ID RBTN2_MOUSE Reviewed; 158 AA.
AC P25801;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Rhombotin-2;
DE AltName: Full=Cysteine-rich protein TTG-2;
DE AltName: Full=LIM domain only protein 2;
DE Short=LMO-2;
DE AltName: Full=T-cell translocation protein 2;
GN Name=Lmo2; Synonyms=Rbtn-2, Rbtn2, Rhom-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=2034676; DOI=10.1073/pnas.88.10.4367;
RA Boehm T., Foroni L., Kaneko Y., Perutz M.F., Rabbitts T.H.;
RT "The rhombotin family of cysteine-rich LIM-domain oncogenes: distinct
RT members are involved in T-cell translocations to human chromosomes 11p15
RT and 11p13.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4367-4371(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH ELF2.
RX PubMed=9001422; DOI=10.1038/sj.leu.2400516;
RA Wilkinson D.A., Neale G.A.M., Mao S., Naeve C.W., Goorha R.M.;
RT "Elf-2, a rhombotin-2 binding ets transcription factor: discovery and
RT potential role in T cell leukemia.";
RL Leukemia 11:86-96(1997).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LDB1 AND TAL1, AND
RP IDENTIFICATION IN A COMPLEX WITH LDB1 AND TAL1.
RX PubMed=9391090; DOI=10.1073/pnas.94.25.13707;
RA Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.;
RT "The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative
RT regulators of erythroid differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997).
RN [5]
RP STRUCTURE BY NMR OF 26-87 IN COMPLEX WITH LDB1.
RX PubMed=12727888; DOI=10.1093/emboj/cdg196;
RA Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E.,
RA Matthews J.M.;
RT "Structural basis for the recognition of ldb1 by the N-terminal LIM domains
RT of LMO2 and LMO4.";
RL EMBO J. 22:2224-2233(2003).
CC -!- FUNCTION: Acts with TAL1/SCL to regulate red blood cell development.
CC Also acts with LDB1 to maintain erythroid precursors in an immature
CC state. {ECO:0000269|PubMed:9391090}.
CC -!- SUBUNIT: Interacts with BEX2 and KDM5A (By similarity). Interacts via
CC its LIM domains with ELF2 and LDB1. Also interacts with basic helix-
CC loop-helix protein TAL1/SCL and can assemble in a complex with LMO2 and
CC TAL1/SCL. {ECO:0000250, ECO:0000269|PubMed:12727888,
CC ECO:0000269|PubMed:9001422, ECO:0000269|PubMed:9391090}.
CC -!- INTERACTION:
CC P25801; P17679: Gata1; NbExp=5; IntAct=EBI-3903256, EBI-3903251;
CC P25801; P22091: Tal1; NbExp=2; IntAct=EBI-3903256, EBI-8006437;
CC P25801; P23769: GATA2; Xeno; NbExp=3; IntAct=EBI-3903256, EBI-2806671;
CC P25801; P17542: TAL1; Xeno; NbExp=5; IntAct=EBI-3903256, EBI-1753878;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9391090}.
CC -!- TISSUE SPECIFICITY: Expressed in early mouse development in central
CC nervous system, lung, kidney, liver and spleen but only very low levels
CC occur in thymus. {ECO:0000269|PubMed:2034676}.
CC -!- DOMAIN: The second LIM zinc-binding domain interacts with KDM5A.
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64360; AAA40054.1; -; mRNA.
DR EMBL; BC057880; AAH57880.1; -; mRNA.
DR CCDS; CCDS50652.1; -.
DR PIR; A39370; A39370.
DR RefSeq; NP_001135808.1; NM_001142336.1.
DR RefSeq; NP_001135809.1; NM_001142337.1.
DR RefSeq; XP_006498883.1; XM_006498820.3.
DR PDB; 1J2O; NMR; -; A=26-87.
DR PDB; 2L6Y; NMR; -; B=84-156.
DR PDB; 2L6Z; NMR; -; C=84-156.
DR PDB; 2LXD; NMR; -; A=84-156.
DR PDBsum; 1J2O; -.
DR PDBsum; 2L6Y; -.
DR PDBsum; 2L6Z; -.
DR PDBsum; 2LXD; -.
DR AlphaFoldDB; P25801; -.
DR BMRB; P25801; -.
DR SMR; P25801; -.
DR BioGRID; 201179; 59.
DR CORUM; P25801; -.
DR DIP; DIP-24247N; -.
DR IntAct; P25801; 7.
DR MINT; P25801; -.
DR STRING; 10090.ENSMUSP00000106770; -.
DR PhosphoSitePlus; P25801; -.
DR PaxDb; 10090-ENSMUSP00000106770; -.
DR ProteomicsDB; 254902; -.
DR Antibodypedia; 4265; 814 antibodies from 42 providers.
DR DNASU; 16909; -.
DR Ensembl; ENSMUST00000123437.8; ENSMUSP00000117703.2; ENSMUSG00000032698.16.
DR Ensembl; ENSMUST00000170926.8; ENSMUSP00000128317.2; ENSMUSG00000032698.16.
DR GeneID; 16909; -.
DR KEGG; mmu:16909; -.
DR UCSC; uc012caj.1; mouse.
DR AGR; MGI:102811; -.
DR CTD; 4005; -.
DR MGI; MGI:102811; Lmo2.
DR VEuPathDB; HostDB:ENSMUSG00000032698; -.
DR eggNOG; KOG0490; Eukaryota.
DR GeneTree; ENSGT00940000160199; -.
DR InParanoid; P25801; -.
DR OMA; MCGGCQQ; -.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR BioGRID-ORCS; 16909; 7 hits in 79 CRISPR screens.
DR ChiTaRS; Lmo2; mouse.
DR EvolutionaryTrace; P25801; -.
DR PRO; PR:P25801; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P25801; Protein.
DR Bgee; ENSMUSG00000032698; Expressed in fetal liver hematopoietic progenitor cell and 280 other cell types or tissues.
DR ExpressionAtlas; P25801; baseline and differential.
DR Genevisible; P25801; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IGI:MGI.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR CDD; cd09384; LIM1_LMO2; 1.
DR CDD; cd09385; LIM2_LMO2; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR IDEAL; IID50043; -.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR45787; LD11652P; 1.
DR PANTHER; PTHR45787:SF3; RHOMBOTIN-2; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; LIM domain; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..158
FT /note="Rhombotin-2"
FT /id="PRO_0000075897"
FT DOMAIN 30..89
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 94..153
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1J2O"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1J2O"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1J2O"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1J2O"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1J2O"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1J2O"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1J2O"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2L6Y"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2L6Y"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2L6Y"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2L6Y"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2L6Y"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2L6Y"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2L6Y"
SQ SEQUENCE 158 AA; 18340 MW; 1B49302505528C93 CRC64;
MSSAIERKSL DPSEEPVDEV LQIPPSLLTC GGCQQNIGDR YFLKAIDQYW HEDCLSCDLC
GCRLGEVGRR LYYKLGRKLC RRDYLRLFGQ DGLCASCDKR IRAYEMTMRV KDKVYHLECF
KCAACQKHFC VGDRYLLINS DIVCEQDIYE WTKINGII
//
