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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
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113368-MONOMER.
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.
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

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 matrix Source: Ensembl
  • 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

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
Modified residuei126PhosphoserineBy similarity1
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei157N6-acetyllysineCombined sources1
Modified residuei158PhosphoserineBy similarity1
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-acetyllysineCombined sources1
Modified residuei278PhosphoserineCombined sources1
Modified residuei302PhosphoserineCombined sources1
Disulfide bondi317Interchain1 Publication
Modified residuei330N6-acetyllysineBy similarity1
Modified residuei375PhosphoserineCombined sources1
Modified residuei413Omega-N-methylarginineBy similarity1
Modified residuei483N6-acetyllysineCombined sources1
Modified residuei534PhosphoserineCombined sources1
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-2DPAGEP20700.

PTM databases

iPTMnetiP20700.
PhosphoSitePlusiP20700.
SwissPalmiP20700.

Miscellaneous databases

PMAP-CutDBP20700.

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 2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA1P522943EBI-968218,EBI-358383

Protein-protein interaction databases

BioGridi110187. 79 interactors.
DIPiDIP-34897N.
IntActiP20700. 45 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
Contains 1 LTD domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027696. Lamin_B.
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]
SMARTiSM01391. Filament. 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)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 rs36105360dbSNPEnsembl.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

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
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...

Protein-protein interaction databases

BioGridi110187. 79 interactors.
DIPiDIP-34897N.
IntActiP20700. 45 interactors.
MINTiMINT-3009331.
STRINGi9606.ENSP00000261366.

PTM databases

iPTMnetiP20700.
PhosphoSitePlusiP20700.
SwissPalmiP20700.

Polymorphism and mutation databases

BioMutaiLMNB1.
DMDMi125953.

2D gel databases

SWISS-2DPAGEP20700.

Proteomic databases

EPDiP20700.
MaxQBiP20700.
PaxDbiP20700.
PeptideAtlasiP20700.
PRIDEiP20700.

Protocols and materials databases

DNASUi4001.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261366; ENSP00000261366; ENSG00000113368.
GeneIDi4001.
KEGGihsa:4001.
UCSCiuc003kud.3. human.

Organism-specific databases

CTDi4001.
DisGeNETi4001.
GeneCardsiLMNB1.
HGNCiHGNC:6637. LMNB1.
HPAiCAB005269.
HPA050524.
HPA053579.
MalaCardsiLMNB1.
MIMi150340. gene.
169500. phenotype.
neXtProtiNX_P20700.
OpenTargetsiENSG00000113368.
Orphaneti99027. Adult-onset autosomal dominant leukodystrophy.
PharmGKBiPA30403.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113368-MONOMER.
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.
SIGNORiP20700.

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027696. Lamin_B.
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]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 180 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

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 one 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.