Q9ERG0 (LIMA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 88.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: LIM domain and actin-binding protein 1 Alternative name(s): Epithelial protein lost in neoplasm Short name=mEPLIN | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 753 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments By similarity. |
| Subcellular location | Cytoplasm. Cytoplasm › cytoskeleton. Note: This cytoskeletal protein colocalizes with actin stress fibers. |
| Tissue specificity | Isoform Alpha is highly expressed in embryos from day 7-11 and in adult spleen and lung. Isoform Beta expression is highest in adult kidney, testis, lung and liver, intermediate in heart, brain, spleen, skeletal muscle and low in embryos. |
| Domain | Contains at least 2 actin-binding domains, one on each side of the LIM domain. Both domains bind actin monomers and filaments. The C-terminal domain binds filaments more efficiently than the N-terminus By similarity. |
| Sequence similarities | Contains 1 LIM zinc-binding domain. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select] | ||||||
| Isoform Beta (identifier: Q9ERG0-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Alpha (identifier: Q9ERG0-2) The sequence of this isoform differs from the canonical sequence as follows: 1-160: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 753 | 753 | LIM domain and actin-binding protein 1 | PRO_0000075731 | |||||
Regions | |||||||||
| Domain | 386 – 446 | 61 | LIM zinc-binding | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 15 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 132 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 225 | 1 | Phosphoserine Ref.5 Ref.7 | ||||||
| Modified residue | 230 | 1 | Phosphoserine Ref.5 Ref.7 | ||||||
| Modified residue | 263 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 348 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 360 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 367 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 372 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 467 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 485 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 488 | 1 | Phosphoserine Ref.5 Ref.6 Ref.7 Ref.9 | ||||||
| Modified residue | 539 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 602 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 607 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 615 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 692 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 720 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 735 | 1 | Phosphoserine Ref.8 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 160 | 160 | Missing in isoform Alpha. | VSP_003118 | |||||
Experimental info | |||||||||
| Sequence conflict | 216 | 1 | S → N in AAG31148. Ref.1 | ||||||
| Sequence conflict | 325 | 1 | T → A in AAG31147. Ref.1 | ||||||
| Sequence conflict | 486 | 1 | P → S in AAG31147. Ref.1 | ||||||
| Sequence conflict | 499 | 1 | V → A in AAG31147. Ref.1 | ||||||
| Sequence conflict | 538 | 1 | G → S in AAG31147. Ref.1 | ||||||
| Sequence conflict | 605 | 1 | A → T in AAG31147. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of mouse epithelial protein lost in neoplasm (EPLIN) and comparison of mammalian and zebrafish EPLIN." Maul R.S., Sachi Gerbin C., Chang D.D. Gene 262:155-160(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). |
| [2] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor. |
| [4] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, MASS SPECTROMETRY. Tissue: Liver. |
| [5] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-230; SER-367; SER-485; SER-488 AND SER-615, MASS SPECTROMETRY. Tissue: Liver. |
| [6] | "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Liver. |
| [7] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-230; SER-467 AND SER-488, MASS SPECTROMETRY. Tissue: Melanoma. |
| [8] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, MASS SPECTROMETRY. Tissue: Macrophage. |
| [9] | "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF307844 mRNA. Translation: AAG31147.1. AF307845 mRNA. Translation: AAG31148.1. BC031490 mRNA. Translation: AAH31490.1. CH466550 Genomic DNA. Translation: EDL04110.1. |
| IPI | IPI00112339. IPI00759925. |
| RefSeq | NP_001107017.1. NM_001113545.1. |
| UniGene | Mm.33207. |
3D structure databases | |
| ProteinModelPortal | Q9ERG0. |
| SMR | Q9ERG0. Positions 372-455. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-29634N. DIP-29637N. |
| IntAct | Q9ERG0. 1 interaction. |
| MINT | MINT-4094516. |
PTM databases | |
| PhosphoSite | Q9ERG0. |
Proteomic databases | |
| PaxDb | Q9ERG0. |
| PRIDE | Q9ERG0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000073691; ENSMUSP00000073371; ENSMUSG00000023022. ENSMUST00000109024; ENSMUSP00000104652; ENSMUSG00000023022. |
| GeneID | 65970. |
| KEGG | mmu:65970. |
| UCSC | uc007xqh.2. mouse. |
Organism-specific databases | |
| CTD | 51474. |
| MGI | MGI:1920992. Lima1. |
Phylogenomic databases | |
| eggNOG | NOG238020. |
| GeneTree | ENSGT00510000046839. |
| HOGENOM | HOG000059621. |
| HOVERGEN | HBG051492. |
| InParanoid | Q8K2H0. |
| OMA | WPPEDEI. |
| OrthoDB | EOG44XJG7. |
Gene expression databases | |
| ArrayExpress | Q9ERG0. |
| Bgee | Q9ERG0. |
| CleanEx | MM_LIMA1. |
| Genevestigator | Q9ERG0. |
| GermOnline | ENSMUSG00000023022. Mus musculus. |
Family and domain databases | |
| Gene3D | 2.10.110.10. 1 hit. |
| InterPro | IPR001781. Znf_LIM. [Graphical view] |
| Pfam | PF00412. LIM. 1 hit. [Graphical view] |
| SMART | SM00132. LIM. 1 hit. [Graphical view] |
| PROSITE | PS00478. LIM_DOMAIN_1. 1 hit. PS50023. LIM_DOMAIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | LIMA1. mouse. |
| NextBio | 320412. |
| SOURCE | Search... |
Entry information
| Entry name | LIMA1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9ERG0 Secondary accession number(s): Q8K2H0, Q9ERG1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
