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Protein

Lamin-B2

Gene

LMNB2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B2
Gene namesi
Name:LMNB2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 597596Lamin-B2PRO_0000063822Add
BLAST
Propeptidei598 – 6003Removed in mature formBy similarityPRO_0000403472

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei597 – 5971Cysteine methyl esterBy similarity
Lipidationi597 – 5971S-farnesyl cysteineBy similarity

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, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP14732.
PRIDEiP14732.

PTM databases

iPTMnetiP14732.

Interactioni

Protein-protein interaction databases

BioGridi676482. 1 interaction.
IntActiP14732. 1 interaction.
STRINGi9031.ENSGALP00000034565.

Structurei

3D structure databases

ProteinModelPortaliP14732.
SMRiP14732. Positions 23-59, 308-380, 452-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini449 – 561113LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2726HeadAdd
BLAST
Regioni28 – 379352RodAdd
BLAST
Regioni28 – 6437Coil 1AAdd
BLAST
Regioni75 – 212138Coil 1BAdd
BLAST
Regioni237 – 379143Coil 2Add
BLAST
Regioni380 – 600221TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4196Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi398 – 4069Poly-Ser
Compositional biasi435 – 44410Poly-Ser
Compositional biasi568 – 58215Asp/Glu-rich (highly acidic; could be involved in chromatin binding)Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP14732.
KOiK07611.
PhylomeDBiP14732.

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:SF152. PTHR23239:SF152. 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.

P14732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTPIRGTP GGTPLSPTRI SRLQEKEELR QLNDRLAVYI DRVRALELEN
60 70 80 90 100
DRLLVKISEK EEVTTREVSG IKNLYESELA DARRVLDETA KERARLQIEI
110 120 130 140 150
GKLRAELEEF NKSYKKKDAD LSVAQGRIKD LEVLFHRSEA ELNTVLNEKR
160 170 180 190 200
SLEAEVADLR AQLAKAEDGH AVAKKQLEKE TLMRVDLENR CQSLQEDLDF
210 220 230 240 250
RKNVFEEEIR ETRKRHEHRL VEVDTSRQQE YENKMAQALE DLRNQHDEQV
260 270 280 290 300
KLYKMELEQT YQAKLENAIL ASDQNDKAAG AAREELKEAR MRIESLSHQL
310 320 330 340 350
SGLQKQASAT EDRIRELKET MAGERDKFRK MLDAKEREMT EMRDQMQLQL
360 370 380 390 400
TEYQELLDVK LALDMEISAY RKLLEGEEER LKLSPSPSSR VTVSRATSSS
410 420 430 440 450
SSSSTSLVRS SRGKRRRIEA EELSGSGTSG IGTGSISGSS SSSSFQMSQQ
460 470 480 490 500
ASATGSISIE EIDLEGKYVQ LKNNSEKDQS LGNWRLKRQI GDGEEIAYKF
510 520 530 540 550
TPKYVLRAGQ TVTIWGADAG VSHSPPSVLV WKNQGSWGTG GNIRTYLVNS
560 570 580 590 600
DGEEVAVRTV TKSVVVRENE EEEDEADFGE EDLFNQQGDP RTTSRGCLVM
Length:600
Mass (Da):67,941
Last modified:April 1, 1990 - v1
Checksum:i670E2985202211C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16880 mRNA. Translation: CAA34763.1.
PIRiS05519.
RefSeqiNP_990616.1. NM_205285.1.
UniGeneiGga.16090.

Genome annotation databases

GeneIDi396222.
KEGGigga:396222.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16880 mRNA. Translation: CAA34763.1.
PIRiS05519.
RefSeqiNP_990616.1. NM_205285.1.
UniGeneiGga.16090.

3D structure databases

ProteinModelPortaliP14732.
SMRiP14732. Positions 23-59, 308-380, 452-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676482. 1 interaction.
IntActiP14732. 1 interaction.
STRINGi9031.ENSGALP00000034565.

PTM databases

iPTMnetiP14732.

Proteomic databases

PaxDbiP14732.
PRIDEiP14732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396222.
KEGGigga:396222.

Organism-specific databases

CTDi84823.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP14732.
KOiK07611.
PhylomeDBiP14732.

Miscellaneous databases

PROiP14732.

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:SF152. PTHR23239:SF152. 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 nameiLMNB2_CHICK
AccessioniPrimary (citable) accession number: P14732
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Complete proteome, Reference proteome

Documents

  1. 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.