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Q14739

- LBR_HUMAN

UniProt

Q14739 - LBR_HUMAN

Protein

Lamin-B receptor

Gene

LBR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (31 Jan 2002)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. chromo shadow domain binding Source: BHF-UCL
    2. DNA binding Source: ProtInc
    3. lamin binding Source: ProtInc
    4. oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. cholesterol biosynthetic process Source: Reactome
    2. small molecule metabolic process Source: Reactome

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6518. LBR.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: MGI
    2. integral component of nuclear inner membrane Source: ProtInc
    3. membrane Source: UniProtKB
    4. mitochondrion Source: HPA
    5. nuclear envelope Source: Reactome
    6. nuclear membrane Source: HPA

    Keywords - Cellular componenti

    Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Pelger-Huet anomaly (PHA) [MIM:169400]: An 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:215140]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Reynolds syndrome (REYNS) [MIM:613471]: A 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.1 Publication
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    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.

    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 CDK12 Publications
    Modified residuei86 – 861Phosphoserine; by CDK12 Publications
    Modified residuei97 – 971Phosphoserine2 Publications
    Modified residuei99 – 991Phosphoserine2 Publications
    Modified residuei118 – 1181Phosphothreonine3 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.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14739.
    PaxDbiQ14739.
    PeptideAtlasiQ14739.
    PRIDEiQ14739.

    PTM databases

    PhosphoSiteiQ14739.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14739.
    BgeeiQ14739.
    CleanExiHS_LBR.
    GenevestigatoriQ14739.

    Organism-specific databases

    HPAiHPA049840.

    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. 27 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 – 155
    Turni17 – 193
    Beta strandi22 – 3110
    Turni32 – 354
    Beta strandi36 – 405
    Beta strandi46 – 505
    Turni51 – 533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DIGNMR-A1-55[»]
    ProteinModelPortaliQ14739.
    SMRiQ14739. Positions 1-55.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14739.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 211211NuclearSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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

    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.
    HOGENOMiHOG000193296.
    HOVERGENiHBG007825.
    InParanoidiQ14739.
    OMAiVYSHFLQ.
    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

    MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK    50
    ENDIKPLTSF RQRKGGSTSS SPSRRRGSRS RSRSRSPGRP PKSARRSASA 100
    SHQADIKEAR REVEVKLTPL ILKPFGNSIS RYNGEPEHIE RNDAPHKNTQ 150
    EKFSLSQESS YIATQYSLRP RREEVKLKEI DSKEEKYVAK ELAVRTFEVT 200
    PIRAKDLEFG GVPGVFLIMF GLPVFLFLLL LMCKQKDPSL LNFPPPLPAL 250
    YELWETRVFG VYLLWFLIQV LFYLLPIGKV VEGTPLIDGR RLKYRLNGFY 300
    AFILTSAVIG TSLFQGVEFH YVYSHFLQFA LAATVFCVVL SVYLYMRSLK 350
    APRNDLSPAS SGNAVYDFFI GRELNPRIGT FDLKYFCELR PGLIGWVVIN 400
    LVMLLAEMKI QDRAVPSLAM ILVNSFQLLY VVDALWNEEA LLTTMDIIHD 450
    GFGFMLAFGD LVWVPFIYSF QAFYLVSHPN EVSWPMASLI IVLKLCGYVI 500
    FRGANSQKNA FRKNPSDPKL AHLKTIHTST GKNLLVSGWW GFVRHPNYLG 550
    DLIMALAWSL PCGFNHILPY FYIIYFTMLL VHREARDEYH CKKKYGVAWE 600
    KYCQRVPYRI FPYIY 615
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti301 – 3011A → P in AAA59494. (PubMed:8157662)Curated
    Sequence conflicti452 – 4521F → L in BAD96554. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi20141468.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGenei Hs.435166.
    Hs.735694.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DIG NMR - A 1-55 [» ]
    ProteinModelPortali Q14739.
    SMRi Q14739. Positions 1-55.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110122. 27 interactions.
    DIPi DIP-5987N.
    IntActi Q14739. 9 interactions.
    MINTi MINT-1631069.
    STRINGi 9606.ENSP00000272163.

    PTM databases

    PhosphoSitei Q14739.

    Polymorphism databases

    DMDMi 20141468.

    Proteomic databases

    MaxQBi Q14739.
    PaxDbi Q14739.
    PeptideAtlasi Q14739.
    PRIDEi Q14739.

    Protocols and materials databases

    DNASUi 3930.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272163 ; ENSP00000272163 ; ENSG00000143815 .
    ENST00000338179 ; ENSP00000339883 ; ENSG00000143815 .
    GeneIDi 3930.
    KEGGi hsa:3930.
    UCSCi uc001hoy.3. human.

    Organism-specific databases

    CTDi 3930.
    GeneCardsi GC01M225589.
    HGNCi HGNC:6518. LBR.
    HPAi HPA049840.
    MIMi 169400. phenotype.
    215140. phenotype.
    600024. gene.
    613471. phenotype.
    neXtProti NX_Q14739.
    Orphaneti 1426. Greenberg dysplasia.
    779. Reynolds syndrome.
    PharmGKBi PA30304.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72042.
    HOGENOMi HOG000193296.
    HOVERGENi HBG007825.
    InParanoidi Q14739.
    OMAi VYSHFLQ.
    OrthoDBi EOG75B85C.
    PhylomeDBi Q14739.
    TreeFami TF101179.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07110-MONOMER.
    BRENDAi 1.3.1.70. 2681.
    Reactomei REACT_9405. Cholesterol biosynthesis.

    Miscellaneous databases

    ChiTaRSi LBR. human.
    EvolutionaryTracei Q14739.
    GeneWikii Lamin_B_receptor.
    GenomeRNAii 3930.
    NextBioi 15431.
    PROi Q14739.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14739.
    Bgeei Q14739.
    CleanExi HS_LBR.
    Genevestigatori Q14739.

    Family and domain databases

    InterProi IPR001171. Ergosterol_biosynth_ERG4_ERG24.
    IPR019023. Lamin-B_rcpt_of_tudor.
    IPR018083. Sterol_reductase_CS.
    IPR002999. Tudor.
    [Graphical view ]
    Pfami PF01222. ERG4_ERG24. 1 hit.
    PF09465. LBR_tudor. 1 hit.
    [Graphical view ]
    SMARTi SM00333. TUDOR. 1 hit.
    [Graphical view ]
    PROSITEi PS01017. STEROL_REDUCT_1. 1 hit.
    PS01018. STEROL_REDUCT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    22. "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.
    23. Cited for: VARIANTS PHA LEU-119 AND ARG-569.
    24. "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: October 1, 2014
    This is version 146 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