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UniProtKB - P20700 (LMNB1_HUMAN)

Protein

Lamin-B1

Gene

LMNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • sequence-specific double-stranded DNA binding Source: Ensembl
  • structural molecule activity Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000113368.11
HGNCiHGNC:6637 LMNB1
MIMi150340 gene
neXtProtiNX_P20700

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
ProteomicsDBi53773

2D gel databases

SWISS-2DPAGEiP20700

PTM databases

iPTMnetiP20700
PhosphoSitePlusiP20700
SwissPalmiP20700

Miscellaneous databases

PMAP-CutDBiP20700

Expressioni

Gene expression databases

BgeeiENSG00000113368 Expressed in 169 organ(s), highest expression level in kidney
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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi110187, 97 interactors
CORUMiP20700
DIPiDIP-34897N
IntActiP20700, 64 interactors
MINTiP20700
STRINGi9606.ENSP00000261366

Structurei

Secondary structure

1586
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP20700
SMRiP20700
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20700

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 388IF rodPROSITE-ProRule annotationAdd BLAST357
Domaini430 – 546LTDPROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 34HeadAdd BLAST33
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.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977 Eukaryota
ENOG410Y2H6 LUCA
GeneTreeiENSGT00910000143989
HOGENOMiHOG000007711
HOVERGENiHBG013015
InParanoidiP20700
KOiK07611
OMAiERAWLQI
OrthoDBiEOG091G063B
PhylomeDBiP20700
TreeFamiTF101181

Family and domain databases

Gene3Di2.60.40.1260, 1 hit
InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR001322 Lamin_tail_dom
IPR036415 Lamin_tail_dom_sf
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_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit
PS51841 LTD, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PBF6E9PBF6_HUMAN
Lamin-B1
LMNB1
387Annotation score:
A0A0D9SFY5A0A0D9SFY5_HUMAN
Lamin-B1
LMNB1
166Annotation score:
A0A0D9SFE5A0A0D9SFE5_HUMAN
Lamin B1, isoform CRA_a
LMNB1 hCG_27033
329Annotation score:

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 PublicationCorresponds to variant dbSNP:rs1380634377Ensembl.1
Natural variantiVAR_031646501A → V. Corresponds to variant dbSNP:rs36105360EnsemblClinVar.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

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[»]
5VVXX-ray2.90B/D389-401[»]
ProteinModelPortaliP20700
SMRiP20700
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110187, 97 interactors
CORUMiP20700
DIPiDIP-34897N
IntActiP20700, 64 interactors
MINTiP20700
STRINGi9606.ENSP00000261366

PTM databases

iPTMnetiP20700
PhosphoSitePlusiP20700
SwissPalmiP20700

Polymorphism and mutation databases

BioMutaiLMNB1
DMDMi125953

2D gel databases

SWISS-2DPAGEiP20700

Proteomic databases

EPDiP20700
MaxQBiP20700
PaxDbiP20700
PeptideAtlasiP20700
PRIDEiP20700
ProteomicsDBi53773

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
EuPathDBiHostDB:ENSG00000113368.11
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
GeneTreeiENSGT00910000143989
HOGENOMiHOG000007711
HOVERGENiHBG013015
InParanoidiP20700
KOiK07611
OMAiERAWLQI
OrthoDBiEOG091G063B
PhylomeDBiP20700
TreeFamiTF101181

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

Miscellaneous databases

ChiTaRSiLMNB1 human
EvolutionaryTraceiP20700
GeneWikiiLMNB1
GenomeRNAii4001
PMAP-CutDBiP20700
PROiPR:P20700
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113368 Expressed in 169 organ(s), highest expression level in kidney
CleanExiHS_LMNB1
ExpressionAtlasiP20700 baseline and differential
GenevisibleiP20700 HS

Family and domain databases

Gene3Di2.60.40.1260, 1 hit
InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR001322 Lamin_tail_dom
IPR036415 Lamin_tail_dom_sf
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_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit
PS51841 LTD, 1 hit
ProtoNetiSearch...

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: November 7, 2018
This is version 198 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
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