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P70662

- LDB1_MOUSE

UniProt

P70662 - LDB1_MOUSE

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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

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 homodimerization activity Source: UniProtKB
  6. protein self-association Source: MGI
  7. transcription cofactor activity Source: InterPro
  8. 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
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:
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
Complete GO annotation...

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

MaxQBiP70662.
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

BgeeiP70662.
CleanExiMM_LDB1.
ExpressionAtlasiP70662. baseline and differential.
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 – 3093Combined sources
Beta strandi315 – 3217Combined sources
Turni322 – 3243Combined sources
Beta strandi325 – 3273Combined sources
Turni329 – 3313Combined sources
Beta strandi336 – 3449Combined sources
Beta strandi346 – 3494Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi359 – 3624Combined sources
Turni369 – 3713Combined sources
Beta strandi379 – 3846Combined sources
Beta strandi387 – 3893Combined sources
Helixi391 – 3933Combined sources
Turni397 – 3993Combined sources
Beta strandi408 – 4114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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 MVAPPAEPAR QQPSKRRKRK
310 320 330 340 350
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF
360 370 380 390 400
GDEDERLITR LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES
410
KSENPTSQAS Q
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:
     1-36: 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:319
Mass (Da):36,667
Checksum:i2FD1D15303732E5E
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:
     1-36: Missing.

Show »
Length:375
Mass (Da):42,779
Checksum:i75FACF0CA0BD2DE7
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 sequencei1 – 3636Missing 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:
EMBLi
GenBanki
DDBJi
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]
ENSMUST00000185355; ENSMUSP00000139562; 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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

MaxQBi P70662.
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 ]
ENSMUST00000185355 ; ENSMUSP00000139562 ; 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

Bgeei P70662.
CleanExi MM_LDB1.
ExpressionAtlasi P70662. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 127 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