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LIMD1 (LIM domains containing 1)

Written2011-03Sybil CK Wong, Gregory D Longmore, Tyson V Sharp
Washington University School of Medicine, BJC-IH BRIGHT Institute, Campus Box 8069, 660 South Euclid Avenue, St Louis MO 63110, USA (GDL); School of Biomedical Sciences, University of Nottingham Medical School, Queen's Medical Centre, Nottingham, NG7 2UH, UK (SCKW, TVS)

(Note : for Links provided by Atlas : click)


LocusID (NCBI) 8994
Atlas_Id 41158
Location 3p21.31  [Link to chromosome band 3p21]
Location_base_pair Starts at 45594751 and ends at 45686340 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping LIMD1.png]
Local_order TMEM158, LARS2, LIMD1, SACM1L, SLC6A20, LZTFL1.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
LIMD1 (3p21.31) / DSP (6p24.3)LIMD1 (3p21.31) / LARS2 (3p21.31)PLEC (8q24.3) / LIMD1 (3p21.31)
SACM1L (3p21.31) / LIMD1 (3p21.31)VGLL4 (3p25.3) / LIMD1 (3p21.31)


  The eight exons of the LIMD1 gene are denoted by open rectangles; the protein coding regions of the exons are coloured in blue. Exons 2 to 8 encode three LIM domains in tandem. Exon 1 encodes the N-terminal pre-LIM region. Regions important for transcriptional regulation upstream of the start codon (ATG, +1) are denoted by black rectangles. Experimental evidence suggests that a negative regulatory element (-ve RE) occurs in the region between -2039 and -1539. The CpG island between -1299 and -439 contains a putative TATA box at -439 (yellow circle) and a 21-bp core promoter region at -727 (green circle).
Description The gene encompasses 86432 bp and lies in the plus strand, starting at 45636323 and ending at 45722754 bp from pter, within C3CER1 (chromosome 3 common eliminated region 1) at chromosome 3p21.3, a region frequently deleted in solid tumours. The 5'-promoter region includes a negative regulatory element and a CpG island that contains a putative TATA box and an experimentally validated core basal promoter region of 21 bp (Sharp et al., 2008). The core promoter region contains four CpG methylation sites (Sharp et al., 2008).
Transcription The transcript (NCBI ID: NM_014240.2) of 6284 bp comprises eight exons, the first of which encodes the N-terminal pre-LIM region. Exons 2 to 8 encode three LIM domains in tandem. The size of the open reading frame is 5129 bp.
Pseudogene None known.


  LIMD1 can be split primarily into the N-terminal pre-LIM region (residues 1 to 471) and the C-terminal triple LIM domains (residues 472 to 676). The pre-LIM region contains a proline/serine-rich region (residues 69 to 471), a LEM-like domain (residues 18 to 68), a nuclear export signal (NES, residues 54 to 134) and the binding site for pRB (residues 404 to 442). The three LIM domains are an inherent nuclear localisation signal (NLS, residues 472 to 676).
Description LIMD1 (676 amino acids, 72 kDa, NCBI ID: NP_055055.1) belongs to the Ajuba LIM protein subgroup of the Ajuba/Zyxin protein family. This six-member family (see Homology) is characterised by a varied proline-rich pre-LIM region at the N-terminus followed by three homologous LIM domains arranged in tandem at the C-terminus. LIM domains (InterPro ID: IPR001781) coordinate two zinc ions in a tandem zinc-finger topology and mediate protein-protein interactions (Kadrmas and Beckerle, 2004). The three LIM domains of LIMD1 are an inherent nuclear localisation signal (NLS) (Sharp et al., 2004). The pre-LIM region includes the pRB binding region and a nuclear export signal (NES) partially overlapping the N-terminal LEM-like domain (Sharp et al., 2004).
Expression LIMD1 is ubiquitously expressed, but at a lower level in the brain and testis (Kiss et al., 1999).
Localisation LIMD1 shuttles between the cytoplasm and nucleus, but is not found in the nucleoli (Sharp et al., 2004). In the cytoplasm, LIMD1 colocalises with focal adhesions (Huggins and Andrulis, 2008; Petit et al., 2005), adherens junctions (Das Thakur et al., 2010) and mRNA processing bodies (P-bodies) (James et al., 2010).
Function LIMD1 is involved in a range of cellular functions (listed below). A common theme is that LIMD1 acts as a protein-protein scaffold or mediator to facilitate signalling between cytoplasmic components and the nucleus. Functional redundancy between LIMD1 and the other Ajuba LIM proteins has also been proposed in a variety of cases (Das Thakur et al., 2010; Feng and Longmore, 2005; James et al., 2010; Langer et al., 2008).
- LIMD1 inhibits E2F-mediated transcription and thus cell proliferation via interaction with pRB and also via a pRB-independent mechanism that has yet to be clarified (Sharp et al., 2004).
- LIMD1 stimulates stress osteoclastogenesis (Feng et al., 2007) and regulates osteoblast differentiation and function (Luderer et al., 2008). LIMD1 can act as both a positive regulator of osteoclast and osteoblast development, by linking the p62/sequestosome protein and TRAF6 to form a p62/TRAF6/a-PKC complex which can activate NF-kB and AP-1 (Feng and Longmore, 2005; Feng et al., 2007), and a negative regulator of osteoblast differentiation, by repressing canonical Wnt/beta-catenin signalling in osteoblasts (Luderer et al., 2008).
- LIMD1 facilitates miRNA-mediated silencing by (i) binding to eIF4E to prevent recruitment of 4EBP1 and eIF4G to the mRNA 5' m(7)GTP cap, and (ii) creating an inhibitory closed-loop complex by acting as a scaffold to link eIF4E at the 5' cap to Ago1/Ago2 in the miRISC complex bound at the 3' UTR of mRNA (James et al., 2010).
- LIMD1 interacts with LATS/Warts and WW45/Sav to inhibit Hippo (Hpo) signalling pathway-mediated phosphorylation and nuclear-targeting of YAP/Yki (Das Thakur et al., 2010). Implication of the Hpo pathway in cell contact growth inhibition, and the observation that in confluent cells with no further proliferation, Ajuba LIM proteins gather at adherens junctions whilst YAP is phosphorylated and returned to the cytosol has led Das Thakur et al. (2010) to propose that Ajuba LIM proteins "release" LATS/Warts upon localisation at adherens junctions, leading to growth inhibition.
- In the nucleus, LIMD1 interacts with the SNAG domain of Snail/Slug transcriptional repressors and acts as a co-repressor of E-cadherin and other Snail-regulated genes to affect neural crest development and possibly epithelial-mesenchymal transitions (Langer et al., 2008).
- Huggins and Andrulis (2008) suggested that LIMD1 may play a part in cell anchoring as a component of focal adhesions and in the cell cycle (especially during mitosis), based on the respective observations that LIMD1 colocalises with vinculin at focal adhesions and that phosphorylation of LIMD1 occurs during mitosis in HeLa cells.
Homology The phylogenetic tree below shows the evolutionary distance (as inferred from amino acid sequence) between LIMD1 and the five other members of the Ajuba/Zyxin protein family (James et al., 2010).
LIMD1 is most closely related to the other Ajuba LIM proteins, Ajuba and WTIP (respectively 41% and 39% identity overall and 64% and 72% identity in the LIM domains). In contrast, LIMD1 shares only 32%, 33% and 34% identity overall and 43%, 46% and 41% identity in the LIM domains with the Zyxin LIM proteins, Zyxin, LPP and TRIP6 respectively.
The orthologue of LIMD1 in mus musculus shares 77% identity overall and 96% identity in the LIM domains with human LIMD1.

Implicated in

Entity Lung cancer
Disease Lung cancer is the primary cause of cancer-related deaths worldwide. Although smoking is the major trigger for lung cancer, another important risk factor involves exposure to harmful air-borne particles, such as asbestos or industrial pollutants.
Cytogenetics Loss of coding sequence from chromosome 3p is one of the most common mutations found in both small cell (almost 100%) and non-small cell (almost 90%) lung cancers. The C3CER1 region (containing LIMD1) of chromosome 3p21.3 is more frequently deleted in solid malignancies than any of the other 3p regions studied (Petursdottir et al., 2004). Particularly in lung tumours, loss of heterozygosity (LOH) at C3CER1 (over 90%) exceeds that of tumour suppressor gene (TSG) VHL (72%) and putative TSG FHIT (65%) (Petursdottir et al., 2004). Homozygous gene deletion, LOH and epigenetic silencing via promoter hypermethylation - but not coding sequence mutations - contribute towards reduced expression of LIMD1 in human lung tumours (Sharp et al., 2008).
Oncogenesis The expression of LIMD1, a bona fide lung tumour suppressor, was down-regulated in all lung cancers analysed compared with normal tissue (Sharp et al., 2008). From a genetic perspective, increased lung tumour incidence and volume was observed in the offspring of LIMD1 knockout (Limd1-/-) mice cross bred with K-RasG12D mice, an established K-Ras-induced lung cancer model (Sharp et al., 2008). LIMD1, which interacts with pRB to repress E2F-responsive transcription, reduces cell proliferation in vitro and incidence of lung metastases in vivo (Sharp et al., 2004). Loss of LIMD1 expression leading to misregulation of pRB and the cell cycle may therefore be an early critical step in lung tumour development (Sharp et al., 2004).
Entity Breast cancer
Disease Breast cancer is the leading cause of cancer-related deaths of women in the western world. Increasing age, non-vegetarian diets, social class, nulliparity and familial history of breast cancer have been observed to increase the probability of breast cancer development.
Prognosis LIMD1 has been proposed to be a prognostic marker for breast cancer, as absence of nuclear LIMD1 staining correlates strongly to poor tumour prognosis and patient mortality (Spendlove et al., 2008).
Cytogenetics Although alteration or deletion of chromosome 3p is common in breast cancers, LIMD1 was not mutated or deleted in most of the breast tumours analysed (Huggins et al., 2007) and LIMD1 mRNA levels were also found to be unchanged in breast cancers compared to normal tissues (Huggins and Andrulis, 2008).
Oncogenesis Delocalisation of LIMD1 from the nucleus may contribute to breast cancer progression, as nuclear LIMD1 acts as a Snail co-repressor of E-cadherin expression and Snail-mediated repression of E-cadherin has been implicated in tumour metastasis (Langer et al., 2008; Spendlove et al., 2008).
Entity Head and neck squamous cell carcinoma (HNSCC)
Disease HNSCCs account for 90% of all head and neck cancers and 30-40% of cancer types in Indian patients. Globally, over 0,5 million new cases are diagnosed every year. Risk factors include smoking, alcohol, betel nut leaf liquid, HPV-16/18 infection and inadequate oral hygiene.
Prognosis Ghosh et al. (2010) have suggested LIMD1 as a "predictive clinical marker" for HNSCC from their multivariate analysis showing significant correlation of LIMD1 alteration (deletion/methylation/mutation) to poor prognosis in HPV-negative patients addicted to tobacco.
Cytogenetics Loss of heterozygosity in chromosome 3p21.3 was found to be highly frequent in Indian HNSCC patients (Ghosh et al., 2008). The same group later reported alteration of LIMD1 in the majority of HNSCC samples studied, and increasing mutation, but not deletion or methylation, with tumour progression (Ghosh et al., 2010). Six mutations in exon 1, an intron 4/exon 5 splice-junction mutation in LIMD1 and a (CA)20 polymorphism of the hmlimd1 microsatellite marker were reported, some of which lead to non-functional LIMD1 or reduced expression of LIMD1 (Ghosh et al., 2010).
Oncogenesis Ghosh et al. (2010) have proposed that repression of LIMD1, rather than pRB, is crucial for HNSCC development, due to the higher frequency of LIMD1 alterations compared with pRB alterations in the HNSCC samples analysed and better survival of patients with LIMD1+/pRB- compared with LIMD1-/pRB+.
Entity Paget's disease of the bone (paget's disease)
Disease Paget's disease involves pathological bone resorption triggering compensatory osteoblast activity, which results in the formation of hypercellular, deformed bones. This chronic disease can be familial or sporadic.
Prognosis In the regulation of osteoclast and osteoblast development, LIMD1 interacts with cytosolic protein p62, which is sometimes mutated in Paget's disease (Feng et al., 2007; Luderer et al., 2008). As none of the reported Pagetic mutations of p62 are predicted to affect its binding to LIMD1, and coinciding phenotypes were observed between LIMD1-null mice and p62-null mice, it was suggested that LIMD1 may act as a complex with mutated p62 in the development of Paget's disease (Feng et al., 2007; Luderer et al., 2008).


Note N/A.

To be noted



Ajuba LIM proteins are negative regulators of the Hippo signaling pathway.
Das Thakur M, Feng Y, Jagannathan R, Seppa MJ, Skeath JB, Longmore GD.
Curr Biol. 2010 Apr 13;20(7):657-62. Epub 2010 Mar 18.
PMID 20303269
The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex.
Feng Y, Longmore GD.
Mol Cell Biol. 2005 May;25(10):4010-22.
PMID 15870274
The LIM protein, Limd1, regulates AP-1 activation through an interaction with Traf6 to influence osteoclast development.
Feng Y, Zhao H, Luderer HF, Epple H, Faccio R, Ross FP, Teitelbaum SL, Longmore GD.
J Biol Chem. 2007 Jan 5;282(1):39-48. Epub 2006 Nov 8.
PMID 17092936
LIMD1 is more frequently altered than RB1 in head and neck squamous cell carcinoma: clinical and prognostic implications.
Ghosh S, Ghosh A, Maiti GP, Mukherjee N, Dutta S, Roy A, Roychoudhury S, Panda CK.
Mol Cancer. 2010 Mar 12;9:58.
PMID 20226061
Cell cycle regulated phosphorylation of LIMD1 in cell lines and expression in human breast cancers.
Huggins CJ, Andrulis IL.
Cancer Lett. 2008 Aug 18;267(1):55-66. Epub 2008 Apr 24.
PMID 18439753
LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing.
James V, Zhang Y, Foxler DE, de Moor CH, Kong YW, Webb TM, Self TJ, Feng Y, Lagos D, Chu CY, Rana TM, Morley SJ, Longmore GD, Bushell M, Sharp TV.
Proc Natl Acad Sci U S A. 2010 Jul 13;107(28):12499-504. Epub 2010 Jun 28.
PMID 20616046
The LIM domain: from the cytoskeleton to the nucleus.
Kadrmas JL, Beckerle MC.
Nat Rev Mol Cell Biol. 2004 Nov;5(11):920-31. (REVIEW)
PMID 15520811
Inactivation of the human fragile histidine triad gene at 3p14.2 in monochromosomal human/mouse microcell hybrid-derived severe combined immunodeficient mouse tumors.
Kholodnyuk ID, Szeles A, Yang Y, Klein G, Imreh S.
Cancer Res. 2000 Dec 15;60(24):7119-25.
PMID 11156420
A novel gene containing LIM domains (LIMD1) is located within the common eliminated region 1 (C3CER1) in 3p21.3.
Kiss H, Kedra D, Yang Y, Kost-Alimova M, Kiss C, O'Brien KP, Fransson I, Klein G, Imreh S, Dumanski JP.
Hum Genet. 1999 Dec;105(6):552-9.
PMID 10647888
Ajuba LIM proteins are snail/slug corepressors required for neural crest development in Xenopus.
Langer EM, Feng Y, Zhaoyuan H, Rauscher FJ 3rd, Kroll KL, Longmore GD.
Dev Cell. 2008 Mar;14(3):424-36.
PMID 18331720
The LIM protein LIMD1 influences osteoblast differentiation and function.
Luderer HF, Bai S, Longmore GD.
Exp Cell Res. 2008 Sep 10;314(15):2884-94. Epub 2008 Jun 9.
PMID 18657804
The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins.
Petit MM, Crombez KR, Vervenne HB, Weyns N, Van de Ven WJ.
FEBS Lett. 2005 Sep 12;579(22):5061-8.
PMID 16137684
Interstitial deletions including chromosome 3 common eliminated region 1 (C3CER1) prevail in human solid tumors from 10 different tissues.
Petursdottir TE, Thorsteinsdottir U, Jonasson JG, Moller PH, Huiping C, Bjornsson J, Egilsson V, Imreh S, Ingvarsson S.
Genes Chromosomes Cancer. 2004 Nov;41(3):232-42.
PMID 15334546
The chromosome 3p21.3-encoded gene, LIMD1, is a critical tumor suppressor involved in human lung cancer development.
Sharp TV, Al-Attar A, Foxler DE, Ding L, de A Vallim TQ, Zhang Y, Nijmeh HS, Webb TM, Nicholson AG, Zhang Q, Kraja A, Spendlove I, Osborne J, Mardis E, Longmore GD.
Proc Natl Acad Sci U S A. 2008 Dec 16;105(50):19932-7. Epub 2008 Dec 5.
PMID 19060205
LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at chromosome 3p21.3, binds pRB and represses E2F-driven transcription.
Sharp TV, Munoz F, Bourboulia D, Presneau N, Darai E, Wang HW, Cannon M, Butcher DN, Nicholson AG, Klein G, Imreh S, Boshoff C.
Proc Natl Acad Sci U S A. 2004 Nov 23;101(47):16531-6. Epub 2004 Nov 12.
PMID 15542589
Differential subcellular localisation of the tumour suppressor protein LIMD1 in breast cancer correlates with patient survival.
Spendlove I, Al-Attar A, Watherstone O, Webb TM, Ellis IO, Longmore GD, Sharp TV.
Int J Cancer. 2008 Nov 15;123(10):2247-53.
PMID 18712738
Genetic abnormalities involved in t(12;21) TEL-AML1 acute lymphoblastic leukemia: analysis by means of array-based comparative genomic hybridization.
Tsuzuki S, Karnan S, Horibe K, Matsumoto K, Kato K, Inukai T, Goi K, Sugita K, Nakazawa S, Kasugai Y, Ueda R, Seto M.
Cancer Sci. 2007 May;98(5):698-706. Epub 2007 Mar 21.
PMID 17374122


This paper should be referenced as such :
Wong, SCK ; Longmore, GD ; Sharp, TV
LIMD1 (LIM domains containing 1)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(10):843-847.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)LIMD1   6612
Entrez_Gene (NCBI)LIMD1    LIM domain containing 1
GeneCards (Weizmann)LIMD1
Ensembl hg19 (Hinxton)ENSG00000144791 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000144791 [Gene_View]  ENSG00000144791 [Sequence]  chr3:45594751-45686340 [Contig_View]  LIMD1 [Vega]
ICGC DataPortalENSG00000144791
TCGA cBioPortalLIMD1
Genatlas (Paris)LIMD1
SOURCE (Princeton)LIMD1
Genetics Home Reference (NIH)LIMD1
Genomic and cartography
GoldenPath hg38 (UCSC)LIMD1  -     chr3:45594751-45686340 +  3p21.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)LIMD1  -     3p21.31   [Description]    (hg19-Feb_2009)
GoldenPathLIMD1 - 3p21.31 [CytoView hg19]  LIMD1 - 3p21.31 [CytoView hg38]
genome Data Viewer NCBILIMD1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AJ132408 AK021508 BC027712 BC117236 BC117238
RefSeq transcript (Entrez)NM_014240
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)LIMD1
Alternative Splicing GalleryENSG00000144791
Gene ExpressionLIMD1 [ NCBI-GEO ]   LIMD1 [ EBI - ARRAY_EXPRESS ]   LIMD1 [ SEEK ]   LIMD1 [ MEM ]
Gene Expression Viewer (FireBrowse)LIMD1 [ Firebrowse - Broad ]
GenevisibleExpression of LIMD1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)8994
GTEX Portal (Tissue expression)LIMD1
Human Protein AtlasENSG00000144791-LIMD1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UGP4   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UGP4  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UGP4
Splice isoforms : SwissVarQ9UGP4
Domaine pattern : Prosite (Expaxy)LIM_DOMAIN_1 (PS00478)    LIM_DOMAIN_2 (PS50023)   
Domains : Interpro (EBI)LIMD1    Znf_LIM   
Domain families : Pfam (Sanger)LIM (PF00412)   
Domain families : Pfam (NCBI)pfam00412   
Domain families : Smart (EMBL)LIM (SM00132)  
Conserved Domain (NCBI)LIMD1
Blocks (Seattle)LIMD1
Human Protein Atlas [tissue]ENSG00000144791-LIMD1 [tissue]
Peptide AtlasQ9UGP4
IPIIPI00003369   IPI00925873   
Protein Interaction databases
IntAct (EBI)Q9UGP4
Ontologies - Pathways
Ontology : AmiGO"P-body  P-body  response to hypoxia  response to hypoxia  osteoblast development  transcription corepressor activity  transcription corepressor activity  protein binding  nucleus  nucleus  nucleoplasm  transcription regulator complex  cytoplasm  cytosol  plasma membrane  adherens junction  adherens junction  focal adhesion  regulation of transcription, DNA-templated  cytoskeleton organization  cytoskeleton organization  regulation of cell shape  phosphorylation  RISC complex  cell migration  P-body assembly  gene silencing by miRNA  negative regulation of hippo signaling  negative regulation of hippo signaling  negative regulation of osteoblast differentiation  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  metal ion binding  regulation of transcription from RNA polymerase II promoter in response to hypoxia  negative regulation of canonical Wnt signaling pathway  positive regulation of gene silencing by miRNA  positive regulation of gene silencing by miRNA"  
Ontology : EGO-EBI"P-body  P-body  response to hypoxia  response to hypoxia  osteoblast development  transcription corepressor activity  transcription corepressor activity  protein binding  nucleus  nucleus  nucleoplasm  transcription regulator complex  cytoplasm  cytosol  plasma membrane  adherens junction  adherens junction  focal adhesion  regulation of transcription, DNA-templated  cytoskeleton organization  cytoskeleton organization  regulation of cell shape  phosphorylation  RISC complex  cell migration  P-body assembly  gene silencing by miRNA  negative regulation of hippo signaling  negative regulation of hippo signaling  negative regulation of osteoblast differentiation  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  metal ion binding  regulation of transcription from RNA polymerase II promoter in response to hypoxia  negative regulation of canonical Wnt signaling pathway  positive regulation of gene silencing by miRNA  positive regulation of gene silencing by miRNA"  
Pathways : KEGGHippo signaling pathway   
REACTOMEQ9UGP4 [protein]
REACTOME PathwaysR-HSA-1234176 [pathway]   
NDEx NetworkLIMD1
Atlas of Cancer Signalling NetworkLIMD1
Wikipedia pathwaysLIMD1
Orthology - Evolution
GeneTree (enSembl)ENSG00000144791
Phylogenetic Trees/Animal Genes : TreeFamLIMD1
Homologs : HomoloGeneLIMD1
Homology/Alignments : Family Browser (UCSC)LIMD1
Gene fusions - Rearrangements
Fusion : MitelmanLIMD1/LARS2 [3p21.31/3p21.31]  
Fusion : MitelmanSACM1L/LIMD1 [3p21.31/3p21.31]  
Fusion : MitelmanVGLL4/LIMD1 [3p25.3/3p21.31]  
Fusion PortalLIMD1 3p21.31 LARS2 3p21.31 LUAD
Fusion PortalSACM1L 3p21.31 LIMD1 3p21.31 BRCA
Fusion PortalVGLL4 3p25.3 LIMD1 3p21.31 BLCA
Fusion : Fusion_HubAGO3--LIMD1    CIC--LIMD1    DHX30--LIMD1    GPRC5B--LIMD1    IGK@--LIMD1    LARS2--LIMD1    LIMD1--ADAMTS13    LIMD1--DSP    LIMD1--ITPR3    LIMD1--LARS2    LIMD1--SSH2    NBPF15--LIMD1    PLEC--LIMD1    SACM1L--LIMD1    STT3B--LIMD1   
Fusion : QuiverLIMD1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerLIMD1 [hg38]
Exome Variant ServerLIMD1
GNOMAD BrowserENSG00000144791
Varsome BrowserLIMD1
Genomic Variants (DGV)LIMD1 [DGVbeta]
DECIPHERLIMD1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisLIMD1 
ICGC Data PortalLIMD1 
TCGA Data PortalLIMD1 
Broad Tumor PortalLIMD1
OASIS PortalLIMD1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICLIMD1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DLIMD1
Mutations and Diseases : HGMDLIMD1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch LIMD1
DgiDB (Drug Gene Interaction Database)LIMD1
DoCM (Curated mutations)LIMD1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)LIMD1 (select a term)
NCG6 (London) select LIMD1
Cancer3DLIMD1(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry LIMD1
NextProtQ9UGP4 [Medical]
Target ValidationLIMD1
Huge Navigator LIMD1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTD
Pharm GKB GenePA30385
Clinical trialLIMD1
canSAR (ICR)LIMD1 (select the gene name)
DataMed IndexLIMD1
PubMed59 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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