
Gene ExpressionFAU [ NCBI-GEO ]   FAU [ EBI - ARRAY_EXPRESS ]   FAU [ SEEK ]   FAU [ MEM ]
Gene Expression Viewer (FireBrowse)FAU [ Firebrowse - Broad ]
GenevisibleExpression of FAU in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2197
GTEX Portal (Tissue expression)FAU
Human Protein AtlasENSG00000149806-FAU [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP62861   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP62861  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP62861
Splice isoforms : SwissVarP62861
Domains : Interpro (EBI)Ribosomal_S30   
Domain families : Pfam (Sanger)Ribosomal_S30 (PF04758)   
Domain families : Pfam (NCBI)pfam04758   
Conserved Domain (NCBI)FAU
Blocks (Seattle)FAU
PDB (RSDB)4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
PDB Europe4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
PDB (PDBSum)4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
PDB (IMB)4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
Structural Biology KnowledgeBase4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
SCOP (Structural Classification of Proteins)4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
CATH (Classification of proteins structures)4UG0    4V6X    5A2Q    5AJ0    5FLX    5OA3    5T2C    6EK0    6FEC    6G18    6G4S    6G4W    6G51    6G53    6G5H    6G5I    6IP5    6IP6    6IP8    6QZP   
Human Protein Atlas [tissue]ENSG00000149806-FAU [tissue]
Peptide AtlasP62861
IPIIPI00383379   IPI00982652   IPI00973736   IPI00974466   IPI00974363   IPI00975495   
Protein Interaction databases
IntAct (EBI)P62861
Complex Portal (EBI)P62861 CPX-5223 40S cytosolic small ribosomal subunit
Ontologies - Pathways
Ontology : AmiGORNA binding  cellular_component  biological_process  
Ontology : EGO-EBIRNA binding  cellular_component  biological_process  
Pathways : KEGGRibosome   
REACTOMEP62861 [protein]
REACTOME PathwaysR-HSA-975957 [pathway]   
NDEx NetworkFAU
Atlas of Cancer Signalling NetworkFAU
Wikipedia pathwaysFAU
Orthology - Evolution
GeneTree (enSembl)ENSG00000149806
Phylogenetic Trees/Animal Genes : TreeFamFAU
Homologs : HomoloGeneFAU
Homology/Alignments : Family Browser (UCSC)FAU
Gene fusions - Rearrangements
Fusion : Fusion_HubANKRD11--FAU    APOL6--FAU    ASXL2--FAU    C9ORF37--FAU    DYNC1H1--FAU    FAU--BAD    FAU--CALR    FAU--CNOT2    FAU--FAUP1    FAU--FLNA    FAU--MIR5095    FAU--MRPL16    FAU--NR2F6    FAU--PLIN3    FAU--RPL8   
FAU--SKIL    FAU--SRRM1    FAU--VPS51    HBA1--FAU    HBA2--FAU    IDE--FAU    IPO13--FAU    KIF18A--FAU    PRKDC--FAU    PTPRC--FAU    PTPRD--FAU    RIMBP2--FAU    RPL38--FAU    RPL4--FAU    RPL5--FAU   
Fusion : QuiverFAU
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFAU [hg38]
Exome Variant ServerFAU
GNOMAD BrowserENSG00000149806
Varsome BrowserFAU
Genomic Variants (DGV)FAU [DGVbeta]
DECIPHERFAU [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFAU 
ICGC Data PortalFAU 
TCGA Data PortalFAU 
Broad Tumor PortalFAU
OASIS PortalFAU [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFAU  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DFAU
Mutations and Diseases : HGMDFAU
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch FAU
DgiDB (Drug Gene Interaction Database)FAU
DoCM (Curated mutations)FAU (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FAU (select a term)
NCG6 (London) select FAU
Cancer3DFAU(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry FAU
NextProtP62861 [Medical]
Target ValidationFAU
Huge Navigator FAU [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTD
Pharm GKB GenePA28010
Clinical trialFAU
canSAR (ICR)FAU (select the gene name)
DataMed IndexFAU
PubMed65 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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indexed on : Fri Jan 1 18:51:37 CET 2021

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