P25791 (RBTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LMO2
Synonyms:	RBTN2, RBTNL1, RHOM2, TTG2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to thyroid hormone stimulus Inferred from direct assay PubMed 19375645. Source: UniProtKB embryonic hemopoiesis Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	transcription factor complex Inferred from direct assay Ref.5. Source: BHF-UCL
Molecular_function	E-box binding Inferred from direct assay 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 chromatin binding Inferred from electronic annotation. Source: Compara cofactor binding Inferred from physical interaction Ref.5. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RELA	Q04206	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 158

158

Rhombotin-2

PRO_0000075896

Regions

Domain

30 – 89

60

LIM zinc-binding 1

Domain

94 – 153

60

LIM zinc-binding 2

Natural variations

Alternative sequence

1

1

M → MEGSAVTVLERGGASSPAER RSKRRRRSGGDGGGGGGARA PEGVRAPAAGQPRATKGAPP PPGTPPPSPM in isoform 3.

VSP_038961

Alternative sequence

15

1

E → SLKGSQVRCPVWPKTISDPR CWSHSGEAVPDAWPSLQGTS G in isoform 2.

VSP_038962

Alternative sequence

16 – 158

143

Missing in isoform 2.

VSP_038963

Secondary structure

1

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158

Helix Strand Turn

Details...

Turn

31 – 33

3

Beta strand

39 – 45

7

Beta strand

48 – 51

4

Turn

52 – 54

3

Turn

58 – 60

3

Turn

64 – 66

3

Beta strand

71 – 74

4

Beta strand

77 – 79

3

Helix

81 – 88

8

Turn

95 – 97

3

Beta strand

105 – 110

6

Beta strand

113 – 116

4

Helix

117 – 119

3

Turn

123 – 125

3

Beta strand

134 – 138

5

Beta strand

141 – 144

4

Helix

145 – 147

3

Helix

148 – 155

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LMO2a) [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 1B4FF02505528C93	FASTA	158	18,358
	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
	Isoform 3 [UniParc]. Checksum: F80DBD6392880361	FASTA	227	25,036
	10 20 30 40 50 60 MEGSAVTVLE RGGASSPAER RSKRRRRSGG DGGGGGGARA PEGVRAPAAG QPRATKGAPP 70 80 90 100 110 120 PPGTPPPSPM SSAIERKSLD PSEEPVDEVL QIPPSLLTCG GCQQNIGDRY FLKAIDQYWH 130 140 150 160 170 180 EDCLSCDLCG CRLGEVGRRL YYKLGRKLCR RDYLRLFGQD GLCASCDKRI RAYEMTMRVK 190 200 210 220 DKVYHLECFK CAACQKHFCV GDRYLLINSD IVCEQDIYEW TKINGMI
	Isoform 2 [UniParc]. Checksum: 0576C718F35DABF3	FASTA	55	5,941
	10 20 30 40 50 MSSAIERKSL DPSESLKGSQ VRCPVWPKTI SDPRCWSHSG EAVPDAWPSL QGTSG

References

	« Hide 'large scale' referencesShow '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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00016852.
IPI00915342.
IPI00926017.

PIR

S29477.

RefSeq

NP_001135787.1. NM_001142315.1.
NP_001135788.1. NM_001142316.1.
NP_005565.2. NM_005574.3.

UniGene

Hs.34560.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XJY	X-ray	2.40	A	26-156	[»]
2XJZ	X-ray	2.80	A/B/C/D/E	26-156	[»]

ProteinModelPortal

P25791.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25791. 23 interactions.

MINT

MINT-233526.

STRING

9606.ENSP00000257818.

PTM databases

PhosphoSite

P25791.

Polymorphism databases

DMDM

132533.

Proteomic databases

PaxDb

P25791.

PRIDE

P25791.

Protocols and materials databases

DNASU

4005.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257818; ENSP00000257818; ENSG00000135363.
ENST00000395833; ENSP00000379175; ENSG00000135363.
ENST00000411482; ENSP00000401967; ENSG00000135363.

GeneID

4005.

KEGG

hsa:4005.

UCSC

uc001mvc.3. human.
uc010rem.2. human.

Organism-specific databases

CTD

4005.

GeneCards

GC11M033880.

H-InvDB

HIX0009544.

HGNC

HGNC:6642. LMO2.

HPA

CAB016258.

MIM

180385. gene.

neXtProt

NX_P25791.

PharmGKB

PA30408.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG319108.

HOGENOM

HOG000232175.

HOVERGEN

HBG054231.

InParanoid

P25791.

KO

K15612.

OMA

CEKRIRA.

OrthoDB

EOG4001KG.

PhylomeDB

P25791.

Gene expression databases

Bgee

P25791.

CleanEx

HS_LMO2.

Genevestigator

P25791.

GermOnline

ENSG00000135363. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 2 hits.

InterPro

IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 2 hits.
[Graphical view]

SMART

SM00132. LIM. 2 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

LMO2. human.

EvolutionaryTrace

P25791.

GenomeRNAi

4005.

NextBio

15712.

SOURCE

Search...

Entry information

Entry name

RBTN2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.