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Protein

LIM domain transcription factor LMO4

Gene

Lmo4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable transcriptional factor.

GO - Molecular functioni

  • enhancer sequence-specific DNA binding Source: MGI
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of protein complex assembly Source: MGI
  • neural tube closure Source: UniProtKB
  • positive regulation of kinase activity Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of cell activation Source: MGI
  • regulation of cell fate specification Source: MGI
  • regulation of cell migration Source: UniProtKB
  • spinal cord association neuron differentiation Source: MGI
  • spinal cord motor neuron differentiation Source: MGI
  • thymus development Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
  • ventral spinal cord interneuron differentiation Source: MGI
  • ventricular septum development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
LIM domain transcription factor LMO4
Alternative name(s):
Breast tumor autoantigen
LIM domain only protein 4
Short name:
LMO-4
Gene namesi
Name:Lmo4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:109360. Lmo4.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: UniProtKB
  • transcription factor complex Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165LIM domain transcription factor LMO4PRO_0000075821Add
BLAST

Proteomic databases

EPDiP61969.
PaxDbiP61969.
PRIDEiP61969.

PTM databases

iPTMnetiP61969.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues.

Gene expression databases

BgeeiP61969.
CleanExiMM_LMO4.
ExpressionAtlasiP61969. baseline and differential.
GenevisibleiP61969. MM.

Interactioni

Subunit structurei

Interacts strongly with LDBS. Interacts with CLIM1 and CLIM2. Interacts (via the LIM zinc-binding domain 1) with RBBP8. Interacts with BRCA1 (via the BRCT domains); the interaction represses BRCA1 transcriptional activity. Interacts with DEAF1; LMO4 blocks export from nucleus.5 Publications

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi201180. 4 interactions.
STRINGi10090.ENSMUSP00000113513.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 263Combined sources
Beta strandi33 – 386Combined sources
Beta strandi41 – 433Combined sources
Helixi45 – 473Combined sources
Turni51 – 533Combined sources
Helixi57 – 604Combined sources
Beta strandi62 – 676Combined sources
Beta strandi70 – 723Combined sources
Helixi74 – 818Combined sources
Turni88 – 903Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi106 – 1094Combined sources
Helixi110 – 1123Combined sources
Turni116 – 1183Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi134 – 1374Combined sources
Helixi138 – 1403Combined sources
Turni143 – 1453Combined sources
Beta strandi158 – 1603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3VNMR-A16-86[»]
1RUTX-ray1.30X16-152[»]
2DFYX-ray1.65C/X18-161[»]
2MBVNMR-A77-147[»]
ProteinModelPortaliP61969.
SMRiP61969. Positions 19-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61969.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8361LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini87 – 14761LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG0490. Eukaryota.
ENOG410YIJ3. LUCA.
HOGENOMiHOG000232175.
HOVERGENiHBG054231.
InParanoidiP61969.
OMAiTIPANDY.
OrthoDBiEOG75J0PF.
PhylomeDBiP61969.
TreeFamiTF351071.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
[Graphical view]
SMARTiSM00132. LIM. 2 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNPGSSSQP PPVTAGSLSW KRCAGCGGKI ADRFLLYAMD SYWHSRCLKC
60 70 80 90 100
SCCQAQLGDI GTSCYTKSGM ILCRNDYIRL FGNSGACSAC GQSIPASELV
110 120 130 140 150
MRAQGNVYHL KCFTCSTCRN RLVPGDRFHY INGSLFCEHD RPTALINGHL
160
NSLQSNPLLP DQKVC
Length:165
Mass (Da):17,994
Last modified:June 7, 2004 - v1
Checksum:iC8AC295144AD7787
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074600 mRNA. Translation: AAC62958.1.
AF102817 mRNA. Translation: AAC98510.1.
AF096996 mRNA. Translation: AAC83789.1.
BC003488 mRNA. Translation: AAH03488.1.
BC004661 mRNA. No translation available.
BC010278 mRNA. Translation: AAH10278.3.
CCDSiCCDS51085.1.
RefSeqiNP_001155241.1. NM_001161769.1.
NP_001155242.1. NM_001161770.1.
NP_034853.1. NM_010723.3.
UniGeneiMm.29187.

Genome annotation databases

EnsembliENSMUST00000120539; ENSMUSP00000113840; ENSMUSG00000028266.
ENSMUST00000121112; ENSMUSP00000113865; ENSMUSG00000028266.
ENSMUST00000121796; ENSMUSP00000113513; ENSMUSG00000028266.
GeneIDi16911.
KEGGimmu:16911.
UCSCiuc008rpl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074600 mRNA. Translation: AAC62958.1.
AF102817 mRNA. Translation: AAC98510.1.
AF096996 mRNA. Translation: AAC83789.1.
BC003488 mRNA. Translation: AAH03488.1.
BC004661 mRNA. No translation available.
BC010278 mRNA. Translation: AAH10278.3.
CCDSiCCDS51085.1.
RefSeqiNP_001155241.1. NM_001161769.1.
NP_001155242.1. NM_001161770.1.
NP_034853.1. NM_010723.3.
UniGeneiMm.29187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3VNMR-A16-86[»]
1RUTX-ray1.30X16-152[»]
2DFYX-ray1.65C/X18-161[»]
2MBVNMR-A77-147[»]
ProteinModelPortaliP61969.
SMRiP61969. Positions 19-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201180. 4 interactions.
STRINGi10090.ENSMUSP00000113513.

PTM databases

iPTMnetiP61969.

Proteomic databases

EPDiP61969.
PaxDbiP61969.
PRIDEiP61969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000120539; ENSMUSP00000113840; ENSMUSG00000028266.
ENSMUST00000121112; ENSMUSP00000113865; ENSMUSG00000028266.
ENSMUST00000121796; ENSMUSP00000113513; ENSMUSG00000028266.
GeneIDi16911.
KEGGimmu:16911.
UCSCiuc008rpl.2. mouse.

Organism-specific databases

CTDi8543.
MGIiMGI:109360. Lmo4.

Phylogenomic databases

eggNOGiKOG0490. Eukaryota.
ENOG410YIJ3. LUCA.
HOGENOMiHOG000232175.
HOVERGENiHBG054231.
InParanoidiP61969.
OMAiTIPANDY.
OrthoDBiEOG75J0PF.
PhylomeDBiP61969.
TreeFamiTF351071.

Miscellaneous databases

ChiTaRSiLmo4. mouse.
EvolutionaryTraceiP61969.
PROiP61969.
SOURCEiSearch...

Gene expression databases

BgeeiP61969.
CleanExiMM_LMO4.
ExpressionAtlasiP61969. baseline and differential.
GenevisibleiP61969. MM.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
[Graphical view]
SMARTiSM00132. LIM. 2 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of LMO4, an LMO gene with a novel pattern of expression during embryogenesis."
    Kenny D.A., Jurata L.W., Saga Y., Gill G.N.
    Proc. Natl. Acad. Sci. U.S.A. 95:11257-11262(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse deformed epidermal autoregulatory factor 1 recruits a LIM domain factor, LMO-4, and CLIM coregulators."
    Sugihara T.M., Bach I., Kioussi C., Rosenfeld M.G., Andersen B.
    Proc. Natl. Acad. Sci. U.S.A. 95:15418-15423(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of the LMO4 gene encoding an interaction partner of the LIM-binding protein LDB1/NLI1: a candidate for displacement by LMO proteins in T cell acute leukaemia."
    Grutz G., Forster A., Rabbitts T.H.
    Oncogene 17:2799-2803(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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].
    Tissue: Mammary tumor.
  5. "The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activity."
    Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J., Visvader J.E.
    J. Biol. Chem. 277:7849-7856(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRCA1 AND RBBP8.
  6. "Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4."
    Cubeddu L., Joseph S., Richard D.J., Matthews J.M.
    PLoS ONE 7:E39218-E39218(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DEAF1.
  7. "Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4."
    Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E., Matthews J.M.
    EMBO J. 22:2224-2233(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 16-86 IN COMPLEX WITH LDB1.
  8. "Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex."
    Deane J.E., Ryan D.P., Sunde M., Maher M.J., Guss J.M., Visvader J.E., Matthews J.M.
    EMBO J. 23:3589-3598(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 16-152 IN COMPLEX WITH LDB1.
  9. "Stabilization of a binary protein complex by intein-mediated cyclization."
    Jeffries C.M., Graham S.C., Stokes P.H., Collyer C.A., Guss J.M., Matthews J.M.
    Protein Sci. 15:2612-2618(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 18-152 IN COMPLEX WITH LDB1.

Entry informationi

Entry nameiLMO4_MOUSE
AccessioniPrimary (citable) accession number: P61969
Secondary accession number(s): O00158, O88894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.