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Protein

Lamin-B1

Gene

LMNB1

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

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

  • structural molecule activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

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_263908. 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 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6637. LMNB1.

Subcellular locationi

GO - Cellular componenti

  • lamin filament Source: ProtInc
  • membrane Source: UniProtKB
  • nuclear envelope Source: Reactome
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nuclear membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy, demyelinating, autosomal dominant, adult-onset (ADLD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:169500

Keywords - Diseasei

Leukodystrophy

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiLMNB1.
DMDMi125953.

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 – 201Phosphothreonine3 Publications
Modified residuei23 – 231Phosphoserine5 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 – 5751Phosphothreonine5 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.

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

BgeeiP20700.
CleanExiHS_LMNB1.
ExpressionAtlasiP20700. baseline and differential.
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. 65 interactions.
DIPiDIP-34897N.
IntActiP20700. 26 interactions.
MINTiMINT-3009331.
STRINGi9606.ENSP00000261366.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118905.
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

        10         20         30         40         50
MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV
60 70 80 90 100
RSLETENSAL QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER
110 120 130 140 150
AKLQIELGKC KAEHDQLLLN YAKKESDLNG AQIKLREYEA ALNSKDAALA
160 170 180 190 200
TALGDKKSLE GDLEDLKDQI AQLEASLAAA KKQLADETLL KVDLENRCQS
210 220 230 240 250
LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY KLAQALHEMR
260 270 280 290 300
EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI
310 320 330 340 350
ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR
360 370 380 390 400
DQMQQQLNDY EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV
410 420 430 440 450
SRASSSRSVR TTRGKRKRVD VEESEASSSV SISHSASATG NVCIEEIDVD
460 470 480 490 500
GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV SYKYTSRYVL KAGQTVTIWA
510 520 530 540 550
ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA QRSTVFKTTI
560 570 580
PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110187. 65 interactions.
DIPiDIP-34897N.
IntActiP20700. 26 interactions.
MINTiMINT-3009331.
STRINGi9606.ENSP00000261366.

PTM databases

PhosphoSiteiP20700.

Polymorphism and mutation databases

BioMutaiLMNB1.
DMDMi125953.

2D gel databases

SWISS-2DPAGEP20700.

Proteomic databases

MaxQBiP20700.
PaxDbiP20700.
PeptideAtlasiP20700.
PRIDEiP20700.

Protocols and materials databases

DNASUi4001.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4001.
GeneCardsiGC05P126112.
HGNCiHGNC:6637. LMNB1.
HPAiCAB005269.
HPA050524.
MIMi150340. gene.
169500. phenotype.
neXtProtiNX_P20700.
Orphaneti99027. Adult-onset autosomal dominant leukodystrophy.
PharmGKBiPA30403.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325506.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP20700.
KOiK07611.
OMAiQKESRAC.
OrthoDBiEOG7MD4PW.
PhylomeDBiP20700.
TreeFamiTF101181.

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_263908. Depolymerisation of the Nuclear Lamina.
REACT_75792. Meiotic synapsis.

Miscellaneous databases

ChiTaRSiLMNB1. human.
EvolutionaryTraceiP20700.
GeneWikiiLMNB1.
GenomeRNAii4001.
NextBioi15700.
PMAP-CutDBP20700.
PROiP20700.
SOURCEiSearch...

Gene expression databases

BgeeiP20700.
CleanExiHS_LMNB1.
ExpressionAtlasiP20700. baseline and differential.
GenevestigatoriP20700.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. 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: May 27, 2015
This is version 163 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

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.