UniProtKB - Q14739 (LBR_HUMAN)
Protein
Delta(14)-sterol reductase LBR
Gene
LBR
Organism
Homo sapiens (Human)
Status
Functioni
Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:9630650, PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963).By similarity6 Publications
Catalytic activityi
- 4,4-dimethyl-5α-cholesta-8,24-dien-3β-ol + NADP+ = 4,4-dimethyl-5α-cholesta-8,14,24-trien-3β-ol + H+ + NADPH2 PublicationsEC:1.3.1.702 Publications
- 4,4-dimethyl-8,14-cholestadien-3β-ol + H+ + NADPH = 4,4-dimethyl-5α-cholest-8-en-3β-ol + NADP+3 Publications
: cholesterol biosynthesis Pathwayi
This protein is involved in the pathway cholesterol biosynthesis, which is part of Steroid biosynthesis.View all proteins of this organism that are known to be involved in the pathway cholesterol biosynthesis and in Steroid biosynthesis.
GO - Molecular functioni
- chromo shadow domain binding Source: BHF-UCL
- delta14-sterol reductase activity Source: UniProtKB
- DNA binding Source: ProtInc
- lamin binding Source: ProtInc
- NADPH binding Source: UniProtKB
- oxidoreductase activity, acting on the CH-CH group of donors Source: GO_Central
- RNA binding Source: UniProtKB
GO - Biological processi
- cholesterol biosynthetic process Source: UniProtKB
- neutrophil differentiation Source: UniProtKB
- sterol biosynthetic process Source: GO_Central
Keywordsi
Molecular function | DNA-binding, Oxidoreductase, Receptor |
Biological process | Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism |
Enzyme and pathway databases
BioCyci | MetaCyc:HS07110-MONOMER |
BRENDAi | 1.3.1.70, 2681 |
PathwayCommonsi | Q14739 |
Reactomei | R-HSA-191273, Cholesterol biosynthesis R-HSA-2995383, Initiation of Nuclear Envelope (NE) Reformation R-HSA-9022692, Regulation of MECP2 expression and activity |
SIGNORi | Q14739 |
UniPathwayi | UPA00063 |
Chemistry databases
SwissLipidsi | SLP:000001239 |
Names & Taxonomyi
Protein namesi | Recommended name: Delta(14)-sterol reductase LBR (EC:1.3.1.702 Publications)Short name: Delta-14-SR Alternative name(s): 3-beta-hydroxysterol Delta (14)-reductase1 Publication C-14 sterol reductase Short name: C14SR Integral nuclear envelope inner membrane protein1 Publication LMN2R Lamin-B receptor2 Publications Sterol C14-reductase |
Gene namesi | Name:LBR |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000143815.14 |
HGNCi | HGNC:6518, LBR |
MIMi | 600024, gene |
neXtProti | NX_Q14739 |
Subcellular locationi
Nucleus
- Nucleus inner membrane 1 Publication; Multi-pass membrane protein Sequence analysis
- Nucleus 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum membrane 1 Publication
Other locations
- Cytoplasm 1 Publication
Note: Nucleus; nuclear rim.1 Publication
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB
Nucleus
- integral component of nuclear inner membrane Source: ProtInc
- nuclear envelope Source: Reactome
- nuclear inner membrane Source: GO_Central
- nuclear membrane Source: HPA
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
- integral component of membrane Source: MGI
- membrane Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 211 | NuclearSequence analysisAdd BLAST | 211 | |
Transmembranei | 212 – 232 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 258 – 278 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 299 – 319 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 326 – 346 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 386 – 406 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 447 – 467 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 481 – 501 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 561 – 581 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, Membrane, NucleusPathology & Biotechi
Involvement in diseasei
Pelger-Huet anomaly (PHA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_017841 | 119 | P → L in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852605Ensembl. | 1 | |
Natural variantiVAR_017842 | 569 | P → R in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852606Ensembl. | 1 |
Greenberg dysplasia (GRBGD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081220 | 547 | N → D in GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability. 2 PublicationsCorresponds to variant dbSNP:rs587777171EnsemblClinVar. | 1 | |
Natural variantiVAR_081221 | 583 | R → Q in GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability. 2 PublicationsCorresponds to variant dbSNP:rs587777172EnsemblClinVar. | 1 |
Reynolds syndrome (REYNS)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_063811 | 372 | R → C in REYNS. 1 PublicationCorresponds to variant dbSNP:rs200180113EnsemblClinVar. | 1 |
Pelger-Huet anomaly with mild skeletal anomalies (PHASK)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by abnormal nuclear shape and chromatin organization in blood granulocytes, short stature, and mild skeletal anomalies. Initial skeletal features may improve with age.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081005 | 76 – 615 | Missing in PHASK. 1 PublicationCorresponds to variant dbSNP:rs869312905Add BLAST | 540 | |
Natural variantiVAR_081006 | 547 | N → S in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs374343844EnsemblClinVar. | 1 | |
Natural variantiVAR_081007 | 586 | R → H in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs573510559EnsemblClinVar. | 1 |
Keywords - Diseasei
Disease mutation, DwarfismOrganism-specific databases
DisGeNETi | 3930 |
MalaCardsi | LBR |
MIMi | 169400, phenotype 215140, phenotype 613471, phenotype 618019, phenotype |
OpenTargetsi | ENSG00000143815 |
Orphaneti | 1426, Greenberg dysplasia 448267, Regressive spondylometaphyseal dysplasia 779, Reynolds syndrome |
PharmGKBi | PA30304 |
Miscellaneous databases
Pharosi | Q14739, Tbio |
Polymorphism and mutation databases
BioMutai | LBR |
DMDMi | 20141468 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207510 | 1 – 615 | Delta(14)-sterol reductase LBRAdd BLAST | 615 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 55 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 58 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 59 | PhosphoserineCombined sources | 1 | |
Modified residuei | 67 | PhosphoserineBy similarity | 1 | |
Modified residuei | 71 | Phosphoserine; by CDK11 Publication | 1 | |
Modified residuei | 86 | Phosphoserine; by CDK11 Publication | 1 | |
Modified residuei | 97 | PhosphoserineCombined sources | 1 | |
Modified residuei | 99 | PhosphoserineCombined sources | 1 | |
Modified residuei | 118 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 128 | PhosphoserineCombined sources | 1 | |
Modified residuei | 200 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 594 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 601 | N6-acetyllysineCombined sources | 1 |
Post-translational modificationi
Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin.2 Publications
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q14739 |
jPOSTi | Q14739 |
MassIVEi | Q14739 |
MaxQBi | Q14739 |
PaxDbi | Q14739 |
PeptideAtlasi | Q14739 |
PRIDEi | Q14739 |
ProteomicsDBi | 60152 |
TopDownProteomicsi | Q14739 |
PTM databases
iPTMneti | Q14739 |
PhosphoSitePlusi | Q14739 |
SwissPalmi | Q14739 |
Expressioni
Tissue specificityi
Expressed in the bone marrow, liver, heart, adrenal gland, lung, placenta and uterus (PubMed:16784888). Expressed in osteoclasts and osteoblast-like cells (PubMed:21327084).2 Publications
Gene expression databases
Bgeei | ENSG00000143815, Expressed in bone marrow and 248 other tissues |
ExpressionAtlasi | Q14739, baseline and differential |
Genevisiblei | Q14739, HS |
Organism-specific databases
HPAi | ENSG00000143815, Tissue enhanced (lymphoid) |
Interactioni
Subunit structurei
Interacts with CBX5 (PubMed:9169472, PubMed:15882967).
Interacts with DNA (PubMed:8157662). Interaction with DNA is sequence independent with higher affinity for supercoiled and relaxed circular DNA than linear DNA (PubMed:8157662).
Interacts with lamin B (PubMed:8157662).
Interacts with CLNK (PubMed:26009488).
4 PublicationsBinary interactionsi
Hide detailsQ14739
With | #Exp. | IntAct |
---|---|---|
CBX3 [Q13185] | 4 | EBI-1055147,EBI-78176 |
CBX5 [P45973] | 4 | EBI-1055147,EBI-78219 |
CD81 [P60033] | 3 | EBI-1055147,EBI-712921 |
GO - Molecular functioni
- chromo shadow domain binding Source: BHF-UCL
- lamin binding Source: ProtInc
Protein-protein interaction databases
BioGRIDi | 110122, 97 interactors |
DIPi | DIP-5987N |
IntActi | Q14739, 53 interactors |
MINTi | Q14739 |
STRINGi | 9606.ENSP00000339883 |
Miscellaneous databases
RNActi | Q14739, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | Q14739 |
SMRi | Q14739 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q14739 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 62 | TudorAdd BLAST | 62 |
Domaini
The Tudor domain may not recognize methylation marks, but rather bind unassembled free histone H3.By similarity
Sequence similaritiesi
Belongs to the ERG4/ERG24 family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1435, Eukaryota |
GeneTreei | ENSGT00390000000417 |
HOGENOMi | CLU_015631_0_2_1 |
InParanoidi | Q14739 |
OMAi | WGVELYY |
OrthoDBi | 532774at2759 |
PhylomeDBi | Q14739 |
TreeFami | TF101179 |
Family and domain databases
InterProi | View protein in InterPro IPR001171, Ergosterol_biosynth_ERG4_ERG24 IPR019023, Lamin-B_rcpt_of_tudor IPR018083, Sterol_reductase_CS IPR002999, Tudor |
Pfami | View protein in Pfam PF01222, ERG4_ERG24, 1 hit PF09465, LBR_tudor, 1 hit |
SMARTi | View protein in SMART SM00333, TUDOR, 1 hit |
PROSITEi | View protein in PROSITE PS01017, STEROL_REDUCT_1, 1 hit PS01018, STEROL_REDUCT_2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
Q14739-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK
60 70 80 90 100
ENDIKPLTSF RQRKGGSTSS SPSRRRGSRS RSRSRSPGRP PKSARRSASA
110 120 130 140 150
SHQADIKEAR REVEVKLTPL ILKPFGNSIS RYNGEPEHIE RNDAPHKNTQ
160 170 180 190 200
EKFSLSQESS YIATQYSLRP RREEVKLKEI DSKEEKYVAK ELAVRTFEVT
210 220 230 240 250
PIRAKDLEFG GVPGVFLIMF GLPVFLFLLL LMCKQKDPSL LNFPPPLPAL
260 270 280 290 300
YELWETRVFG VYLLWFLIQV LFYLLPIGKV VEGTPLIDGR RLKYRLNGFY
310 320 330 340 350
AFILTSAVIG TSLFQGVEFH YVYSHFLQFA LAATVFCVVL SVYLYMRSLK
360 370 380 390 400
APRNDLSPAS SGNAVYDFFI GRELNPRIGT FDLKYFCELR PGLIGWVVIN
410 420 430 440 450
LVMLLAEMKI QDRAVPSLAM ILVNSFQLLY VVDALWNEEA LLTTMDIIHD
460 470 480 490 500
GFGFMLAFGD LVWVPFIYSF QAFYLVSHPN EVSWPMASLI IVLKLCGYVI
510 520 530 540 550
FRGANSQKNA FRKNPSDPKL AHLKTIHTST GKNLLVSGWW GFVRHPNYLG
560 570 580 590 600
DLIMALAWSL PCGFNHILPY FYIIYFTMLL VHREARDEYH CKKKYGVAWE
610
KYCQRVPYRI FPYIY
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A494C1L1 | A0A494C1L1_HUMAN | 3-beta-hydroxysterol Delta (14)-red... | LBR | 411 | Annotation score: | ||
C9JXK0 | C9JXK0_HUMAN | Delta(14)-sterol reductase LBR | LBR | 213 | Annotation score: | ||
C9JES9 | C9JES9_HUMAN | Delta(14)-sterol reductase LBR | LBR | 51 | Annotation score: |
Sequence cautioni
The sequence BAD92751 differs from that shown. Reason: Erroneous initiation.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 301 | A → P in AAA59494 (PubMed:8157662).Curated | 1 | |
Sequence conflicti | 452 | F → L in BAD96554 (Ref. 5) Curated | 1 | |
Sequence conflicti | 530 | T → S in AAA59494 (PubMed:8157662).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081005 | 76 – 615 | Missing in PHASK. 1 PublicationCorresponds to variant dbSNP:rs869312905Add BLAST | 540 | |
Natural variantiVAR_017841 | 119 | P → L in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852605Ensembl. | 1 | |
Natural variantiVAR_024318 | 154 | S → N5 PublicationsCorresponds to variant dbSNP:rs2230419EnsemblClinVar. | 1 | |
Natural variantiVAR_052155 | 169 | R → C. Corresponds to variant dbSNP:rs2230420Ensembl. | 1 | |
Natural variantiVAR_020209 | 311 | T → A. Corresponds to variant dbSNP:rs2275601EnsemblClinVar. | 1 | |
Natural variantiVAR_063811 | 372 | R → C in REYNS. 1 PublicationCorresponds to variant dbSNP:rs200180113EnsemblClinVar. | 1 | |
Natural variantiVAR_081220 | 547 | N → D in GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability. 2 PublicationsCorresponds to variant dbSNP:rs587777171EnsemblClinVar. | 1 | |
Natural variantiVAR_081006 | 547 | N → S in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs374343844EnsemblClinVar. | 1 | |
Natural variantiVAR_017842 | 569 | P → R in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852606Ensembl. | 1 | |
Natural variantiVAR_081221 | 583 | R → Q in GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability. 2 PublicationsCorresponds to variant dbSNP:rs587777172EnsemblClinVar. | 1 | |
Natural variantiVAR_081007 | 586 | R → H in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs573510559EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L25931 mRNA Translation: AAA59494.1 L25941 , L25932, L25933, L25934, L25935, L25936, L25937, L25938, L25939, L25940 Genomic DNA Translation: AAA59495.1 AB209514 mRNA Translation: BAD92751.1 Different initiation. AK222834 mRNA Translation: BAD96554.1 AK312258 mRNA Translation: BAG35190.1 CH471098 Genomic DNA Translation: EAW69741.1 BC020079 mRNA Translation: AAH20079.1 |
CCDSi | CCDS1545.1 |
PIRi | A53616 |
RefSeqi | NP_002287.2, NM_002296.3 NP_919424.1, NM_194442.2 XP_011542487.1, XM_011544185.2 |
Genome annotation databases
Ensembli | ENST00000272163; ENSP00000272163; ENSG00000143815 ENST00000338179; ENSP00000339883; ENSG00000143815 |
GeneIDi | 3930 |
KEGGi | hsa:3930 |
UCSCi | uc001hoy.4, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L25931 mRNA Translation: AAA59494.1 L25941 , L25932, L25933, L25934, L25935, L25936, L25937, L25938, L25939, L25940 Genomic DNA Translation: AAA59495.1 AB209514 mRNA Translation: BAD92751.1 Different initiation. AK222834 mRNA Translation: BAD96554.1 AK312258 mRNA Translation: BAG35190.1 CH471098 Genomic DNA Translation: EAW69741.1 BC020079 mRNA Translation: AAH20079.1 |
CCDSi | CCDS1545.1 |
PIRi | A53616 |
RefSeqi | NP_002287.2, NM_002296.3 NP_919424.1, NM_194442.2 XP_011542487.1, XM_011544185.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2DIG | NMR | - | A | 1-55 | [»] | |
BMRBi | Q14739 | |||||
SMRi | Q14739 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 110122, 97 interactors |
DIPi | DIP-5987N |
IntActi | Q14739, 53 interactors |
MINTi | Q14739 |
STRINGi | 9606.ENSP00000339883 |
Chemistry databases
SwissLipidsi | SLP:000001239 |
PTM databases
iPTMneti | Q14739 |
PhosphoSitePlusi | Q14739 |
SwissPalmi | Q14739 |
Polymorphism and mutation databases
BioMutai | LBR |
DMDMi | 20141468 |
Proteomic databases
EPDi | Q14739 |
jPOSTi | Q14739 |
MassIVEi | Q14739 |
MaxQBi | Q14739 |
PaxDbi | Q14739 |
PeptideAtlasi | Q14739 |
PRIDEi | Q14739 |
ProteomicsDBi | 60152 |
TopDownProteomicsi | Q14739 |
Protocols and materials databases
Antibodypediai | 34642, 233 antibodies |
DNASUi | 3930 |
Genome annotation databases
Ensembli | ENST00000272163; ENSP00000272163; ENSG00000143815 ENST00000338179; ENSP00000339883; ENSG00000143815 |
GeneIDi | 3930 |
KEGGi | hsa:3930 |
UCSCi | uc001hoy.4, human |
Organism-specific databases
CTDi | 3930 |
DisGeNETi | 3930 |
EuPathDBi | HostDB:ENSG00000143815.14 |
GeneCardsi | LBR |
HGNCi | HGNC:6518, LBR |
HPAi | ENSG00000143815, Tissue enhanced (lymphoid) |
MalaCardsi | LBR |
MIMi | 169400, phenotype 215140, phenotype 600024, gene 613471, phenotype 618019, phenotype |
neXtProti | NX_Q14739 |
OpenTargetsi | ENSG00000143815 |
Orphaneti | 1426, Greenberg dysplasia 448267, Regressive spondylometaphyseal dysplasia 779, Reynolds syndrome |
PharmGKBi | PA30304 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1435, Eukaryota |
GeneTreei | ENSGT00390000000417 |
HOGENOMi | CLU_015631_0_2_1 |
InParanoidi | Q14739 |
OMAi | WGVELYY |
OrthoDBi | 532774at2759 |
PhylomeDBi | Q14739 |
TreeFami | TF101179 |
Enzyme and pathway databases
UniPathwayi | UPA00063 |
BioCyci | MetaCyc:HS07110-MONOMER |
BRENDAi | 1.3.1.70, 2681 |
PathwayCommonsi | Q14739 |
Reactomei | R-HSA-191273, Cholesterol biosynthesis R-HSA-2995383, Initiation of Nuclear Envelope (NE) Reformation R-HSA-9022692, Regulation of MECP2 expression and activity |
SIGNORi | Q14739 |
Miscellaneous databases
BioGRID-ORCSi | 3930, 4 hits in 851 CRISPR screens |
ChiTaRSi | LBR, human |
EvolutionaryTracei | Q14739 |
GeneWikii | Lamin_B_receptor |
GenomeRNAii | 3930 |
Pharosi | Q14739, Tbio |
PROi | PR:Q14739 |
RNActi | Q14739, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000143815, Expressed in bone marrow and 248 other tissues |
ExpressionAtlasi | Q14739, baseline and differential |
Genevisiblei | Q14739, HS |
Family and domain databases
InterProi | View protein in InterPro IPR001171, Ergosterol_biosynth_ERG4_ERG24 IPR019023, Lamin-B_rcpt_of_tudor IPR018083, Sterol_reductase_CS IPR002999, Tudor |
Pfami | View protein in Pfam PF01222, ERG4_ERG24, 1 hit PF09465, LBR_tudor, 1 hit |
SMARTi | View protein in SMART SM00333, TUDOR, 1 hit |
PROSITEi | View protein in PROSITE PS01017, STEROL_REDUCT_1, 1 hit PS01018, STEROL_REDUCT_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LBR_HUMAN | |
Accessioni | Q14739Primary (citable) accession number: Q14739 Secondary accession number(s): B2R5P3 Q59FE6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | January 31, 2002 | |
Last modified: | December 2, 2020 | |
This is version 202 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations