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Q86U70

- LDB1_HUMAN

UniProt

Q86U70 - LDB1_HUMAN

Protein

LIM domain-binding protein 1

Gene

LDB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (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 By similarity.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. enhancer sequence-specific DNA binding Source: Ensembl
    3. enzyme binding Source: UniProt
    4. LIM domain binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    7. transcription corepressor activity Source: ProtInc

    GO - Biological processi

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

    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:
    hLdb1
    Nuclear LIM interactor
    Gene namesi
    Name:LDB1
    Synonyms:CLIM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6532. LDB1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nuclear chromatin Source: BHF-UCL
    2. nucleus Source: UniProtKB
    3. protein complex Source: UniProtKB
    4. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi245 – 2495LCVIL → ACVAA: Abolishes interaction with ESR1. 1 Publication

    Organism-specific databases

    PharmGKBiPA30316.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 411410LIM domain-binding protein 1PRO_0000084384Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Post-translational modificationi

    Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome.By similarity

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ86U70.
    PaxDbiQ86U70.
    PRIDEiQ86U70.

    PTM databases

    PhosphoSiteiQ86U70.

    Expressioni

    Tissue specificityi

    Expressed in a wide range of adult tissues including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes.1 Publication

    Gene expression databases

    BgeeiQ86U70.
    CleanExiHS_LDB1.
    GenevestigatoriQ86U70.

    Organism-specific databases

    HPAiHPA034488.

    Interactioni

    Subunit structurei

    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 similarity. Interacts with ESR1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi114384. 25 interactions.
    DIPiDIP-31826N.
    IntActiQ86U70. 18 interactions.
    MINTiMINT-233462.
    STRINGi9606.ENSP00000392466.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi337 – 3393
    Turni346 – 3494
    Beta strandi355 – 3573
    Beta strandi359 – 3624

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XJYX-ray2.40B334-368[»]
    2XJZX-ray2.80I/J/K/L/M334-368[»]
    2YPAX-ray2.80D336-375[»]
    ProteinModelPortaliQ86U70.
    SMRiQ86U70. Positions 336-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86U70.

    Family & Domainsi

    Region

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

    Domaini

    The dimerization domain is located in the N-terminus.By similarity

    Sequence similaritiesi

    Belongs to the LDB family.Curated

    Phylogenomic databases

    eggNOGiNOG282114.
    HOGENOMiHOG000030908.
    HOVERGENiHBG000135.
    InParanoidiQ86U70.
    KOiK15617.
    OMAiGSNSPWN.
    OrthoDBiEOG7DC24T.
    PhylomeDBiQ86U70.
    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: Q86U70-1) [UniParc]FASTAAdd to Basket

    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 MVAPPAEPTR QQPSKRRKRK 300
    MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF 350
    GDEDERLITR LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES 400
    KSENPTSQAS Q 411

    Note: No experimental confirmation available.

    Length:411
    Mass (Da):46,533
    Last modified:September 11, 2007 - v2
    Checksum:i5BB5348A36044580
    GO
    Isoform 2 (identifier: Q86U70-3) [UniParc]FASTAAdd to Basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.
         336-352: DVMVVGEPTLMGGEFGD → VSISAFFSLLGCPTTHP
         353-411: Missing.

    Note: Due to intron retention. Lacks LIM-binding domain.

    Show »
    Length:316
    Mass (Da):36,428
    Checksum:iB086EB4D28FC8E56
    GO
    Isoform 3 (identifier: Q86U70-2) [UniParc]FASTAAdd to Basket

    Also known as: a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.

    Show »
    Length:375
    Mass (Da):42,809
    Checksum:i698AC67CB5BD2DE7
    GO

    Sequence cautioni

    The sequence CAB45409.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti299 – 2991R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036366

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3636Missing in isoform 2 and isoform 3. 7 PublicationsVSP_027830Add
    BLAST
    Alternative sequencei336 – 35217DVMVV…GEFGD → VSISAFFSLLGCPTTHP in isoform 2. 2 PublicationsVSP_027831Add
    BLAST
    Alternative sequencei353 – 41159Missing in isoform 2. 2 PublicationsVSP_027832Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068652 mRNA. Translation: AAC77818.1.
    AJ243098 Genomic DNA. Translation: CAB45409.1. Different initiation.
    AB016485 mRNA. Translation: BAA31991.1.
    AB250384 mRNA. Translation: BAE95402.1.
    AF064491 mRNA. Translation: AAC28341.1.
    BT007054 mRNA. Translation: AAP35703.1.
    AK300588 mRNA. Translation: BAG62286.1.
    AL500527 Genomic DNA. No translation available.
    BC000482 mRNA. Translation: AAH00482.1.
    BC009246 mRNA. Translation: AAH09246.1.
    CCDSiCCDS44472.1. [Q86U70-1]
    CCDS7528.1. [Q86U70-2]
    RefSeqiNP_001106878.1. NM_001113407.1. [Q86U70-1]
    NP_003884.1. NM_003893.4. [Q86U70-2]
    UniGeneiHs.454418.

    Genome annotation databases

    EnsembliENST00000361198; ENSP00000354616; ENSG00000198728. [Q86U70-2]
    ENST00000425280; ENSP00000392466; ENSG00000198728. [Q86U70-1]
    GeneIDi8861.
    KEGGihsa:8861.
    UCSCiuc001kuk.4. human. [Q86U70-1]
    uc001kul.3. human. [Q86U70-3]

    Polymorphism databases

    DMDMi158518615.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068652 mRNA. Translation: AAC77818.1 .
    AJ243098 Genomic DNA. Translation: CAB45409.1 . Different initiation.
    AB016485 mRNA. Translation: BAA31991.1 .
    AB250384 mRNA. Translation: BAE95402.1 .
    AF064491 mRNA. Translation: AAC28341.1 .
    BT007054 mRNA. Translation: AAP35703.1 .
    AK300588 mRNA. Translation: BAG62286.1 .
    AL500527 Genomic DNA. No translation available.
    BC000482 mRNA. Translation: AAH00482.1 .
    BC009246 mRNA. Translation: AAH09246.1 .
    CCDSi CCDS44472.1. [Q86U70-1 ]
    CCDS7528.1. [Q86U70-2 ]
    RefSeqi NP_001106878.1. NM_001113407.1. [Q86U70-1 ]
    NP_003884.1. NM_003893.4. [Q86U70-2 ]
    UniGenei Hs.454418.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XJY X-ray 2.40 B 334-368 [» ]
    2XJZ X-ray 2.80 I/J/K/L/M 334-368 [» ]
    2YPA X-ray 2.80 D 336-375 [» ]
    ProteinModelPortali Q86U70.
    SMRi Q86U70. Positions 336-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114384. 25 interactions.
    DIPi DIP-31826N.
    IntActi Q86U70. 18 interactions.
    MINTi MINT-233462.
    STRINGi 9606.ENSP00000392466.

    PTM databases

    PhosphoSitei Q86U70.

    Polymorphism databases

    DMDMi 158518615.

    Proteomic databases

    MaxQBi Q86U70.
    PaxDbi Q86U70.
    PRIDEi Q86U70.

    Protocols and materials databases

    DNASUi 8861.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361198 ; ENSP00000354616 ; ENSG00000198728 . [Q86U70-2 ]
    ENST00000425280 ; ENSP00000392466 ; ENSG00000198728 . [Q86U70-1 ]
    GeneIDi 8861.
    KEGGi hsa:8861.
    UCSCi uc001kuk.4. human. [Q86U70-1 ]
    uc001kul.3. human. [Q86U70-3 ]

    Organism-specific databases

    CTDi 8861.
    GeneCardsi GC10M103857.
    H-InvDB HIX0009148.
    HGNCi HGNC:6532. LDB1.
    HPAi HPA034488.
    MIMi 603451. gene.
    neXtProti NX_Q86U70.
    PharmGKBi PA30316.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282114.
    HOGENOMi HOG000030908.
    HOVERGENi HBG000135.
    InParanoidi Q86U70.
    KOi K15617.
    OMAi GSNSPWN.
    OrthoDBi EOG7DC24T.
    PhylomeDBi Q86U70.
    TreeFami TF319923.

    Miscellaneous databases

    EvolutionaryTracei Q86U70.
    GeneWikii LDB1.
    GenomeRNAii 8861.
    NextBioi 33273.
    PROi Q86U70.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q86U70.
    CleanExi HS_LDB1.
    Genevestigatori Q86U70.

    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. "Cloning and chromosomal localization of two novel human genes encoding LIM-domain binding factors CLIM1 and CLIM2/LDB1/NLI."
      Semina E.V., Altherr M.R., Murray J.C.
      Mamm. Genome 9:921-924(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Craniofacial.
    2. "Genomic structure, alternative transcripts and chromosome location of the human LIM domain binding protein gene LDB1."
      Drechsler M., Schumacher V., Friedrich S., Wildhardt G., Giesler S., Schroth A., Bodem J., Royer-Pokora B.
      Cytogenet. Cell Genet. 87:119-124(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Isolation and chromosomal assignment of human genes encoding cofactor of LIM homeodomain proteins, CLIM1 and CLIM2."
      Ueki N., Seki N., Yano K., Ohira M., Saito T., Masuho Y., Muramatsu M.
      J. Hum. Genet. 44:112-115(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "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), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    5. "Cloning, characterization, and physical mapping of the human homologs of the mouse C-LIM gene."
      Phillips J.C., Goldman D.A., Wiggs J.L.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Fetal brain.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    8. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
      Tissue: Muscle.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer."
      Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L., Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G., Scheffner M., Pantel K., Gannon F., Bach I.
      Cancer Res. 69:128-136(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESR1, MUTAGENESIS OF 245-LEU--LEU-249, MISCELLANEOUS.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structure of the leukemia oncogene LMO2: implications for the assembly of a hematopoietic transcription factor complex."
      El Omari K., Hoosdally S.J., Tuladhar K., Karia D., Vyas P., Patient R., Porcher C., Mancini E.J.
      Blood 117:2146-2156(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 334-368 ALONE AND IN COMPLEX WITH LMO2, SUBUNIT.
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-299.

    Entry informationi

    Entry nameiLDB1_HUMAN
    AccessioniPrimary (citable) accession number: Q86U70
    Secondary accession number(s): B4DUC4
    , O75479, O96010, Q1EQX1, Q9UGM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 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

    Miscellaneous

    Acts as a negative coregulator of ESR1-mediated transcription in breast cancer cells.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3