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Protein

Rhombotin-2

Gene

LMO2

Organism
Homo sapiens (Human)
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.

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL
  • chromatin binding Source: Ensembl
  • cofactor binding Source: BHF-UCL
  • E-box binding Source: BHF-UCL
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  • sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • embryonic hemopoiesis Source: Ensembl
  • mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • multicellular organismal development Source: ProtInc
  • negative regulation of erythrocyte differentiation Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
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:RBTN2, RBTNL1, RHOM2, TTG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:6642. LMO2.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA30408.

Polymorphism and mutation databases

BioMutaiLMO2.
DMDMi132533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Rhombotin-2PRO_0000075896Add
BLAST

Proteomic databases

MaxQBiP25791.
PaxDbiP25791.
PRIDEiP25791.

PTM databases

PhosphoSiteiP25791.

Expressioni

Gene expression databases

BgeeiP25791.
CleanExiHS_LMO2.
GenevisibleiP25791. HS.

Organism-specific databases

HPAiCAB016258.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2Q9NYB93EBI-739696,EBI-743598
ADAMTSL4Q6UY14-33EBI-739696,EBI-10173507
AESQ081173EBI-739696,EBI-717810
AGTRAPQ6RW133EBI-739696,EBI-741181
AIMP2Q131553EBI-739696,EBI-745226
BANPQ8N9N53EBI-739696,EBI-744695
BLZF1Q9H2G93EBI-739696,EBI-2548012
C1orf94Q6P1W53EBI-739696,EBI-946029
C9orf138A8K8803EBI-739696,EBI-10174528
CALCOCO2Q131373EBI-739696,EBI-739580
CCDC36Q8IYA83EBI-739696,EBI-8638439
CDX4O146273EBI-739696,EBI-10181162
CLHC1Q8NHS43EBI-739696,EBI-10203156
CMTM5Q96DZ93EBI-739696,EBI-2548702
DBF4BQ8NFT63EBI-739696,EBI-749662
DDIT3P35638-23EBI-739696,EBI-10173632
DRAP1Q149193EBI-739696,EBI-712941
FHL3Q136433EBI-739696,EBI-741101
GFAPP141363EBI-739696,EBI-744302
GOLGA2Q083793EBI-739696,EBI-618309
GRB2P629933EBI-739696,EBI-401755
HNRNPCP079103EBI-739696,EBI-357966
HNRNPMP522724EBI-739696,EBI-486809
HOOK1Q9UJC33EBI-739696,EBI-746704
IFT43Q96FT93EBI-739696,EBI-10189681
IKZF3Q9UKT93EBI-739696,EBI-747204
KANK2Q63ZY33EBI-739696,EBI-2556193
KRT15P190123EBI-739696,EBI-739566
KRT40Q6A1623EBI-739696,EBI-10171697
KRTAP10-7P604093EBI-739696,EBI-10172290
LDB1Q86U706EBI-739696,EBI-677177
LZTS2Q9BRK43EBI-739696,EBI-741037
MAGEA8P433613EBI-739696,EBI-10182930
MAPRE1Q156916EBI-739696,EBI-1004115
MAPRE2Q155554EBI-739696,EBI-739717
MAPRE3Q9UPY85EBI-739696,EBI-726739
MBIPQ9NS73-53EBI-739696,EBI-10182361
MRFAP1L1Q96HT83EBI-739696,EBI-748896
MTUS2Q5JR593EBI-739696,EBI-742948
N4BP2L2Q928023EBI-739696,EBI-2514973
NIF3L1Q9GZT83EBI-739696,EBI-740897
NOTCH2NLQ7Z3S93EBI-739696,EBI-945833
NUP62P371983EBI-739696,EBI-347978
NUTM1Q86Y263EBI-739696,EBI-10178410
PDE9AO760833EBI-739696,EBI-742764
PHC2Q8IXK04EBI-739696,EBI-713786
PRKG1Q139763EBI-739696,EBI-3952014
RELQ048643EBI-739696,EBI-307352
RELAQ042063EBI-739696,EBI-73886
RINT1Q6NUQ13EBI-739696,EBI-726876
ROCK1Q134643EBI-739696,EBI-876651
SKP1P632083EBI-739696,EBI-307486
SOX5P357113EBI-739696,EBI-3505701
SPERTQ8NA613EBI-739696,EBI-741724
SSX2IPQ9Y2D83EBI-739696,EBI-2212028
STAT3P407633EBI-739696,EBI-518675
TFPTG5E9B53EBI-739696,EBI-10178002
TRIM23P364063EBI-739696,EBI-740098
TRIM54Q9BYV23EBI-739696,EBI-2130429
TRIP6Q156543EBI-739696,EBI-742327
TSC22D4Q9Y3Q83EBI-739696,EBI-739485
TUFT1Q9NNX13EBI-739696,EBI-2557363
UBE2IQ7KZS03EBI-739696,EBI-10180829
ZFP64Q9NTW73EBI-739696,EBI-745730
ZNF24P170283EBI-739696,EBI-707773

Protein-protein interaction databases

BioGridi110191. 96 interactions.
IntActiP25791. 84 interactions.
MINTiMINT-233526.
STRINGi9606.ENSP00000257818.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273Combined sources
Turni31 – 333Combined sources
Beta strandi39 – 457Combined sources
Beta strandi48 – 514Combined sources
Turni52 – 543Combined sources
Turni58 – 603Combined sources
Turni64 – 663Combined sources
Beta strandi71 – 744Combined sources
Beta strandi77 – 793Combined sources
Helixi81 – 888Combined sources
Turni95 – 973Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1193Combined sources
Turni123 – 1253Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi141 – 1444Combined sources
Helixi145 – 1473Combined sources
Helixi148 – 1558Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XJYX-ray2.40A26-156[»]
2XJZX-ray2.80A/B/C/D/E26-156[»]
2YPAX-ray2.80C25-156[»]
4KFZX-ray2.80A/B9-158[»]
ProteinModelPortaliP25791.
SMRiP25791. Positions 9-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25791.

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.

Sequence similaritiesi

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

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG319108.
GeneTreeiENSGT00720000108603.
HOGENOMiHOG000232175.
HOVERGENiHBG054231.
InParanoidiP25791.
KOiK15612.
OMAiEMTMRVR.
PhylomeDBiP25791.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25791-1) [UniParc]FASTAAdd to basket

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.

« 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

WTKINGMI
Length:158
Mass (Da):18,358
Last modified:May 1, 1992 - v1
Checksum:i1B4FF02505528C93
GO
Isoform 3 (identifier: P25791-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGSAVTVLERGGASSPAERRSKRRRRSGGDGGGGGGARAPEGVRAPAAGQPRATKGAPPPPGTPPPSPM

Show »
Length:227
Mass (Da):25,036
Checksum:iF80DBD6392880361
GO
Isoform 2 (identifier: P25791-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:55
Mass (Da):5,941
Checksum:i0576C718F35DABF3
GO

Sequence cautioni

The sequence AAF98804.1 differs from that shown.Intron retention.Curated
The sequence AAH73973.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
The sequence CAA43430.1 differs from that shown. Reason: Frameshift at several positions. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEGSAVTVLERGGASSPAER RSKRRRRSGGDGGGGGGARA PEGVRAPAAGQPRATKGAPP PPGTPPPSPM in isoform 3. 1 PublicationVSP_038961
Alternative sequencei15 – 151E → SLKGSQVRCPVWPKTISDPR CWSHSGEAVPDAWPSLQGTS G in isoform 2. 1 PublicationVSP_038962
Alternative sequencei16 – 158143Missing in isoform 2. 1 PublicationVSP_038963Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44567.1. [P25791-1]
CCDS7888.2. [P25791-3]
PIRiS29477.
RefSeqiNP_001135787.1. NM_001142315.1. [P25791-1]
NP_001135788.1. NM_001142316.1. [P25791-1]
NP_005565.2. NM_005574.3. [P25791-3]
XP_005252978.1. XM_005252921.1. [P25791-1]
UniGeneiHs.34560.

Genome annotation databases

EnsembliENST00000257818; ENSP00000257818; ENSG00000135363. [P25791-3]
ENST00000395833; ENSP00000379175; ENSG00000135363. [P25791-1]
ENST00000411482; ENSP00000401967; ENSG00000135363. [P25791-4]
GeneIDi4005.
KEGGihsa:4005.
UCSCiuc001mvc.3. human. [P25791-1]
uc010rem.2. human. [P25791-3]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44567.1. [P25791-1]
CCDS7888.2. [P25791-3]
PIRiS29477.
RefSeqiNP_001135787.1. NM_001142315.1. [P25791-1]
NP_001135788.1. NM_001142316.1. [P25791-1]
NP_005565.2. NM_005574.3. [P25791-3]
XP_005252978.1. XM_005252921.1. [P25791-1]
UniGeneiHs.34560.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XJYX-ray2.40A26-156[»]
2XJZX-ray2.80A/B/C/D/E26-156[»]
2YPAX-ray2.80C25-156[»]
4KFZX-ray2.80A/B9-158[»]
ProteinModelPortaliP25791.
SMRiP25791. Positions 9-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110191. 96 interactions.
IntActiP25791. 84 interactions.
MINTiMINT-233526.
STRINGi9606.ENSP00000257818.

Chemistry

ChEMBLiCHEMBL3217402.

PTM databases

PhosphoSiteiP25791.

Polymorphism and mutation databases

BioMutaiLMO2.
DMDMi132533.

Proteomic databases

MaxQBiP25791.
PaxDbiP25791.
PRIDEiP25791.

Protocols and materials databases

DNASUi4005.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257818; ENSP00000257818; ENSG00000135363. [P25791-3]
ENST00000395833; ENSP00000379175; ENSG00000135363. [P25791-1]
ENST00000411482; ENSP00000401967; ENSG00000135363. [P25791-4]
GeneIDi4005.
KEGGihsa:4005.
UCSCiuc001mvc.3. human. [P25791-1]
uc010rem.2. human. [P25791-3]

Organism-specific databases

CTDi4005.
GeneCardsiGC11M033880.
H-InvDBHIX0009544.
HGNCiHGNC:6642. LMO2.
HPAiCAB016258.
MIMi180385. gene.
neXtProtiNX_P25791.
PharmGKBiPA30408.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG319108.
GeneTreeiENSGT00720000108603.
HOGENOMiHOG000232175.
HOVERGENiHBG054231.
InParanoidiP25791.
KOiK15612.
OMAiEMTMRVR.
PhylomeDBiP25791.
TreeFamiTF351071.

Miscellaneous databases

ChiTaRSiLMO2. human.
EvolutionaryTraceiP25791.
GeneWikiiLMO2.
GenomeRNAii4005.
NextBioi15712.
PROiP25791.
SOURCEiSearch...

Gene expression databases

BgeeiP25791.
CleanExiHS_LMO2.
GenevisibleiP25791. HS.

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. "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.

Entry informationi

Entry nameiRBTN2_HUMAN
AccessioniPrimary (citable) accession number: P25791
Secondary accession number(s): Q9HD58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.