P14732 (LMNB2_CHICK) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 89.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lamin-B2 | ||
| Gene names |
| ||
| Organism | Gallus gallus (Chicken) [Reference proteome] | ||
| Taxonomic identifier | 9031 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus![]() |
Protein attributes
| Sequence length | 600 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Intermediate filament Membrane Nucleus |
| Domain | Coiled coil |
| PTM | Acetylation Lipoprotein Methylation Phosphoprotein Prenylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | intermediate filament Inferred from electronic annotation. Source: UniProtKB-KW nuclear inner membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | structural molecule activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 597 | 596 | Lamin-B2 | PRO_0000063822 | |||||
| Propeptide | 598 – 600 | 3 | Removed in mature form By similarity | PRO_0000403472 | |||||
Regions | |||||||||
| Region | 2 – 27 | 26 | Head | ||||||
| Region | 28 – 379 | 352 | Rod | ||||||
| Region | 28 – 64 | 37 | Coil 1A | ||||||
| Region | 75 – 212 | 138 | Coil 1B | ||||||
| Region | 237 – 379 | 143 | Coil 2 | ||||||
| Region | 380 – 600 | 221 | Tail | ||||||
| Motif | 414 – 419 | 6 | Nuclear localization signal Potential | ||||||
| Compositional bias | 398 – 406 | 9 | Poly-Ser | ||||||
| Compositional bias | 435 – 444 | 10 | Poly-Ser | ||||||
| Compositional bias | 568 – 582 | 15 | Asp/Glu-rich (highly acidic; could be involved in chromatin binding) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 597 | 1 | Cysteine methyl ester By similarity | ||||||
| Lipidation | 597 | 1 | S-farnesyl cysteine By similarity | ||||||
Sequences
| ||||||||||||||||||
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. |
| IPI | IPI00601210. |
| PIR | S05519. |
| RefSeq | NP_990616.1. NM_205285.1. |
| UniGene | Gga.16090. |
3D structure databases | |
| ProteinModelPortal | P14732. |
| SMR | P14732. Positions 23-59, 308-380, 452-560. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P14732. 1 interaction. |
| STRING | 9031.ENSGALP00000034565. |
Proteomic databases | |
| PaxDb | P14732. |
| PRIDE | P14732. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 396222. |
| KEGG | gga:396222. |
Organism-specific databases | |
| CTD | 84823. |
Phylogenomic databases | |
| eggNOG | NOG325506. |
| HOGENOM | HOG000007711. |
| HOVERGEN | HBG013015. |
| InParanoid | P14732. |
| KO | K07611. |
| OrthoDB | EOG4ZCT4D. |
Family and domain databases | |
| InterPro | IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR001322. Lamin_tail_dom. [Graphical view] |
| PANTHER | PTHR23239. PTHR23239. 1 hit. |
| Pfam | PF00038. Filament. 1 hit. PF00932. LTD. 1 hit. [Graphical view] |
| PROSITE | PS00226. IF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20816274. |
Entry information
| Entry name | LMNB2_CHICK | ||||||||
| Accession | Primary (citable) accession number: P14732 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
