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P14732 (LMNB2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lamin-B2
Gene names
Name:LMNB2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subcellular location

Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 597596Lamin-B2
PRO_0000063822
Propeptide598 – 6003Removed in mature form By similarity
PRO_0000403472

Regions

Region2 – 2726Head
Region28 – 379352Rod
Region28 – 6437Coil 1A
Region75 – 212138Coil 1B
Region237 – 379143Coil 2
Region380 – 600221Tail
Motif414 – 4196Nuclear localization signal Potential
Compositional bias398 – 4069Poly-Ser
Compositional bias435 – 44410Poly-Ser
Compositional bias568 – 58215Asp/Glu-rich (highly acidic; could be involved in chromatin binding)

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue5971Cysteine methyl ester By similarity
Lipidation5971S-farnesyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P14732 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 670E2985202211C0

FASTA60067,941
        10         20         30         40         50         60 
MSGTPIRGTP GGTPLSPTRI SRLQEKEELR QLNDRLAVYI DRVRALELEN DRLLVKISEK 

        70         80         90        100        110        120 
EEVTTREVSG IKNLYESELA DARRVLDETA KERARLQIEI GKLRAELEEF NKSYKKKDAD 

       130        140        150        160        170        180 
LSVAQGRIKD LEVLFHRSEA ELNTVLNEKR SLEAEVADLR AQLAKAEDGH AVAKKQLEKE 

       190        200        210        220        230        240 
TLMRVDLENR CQSLQEDLDF RKNVFEEEIR ETRKRHEHRL VEVDTSRQQE YENKMAQALE 

       250        260        270        280        290        300 
DLRNQHDEQV KLYKMELEQT YQAKLENAIL ASDQNDKAAG AAREELKEAR MRIESLSHQL 

       310        320        330        340        350        360 
SGLQKQASAT EDRIRELKET MAGERDKFRK MLDAKEREMT EMRDQMQLQL TEYQELLDVK 

       370        380        390        400        410        420 
LALDMEISAY RKLLEGEEER LKLSPSPSSR VTVSRATSSS SSSSTSLVRS SRGKRRRIEA 

       430        440        450        460        470        480 
EELSGSGTSG IGTGSISGSS SSSSFQMSQQ ASATGSISIE EIDLEGKYVQ LKNNSEKDQS 

       490        500        510        520        530        540 
LGNWRLKRQI GDGEEIAYKF TPKYVLRAGQ TVTIWGADAG VSHSPPSVLV WKNQGSWGTG 

       550        560        570        580        590        600 
GNIRTYLVNS DGEEVAVRTV TKSVVVRENE EEEDEADFGE EDLFNQQGDP RTTSRGCLVM 

« Hide

References

[1]"A second higher vertebrate B-type lamin. cDNA sequence determination and in vitro processing of chicken lamin B2."
Vorburger K., Lehner C.F., Kitten G.T., Eppenberger H.M., Nigg E.A.
J. Mol. Biol. 208:405-415(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16880 mRNA. Translation: CAA34763.1.
IPIIPI00601210.
PIRS05519.
RefSeqNP_990616.1. NM_205285.1.
UniGeneGga.16090.

3D structure databases

ProteinModelPortalP14732.
SMRP14732. Positions 23-59, 308-380, 452-560.
ModBaseSearch...

Protein-protein interaction databases

IntActP14732. 1 interaction.
STRING9031.ENSGALP00000034565.

Proteomic databases

PaxDbP14732.
PRIDEP14732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396222.
KEGGgga:396222.

Organism-specific databases

CTD84823.

Phylogenomic databases

eggNOGNOG325506.
HOGENOMHOG000007711.
HOVERGENHBG013015.
InParanoidP14732.
KOK07611.
OrthoDBEOG4ZCT4D.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816274.

Entry information

Entry nameLMNB2_CHICK
AccessionPrimary (citable) accession number: P14732
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families