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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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Lamin-B2PRO_0000063821Add
BLAST
Propeptidei594 – 5963Removed in mature formBy similarityPRO_0000403471

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphothreonineBy similarity
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei59 – 591N6-acetyllysine; alternateBy similarity
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki173 – 173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei398 – 3981PhosphoserineBy similarity
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei593 – 5931Cysteine methyl esterBy similarity
Lipidationi593 – 5931S-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, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

EPDiP21619.
MaxQBiP21619.
PaxDbiP21619.
PRIDEiP21619.

PTM databases

iPTMnetiP21619.
PhosphoSiteiP21619.

Expressioni

Tissue specificityi

Isoform B3 is germ cell specific.

Gene expression databases

BgeeiP21619.
CleanExiMM_LMNB2.
ExpressionAtlasiP21619. baseline and differential.
GenevisibleiP21619. MM.

Interactioni

Subunit structurei

Interacts with TMEM43.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP21619.
SMRiP21619. Positions 321-375, 446-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini442 – 550109LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2626HeadAdd
BLAST
Regioni27 – 378352RodAdd
BLAST
Regioni27 – 6135Coil 1AAdd
BLAST
Regioni62 – 7312Linker 1Add
BLAST
Regioni74 – 207134Coil 1BAdd
BLAST
Regioni208 – 23427Linker 2Add
BLAST
Regioni235 – 378144Coil 2Add
BLAST
Regioni379 – 596218TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi415 – 4206Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi565 – 57814Asp/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.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP21619.
KOiK07611.
OrthoDBiEOG7MD4PW.
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 AAH42430.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH51985.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1492KQ → NE in CAA38032 (PubMed:2102682).Curated
Sequence conflicti314 – 3141H → R AA sequence (PubMed:2311764).Curated
Sequence conflicti321 – 3211A → R in CAA38032 (PubMed:2102682).Curated
Sequence conflicti344 – 3441A → R in CAA38032 (PubMed:2102682).Curated
Sequence conflicti403 – 4031Missing in CAA38032 (PubMed:2102682).Curated
Sequence conflicti412 – 4132GR → RG in CAA38032 (PubMed:2102682).Curated
Sequence conflicti421 – 4222Missing (PubMed:2102682).Curated
Sequence conflicti443 – 4431Missing in CAA38032 (PubMed:2102682).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 206206MASLP…SVFEE → MGESESMRGTGEGCGRDCPE AARPLMETVEGALPELRGRP LREYVKRRPRGLGKTPVEDP VKSEGAVGYPRTWNNHLRVP TREQ in isoform B3. 1 PublicationVSP_017070Add
BLAST

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. Positions 321-375, 446-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP21619.
PhosphoSiteiP21619.

Proteomic databases

EPDiP21619.
MaxQBiP21619.
PaxDbiP21619.
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.
OrthoDBiEOG7MD4PW.
PhylomeDBiP21619.
TreeFamiTF101181.

Miscellaneous databases

ChiTaRSiLmnb2. mouse.
NextBioi290944.
PROiP21619.
SOURCEiSearch...

Gene expression databases

BgeeiP21619.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin."
    Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.
    Chromosoma 99:379-390(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B2).
  2. "cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells."
    Furukawa K., Hotta Y.
    EMBO J. 12:97-106(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B3).
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.
  4. "Identification of lamin B2 as a substrate of protein kinase C in BALB/MK-2 mouse keratinocytes."
    Kasahara K., Chida K., Tsunenaga M., Kohno Y., Ikuta T., Kuroki T.
    J. Biol. Chem. 266:20018-20023(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 165-172; 254-262 AND 482-491.
  5. "Protein chemical analysis of purified murine lamin B identifies two distinct polypeptides B1 and B2."
    Weber K., Plessmann U., Traub P.
    FEBS Lett. 261:361-364(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 182-206; 234-286; 290-319; 364-401 AND 470-496.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "LUMA interacts with emerin and influences its distribution at the inner nuclear membrane."
    Bengtsson L., Otto H.
    J. Cell Sci. 121:536-548(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM43.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas and Spleen.

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: May 11, 2016
This is version 148 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.