Q86U70 (LDB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LDB1
Synonyms:	CLIM2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.11 Ref.14
Subcellular location	Nucleus Probable.
Tissue specificity	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. Ref.4
Domain	The dimerization domain is located in the N-terminus By similarity.
Post-translational modification	Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome By similarity.
Miscellaneous	Acts as a negative coregulator of ESR1-mediated transcription in breast cancer cells.
Sequence similarities	Belongs to the LDB family.
Sequence caution	The sequence CAB45409.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Developmental protein
PTM	Acetylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt signaling pathway Inferred from electronic annotation. Source: Ensembl anterior/posterior axis specification Inferred from electronic annotation. Source: Ensembl cellular component assembly Inferred from electronic annotation. Source: Ensembl cerebellar Purkinje cell differentiation Inferred from electronic annotation. Source: Ensembl epithelial structure maintenance Inferred from electronic annotation. Source: Ensembl gastrulation with mouth forming second Inferred from electronic annotation. Source: Ensembl hair follicle development Inferred from electronic annotation. Source: Ensembl head development Inferred from electronic annotation. Source: Ensembl histone H3-K4 acetylation Inferred from sequence or structural similarity. Source: BHF-UCL multicellular organismal development Non-traceable author statement PubMed 12792813. Source: UniProtKB negative regulation of erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-templated Inferred from direct assay PubMed 10767331. Source: UniProtKB neuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell adhesion Inferred from electronic annotation. Source: Ensembl positive regulation of hemoglobin biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 20855495. Source: BHF-UCL regulation of DNA-templated transcription, elongation Inferred from sequence or structural similarity. Source: BHF-UCL regulation of transcription, DNA-templated Non-traceable author statement PubMed 12792813. Source: ProtInc somatic stem cell maintenance Inferred from electronic annotation. Source: Ensembl transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl transcription, DNA-templated Non-traceable author statement PubMed 12792813. Source: UniProtKB transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	nuclear chromatin Inferred from direct assay PubMed 20855495. Source: BHF-UCL nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from sequence or structural similarity. Source: UniProtKB transcription factor complex Inferred from direct assay PubMed 16314316. Source: BHF-UCL
Molecular_function	LIM domain binding Inferred from physical interaction PubMed 12792813. Source: UniProtKB RNA polymerase II activating transcription factor binding Inferred from physical interaction PubMed 16314316. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: Ensembl enhancer sequence-specific DNA binding Inferred from electronic annotation. Source: Ensembl enzyme binding Inferred from physical interaction PubMed 23382074. Source: UniProt protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB transcription corepressor activity Traceable author statement PubMed 9391090. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86U70-1)

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.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q86U70-3)

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.

Isoform 3 (identifier: Q86U70-2)

Also known as: a;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 411

410

LIM domain-binding protein 1

PRO_0000084384

Regions

Region

336 – 374

39

LIM-binding domain (LID) By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.10

Natural variations

Alternative sequence

1 – 36

36

Missing in isoform 2 and isoform 3.

VSP_027830

Alternative sequence

336 – 352

17

DVMVV…GEFGD → VSISAFFSLLGCPTTHP in isoform 2.

VSP_027831

Alternative sequence

353 – 411

59

Missing in isoform 2.

VSP_027832

Natural variant

299

1

R → Q in a colorectal cancer sample; somatic mutation. Ref.15

VAR_036366

Experimental info

Mutagenesis

245 – 249

5

LCVIL → ACVAA: Abolishes interaction with ESR1. Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

411

Helix Strand Turn

Details...

Beta strand

337 – 339

3

Turn

346 – 349

4

Beta strand

355 – 357

3

Beta strand

359 – 362

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 5BB5348A36044580	FASTA	411	46,533
	10 20 30 40 50 60 MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP TYLEPGIGRH 70 80 90 100 110 120 TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED DAMLTITFCL EDGPKRYTIG 130 140 150 160 170 180 RTLIPRYFRS IFEGGATELY YVLKHPKEAF HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG 190 200 210 220 230 240 RLYLEFMFDD MMRIKTWHFS IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL 250 260 270 280 290 300 NYLRLCVILE PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPTR QQPSKRRKRK 310 320 330 340 350 360 MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR 370 380 390 400 410 LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q
	Isoform 2 (b) [UniParc]. Checksum: B086EB4D28FC8E56	FASTA	316	36,428
	10 20 30 40 50 60 MLDRDVGPTP MYPPTYLEPG IGRHTPYGNQ TDYRIFELNK RLQNWTEECD NLWWDAFTTE 70 80 90 100 110 120 FFEDDAMLTI TFCLEDGPKR YTIGRTLIPR YFRSIFEGGA TELYYVLKHP KEAFHSNFVS 130 140 150 160 170 180 LDCDQGSMVT QHGKPMFTQV CVEGRLYLEF MFDDMMRIKT WHFSIRQHRE LIPRSILAMH 190 200 210 220 230 240 AQDPQMLDQL SKNITRCGLS NSTLNYLRLC VILEPMQELM SRHKTYSLSP RDCLKTCLFQ 250 260 270 280 290 300 KWQRMVAPPA EPTRQQPSKR RKRKMSGGST MSSGGGNTNN SNSKKKSPAS TFALSSQVPV 310 SISAFFSLLG CPTTHP
	Isoform 3 (a) [UniParc]. Checksum: 698AC67CB5BD2DE7	FASTA	375	42,809
	10 20 30 40 50 60 MLDRDVGPTP MYPPTYLEPG IGRHTPYGNQ TDYRIFELNK RLQNWTEECD NLWWDAFTTE 70 80 90 100 110 120 FFEDDAMLTI TFCLEDGPKR YTIGRTLIPR YFRSIFEGGA TELYYVLKHP KEAFHSNFVS 130 140 150 160 170 180 LDCDQGSMVT QHGKPMFTQV CVEGRLYLEF MFDDMMRIKT WHFSIRQHRE LIPRSILAMH 190 200 210 220 230 240 AQDPQMLDQL SKNITRCGLS NSTLNYLRLC VILEPMQELM SRHKTYSLSP RDCLKTCLFQ 250 260 270 280 290 300 KWQRMVAPPA EPTRQQPSKR RKRKMSGGST MSSGGGNTNN SNSKKKSPAS TFALSSQVPD 310 320 330 340 350 360 VMVVGEPTLM GGEFGDEDER LITRLENTQF DAANGIDDED SFNNSPALGA NSPWNSKPPS 370 SQESKSENPT SQASQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-299.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

CCDS

CCDS44472.1. [Q86U70-1]
CCDS7528.1. [Q86U70-2]

RefSeq

NP_001106878.1. NM_001113407.1. [Q86U70-1]
NP_003884.1. NM_003893.4. [Q86U70-2]

UniGene

Hs.454418.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	[»]

ProteinModelPortal

Q86U70.

SMR

Q86U70. Positions 336-363.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

114384. 25 interactions.

DIP

DIP-31826N.

IntAct

Q86U70. 18 interactions.

MINT

MINT-233462.

STRING

9606.ENSP00000392466.

PTM databases

PhosphoSite

Q86U70.

Polymorphism databases

DMDM

158518615.

Proteomic databases

MaxQB

Q86U70.

PaxDb

Q86U70.

PRIDE

Q86U70.

Protocols and materials databases

DNASU

8861.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361198; ENSP00000354616; ENSG00000198728. [Q86U70-2]
ENST00000425280; ENSP00000392466; ENSG00000198728. [Q86U70-1]

GeneID

8861.

KEGG

hsa:8861.

UCSC

uc001kuk.4. human. [Q86U70-1]
uc001kul.3. human. [Q86U70-3]

Organism-specific databases

CTD

8861.

GeneCards

GC10M103857.

H-InvDB

HIX0009148.

HGNC

HGNC:6532. LDB1.

HPA

HPA034488.

MIM

603451. gene.

neXtProt

NX_Q86U70.

PharmGKB

PA30316.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282114.

HOGENOM

HOG000030908.

HOVERGEN

HBG000135.

InParanoid

Q86U70.

KO

K15617.

OMA

GSNSPWN.

OrthoDB

EOG7DC24T.

PhylomeDB

Q86U70.

TreeFam

TF319923.

Gene expression databases

Bgee

Q86U70.

CleanEx

HS_LDB1.

Genevestigator

Q86U70.

Family and domain databases

InterPro

IPR029005. LIM-bd/SEUSS.
IPR002691. LIM-dom-bd.
[Graphical view]

PANTHER

PTHR10378. PTHR10378. 1 hit.

Pfam

PF01803. LIM_bind. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q86U70.

GeneWiki

LDB1.

GenomeRNAi

8861.

NextBio

33273.

PRO

Q86U70.

SOURCE

Search...

Entry information

Entry name

LDB1_HUMAN

Accession

Primary (citable) accession number: Q86U70
Secondary accession number(s): B4DUC4 , O75479, O96010, Q1EQX1, Q9UGM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	September 11, 2007
Last modified:	July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.