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Protein

Lamin-B receptor

Gene

LBR

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

Functioni

Anchors the lamina and the heterochromatin to the inner nuclear membrane.1 Publication

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • DNA binding Source: ProtInc
  • lamin binding Source: ProtInc
  • oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07110-MONOMER.
BRENDAi1.3.1.70. 2681.
ReactomeiREACT_9405. Cholesterol biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B receptor
Alternative name(s):
Integral nuclear envelope inner membrane protein
LMN2R
Gene namesi
Name:LBR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6518. LBR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 211211NuclearSequence AnalysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence AnalysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence AnalysisAdd
BLAST
Transmembranei299 – 31921HelicalSequence AnalysisAdd
BLAST
Transmembranei326 – 34621HelicalSequence AnalysisAdd
BLAST
Transmembranei386 – 40621HelicalSequence AnalysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence AnalysisAdd
BLAST
Transmembranei481 – 50121HelicalSequence AnalysisAdd
BLAST
Transmembranei561 – 58121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: MGI
  • integral component of nuclear inner membrane Source: ProtInc
  • membrane Source: UniProtKB
  • nuclear envelope Source: Reactome
  • nuclear membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & 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. Some individuals occasionally have skeletal anomalies, developmental delay, and seizures.

See also OMIM:169400
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191P → L in PHA. 1 Publication
VAR_017841
Natural varianti569 – 5691P → R in PHA. 1 Publication
VAR_017842
Greenberg dysplasia (GRBGD)1 Publication

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.

See also OMIM:215140
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.

See also OMIM:613471
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti372 – 3721R → C in REYNS. 1 Publication
VAR_063811

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi169400. phenotype.
215140. phenotype.
613471. phenotype.
Orphaneti1426. Greenberg dysplasia.
779. Reynolds syndrome.
PharmGKBiPA30304.

Polymorphism and mutation databases

BioMutaiLBR.
DMDMi20141468.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 615615Lamin-B receptorPRO_0000207510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei71 – 711Phosphoserine; by CDK11 Publication
Modified residuei86 – 861Phosphoserine; by CDK11 Publication
Modified residuei97 – 971Phosphoserine1 Publication
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei118 – 1181Phosphothreonine2 Publications
Modified residuei594 – 5941N6-acetyllysine1 Publication
Modified residuei601 – 6011N6-acetyllysine1 Publication

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, Phosphoprotein

Proteomic databases

MaxQBiQ14739.
PaxDbiQ14739.
PeptideAtlasiQ14739.
PRIDEiQ14739.

PTM databases

PhosphoSiteiQ14739.

Expressioni

Gene expression databases

BgeeiQ14739.
CleanExiHS_LBR.
ExpressionAtlasiQ14739. baseline and differential.
GenevisibleiQ14739. HS.

Organism-specific databases

HPAiHPA049840.
HPA062236.

Interactioni

Subunit structurei

Interacts directly with CBX5. Can interact with chromodomain proteins. Interacts directly with DNA. Interaction with DNA is sequence independent with higher affinity for supercoiled and relaxed circular DNA than linear DNA.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX3Q131854EBI-1055147,EBI-78176
CBX5P459734EBI-1055147,EBI-78219

Protein-protein interaction databases

BioGridi110122. 33 interactions.
DIPiDIP-5987N.
IntActiQ14739. 9 interactions.
MINTiMINT-1631069.
STRINGi9606.ENSP00000272163.

Structurei

Secondary structure

1
615
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 155Combined sources
Turni17 – 193Combined sources
Beta strandi22 – 3110Combined sources
Turni32 – 354Combined sources
Beta strandi36 – 405Combined sources
Beta strandi46 – 505Combined sources
Turni51 – 533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIGNMR-A1-55[»]
ProteinModelPortaliQ14739.
SMRiQ14739. Positions 1-55, 216-615.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14739.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6262TudorAdd
BLAST

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
Contains 1 Tudor domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG72042.
GeneTreeiENSGT00390000000417.
HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiQ14739.
OMAiIFRSANK.
OrthoDBiEOG75B85C.
PhylomeDBiQ14739.
TreeFamiTF101179.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR019023. Lamin-B_rcpt_of_tudor.
IPR018083. Sterol_reductase_CS.
IPR002999. Tudor.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
PF09465. LBR_tudor. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14739-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:615
Mass (Da):70,703
Last modified:January 31, 2002 - v2
Checksum:i5A7388776F43C66D
GO

Sequence cautioni

The sequence BAD92751.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011A → P in AAA59494 (PubMed:8157662).Curated
Sequence conflicti452 – 4521F → L in BAD96554 (Ref. 5) Curated
Sequence conflicti530 – 5301T → S in AAA59494 (PubMed:8157662).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191P → L in PHA. 1 Publication
VAR_017841
Natural varianti154 – 1541S → N.5 Publications
Corresponds to variant rs2230419 [ dbSNP | Ensembl ].
VAR_024318
Natural varianti169 – 1691R → C.
Corresponds to variant rs2230420 [ dbSNP | Ensembl ].
VAR_052155
Natural varianti311 – 3111T → A.
Corresponds to variant rs2275601 [ dbSNP | Ensembl ].
VAR_020209
Natural varianti372 – 3721R → C in REYNS. 1 Publication
VAR_063811
Natural varianti569 – 5691P → R in PHA. 1 Publication
VAR_017842

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.
CCDSiCCDS1545.1.
PIRiA53616.
RefSeqiNP_002287.2. NM_002296.3.
NP_919424.1. NM_194442.2.
UniGeneiHs.435166.
Hs.735694.

Genome annotation databases

EnsembliENST00000272163; ENSP00000272163; ENSG00000143815.
ENST00000338179; ENSP00000339883; ENSG00000143815.
GeneIDi3930.
KEGGihsa:3930.
UCSCiuc001hoy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

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.
CCDSiCCDS1545.1.
PIRiA53616.
RefSeqiNP_002287.2. NM_002296.3.
NP_919424.1. NM_194442.2.
UniGeneiHs.435166.
Hs.735694.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIGNMR-A1-55[»]
ProteinModelPortaliQ14739.
SMRiQ14739. Positions 1-55, 216-615.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110122. 33 interactions.
DIPiDIP-5987N.
IntActiQ14739. 9 interactions.
MINTiMINT-1631069.
STRINGi9606.ENSP00000272163.

PTM databases

PhosphoSiteiQ14739.

Polymorphism and mutation databases

BioMutaiLBR.
DMDMi20141468.

Proteomic databases

MaxQBiQ14739.
PaxDbiQ14739.
PeptideAtlasiQ14739.
PRIDEiQ14739.

Protocols and materials databases

DNASUi3930.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272163; ENSP00000272163; ENSG00000143815.
ENST00000338179; ENSP00000339883; ENSG00000143815.
GeneIDi3930.
KEGGihsa:3930.
UCSCiuc001hoy.3. human.

Organism-specific databases

CTDi3930.
GeneCardsiGC01M225589.
HGNCiHGNC:6518. LBR.
HPAiHPA049840.
HPA062236.
MIMi169400. phenotype.
215140. phenotype.
600024. gene.
613471. phenotype.
neXtProtiNX_Q14739.
Orphaneti1426. Greenberg dysplasia.
779. Reynolds syndrome.
PharmGKBiPA30304.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72042.
GeneTreeiENSGT00390000000417.
HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiQ14739.
OMAiIFRSANK.
OrthoDBiEOG75B85C.
PhylomeDBiQ14739.
TreeFamiTF101179.

Enzyme and pathway databases

BioCyciMetaCyc:HS07110-MONOMER.
BRENDAi1.3.1.70. 2681.
ReactomeiREACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSiLBR. human.
EvolutionaryTraceiQ14739.
GeneWikiiLamin_B_receptor.
GenomeRNAii3930.
NextBioi15431.
PROiQ14739.
SOURCEiSearch...

Gene expression databases

BgeeiQ14739.
CleanExiHS_LBR.
ExpressionAtlasiQ14739. baseline and differential.
GenevisibleiQ14739. HS.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR019023. Lamin-B_rcpt_of_tudor.
IPR018083. Sterol_reductase_CS.
IPR002999. Tudor.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
PF09465. LBR_tudor. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane."
    Ye Q., Worman H.J.
    J. Biol. Chem. 269:11306-11311(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DNA; LMNB1 AND LMNB2.
  2. "Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane."
    Schuler E., Lin F., Worman H.J.
    J. Biol. Chem. 269:11312-11317(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-154.
  3. "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], VARIANT ASN-154.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-154.
    Tissue: Brain.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-154.
    Tissue: Liver.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-154.
  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].
    Tissue: Skin.
  8. "Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR."
    Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.
    J. Biol. Chem. 272:14983-14989(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CBX5.
  9. "SRPK1 and LBR protein kinases show identical substrate specificities."
    Papoutsopoulou S., Nikolakaki E., Giannakouros T.
    Biochem. Biophys. Res. Commun. 255:602-607(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRPK1.
  10. "Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker."
    Duband-Goulet I., Courvalin J.-C.
    Biochemistry 39:6483-6488(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)."
    Hoffmann K., Dreger C.K., Olins A.L., Olins D.E., Shultz L.D., Lucke B., Karl H., Kaps R., Mueller D., Vaya A., Aznar J., Ware R.E., Sotelo Cruz N., Lindner T.H., Herrmann H., Reis A., Sperling K.
    Nat. Genet. 31:410-414(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  12. "Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene."
    Waterham H.R., Koster J., Mooyer P., van Noort G., Kelley R.I., Wilcox W.R., Wanders R.J., Hennekam R.C.M., Oosterwijk J.C.
    Am. J. Hum. Genet. 72:1013-1017(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN GRBGD.
  13. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
    Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
    Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CBX5.
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-594 AND LYS-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor."
    Tseng L.C., Chen R.H.
    Mol. Biol. Cell 22:3306-3317(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-71 AND SER-86 BY CDK1.
  20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "Solution structure of the Tudor domain of human lamin-B receptor."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-55.
  23. "Solution structure of the Tudor domain of human lamin-B receptor."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-55.
  24. Cited for: VARIANTS PHA LEU-119 AND ARG-569.
  25. "LBR mutation and nuclear envelope defects in a patient affected with Reynolds syndrome."
    Gaudy-Marqueste C., Roll P., Esteves-Vieira V., Weiller P.J., Grob J.J., Cau P., Levy N., De Sandre-Giovannoli A.
    J. Med. Genet. 47:361-370(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT REYNS CYS-372.

Entry informationi

Entry nameiLBR_HUMAN
AccessioniPrimary (citable) accession number: Q14739
Secondary accession number(s): B2R5P3
, Q14740, Q53GU7, Q59FE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 31, 2002
Last modified: June 24, 2015
This is version 154 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.