ABLIM1

Protein-coding gene in the species Homo sapiens
ABLIM1
Identifiers
AliasesABLIM1, ABLIM, LIMAB1, LIMATIN, abLIM-1, actin binding LIM protein 1
External IDsOMIM: 602330; MGI: 1194500; HomoloGene: 40994; GeneCards: ABLIM1; OMA:ABLIM1 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for ABLIM1
Genomic location for ABLIM1
Band10q25.3Start114,431,112 bp[1]
End114,768,061 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for ABLIM1
Genomic location for ABLIM1
Band19 D2|19 52.09 cMStart57,021,165 bp[2]
End57,303,351 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • myocardium of left ventricle

  • cerebellar vermis

  • cardiac muscle tissue of right atrium

  • right ventricle

  • mucosa of pharynx

  • cerebellar hemisphere

  • parotid gland

  • gums

  • gingival epithelium

  • oral cavity
Top expressed in
  • cardiac muscle tissue of left ventricle

  • conjunctival fornix

  • right ventricle

  • thymus

  • lobe of cerebellum

  • cerebellar vermis

  • esophagus

  • epithelium of stomach

  • mesenteric lymph nodes

  • subcutaneous adipose tissue
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • actin binding
  • protein binding
  • metal ion binding
  • actin filament binding
Cellular component
  • cytoplasm
  • lamellipodium
  • cytoskeleton
  • stress fiber
  • actin cytoskeleton
Biological process
  • animal organ morphogenesis
  • cytoskeleton organization
  • lamellipodium assembly
  • visual perception
  • cilium assembly
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3983

226251

Ensembl

ENSG00000099204

ENSMUSG00000025085

UniProt

O14639

Q8K4G5

RefSeq (mRNA)
NM_001003407
NM_001003408
NM_002313
NM_006720
NM_001322882

NM_001322883
NM_001322884
NM_001322885
NM_001322886
NM_001322887
NM_001322888
NM_001322889
NM_001322890
NM_001322891
NM_001322892
NM_001322893
NM_001322894
NM_001322895
NM_001322896
NM_001322897
NM_001322898
NM_001322899
NM_001322900
NM_001352440
NM_001352441
NM_001352442
NM_001352443

NM_001103177
NM_001103178
NM_001290813
NM_001290815
NM_001290816

NM_178688
NM_001347459
NM_001362445
NM_001362446

RefSeq (protein)
NP_001003407
NP_001309811
NP_001309812
NP_001309813
NP_001309814

NP_001309815
NP_001309816
NP_001309817
NP_001309818
NP_001309819
NP_001309820
NP_001309821
NP_001309822
NP_001309823
NP_001309824
NP_001309825
NP_001309826
NP_001309827
NP_001309828
NP_001309829
NP_002304
NP_006711
NP_001339369
NP_001339370
NP_001339371
NP_001339372

NP_001096647
NP_001096648
NP_001277742
NP_001277744
NP_001277745

NP_001334388
NP_848803
NP_001349374
NP_001349375

Location (UCSC)Chr 10: 114.43 – 114.77 MbChr 19: 57.02 – 57.3 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Actin binding LIM protein 1, also known as ABLIM1, is a protein which in humans is encoded by the ABLIM1 gene.[5][6]

Function

This gene encodes a cytoskeletal LIM protein that binds to actin filaments via a domain that is homologous to erythrocyte dematin. LIM domains, found in over 60 proteins, play key roles in the regulation of developmental pathways. LIM domains also function as protein-binding interfaces, mediating specific protein-protein interactions. The protein encoded by this gene could mediate such interactions between actin filaments and cytoplasmic targets. Alternatively spliced transcript variants encoding different isoforms have been identified.[5]

Interactions

ABLIM1 has been shown to interact with LDOC1.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000099204 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025085 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: ABLIM1 actin binding LIM protein 1".
  6. ^ Roof DJ, Hayes A, Adamian M, Chishti AH, Li T (August 1997). "Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein". The Journal of Cell Biology. 138 (3): 575–88. doi:10.1083/jcb.138.3.575. PMC 2141644. PMID 9245787.
  7. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

Further reading

  • Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
  • Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (September 1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
  • Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
  • Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Roof DJ, Hayes A, Adamian M, Chishti AH, Li T (August 1997). "Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein". The Journal of Cell Biology. 138 (3): 575–88. doi:10.1083/jcb.138.3.575. PMC 2141644. PMID 9245787.
  • Kim AC, Peters LL, Knoll JH, Van Huffel C, Ciciotte SL, Kleyn PW, Chishti AH (December 1997). "Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse chromosome 19 and human chromosome 10q25, a region frequently deleted in human cancers". Genomics. 46 (2): 291–3. doi:10.1006/geno.1997.5029. PMID 9417918.
  • Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". The Journal of Biological Chemistry. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.
  • Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (May 2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Analytical Chemistry. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (August 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
  • Ficarro SB, Salomon AR, Brill LM, Mason DE, Stettler-Gill M, Brock A, Peters EC (2005). "Automated immobilized metal affinity chromatography/nano-liquid chromatography/electrospray ionization mass spectrometry platform for profiling protein phosphorylation sites". Rapid Communications in Mass Spectrometry. 19 (1): 57–71. Bibcode:2005RCMS...19...57F. doi:10.1002/rcm.1746. PMID 15570572.
  • Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (June 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
  • Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (August 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nature Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384. S2CID 20475874.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.



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