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P25791 (RBTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LMO2
Synonyms:RBTN2, RBTNL1, RHOM2, TTG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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 similarity. Interacts with BEX2 and KDM5A. Ref.4 Ref.5

Subcellular location

Nucleus Potential.

Domain

The second LIM zinc-binding domain interacts with KDM5A.

Involvement in disease

A chromosomal aberration involving LMO2 may be a cause of a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(11,14)(p13;q11) with TCRD.

Sequence similarities

Contains 2 LIM zinc-binding domains.

Sequence caution

The sequence AAF98804.1 differs from that shown. Reason: Intron retention.

The sequence AAH73973.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence CAA43430.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to thyroid hormone stimulus

Inferred from direct assay PubMed 19375645. Source: UniProtKB

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

mRNA transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5. Source: BHF-UCL

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

negative regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5. Source: BHF-UCL

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from direct assay Ref.5. Source: BHF-UCL

   Molecular_functionE-box binding

Inferred from direct assay Ref.5. Source: BHF-UCL

RNA polymerase II activating transcription factor binding

Inferred from physical interaction Ref.5. Source: BHF-UCL

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay Ref.5. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay Ref.5. Source: BHF-UCL

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay Ref.5. Source: BHF-UCL

bHLH transcription factor binding

Inferred from physical interaction Ref.5. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

cofactor binding

Inferred from physical interaction Ref.5. Source: BHF-UCL

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay Ref.5. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RELAQ042063EBI-739696,EBI-73886

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P25791-1)

Also known as: LMO2a;

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 3 (identifier: P25791-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGSAVTVLERGGASSPAERRSKRRRRSGGDGGGGGGARAPEGVRAPAAGQPRATKGAPPPPGTPPPSPM
Isoform 2 (identifier: P25791-4)

The sequence of this isoform differs from the canonical sequence as follows:
     15-15: E → SLKGSQVRCPVWPKTISDPRCWSHSGEAVPDAWPSLQGTSG
     16-158: Missing.
Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Rhombotin-2
PRO_0000075896

Regions

Domain30 – 8960LIM zinc-binding 1
Domain94 – 15360LIM zinc-binding 2

Natural variations

Alternative sequence11M → MEGSAVTVLERGGASSPAER RSKRRRRSGGDGGGGGGARA PEGVRAPAAGQPRATKGAPP PPGTPPPSPM in isoform 3.
VSP_038961
Alternative sequence151E → SLKGSQVRCPVWPKTISDPR CWSHSGEAVPDAWPSLQGTS G in isoform 2.
VSP_038962
Alternative sequence16 – 158143Missing in isoform 2.
VSP_038963

Secondary structure

................................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LMO2a) [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 1B4FF02505528C93

FASTA15818,358
        10         20         30         40         50         60 
MSSAIERKSL DPSEEPVDEV LQIPPSLLTC GGCQQNIGDR YFLKAIDQYW HEDCLSCDLC 

        70         80         90        100        110        120 
GCRLGEVGRR LYYKLGRKLC RRDYLRLFGQ DGLCASCDKR IRAYEMTMRV KDKVYHLECF 

       130        140        150 
KCAACQKHFC VGDRYLLINS DIVCEQDIYE WTKINGMI 

« Hide

Isoform 3 [UniParc].

Checksum: F80DBD6392880361
Show »

FASTA22725,036
Isoform 2 [UniParc].

Checksum: 0576C718F35DABF3
Show »

FASTA555,941

References

« Hide 'large scale' references
[1]"TTG-2, a new gene encoding a cysteine-rich protein with the LIM motif, is overexpressed in acute T-cell leukaemia with the t(11;14)(p13;q11)."
Royer-Pokora B., Loos L., Ludwig W.D.
Oncogene 6:1887-1893(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INVOLVEMENT IN T-CELL ACUTE LYMPHOBLASTIC LEUKEMIA.
Tissue: Kidney.
[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] (ISOFORMS 1 AND 2).
Tissue: Brain and Colon.
[3]"New 5'-end of LMO2 (TTG-2/RBTN2)."
Zhu T.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-158 (ISOFORM 1).
Tissue: Kidney.
[4]"T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2."
Mao S., Neale G.A.M., Goorha R.M.
Oncogene 14:1531-1539(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM5A.
[5]"Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BEX2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61118 mRNA. Translation: CAA43430.1. Frameshift.
BC034041 mRNA. Translation: AAH34041.1.
BC035607 mRNA. Translation: AAH35607.1.
BC042426 mRNA. Translation: AAH42426.1.
BC073973 mRNA. Translation: AAH73973.1. Sequence problems.
AF257211 mRNA. Translation: AAF98804.1. Sequence problems.
PIRS29477.
RefSeqNP_001135787.1. NM_001142315.1.
NP_001135788.1. NM_001142316.1.
NP_005565.2. NM_005574.3.
XP_005252978.1. XM_005252921.1.
UniGeneHs.34560.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XJYX-ray2.40A26-156[»]
2XJZX-ray2.80A/B/C/D/E26-156[»]
2YPAX-ray2.80C25-156[»]
4KFZX-ray2.80A/B9-158[»]
ProteinModelPortalP25791.
SMRP25791. Positions 26-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110191. 35 interactions.
IntActP25791. 26 interactions.
MINTMINT-233526.
STRING9606.ENSP00000257818.

PTM databases

PhosphoSiteP25791.

Polymorphism databases

DMDM132533.

Proteomic databases

PaxDbP25791.
PRIDEP25791.

Protocols and materials databases

DNASU4005.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257818; ENSP00000257818; ENSG00000135363. [P25791-3]
ENST00000395833; ENSP00000379175; ENSG00000135363. [P25791-1]
ENST00000411482; ENSP00000401967; ENSG00000135363. [P25791-4]
GeneID4005.
KEGGhsa:4005.
UCSCuc001mvc.3. human. [P25791-1]
uc010rem.2. human. [P25791-3]

Organism-specific databases

CTD4005.
GeneCardsGC11M033880.
H-InvDBHIX0009544.
HGNCHGNC:6642. LMO2.
HPACAB016258.
MIM180385. gene.
neXtProtNX_P25791.
PharmGKBPA30408.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319108.
HOGENOMHOG000232175.
HOVERGENHBG054231.
InParanoidP25791.
KOK15612.
OMACEKRIRA.
PhylomeDBP25791.
TreeFamTF351071.

Gene expression databases

BgeeP25791.
CleanExHS_LMO2.
GenevestigatorP25791.

Family and domain databases

Gene3D2.10.110.10. 2 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 2 hits.
[Graphical view]
SMARTSM00132. LIM. 2 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLMO2. human.
EvolutionaryTraceP25791.
GeneWikiLMO2.
GenomeRNAi4005.
NextBio15712.
PROP25791.
SOURCESearch...

Entry information

Entry nameRBTN2_HUMAN
AccessionPrimary (citable) accession number: P25791
Secondary accession number(s): Q9HD58
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM