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P70662

- LDB1_MOUSE

UniProt

P70662 - LDB1_MOUSE

Protein

LIM domain-binding protein 1

Gene

Ldb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state.7 Publications

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. enhancer sequence-specific DNA binding Source: MGI
    3. enzyme binding Source: UniProtKB
    4. LIM domain binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. protein self-association Source: MGI
    8. transcription cofactor activity Source: InterPro
    9. transcription factor binding transcription factor activity Source: MGI

    GO - Biological processi

    1. anterior/posterior axis specification Source: MGI
    2. cellular component assembly Source: MGI
    3. cerebellar Purkinje cell differentiation Source: MGI
    4. cerebellum development Source: MGI
    5. epithelial structure maintenance Source: MGI
    6. gastrulation with mouth forming second Source: MGI
    7. hair follicle development Source: MGI
    8. head development Source: UniProtKB
    9. histone H3-K4 acetylation Source: BHF-UCL
    10. negative regulation of erythrocyte differentiation Source: UniProtKB
    11. negative regulation of transcription, DNA-templated Source: Ensembl
    12. neuron differentiation Source: UniProtKB
    13. positive regulation of cell adhesion Source: MGI
    14. positive regulation of hemoglobin biosynthetic process Source: BHF-UCL
    15. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    16. primitive erythrocyte differentiation Source: BHF-UCL
    17. regulation of DNA-templated transcription, elongation Source: BHF-UCL
    18. somatic stem cell maintenance Source: MGI
    19. transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: BHF-UCL
    20. transcription from RNA polymerase II promoter Source: UniProtKB
    21. Wnt signaling pathway Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LIM domain-binding protein 1
    Short name:
    LDB-1
    Alternative name(s):
    Carboxyl-terminal LIM domain-binding protein 2
    Short name:
    CLIM-2
    LIM domain-binding factor CLIM2
    Short name:
    mLdb1
    Nuclear LIM interactor
    Gene namesi
    Name:Ldb1
    Synonyms:Nli
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:894762. Ldb1.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. nuclear chromatin Source: Ensembl
    2. nucleus Source: UniProtKB
    3. protein complex Source: UniProtKB
    4. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 411410LIM domain-binding protein 1PRO_0000084385Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Post-translational modificationi

    Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    PaxDbiP70662.
    PRIDEiP70662.

    PTM databases

    PhosphoSiteiP70662.

    Expressioni

    Tissue specificityi

    Expression overlaps that of LIM domain-containing proteins. Expressed widely in the embryo with highest expression in several regions of the brain the central nervous system ganglia. Also expressed in fetal liver, lung, kidney, thymus and olfactory epithelium. Expressed in multiple adult tissues including heart, brain, liver, kidney, testis, lung and muscle and a diverse range of neuronal cell types, with expression highest in the pituitary gland and skin. Expressed in both embryonic and adult hemopoietic cells, including the erythroid lineage.4 Publications

    Gene expression databases

    ArrayExpressiP70662.
    BgeeiP70662.
    CleanExiMM_LDB1.
    GenevestigatoriP70662.

    Interactioni

    Subunit structurei

    Interacts with ESR1 By similarity. Forms homodimers and heterodimers. Interacts with and activates LHX1/LIM1. Interacts with the LIM domains of ISL1 and LMO2. Can assemble in a complex with LMO2 and TAL1/SCL but does not interact with TAL1/SCL directly. Strongly interacts with the LIM2 domain of LMX1A and more weakly with the LIM1 domain. Homodimerization is not required for, and does not effect, LMX1A-binding. Component of a nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3. Interacts with LHX6 and LHX9. At neuronal promoters, forms a complex with LHX3 involved in the specification of interneurons, in motor neurons, it is displaced by ISL1 to form a ternary complex in which ISL1 contacts both LHX3 and LDB1.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cbfa2t3O549722EBI-6272082,EBI-8006703
    Isl1P613723EBI-6272082,EBI-7988215
    Lhx3P504815EBI-6272082,EBI-7988290
    Tal1P220913EBI-6272082,EBI-8006437
    Tcf4Q607222EBI-6272082,EBI-310070

    Protein-protein interaction databases

    BioGridi201125. 27 interactions.
    IntActiP70662. 6 interactions.
    MINTiMINT-2779250.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi307 – 3093
    Beta strandi315 – 3217
    Turni322 – 3243
    Beta strandi325 – 3273
    Turni329 – 3313
    Beta strandi336 – 3449
    Beta strandi346 – 3494
    Beta strandi355 – 3573
    Beta strandi359 – 3624
    Turni369 – 3713
    Beta strandi379 – 3846
    Beta strandi387 – 3893
    Helixi391 – 3933
    Turni397 – 3993
    Beta strandi408 – 4114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J2ONMR-A336-375[»]
    1M3VNMR-A336-375[»]
    1RUTX-ray1.30X336-375[»]
    2JTNNMR-A331-375[»]
    2L6YNMR-B336-348[»]
    2L6ZNMR-C336-348[»]
    2LXDNMR-A336-375[»]
    4JCJX-ray3.00A/B/C300-411[»]
    ProteinModelPortaliP70662.
    SMRiP70662. Positions 336-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP70662.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni336 – 37439LIM-binding domain (LID)Add
    BLAST

    Domaini

    The dimerization domain is located in the N-terminus.1 Publication

    Sequence similaritiesi

    Belongs to the LDB family.Curated

    Phylogenomic databases

    eggNOGiNOG282114.
    GeneTreeiENSGT00390000005639.
    HOGENOMiHOG000030908.
    HOVERGENiHBG000135.
    InParanoidiP70662.
    KOiK15617.
    OMAiGSNSPWN.
    PhylomeDBiP70662.
    TreeFamiTF319923.

    Family and domain databases

    InterProiIPR029005. LIM-bd/SEUSS.
    IPR002691. LIM-dom-bd.
    [Graphical view]
    PANTHERiPTHR10378. PTHR10378. 1 hit.
    PfamiPF01803. LIM_bind. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70662-1) [UniParc]FASTAAdd to Basket

    Also known as: Visvader-a

    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

    MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP    50
    TYLEPGIGRH TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED 100
    DAMLTITFCL EDGPKRYTIG RTLIPRYFRS IFEGGATELY YVLKHPKEAF 150
    HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG RLYLEFMFDD MMRIKTWHFS 200
    IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL NYLRLCVILE 250
    PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPAR QQPSKRRKRK 300
    MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF 350
    GDEDERLITR LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES 400
    KSENPTSQAS Q 411
    Length:411
    Mass (Da):46,503
    Last modified:September 11, 2007 - v2
    Checksum:i47C53DFA23044580
    GO
    Isoform 2 (identifier: P70662-2) [UniParc]FASTAAdd to Basket

    Also known as: Tran-b

    The sequence of this isoform differs from the canonical sequence as follows:
         2-36: Missing.
         336-355: DVMVVGEPTLMGGEFGDEDE → VSISAFFSSGLPHCSPLTPV
         356-411: Missing.

    Note: Due to intron retention. Lacks LIM-binding domain. Lacks ability to activate LIM domain-dependent transcription.

    Show »
    Length:320
    Mass (Da):36,798
    Checksum:iAE90F933828A17BC
    GO
    Isoform 3 (identifier: P70662-3) [UniParc]FASTAAdd to Basket

    Also known as: Tran-a

    The sequence of this isoform differs from the canonical sequence as follows:
         2-36: Missing.

    Show »
    Length:376
    Mass (Da):42,910
    Checksum:iFDE13F1E9984E4EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti262 – 2621Y → C in AAB96885. (PubMed:9192866)Curated
    Sequence conflicti334 – 3341V → A in AAB96885. (PubMed:9192866)Curated
    Sequence conflicti389 – 3902PW → QR in AAB96885. (PubMed:9192866)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 3635Missing in isoform 2 and isoform 3. 5 PublicationsVSP_027833Add
    BLAST
    Alternative sequencei336 – 35520DVMVV…GDEDE → VSISAFFSSGLPHCSPLTPV in isoform 2. 1 PublicationVSP_027834Add
    BLAST
    Alternative sequencei356 – 41156Missing in isoform 2. 1 PublicationVSP_027835Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70375 mRNA. Translation: AAC52933.1.
    U69270 mRNA. Translation: AAC52887.1.
    U89488 mRNA. Translation: AAB96885.1.
    AF030333 mRNA. Translation: AAB94131.1.
    AF024524 Genomic DNA. Translation: AAC40064.1.
    AB250383 mRNA. Translation: BAE95401.1.
    BC013624 mRNA. Translation: AAH13624.1.
    CCDSiCCDS50455.1. [P70662-1]
    RefSeqiNP_001106879.1. NM_001113408.1. [P70662-1]
    NP_034827.1. NM_010697.1.
    UniGeneiMm.327442.

    Genome annotation databases

    EnsembliENSMUST00000026252; ENSMUSP00000026252; ENSMUSG00000025223.
    ENSMUST00000056931; ENSMUSP00000053680; ENSMUSG00000025223.
    ENSMUST00000137771; ENSMUSP00000114667; ENSMUSG00000025223.
    ENSMUST00000156585; ENSMUSP00000118546; ENSMUSG00000025223. [P70662-1]
    GeneIDi16825.
    KEGGimmu:16825.
    UCSCiuc008hrz.1. mouse. [P70662-1]
    uc008hsa.1. mouse. [P70662-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70375 mRNA. Translation: AAC52933.1 .
    U69270 mRNA. Translation: AAC52887.1 .
    U89488 mRNA. Translation: AAB96885.1 .
    AF030333 mRNA. Translation: AAB94131.1 .
    AF024524 Genomic DNA. Translation: AAC40064.1 .
    AB250383 mRNA. Translation: BAE95401.1 .
    BC013624 mRNA. Translation: AAH13624.1 .
    CCDSi CCDS50455.1. [P70662-1 ]
    RefSeqi NP_001106879.1. NM_001113408.1. [P70662-1 ]
    NP_034827.1. NM_010697.1.
    UniGenei Mm.327442.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J2O NMR - A 336-375 [» ]
    1M3V NMR - A 336-375 [» ]
    1RUT X-ray 1.30 X 336-375 [» ]
    2JTN NMR - A 331-375 [» ]
    2L6Y NMR - B 336-348 [» ]
    2L6Z NMR - C 336-348 [» ]
    2LXD NMR - A 336-375 [» ]
    4JCJ X-ray 3.00 A/B/C 300-411 [» ]
    ProteinModelPortali P70662.
    SMRi P70662. Positions 336-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201125. 27 interactions.
    IntActi P70662. 6 interactions.
    MINTi MINT-2779250.

    PTM databases

    PhosphoSitei P70662.

    Proteomic databases

    PaxDbi P70662.
    PRIDEi P70662.

    Protocols and materials databases

    DNASUi 16825.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026252 ; ENSMUSP00000026252 ; ENSMUSG00000025223 .
    ENSMUST00000056931 ; ENSMUSP00000053680 ; ENSMUSG00000025223 .
    ENSMUST00000137771 ; ENSMUSP00000114667 ; ENSMUSG00000025223 .
    ENSMUST00000156585 ; ENSMUSP00000118546 ; ENSMUSG00000025223 . [P70662-1 ]
    GeneIDi 16825.
    KEGGi mmu:16825.
    UCSCi uc008hrz.1. mouse. [P70662-1 ]
    uc008hsa.1. mouse. [P70662-2 ]

    Organism-specific databases

    CTDi 8861.
    MGIi MGI:894762. Ldb1.

    Phylogenomic databases

    eggNOGi NOG282114.
    GeneTreei ENSGT00390000005639.
    HOGENOMi HOG000030908.
    HOVERGENi HBG000135.
    InParanoidi P70662.
    KOi K15617.
    OMAi GSNSPWN.
    PhylomeDBi P70662.
    TreeFami TF319923.

    Miscellaneous databases

    ChiTaRSi LDB1. mouse.
    EvolutionaryTracei P70662.
    NextBioi 290724.
    PROi P70662.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70662.
    Bgeei P70662.
    CleanExi MM_LDB1.
    Genevestigatori P70662.

    Family and domain databases

    InterProi IPR029005. LIM-bd/SEUSS.
    IPR002691. LIM-dom-bd.
    [Graphical view ]
    PANTHERi PTHR10378. PTHR10378. 1 hit.
    Pfami PF01803. LIM_bind. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Interactions of the LIM-domain-binding factor Ldb1 with LIM homeodomain proteins."
      Agulnick A.D., Taira M., Breen J.J., Tanaka T., Dawid I.B., Westphal H.
      Nature 384:270-272(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH LHX1, TISSUE SPECIFICITY.
      Strain: Swiss Webster.
      Tissue: Embryo.
    2. "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development."
      Jurata L.W., Kenny D.A., Gill G.N.
      Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Embryo.
    3. "A family of LIM domain-associated cofactors confer transcriptional synergism between LIM and Otx homeodomain proteins."
      Bach I., Carriere C., Ostendorff H.P., Andersen B., Rosenfeld M.G.
      Genes Dev. 11:1370-1380(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryonic head.
    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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH LMO2, IDENTIFICATION IN A COMPLEX WITH LMO2 AND TAL1.
      Tissue: Yolk sac.
    5. "Genomic structure and chromosomal localization of the mouse LIM domain-binding protein 1 gene, Ldb1."
      Yamashita T., Agulnick A.D., Copeland N.G., Gilbert D.J., Jenkins N.A., Westphal H.
      Genomics 48:87-92(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    6. "Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the LIM-interaction domain."
      Tran Y.H., Xu Z., Kato A., Mistry A.C., Goya Y., Taira M., Brandt S.J., Hirose S.
      J. Biochem. 140:105-119(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Heart.
    7. "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] (ISOFORM 3).
      Strain: FVB/N.
      Tissue: Mammary gland.
    8. "Functional analysis of the nuclear LIM domain interactor NLI."
      Jurata L.W., Gill G.N.
      Mol. Cell. Biol. 17:5688-5698(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION OF LIM-BINDING DOMAIN.
    9. "Interactions between LIM domains and the LIM domain-binding protein Ldb1."
      Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.
      J. Biol. Chem. 273:4712-4717(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LHX1, DOMAIN, HOMODIMERIZATION.
    10. "A brain region-specific gene product Lhx6.1 interacts with Ldb1 through tandem LIM-domains."
      Kimura N., Ueno M., Nakashima K., Taga T.
      J. Biochem. 126:180-187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LHX6.
      Tissue: Fetal brain.
    11. "Characterization of Lhx9, a novel LIM/homeobox gene expressed by the pioneer neurons in the mouse cerebral cortex."
      Bertuzzi S., Porter F.D., Pitts A., Kumar M., Agulnick A., Wassif C., Westphal H.
      Mech. Dev. 81:193-198(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LHX9.
    12. "LIM factor Lhx3 contributes to the specification of motor neuron and interneuron identity through cell-type-specific protein-protein interactions."
      Thaler J.P., Lee S.K., Jurata L.W., Gill G.N., Pfaff S.L.
      Cell 110:237-249(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LHX3 AND ISL1.
    13. "Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors."
      Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M., Scheffner M., Bach I.
      Nature 416:99-103(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RLIM, UBIQUITINATION.
    14. "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis."
      Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S., Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.
      EMBO J. 25:357-366(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX.
    15. "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 336-375 IN COMPLEXES WITH LMO2 AND LMO4.
    16. "Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex."
      Deane J.E., Ryan D.P., Sunde M., Maher M.J., Guss J.M., Visvader J.E., Matthews J.M.
      EMBO J. 23:3589-3598(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-375 IN COMPLEX WITH LMO4.

    Entry informationi

    Entry nameiLDB1_MOUSE
    AccessioniPrimary (citable) accession number: P70662
    Secondary accession number(s): O55204, Q1EQX2, Q71V68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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