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Protein

Rhombotin-2

Gene

Lmo2

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

Functioni

Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state.1 Publication

GO - Molecular functioni

  1. bHLH transcription factor binding Source: MGI
  2. chromatin binding Source: MGI
  3. cofactor binding Source: MGI
  4. E-box binding Source: MGI
  5. RNA polymerase II activating transcription factor binding Source: MGI
  6. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  7. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: MGI
  8. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  9. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  10. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to thyroid hormone stimulus Source: MGI
  2. embryonic hemopoiesis Source: MGI
  3. mRNA transcription from RNA polymerase II promoter Source: MGI
  4. negative regulation of erythrocyte differentiation Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Rhombotin-2
Alternative name(s):
Cysteine-rich protein TTG-2
LIM domain only protein 2
Short name:
LMO-2
T-cell translocation protein 2
Gene namesi
Name:Lmo2
Synonyms:Rbtn-2, Rbtn2, Rhom-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:102811. Lmo2.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. protein complex Source: UniProtKB
  3. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Rhombotin-2PRO_0000075897Add
BLAST

Proteomic databases

PRIDEiP25801.

PTM databases

PhosphoSiteiP25801.

Expressioni

Tissue specificityi

Expressed in early mouse development in central nervous system, lung, kidney, liver and spleen but only very low levels occur in thymus.1 Publication

Gene expression databases

BgeeiP25801.
CleanExiMM_LMO2.
ExpressionAtlasiP25801. baseline and differential.
GenevestigatoriP25801.

Interactioni

Subunit structurei

Interacts with BEX2 and KDM5A (By similarity). Interacts via its LIM domains with ELF2 and LDB1. Also interacts with basic helix-loop-helix protein TAL1/SCL and can assemble in a complex with LMO2 and TAL1/SCL.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Gata1P176795EBI-3903256,EBI-3903251
GATA2P237693EBI-3903256,EBI-2806671From a different organism.
TAL1P175425EBI-3903256,EBI-1753878From a different organism.

Protein-protein interaction databases

BioGridi201179. 4 interactions.
DIPiDIP-24247N.
IntActiP25801. 5 interactions.
MINTiMINT-2567948.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 334Combined sources
Beta strandi39 – 446Combined sources
Beta strandi46 – 505Combined sources
Turni52 – 543Combined sources
Beta strandi58 – 603Combined sources
Beta strandi67 – 693Combined sources
Helixi81 – 877Combined sources
Beta strandi95 – 984Combined sources
Turni117 – 1193Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi139 – 1435Combined sources
Beta strandi145 – 1473Combined sources
Helixi148 – 1558Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2ONMR-A26-87[»]
2L6YNMR-B84-156[»]
2L6ZNMR-C84-156[»]
2LXDNMR-A84-156[»]
SMRiP25801. Positions 9-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 8960LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 15360LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The second LIM zinc-binding domain interacts with KDM5A.By similarity

Sequence similaritiesi

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

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG319108.
HOGENOMiHOG000232175.
HOVERGENiHBG054231.
InParanoidiP25801.
KOiK15612.

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.

P25801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAIERKSL DPSEEPVDEV LQIPPSLLTC GGCQQNIGDR YFLKAIDQYW
60 70 80 90 100
HEDCLSCDLC GCRLGEVGRR LYYKLGRKLC RRDYLRLFGQ DGLCASCDKR
110 120 130 140 150
IRAYEMTMRV KDKVYHLECF KCAACQKHFC VGDRYLLINS DIVCEQDIYE

WTKINGII
Length:158
Mass (Da):18,340
Last modified:May 1, 1992 - v1
Checksum:i1B49302505528C93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64360 mRNA. Translation: AAA40054.1.
BC057880 mRNA. Translation: AAH57880.1.
CCDSiCCDS50652.1.
PIRiA39370.
RefSeqiNP_001135808.1. NM_001142336.1.
NP_001135809.1. NM_001142337.1.
XP_006498883.1. XM_006498820.2.
UniGeneiMm.29266.

Genome annotation databases

EnsembliENSMUST00000123437; ENSMUSP00000117703; ENSMUSG00000032698.
ENSMUST00000170926; ENSMUSP00000128317; ENSMUSG00000032698.
GeneIDi16909.
KEGGimmu:16909.
UCSCiuc012caj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64360 mRNA. Translation: AAA40054.1.
BC057880 mRNA. Translation: AAH57880.1.
CCDSiCCDS50652.1.
PIRiA39370.
RefSeqiNP_001135808.1. NM_001142336.1.
NP_001135809.1. NM_001142337.1.
XP_006498883.1. XM_006498820.2.
UniGeneiMm.29266.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2ONMR-A26-87[»]
2L6YNMR-B84-156[»]
2L6ZNMR-C84-156[»]
2LXDNMR-A84-156[»]
SMRiP25801. Positions 9-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201179. 4 interactions.
DIPiDIP-24247N.
IntActiP25801. 5 interactions.
MINTiMINT-2567948.

PTM databases

PhosphoSiteiP25801.

Proteomic databases

PRIDEiP25801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000123437; ENSMUSP00000117703; ENSMUSG00000032698.
ENSMUST00000170926; ENSMUSP00000128317; ENSMUSG00000032698.
GeneIDi16909.
KEGGimmu:16909.
UCSCiuc012caj.1. mouse.

Organism-specific databases

CTDi4005.
MGIiMGI:102811. Lmo2.

Phylogenomic databases

eggNOGiNOG319108.
HOGENOMiHOG000232175.
HOVERGENiHBG054231.
InParanoidiP25801.
KOiK15612.

Miscellaneous databases

ChiTaRSiLmo2. mouse.
EvolutionaryTraceiP25801.
NextBioi290948.
PROiP25801.
SOURCEiSearch...

Gene expression databases

BgeeiP25801.
CleanExiMM_LMO2.
ExpressionAtlasiP25801. baseline and differential.
GenevestigatoriP25801.

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. "The rhombotin family of cysteine-rich LIM-domain oncogenes: distinct members are involved in T-cell translocations to human chromosomes 11p15 and 11p13."
    Boehm T., Foroni L., Kaneko Y., Perutz M.F., Rabbitts T.H.
    Proc. Natl. Acad. Sci. U.S.A. 88:4367-4371(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Embryo.
  2. "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: NMRI.
    Tissue: Mammary gland.
  3. "Elf-2, a rhombotin-2 binding ets transcription factor: discovery and potential role in T cell leukemia."
    Wilkinson D.A., Neale G.A.M., Mao S., Naeve C.W., Goorha R.M.
    Leukemia 11:86-96(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELF2.
  4. "The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation."
    Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.
    Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LDB1 AND TAL1, IDENTIFICATION IN A COMPLEX WITH LDB1 AND TAL1.
  5. "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 26-87 IN COMPLEX WITH LDB1.

Entry informationi

Entry nameiRBTN2_MOUSE
AccessioniPrimary (citable) accession number: P25801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 1, 2015
This is version 135 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

External Data

Dasty 3

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 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.