Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lamin-B2

Gene

Lmnb2

Organism
Mus musculus (Mouse)
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

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B2
Gene namesi
Name:Lmnb2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96796. Lmnb2.

Subcellular locationi

GO - Cellular componenti

  • lamin filament Source: MGI
  • nuclear envelope Source: MGI
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000638211 – 593Lamin-B2Add BLAST593
PropeptideiPRO_0000403471594 – 596Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12PhosphothreonineBy similarity1
Modified residuei15PhosphoserineBy similarity1
Modified residuei59N6-acetyllysine; alternateBy similarity1
Cross-linki59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei294PhosphoserineBy similarity1
Modified residuei398PhosphoserineBy similarity1
Modified residuei400PhosphoserineBy similarity1
Modified residuei402PhosphoserineBy similarity1
Modified residuei413Omega-N-methylarginineCombined sources1
Modified residuei473PhosphoserineBy similarity1
Modified residuei593Cysteine methyl esterBy similarity1
Lipidationi593S-farnesyl cysteineBy similarity1

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

Proteomic databases

EPDiP21619.
MaxQBiP21619.
PaxDbiP21619.
PeptideAtlasiP21619.
PRIDEiP21619.

PTM databases

iPTMnetiP21619.
PhosphoSitePlusiP21619.

Expressioni

Tissue specificityi

Isoform B3 is germ cell specific.

Gene expression databases

BgeeiENSMUSG00000062075.
CleanExiMM_LMNB2.
ExpressionAtlasiP21619. baseline and differential.
GenevisibleiP21619. MM.

Interactioni

Subunit structurei

Interacts with TMEM43.1 Publication

Protein-protein interaction databases

BioGridi201178. 1 interactor.
IntActiP21619. 1 interactor.
MINTiMINT-4100052.
STRINGi10090.ENSMUSP00000136524.

Structurei

3D structure databases

ProteinModelPortaliP21619.
SMRiP21619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini442 – 550LTDAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 26HeadAdd BLAST26
Regioni27 – 378RodAdd BLAST352
Regioni27 – 61Coil 1AAdd BLAST35
Regioni62 – 73Linker 1Add BLAST12
Regioni74 – 207Coil 1BAdd BLAST134
Regioni208 – 234Linker 2Add BLAST27
Regioni235 – 378Coil 2Add BLAST144
Regioni379 – 596TailAdd BLAST218

Motif

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi565 – 578Asp/Glu-rich (highly acidic; could be involved in chromatin binding)Add BLAST14

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.
InParanoidiP21619.
KOiK07611.
PhylomeDBiP21619.
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: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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B2 (identifier: P21619-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASLPPHAGP ATPLSPTRLS RLQEKEELRE LNDRLAHYID RVRALELEND
60 70 80 90 100
RLLLRISEKE EVTTREVSGI KTLYESELAD ARRVLDETAR ERARLQIEIG
110 120 130 140 150
KVQAELEEAR KSAKKREGEL TVAQGRVKDL ESLFHRSEAE LATALSDKQG
160 170 180 190 200
LETEVAELRA QLAKAEDGHA VAKKQLEKET LMRVDLENRC QSLQEELAFS
210 220 230 240 250
KSVFEEEVRE TRRRHERRLV EVDSSRQQEY DFKMAQALED LRSQHDEQVR
260 270 280 290 300
LYRVELEQTY QAKLDNAKLL SDQNDKAAHA AREELKEARM RVESLSYQLL
310 320 330 340 350
GLQKQASAAE NHIHELEEAL AGERDKFRKM LDAKEQEMTE VRDAMQQQLA
360 370 380 390 400
EYQELLDIKL ALDMEISAYR KLLEGEEERL KLSPSPSSRI TISRATSSSS
410 420 430 440 450
SSSGVGMSVG QGRGKRRRLE TEDTSGSPSR ASRVSSGSRL AQQTVATGVV
460 470 480 490 500
NIDEVDPEGR FVRLKNSSDK DQSLGNWRIK RQVLEGEDIA YKFTPKYVLR
510 520 530 540 550
AGQTVTVWAA GAGATHSPPS TLVWKSQTNW GPGESFRTAL VSADGEEVAV
560 570 580 590
KAAKHSSVQG RENGEEEEEE EAEFGEEDLF HQQGDPRTTS RGCRLM
Length:596
Mass (Da):67,318
Last modified:January 24, 2006 - v2
Checksum:i4FEF5A76FFDF2D96
GO
Isoform B3 (identifier: P21619-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: MASLPPHAGP...LAFSKSVFEE → MGESESMRGT...NHLRVPTREQ

Note: No experimental confirmation available.
Show »
Length:474
Mass (Da):53,268
Checksum:i9303CBEC3C77DE75
GO

Sequence cautioni

The sequence AAH42430 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH51985 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti148 – 149KQ → NE in CAA38032 (PubMed:2102682).Curated2
Sequence conflicti314H → R AA sequence (PubMed:2311764).Curated1
Sequence conflicti321A → R in CAA38032 (PubMed:2102682).Curated1
Sequence conflicti344A → R in CAA38032 (PubMed:2102682).Curated1
Sequence conflicti403Missing in CAA38032 (PubMed:2102682).Curated1
Sequence conflicti412 – 413GR → RG in CAA38032 (PubMed:2102682).Curated2
Sequence conflicti421 – 422Missing (PubMed:2102682).Curated2
Sequence conflicti443Missing in CAA38032 (PubMed:2102682).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0170701 – 206MASLP…SVFEE → MGESESMRGTGEGCGRDCPE AARPLMETVEGALPELRGRP LREYVKRRPRGLGKTPVEDP VKSEGAVGYPRTWNNHLRVP TREQ in isoform B3. 1 PublicationAdd BLAST206

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54098 mRNA. Translation: CAA38032.1.
D13455 mRNA. Translation: BAA02708.1.
BC042430 mRNA. Translation: AAH42430.1. Different initiation.
BC051985 mRNA. Translation: AAH51985.1. Different initiation.
CCDSiCCDS24037.1. [P21619-1]
PIRiB48315.
S28419.
RefSeqiNP_034852.2. NM_010722.5. [P21619-1]
XP_006513341.1. XM_006513278.2. [P21619-2]
UniGeneiMm.7362.

Genome annotation databases

EnsembliENSMUST00000105332; ENSMUSP00000100969; ENSMUSG00000062075. [P21619-2]
ENSMUST00000179022; ENSMUSP00000136524; ENSMUSG00000062075. [P21619-1]
GeneIDi16907.
KEGGimmu:16907.
UCSCiuc007gfk.1. mouse. [P21619-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54098 mRNA. Translation: CAA38032.1.
D13455 mRNA. Translation: BAA02708.1.
BC042430 mRNA. Translation: AAH42430.1. Different initiation.
BC051985 mRNA. Translation: AAH51985.1. Different initiation.
CCDSiCCDS24037.1. [P21619-1]
PIRiB48315.
S28419.
RefSeqiNP_034852.2. NM_010722.5. [P21619-1]
XP_006513341.1. XM_006513278.2. [P21619-2]
UniGeneiMm.7362.

3D structure databases

ProteinModelPortaliP21619.
SMRiP21619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201178. 1 interactor.
IntActiP21619. 1 interactor.
MINTiMINT-4100052.
STRINGi10090.ENSMUSP00000136524.

PTM databases

iPTMnetiP21619.
PhosphoSitePlusiP21619.

Proteomic databases

EPDiP21619.
MaxQBiP21619.
PaxDbiP21619.
PeptideAtlasiP21619.
PRIDEiP21619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000105332; ENSMUSP00000100969; ENSMUSG00000062075. [P21619-2]
ENSMUST00000179022; ENSMUSP00000136524; ENSMUSG00000062075. [P21619-1]
GeneIDi16907.
KEGGimmu:16907.
UCSCiuc007gfk.1. mouse. [P21619-1]

Organism-specific databases

CTDi84823.
MGIiMGI:96796. Lmnb2.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP21619.
KOiK07611.
PhylomeDBiP21619.
TreeFamiTF101181.

Miscellaneous databases

ChiTaRSiLmnb2. mouse.
PROiP21619.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000062075.
CleanExiMM_LMNB2.
ExpressionAtlasiP21619. baseline and differential.
GenevisibleiP21619. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P21619
Secondary accession number(s): P48680, Q8CGB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 153 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.