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P25801

- RBTN2_MOUSE

UniProt

P25801 - RBTN2_MOUSE

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Protein
Rhombotin-2
Gene
Lmo2, Rbtn-2, Rbtn2, Rhom-2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. chromatin binding Source: MGI
  2. protein binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. embryonic hemopoiesis Source: MGI
  2. negative regulation of erythrocyte differentiation Source: UniProtKB
  3. 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: Chromosome 2

Organism-specific databases

MGIiMGI:102811. Lmo2.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

ArrayExpressiP25801.
BgeeiP25801.
CleanExiMM_LMO2.
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.2 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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2ONMR-A26-87[»]
2L6YNMR-B84-156[»]
2L6ZNMR-C84-156[»]
2LXDNMR-A84-156[»]
ProteinModelPortaliP25801.
SMRiP25801. Positions 9-156.

Miscellaneous databases

EvolutionaryTraceiP25801.

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

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

MSSAIERKSL DPSEEPVDEV LQIPPSLLTC GGCQQNIGDR YFLKAIDQYW    50
HEDCLSCDLC GCRLGEVGRR LYYKLGRKLC RRDYLRLFGQ DGLCASCDKR 100
IRAYEMTMRV KDKVYHLECF KCAACQKHFC VGDRYLLINS DIVCEQDIYE 150
WTKINGII 158
Length:158
Mass (Da):18,340
Last modified:May 1, 1992 - v1
Checksum:i1B49302505528C93
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006498820.1.
XP_006498884.1. XM_006498821.1.
UniGeneiMm.29266.

Genome annotation databases

EnsembliENSMUST00000123437; ENSMUSP00000117703; ENSMUSG00000032698.
ENSMUST00000163256; ENSMUSP00000129211; ENSMUSG00000032698.
ENSMUST00000170926; ENSMUSP00000128317; ENSMUSG00000032698.
GeneIDi16909.
KEGGimmu:16909.
UCSCiuc012caj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64360 mRNA. Translation: AAA40054.1 .
BC057880 mRNA. Translation: AAH57880.1 .
CCDSi CCDS50652.1.
PIRi A39370.
RefSeqi NP_001135808.1. NM_001142336.1.
NP_001135809.1. NM_001142337.1.
XP_006498883.1. XM_006498820.1.
XP_006498884.1. XM_006498821.1.
UniGenei Mm.29266.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J2O NMR - A 26-87 [» ]
2L6Y NMR - B 84-156 [» ]
2L6Z NMR - C 84-156 [» ]
2LXD NMR - A 84-156 [» ]
ProteinModelPortali P25801.
SMRi P25801. Positions 9-156.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201179. 4 interactions.
DIPi DIP-24247N.
IntActi P25801. 5 interactions.
MINTi MINT-2567948.

PTM databases

PhosphoSitei P25801.

Proteomic databases

PRIDEi P25801.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000123437 ; ENSMUSP00000117703 ; ENSMUSG00000032698 .
ENSMUST00000163256 ; ENSMUSP00000129211 ; ENSMUSG00000032698 .
ENSMUST00000170926 ; ENSMUSP00000128317 ; ENSMUSG00000032698 .
GeneIDi 16909.
KEGGi mmu:16909.
UCSCi uc012caj.1. mouse.

Organism-specific databases

CTDi 4005.
MGIi MGI:102811. Lmo2.

Phylogenomic databases

eggNOGi NOG319108.
HOGENOMi HOG000232175.
HOVERGENi HBG054231.
InParanoidi P25801.
KOi K15612.

Miscellaneous databases

ChiTaRSi LMO2. mouse.
EvolutionaryTracei P25801.
NextBioi 290948.
PROi P25801.
SOURCEi Search...

Gene expression databases

ArrayExpressi P25801.
Bgeei P25801.
CleanExi MM_LMO2.
Genevestigatori P25801.

Family and domain databases

Gene3Di 2.10.110.10. 2 hits.
InterProi IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 2 hits.
[Graphical view ]
SMARTi SM00132. LIM. 2 hits.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 129 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

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