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Q9ERG0 (LIMA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LIM domain and actin-binding protein 1
Alternative name(s):
Epithelial protein lost in neoplasm
Short name=mEPLIN
Gene names
Name:Lima1
Synonyms:D15Ertd366e, Eplin
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Cytoplasmcytoskeleton. 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753LIM domain and actin-binding protein 1
PRO_0000075731

Regions

Domain386 – 44661LIM zinc-binding

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue151Phosphoserine By similarity
Modified residue1321Phosphoserine By similarity
Modified residue2251Phosphoserine Ref.4 Ref.6
Modified residue2301Phosphoserine Ref.4
Modified residue2631Phosphoserine By similarity
Modified residue3481Phosphoserine By similarity
Modified residue3601Phosphoserine Ref.4
Modified residue3671Phosphoserine By similarity
Modified residue3721Phosphoserine By similarity
Modified residue4371N6-succinyllysine Ref.8
Modified residue4851Phosphoserine Ref.4
Modified residue4881Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7
Modified residue6021Phosphoserine By similarity
Modified residue6071Phosphoserine By similarity
Modified residue6151Phosphoserine By similarity
Modified residue6921Phosphoserine By similarity
Modified residue7201Phosphoserine By similarity

Natural variations

Alternative sequence1 – 160160Missing in isoform Alpha.
VSP_003118

Experimental info

Sequence conflict2161S → N in AAG31148. Ref.1
Sequence conflict3251T → A in AAG31147. Ref.1
Sequence conflict4861P → S in AAG31147. Ref.1
Sequence conflict4991V → A in AAG31147. Ref.1
Sequence conflict5381G → S in AAG31147. Ref.1
Sequence conflict6051A → T in AAG31147. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 79F98E47C100CF22

FASTA75384,060
        10         20         30         40         50         60 
MESTPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEEANM ERKKNNPESL 

        70         80         90        100        110        120 
PQHFRRGTLS VLKKKWENPV AGAEFHTDSL PNSSSEGGHT ADYPPAEVTD KPAPGVRADR 

       130        140        150        160        170        180 
EEHTQPKPRF GSRPEAVIQS RYPRSENSHD FKAQATESQK MENCLGDSRH EAEKPETSEN 

       190        200        210        220        230        240 
TETSGKIEKY NVPLNRLKMM FEKGEHNQTK SLWTQSRNAG GRRLSENNCS LDDWEIGAGH 

       250        260        270        280        290        300 
LSSSAFNSEK NESKRNLELP RLSETSIKDR MAKYQAAVSK QSSPASYTNE LKTSESKTHK 

       310        320        330        340        350        360 
WEQKENVPPG PEACSVHQEG SKVSTTENSL VALSVPAEDD TCNSQVKSEA QQPMHPKPLS 

       370        380        390        400        410        420 
PDARTSSLPE SSPSKTAKKF QAPAKESCVE CQKTVYPMER LLANQQVFHI SCFRCSYCNN 

       430        440        450        460        470        480 
KLSLGTYASL HGRIYCKPHF NQLFKSKGNY DEGFGHKQHK DLWASKSDNE ETLGRPAQPP 

       490        500        510        520        530        540 
NAGESPHSPG VEDAPIAKVG VLAASMEAKA SSQREREDKP AETKKLRIAW PPPAELGGSG 

       550        560        570        580        590        600 
SALEEGIKVS KPKWPPEDDV CKTEAPEDVD LDLKKLRRSS SLKERSRPFT VAASFRTSSI 

       610        620        630        640        650        660 
KSPKASSPSL RKGWSESEQS EEFGGGIATM ERKQTENARP SGEKENVGKS RWQGEEVPRS 

       670        680        690        700        710        720 
KDRSSFELES ENFMENGANI AEDDNHVHAQ QSPLEPEAPG WSGFVDTTAA KEFTTQNQKS 

       730        740        750 
QDVGFWEGEV VRELSVEEQI KRNRYYDEDE DEE 

« Hide

Isoform Alpha [UniParc].

Checksum: 122AB8AA07E1FC0A
Show »

FASTA59366,018

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]"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-360; SER-485 AND SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"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-225 AND SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS37206.1. [Q9ERG0-2]
CCDS49729.1. [Q9ERG0-1]
RefSeqNP_001107017.1. NM_001113545.1. [Q9ERG0-1]
UniGeneMm.33207.

3D structure databases

ProteinModelPortalQ9ERG0.
SMRQ9ERG0. Positions 372-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211164. 4 interactions.
DIPDIP-29634N.
DIP-29637N.
IntActQ9ERG0. 4 interactions.
MINTMINT-4094516.

PTM databases

PhosphoSiteQ9ERG0.

Proteomic databases

MaxQBQ9ERG0.
PaxDbQ9ERG0.
PRIDEQ9ERG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073691; ENSMUSP00000073371; ENSMUSG00000023022. [Q9ERG0-1]
ENSMUST00000109024; ENSMUSP00000104652; ENSMUSG00000023022. [Q9ERG0-2]
GeneID65970.
KEGGmmu:65970.
UCSCuc007xqh.2. mouse. [Q9ERG0-1]

Organism-specific databases

CTD51474.
MGIMGI:1920992. Lima1.

Phylogenomic databases

eggNOGNOG238020.
GeneTreeENSGT00510000046839.
HOGENOMHOG000059621.
HOVERGENHBG051492.
InParanoidQ8K2H0.
OMADEISKPE.
OrthoDBEOG7PCJH8.
TreeFamTF350273.

Gene expression databases

ArrayExpressQ9ERG0.
BgeeQ9ERG0.
CleanExMM_LIMA1.
GenevestigatorQ9ERG0.

Family and domain databases

Gene3D2.10.110.10. 1 hit.
InterProIPR028740. EPLIN.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERPTHR24206:SF27. PTHR24206:SF27. 1 hit.
PfamPF00412. LIM. 1 hit.
[Graphical view]
SMARTSM00132. LIM. 1 hit.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLIMA1. mouse.
NextBio320412.
PROQ9ERG0.
SOURCESearch...

Entry information

Entry nameLIMA1_MOUSE
AccessionPrimary (citable) accession number: Q9ERG0
Secondary accession number(s): Q8K2H0, Q9ERG1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot