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P20700

- LMNB1_HUMAN

UniProt

P20700 - LMNB1_HUMAN

Protein

Lamin-B1

Gene

LMNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.

    GO - Molecular functioni

    1. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_13472. Breakdown of the nuclear lamina.
    REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_200828. Depolymerisation of the Nuclear Lamina.
    REACT_75792. Meiotic synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lamin-B1
    Gene namesi
    Name:LMNB1
    Synonyms:LMN2, LMNB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6637. LMNB1.

    Subcellular locationi

    GO - Cellular componenti

    1. lamin filament Source: ProtInc
    2. membrane Source: UniProtKB
    3. nuclear envelope Source: Reactome
    4. nuclear inner membrane Source: UniProtKB-SubCell
    5. nuclear membrane Source: HPA
    6. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Intermediate filament, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Leukodystrophy, demyelinating, autosomal dominant, adult-onset (ADLD) [MIM:169500]: A slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Leukodystrophy

    Organism-specific databases

    MIMi169500. phenotype.
    Orphaneti99027. Adult-onset autosomal dominant leukodystrophy.
    PharmGKBiPA30403.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 583582Lamin-B1PRO_0000063816Add
    BLAST
    Propeptidei584 – 5863Removed in mature formCuratedPRO_0000393945

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei3 – 31Phosphothreonine1 Publication
    Modified residuei5 – 51Phosphothreonine1 Publication
    Modified residuei20 – 201Phosphothreonine2 Publications
    Modified residuei23 – 231Phosphoserine4 Publications
    Modified residuei111 – 1111N6-acetyllysineBy similarity
    Modified residuei157 – 1571N6-acetyllysine1 Publication
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei271 – 2711N6-acetyllysine1 Publication
    Disulfide bondi317 – 317Interchain1 Publication
    Modified residuei330 – 3301N6-acetyllysineBy similarity
    Modified residuei375 – 3751Phosphoserine2 Publications
    Modified residuei483 – 4831N6-acetyllysine1 Publication
    Modified residuei575 – 5751Phosphothreonine4 Publications
    Modified residuei583 – 5831Cysteine methyl esterCurated
    Lipidationi583 – 5831S-farnesyl cysteine1 Publication

    Post-translational modificationi

    B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.6 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP20700.
    PaxDbiP20700.
    PeptideAtlasiP20700.
    PRIDEiP20700.

    2D gel databases

    SWISS-2DPAGEP20700.

    PTM databases

    PhosphoSiteiP20700.

    Miscellaneous databases

    PMAP-CutDBP20700.

    Expressioni

    Gene expression databases

    ArrayExpressiP20700.
    BgeeiP20700.
    CleanExiHS_LMNB1.
    GenevestigatoriP20700.

    Organism-specific databases

    HPAiCAB005269.
    HPA050524.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with lamin-associated polypeptides IA, IB and 2.1 Publication

    Protein-protein interaction databases

    BioGridi110187. 59 interactions.
    DIPiDIP-34897N.
    IntActiP20700. 25 interactions.
    MINTiMINT-3009331.
    STRINGi9606.ENSP00000261366.

    Structurei

    Secondary structure

    1
    586
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi315 – 38167
    Beta strandi432 – 44716
    Beta strandi451 – 4588
    Beta strandi460 – 4623
    Beta strandi470 – 4756
    Beta strandi478 – 4836
    Beta strandi495 – 5006
    Turni509 – 5113
    Beta strandi512 – 5154
    Beta strandi523 – 5253
    Beta strandi527 – 5326
    Beta strandi538 – 5469

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KPWNMR-A439-549[»]
    3JT0X-ray2.39A/B426-558[»]
    3TYYX-ray2.40A/B311-388[»]
    3UMNX-ray2.00A/B/C428-550[»]
    ProteinModelPortaliP20700.
    SMRiP20700. Positions 311-385, 431-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20700.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini434 – 546113LTDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 3433HeadAdd
    BLAST
    Regioni35 – 386352RodAdd
    BLAST
    Regioni35 – 6935Coil 1AAdd
    BLAST
    Regioni70 – 8112Linker 1Add
    BLAST
    Regioni82 – 215134Coil 1BAdd
    BLAST
    Regioni216 – 24328Linker 2Add
    BLAST
    Regioni244 – 386143Coil 2Add
    BLAST
    Regioni387 – 586200TailAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi415 – 4206Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi552 – 5598Glu-rich (highly acidic; could be involved in chromatin binding)

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated
    Contains 1 LTD domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG325506.
    HOGENOMiHOG000007711.
    HOVERGENiHBG013015.
    InParanoidiP20700.
    KOiK07611.
    OMAiQKESRAC.
    OrthoDBiEOG7MD4PW.
    PhylomeDBiP20700.
    TreeFamiTF101181.

    Family and domain databases

    Gene3Di2.60.40.1260. 1 hit.
    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR027696. Lamin.
    IPR001322. Lamin_tail_dom.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PTHR23239:SF157. PTHR23239:SF157. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    PF00932. LTD. 1 hit.
    [Graphical view]
    SUPFAMiSSF74853. SSF74853. 1 hit.
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20700-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV    50
    RSLETENSAL QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER 100
    AKLQIELGKC KAEHDQLLLN YAKKESDLNG AQIKLREYEA ALNSKDAALA 150
    TALGDKKSLE GDLEDLKDQI AQLEASLAAA KKQLADETLL KVDLENRCQS 200
    LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY KLAQALHEMR 250
    EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI 300
    ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR 350
    DQMQQQLNDY EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV 400
    SRASSSRSVR TTRGKRKRVD VEESEASSSV SISHSASATG NVCIEEIDVD 450
    GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV SYKYTSRYVL KAGQTVTIWA 500
    ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA QRSTVFKTTI 550
    PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM 586
    Length:586
    Mass (Da):66,408
    Last modified:January 23, 2007 - v2
    Checksum:i73292877745722C4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti382 – 3821E → Q in AAH12295. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti436 – 4361A → V Found in a family with amyotrophic lateral sclerosis carrying a probable causative mutation in MATR3; unknown pathological significance. 1 Publication
    VAR_071077
    Natural varianti501 – 5011A → V.
    Corresponds to variant rs36105360 [ dbSNP | Ensembl ].
    VAR_031646

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34458 mRNA. Translation: AAA36162.1.
    L37747
    , L37737, L37738, L37739, L37740, L37741, L37742, L37743, L37744, L37745, L37746 Genomic DNA. Translation: AAC37575.1.
    AK312603 mRNA. Translation: BAG35493.1.
    CH471086 Genomic DNA. Translation: EAW48846.1.
    BC012295 mRNA. Translation: AAH12295.1.
    BC103723 mRNA. Translation: AAI03724.1.
    CCDSiCCDS4140.1.
    PIRiA34707. VEHULB.
    RefSeqiNP_005564.1. NM_005573.3.
    UniGeneiHs.89497.

    Genome annotation databases

    EnsembliENST00000261366; ENSP00000261366; ENSG00000113368.
    GeneIDi4001.
    KEGGihsa:4001.
    UCSCiuc003kud.2. human.

    Polymorphism databases

    DMDMi125953.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34458 mRNA. Translation: AAA36162.1 .
    L37747
    , L37737 , L37738 , L37739 , L37740 , L37741 , L37742 , L37743 , L37744 , L37745 , L37746 Genomic DNA. Translation: AAC37575.1 .
    AK312603 mRNA. Translation: BAG35493.1 .
    CH471086 Genomic DNA. Translation: EAW48846.1 .
    BC012295 mRNA. Translation: AAH12295.1 .
    BC103723 mRNA. Translation: AAI03724.1 .
    CCDSi CCDS4140.1.
    PIRi A34707. VEHULB.
    RefSeqi NP_005564.1. NM_005573.3.
    UniGenei Hs.89497.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KPW NMR - A 439-549 [» ]
    3JT0 X-ray 2.39 A/B 426-558 [» ]
    3TYY X-ray 2.40 A/B 311-388 [» ]
    3UMN X-ray 2.00 A/B/C 428-550 [» ]
    ProteinModelPortali P20700.
    SMRi P20700. Positions 311-385, 431-548.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110187. 59 interactions.
    DIPi DIP-34897N.
    IntActi P20700. 25 interactions.
    MINTi MINT-3009331.
    STRINGi 9606.ENSP00000261366.

    PTM databases

    PhosphoSitei P20700.

    Polymorphism databases

    DMDMi 125953.

    2D gel databases

    SWISS-2DPAGE P20700.

    Proteomic databases

    MaxQBi P20700.
    PaxDbi P20700.
    PeptideAtlasi P20700.
    PRIDEi P20700.

    Protocols and materials databases

    DNASUi 4001.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261366 ; ENSP00000261366 ; ENSG00000113368 .
    GeneIDi 4001.
    KEGGi hsa:4001.
    UCSCi uc003kud.2. human.

    Organism-specific databases

    CTDi 4001.
    GeneCardsi GC05P126112.
    HGNCi HGNC:6637. LMNB1.
    HPAi CAB005269.
    HPA050524.
    MIMi 150340. gene.
    169500. phenotype.
    neXtProti NX_P20700.
    Orphaneti 99027. Adult-onset autosomal dominant leukodystrophy.
    PharmGKBi PA30403.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325506.
    HOGENOMi HOG000007711.
    HOVERGENi HBG013015.
    InParanoidi P20700.
    KOi K07611.
    OMAi QKESRAC.
    OrthoDBi EOG7MD4PW.
    PhylomeDBi P20700.
    TreeFami TF101181.

    Enzyme and pathway databases

    Reactomei REACT_13472. Breakdown of the nuclear lamina.
    REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_200828. Depolymerisation of the Nuclear Lamina.
    REACT_75792. Meiotic synapsis.

    Miscellaneous databases

    ChiTaRSi LMNB1. human.
    EvolutionaryTracei P20700.
    GeneWikii LMNB1.
    GenomeRNAii 4001.
    NextBioi 15700.
    PMAP-CutDB P20700.
    PROi P20700.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20700.
    Bgeei P20700.
    CleanExi HS_LMNB1.
    Genevestigatori P20700.

    Family and domain databases

    Gene3Di 2.60.40.1260. 1 hit.
    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR027696. Lamin.
    IPR001322. Lamin_tail_dom.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    PTHR23239:SF157. PTHR23239:SF157. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    PF00932. LTD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74853. SSF74853. 1 hit.
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "In vitro posttranslational modification of lamin B cloned from a human T-cell line."
      Pollard K.M., Chan E.K.L., Grant B.J., Sullivan K.F., Tan E.M., Glass C.A.
      Mol. Cell. Biol. 10:2164-2175(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural organization of the human gene (LMNB1) encoding nuclear lamin B1."
      Lin F., Worman H.J.
      Genomics 27:230-236(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Eye and Placenta.
    6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 15-26; 43-49; 80-90; 103-109; 112-123; 125-191; 198-220; 235-250; 259-271; 277-290; 300-312; 321-330; 351-387; 475-483 AND 517-528, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 52-67; 80-90; 112-123; 146-156; 198-208; 210-220; 300-312; 321-330; 351-378 AND 458-473, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Human lamin B contains a farnesylated cysteine residue."
      Farnsworth C.C., Wolda S.L., Gelb M.H., Glomset J.A.
      J. Biol. Chem. 264:20422-20429(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-583.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: INVOLVEMENT IN ADLD.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-157; LYS-271 AND LYS-483, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; THR-5; SER-23; SER-375 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-23; SER-210 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1."
      Ruan J., Xu C., Bian C., Lam R., Wang J.P., Kania J., Min J., Zang J.
      FEBS Lett. 586:314-318(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 311-388, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 428-550, DISULFIDE BOND, SUBUNIT.
    22. Cited for: VARIANT VAL-436.

    Entry informationi

    Entry nameiLMNB1_HUMAN
    AccessioniPrimary (citable) accession number: P20700
    Secondary accession number(s): B2R6J6, Q3SYN7, Q96EI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 155 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

    Miscellaneous

    The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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