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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.

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.

GO - Molecular functioni

  • phospholipase binding Source: Ensembl
  • structural molecule activity Source: ProtInc

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
R-HSA-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
R-HSA-352238. Breakdown of the nuclear lamina.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-8862803. Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
R-HSA-8950505. Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNORiP20700.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B1
Gene namesi
Name:LMNB1
Synonyms:LMN2, LMNB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000113368.11.
HGNCiHGNC:6637. LMNB1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

DisGeNETi4001.
MalaCardsiLMNB1.
MIMi169500. phenotype.
OpenTargetsiENSG00000113368.
Orphaneti99027. Adult-onset autosomal dominant leukodystrophy.
PharmGKBiPA30403.

Polymorphism and mutation databases

BioMutaiLMNB1.
DMDMi125953.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000638162 – 583Lamin-B1Add BLAST582
PropeptideiPRO_0000393945584 – 586Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei3PhosphothreonineCombined sources1
Modified residuei5PhosphothreonineCombined sources1
Modified residuei14Omega-N-methylarginineCombined sources1
Modified residuei20PhosphothreonineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei25PhosphothreonineCombined sources1
Modified residuei28PhosphoserineCombined sources1
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei111N6-acetyllysineBy similarity1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei126PhosphoserineBy similarity1
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei157N6-acetyllysine; alternateCombined sources1
Cross-linki157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei158PhosphoserineBy similarity1
Cross-linki181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei200PhosphoserineCombined sources1
Modified residuei210PhosphoserineCombined sources1
Modified residuei232PhosphoserineCombined sources1
Cross-linki241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei271N6-acetyllysine; alternateCombined sources1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei278PhosphoserineCombined sources1
Modified residuei302PhosphoserineCombined sources1
Cross-linki312Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Disulfide bondi317Interchain1 Publication
Modified residuei330N6-acetyllysine; alternateBy similarity1
Cross-linki330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei375PhosphoserineCombined sources1
Modified residuei413Omega-N-methylarginineBy similarity1
Modified residuei483N6-acetyllysineCombined sources1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei534PhosphoserineCombined sources1
Cross-linki547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei575PhosphothreonineCombined sources1
Modified residuei583Cysteine methyl esterCurated1
Lipidationi583S-farnesyl cysteine1 Publication1

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, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

EPDiP20700.
MaxQBiP20700.
PaxDbiP20700.
PeptideAtlasiP20700.
PRIDEiP20700.

2D gel databases

SWISS-2DPAGEiP20700.

PTM databases

iPTMnetiP20700.
PhosphoSitePlusiP20700.
SwissPalmiP20700.

Miscellaneous databases

PMAP-CutDBiP20700.

Expressioni

Gene expression databases

BgeeiENSG00000113368.
CleanExiHS_LMNB1.
ExpressionAtlasiP20700. baseline and differential.
GenevisibleiP20700. HS.

Organism-specific databases

HPAiCAB005269.
HPA050524.
HPA053579.

Interactioni

Subunit structurei

Homodimer. Interacts with lamin-associated polypeptides IA, IB and 2. Interacts with SPAG4 and SEPT12.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110187. 80 interactors.
CORUMiP20700.
DIPiDIP-34897N.
IntActiP20700. 51 interactors.
MINTiMINT-3009331.
STRINGi9606.ENSP00000261366.

Structurei

Secondary structure

1586
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi315 – 381Combined sources67
Beta strandi432 – 447Combined sources16
Beta strandi451 – 458Combined sources8
Beta strandi460 – 462Combined sources3
Beta strandi470 – 475Combined sources6
Beta strandi478 – 483Combined sources6
Beta strandi495 – 500Combined sources6
Turni509 – 511Combined sources3
Beta strandi512 – 515Combined sources4
Beta strandi523 – 525Combined sources3
Beta strandi527 – 532Combined sources6
Beta strandi538 – 546Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KPWNMR-A439-549[»]
3JT0X-ray2.39A/B426-558[»]
3TYYX-ray2.40A/B311-388[»]
3UMNX-ray2.00A/B/C428-550[»]
ProteinModelPortaliP20700.
SMRiP20700.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20700.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini434 – 546LTDAdd BLAST113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 34HeadAdd BLAST33
Regioni35 – 386RodAdd BLAST352
Regioni35 – 69Coil 1AAdd BLAST35
Regioni70 – 81Linker 1Add BLAST12
Regioni82 – 215Coil 1BAdd BLAST134
Regioni216 – 243Linker 2Add BLAST28
Regioni244 – 386Coil 2Add BLAST143
Regioni387 – 586TailAdd BLAST200

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi415 – 420Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi552 – 559Glu-rich (highly acidic; could be involved in chromatin binding)8

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP20700.
KOiK07611.
OMAiFHQQGAP.
OrthoDBiEOG091G063B.
PhylomeDBiP20700.
TreeFamiTF101181.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiView protein in InterPro
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiView protein in Pfam
PF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
SMARTiView protein in SMART
SM01391. Filament. 1 hit.
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiView protein in PROSITE
PS00226. IF. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti382E → Q in AAH12295 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071077436A → V Found in a family with amyotrophic lateral sclerosis carrying a probable causative mutation in MATR3; unknown pathological significance. 1 Publication1
Natural variantiVAR_031646501A → V. Corresponds to variant dbSNP:rs36105360Ensembl.1

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.3. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLMNB1_HUMAN
AccessioniPrimary (citable) accession number: P20700
Secondary accession number(s): B2R6J6, Q3SYN7, Q96EI6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 187 of the entry and version 2 of the sequence. See 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, 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