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Q86U70 - LDB1_HUMAN

UniProt

Q86U70 - LDB1_HUMAN

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Protein

LIM domain-binding protein 1

Gene

LDB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB
  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. histone H3-K4 acetylation Source: BHF-UCL
  8. multicellular organismal development Source: UniProtKB
  9. negative regulation of erythrocyte differentiation Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. neuron differentiation Source: UniProtKB
  12. positive regulation of cell adhesion Source: Ensembl
  13. positive regulation of hemoglobin biosynthetic process Source: BHF-UCL
  14. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  15. regulation of DNA-templated transcription, elongation Source: BHF-UCL
  16. regulation of transcription, DNA-templated Source: ProtInc
  17. somatic stem cell maintenance Source: Ensembl
  18. transcription, DNA-templated Source: UniProtKB
  19. transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: BHF-UCL
  20. transcription from RNA polymerase II promoter Source: Ensembl
  21. Wnt signaling pathway Source: Ensembl
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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
Complete GO annotation...

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. 33 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 – 3393Combined sources
Turni346 – 3494Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi359 – 3624Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000005639.
HOGENOMiHOG000030908.
HOVERGENiHBG000135.
InParanoidiQ86U70.
KOiK15617.
OMAiGSNSPWN.
OrthoDBiEOG7DC24T.
PhylomeDBiQ86U70.
TreeFamiTF319923.

Family and domain databases

InterProiIPR030167. LDB1.
IPR029005. LIM-bd/SEUSS.
IPR002691. LIM-dom-bd.
[Graphical view]
PANTHERiPTHR10378. PTHR10378. 1 hit.
PTHR10378:SF7. PTHR10378:SF7. 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

        10         20         30         40         50
MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP 
        60         70         80         90        100
TYLEPGIGRH TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED 
       110        120        130        140        150
DAMLTITFCL EDGPKRYTIG RTLIPRYFRS IFEGGATELY YVLKHPKEAF 
       160        170        180        190        200
HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG RLYLEFMFDD MMRIKTWHFS 
       210        220        230        240        250
IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL NYLRLCVILE 
       260        270        280        290        300
PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPTR QQPSKRRKRK 
       310        320        330        340        350
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF 
       360        370        380        390        400
GDEDERLITR LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES 
       410 
KSENPTSQAS Q

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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi114384. 33 interactions.
DIPiDIP-31826N.
IntActiQ86U70. 18 interactions.
MINTiMINT-233462.
STRINGi9606.ENSP00000392466.

PTM databases

PhosphoSiteiQ86U70.

Polymorphism databases

DMDMi158518615.

Proteomic databases

MaxQBiQ86U70.
PaxDbiQ86U70.
PRIDEiQ86U70.

Protocols and materials databases

DNASUi8861.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi8861.
GeneCardsiGC10M103857.
H-InvDBHIX0009148.
HGNCiHGNC:6532. LDB1.
HPAiHPA034488.
MIMi603451. gene.
neXtProtiNX_Q86U70.
PharmGKBiPA30316.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282114.
GeneTreeiENSGT00390000005639.
HOGENOMiHOG000030908.
HOVERGENiHBG000135.
InParanoidiQ86U70.
KOiK15617.
OMAiGSNSPWN.
OrthoDBiEOG7DC24T.
PhylomeDBiQ86U70.
TreeFamiTF319923.

Miscellaneous databases

ChiTaRSiLDB1. human.
EvolutionaryTraceiQ86U70.
GeneWikiiLDB1.
GenomeRNAii8861.
NextBioi33273.
PROiQ86U70.
SOURCEiSearch...

Gene expression databases

BgeeiQ86U70.
CleanExiHS_LDB1.
GenevestigatoriQ86U70.

Family and domain databases

InterProiIPR030167. LDB1.
IPR029005. LIM-bd/SEUSS.
IPR002691. LIM-dom-bd.
[Graphical view]
PANTHERiPTHR10378. PTHR10378. 1 hit.
PTHR10378:SF7. PTHR10378:SF7. 1 hit.
PfamiPF01803. LIM_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 115 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

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.