P20700 (LMNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 16, 2012.
Version 131.
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-B1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 586 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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. |
| Subunit structure | Interacts with lamin-associated polypeptides IA, IB and 2. |
| 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. |
| Involvement in disease | Defects in LMNB1 are the cause of leukodystrophy demyelinating autosomal dominant adult-onset (ADLD) [MIM:169500]. ADLD is a slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis. Ref.12 |
| 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 |
| Coding sequence diversity | Chromosomal rearrangement Polymorphism |
| Disease | Leukodystrophy |
| Domain | Coiled coil |
| PTM | Acetylation Lipoprotein Methylation Phosphoprotein Prenylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome |
| Cellular component | lamin filament Traceable author statement Ref.2. Source: ProtInc nuclear inner membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | structural molecule activity Traceable author statement Ref.2. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.6 | |||||||||||||||||||||||||||
| Chain | 2 – 583 | 582 | Lamin-B1 | PRO_0000063816 | ||||||||||||||||||||||||||
| Propeptide | 584 – 586 | 3 | Removed in mature form Probable | PRO_0000393945 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Region | 2 – 34 | 33 | Head | |||||||||||||||||||||||||||
| Region | 35 – 386 | 352 | Rod | |||||||||||||||||||||||||||
| Region | 35 – 69 | 35 | Coil 1A | |||||||||||||||||||||||||||
| Region | 70 – 81 | 12 | Linker 1 | |||||||||||||||||||||||||||
| Region | 82 – 215 | 134 | Coil 1B | |||||||||||||||||||||||||||
| Region | 216 – 243 | 28 | Linker 2 | |||||||||||||||||||||||||||
| Region | 244 – 386 | 143 | Coil 2 | |||||||||||||||||||||||||||
| Region | 387 – 586 | 200 | Tail | |||||||||||||||||||||||||||
| Motif | 415 – 420 | 6 | Nuclear localization signal Potential | |||||||||||||||||||||||||||
| Compositional bias | 552 – 559 | 8 | Glu-rich (highly acidic; could be involved in chromatin binding) | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.6 Ref.20 | |||||||||||||||||||||||||||
| Modified residue | 5 | 1 | Phosphothreonine Ref.20 | |||||||||||||||||||||||||||
| Modified residue | 13 | 1 | Phosphoserine Ref.16 | |||||||||||||||||||||||||||
| Modified residue | 19 | 1 | Phosphothreonine Ref.10 | |||||||||||||||||||||||||||
| Modified residue | 20 | 1 | Phosphothreonine Ref.11 Ref.13 Ref.18 Ref.19 Ref.20 Ref.21 | |||||||||||||||||||||||||||
| Modified residue | 23 | 1 | Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 | |||||||||||||||||||||||||||
| Modified residue | 28 | 1 | Phosphoserine Ref.10 | |||||||||||||||||||||||||||
| Modified residue | 157 | 1 | N6-acetyllysine Ref.22 | |||||||||||||||||||||||||||
| Modified residue | 200 | 1 | Phosphoserine Ref.10 | |||||||||||||||||||||||||||
| Modified residue | 271 | 1 | N6-acetyllysine Ref.22 | |||||||||||||||||||||||||||
| Modified residue | 278 | 1 | Phosphoserine Ref.15 | |||||||||||||||||||||||||||
| Modified residue | 279 | 1 | Phosphoserine Ref.15 | |||||||||||||||||||||||||||
| Modified residue | 284 | 1 | Phosphoserine Ref.15 | |||||||||||||||||||||||||||
| Modified residue | 375 | 1 | Phosphoserine Ref.21 | |||||||||||||||||||||||||||
| Modified residue | 391 | 1 | Phosphoserine Ref.9 Ref.13 Ref.15 | |||||||||||||||||||||||||||
| Modified residue | 393 | 1 | Phosphoserine Ref.9 | |||||||||||||||||||||||||||
| Modified residue | 404 | 1 | Phosphoserine Ref.10 | |||||||||||||||||||||||||||
| Modified residue | 483 | 1 | N6-acetyllysine Ref.22 | |||||||||||||||||||||||||||
| Modified residue | 575 | 1 | Phosphothreonine Ref.10 Ref.19 Ref.21 | |||||||||||||||||||||||||||
| Modified residue | 579 | 1 | Phosphoserine Ref.15 | |||||||||||||||||||||||||||
| Modified residue | 583 | 1 | Cysteine methyl ester Probable | |||||||||||||||||||||||||||
| Lipidation | 583 | 1 | S-farnesyl cysteine Ref.8 | |||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||
| Natural variant | 501 | 1 | A → V. Corresponds to variant rs36105360 [ dbSNP | Ensembl ]. | VAR_031646 | ||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 382 | 1 | E → Q in AAH12295. Ref.5 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 432 – 438 | 7 | ||||||||||||||||||||||||||||
| Beta strand | 442 – 447 | 6 | ||||||||||||||||||||||||||||
| Beta strand | 453 – 458 | 6 | ||||||||||||||||||||||||||||
| Beta strand | 460 – 462 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 470 – 474 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 479 – 483 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 495 – 500 | 6 | ||||||||||||||||||||||||||||
| Turn | 509 – 511 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 512 – 515 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 527 – 532 | 6 | ||||||||||||||||||||||||||||
| Beta strand | 538 – 546 | 9 | ||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "In vitro posttranslational modification of lamin B cloned from a human T-cell line." Pollard K.M., Chan E.K.L., Grant B.J., Sullivan K.F., Tan E.M., Glass C.A. Mol. Cell. Biol. 10:2164-2175(1990) [PubMed: 2325650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Structural organization of the human gene (LMNB1) encoding nuclear lamin B1." Lin F., Worman H.J. Genomics 27:230-236(1995) [PubMed: 7557986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [4] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye and Placenta. |
| [6] | Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 15-26; 43-49; 80-90; 103-109; 112-123; 125-191; 198-220; 235-250; 259-271; 277-290; 300-312; 321-330; 351-387; 475-483 AND 517-528, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma. |
| [7] | Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 52-67; 80-90; 112-123; 146-156; 198-208; 210-220; 300-312; 321-330; 351-378 AND 458-473, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex. |
| [8] | "Human lamin B contains a farnesylated cysteine residue." Farnsworth C.C., Wolda S.L., Gelb M.H., Glomset J.A. J. Biol. Chem. 264:20422-20429(1989) [PubMed: 2684976] [Abstract] Cited for: ISOPRENYLATION AT CYS-583. |
| [9] | "Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-393, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma. |
| [10] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-23; SER-28; SER-200; SER-404 AND THR-575, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "Lamin B1 duplications cause autosomal dominant leukodystrophy." Padiath Q.S., Saigoh K., Schiffmann R., Asahara H., Yamada T., Koeppen A., Hogan K., Ptacek L.J., Fu Y.-H. Nat. Genet. 38:1114-1123(2006) [PubMed: 16951681] [Abstract] Cited for: INVOLVEMENT IN ADLD. |
| [13] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND SER-391, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma. |
| [14] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [15] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-278; SER-279; SER-284; SER-391 AND SER-579, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [19] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [20] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; THR-20 AND SER-23, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [21] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23; SER-375 AND THR-575, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [22] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-271 AND LYS-483, MASS SPECTROMETRY. |
| [23] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M34458 mRNA. Translation: AAA36162.1. L37747 L37746 Genomic DNA. Translation: AAC37575.1.AK312603 mRNA. Translation: BAG35493.1. CH471086 Genomic DNA. Translation: EAW48846.1. BC012295 mRNA. Translation: AAH12295.1. BC103723 mRNA. Translation: AAI03724.1. | ||||||||||||||||||||||||||||||
| IPI | IPI00217975. | ||||||||||||||||||||||||||||||
| PIR | VEHULB. A34707. | ||||||||||||||||||||||||||||||
| RefSeq | NP_005564.1. NM_005573.3. | ||||||||||||||||||||||||||||||
| UniGene | Hs.89497. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P20700. | ||||||||||||||||||||||||||||||
| SMR | P20700. Positions 31-67, 242-309, 311-385, 431-548. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| DIP | DIP-34897N. | ||||||||||||||||||||||||||||||
| IntAct | P20700. 17 interactions. | ||||||||||||||||||||||||||||||
| MINT | MINT-3009331. | ||||||||||||||||||||||||||||||
| STRING | P20700. | ||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||
| PhosphoSite | P20700. | ||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||
| DMDM | 125953. | ||||||||||||||||||||||||||||||
2D gel databases | |||||||||||||||||||||||||||||||
| Aarhus/Ghent-2DPAGE | 7510. IEF. | ||||||||||||||||||||||||||||||
| SWISS-2DPAGE | P20700. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PeptideAtlas | P20700. | ||||||||||||||||||||||||||||||
| PRIDE | P20700. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| DNASU | 4001. | ||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENST00000261366; ENSP00000261366; ENSG00000113368. | ||||||||||||||||||||||||||||||
| GeneID | 4001. | ||||||||||||||||||||||||||||||
| KEGG | hsa:4001. | ||||||||||||||||||||||||||||||
| UCSC | uc003kud.2. human. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 4001. | ||||||||||||||||||||||||||||||
| GeneCards | GC05P126112. | ||||||||||||||||||||||||||||||
| H-InvDB | HIX0005134. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:6637. LMNB1. | ||||||||||||||||||||||||||||||
| HPA | CAB005269. | ||||||||||||||||||||||||||||||
| MIM | 150340. gene. 169500. phenotype. | ||||||||||||||||||||||||||||||
| neXtProt | NX_P20700. | ||||||||||||||||||||||||||||||
| Orphanet | 99027. Adult-onset autosomal dominant leukodystrophy. | ||||||||||||||||||||||||||||||
| PharmGKB | PA30403. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | NOG325506. | ||||||||||||||||||||||||||||||
| GeneTree | ENSGT00560000076873. | ||||||||||||||||||||||||||||||
| HOGENOM | HOG000007711. | ||||||||||||||||||||||||||||||
| HOVERGEN | HBG013015. | ||||||||||||||||||||||||||||||
| InParanoid | P20700. | ||||||||||||||||||||||||||||||
| KO | K07611. | ||||||||||||||||||||||||||||||
| OMA | HQQGTPR. | ||||||||||||||||||||||||||||||
| OrthoDB | EOG45MN55. | ||||||||||||||||||||||||||||||
| PhylomeDB | P20700. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| Pathway_Interaction_DB | caspase_pathway. Caspase cascade in apoptosis. | ||||||||||||||||||||||||||||||
| Reactome | REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_578. Apoptosis. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| ArrayExpress | P20700. | ||||||||||||||||||||||||||||||
| Bgee | P20700. | ||||||||||||||||||||||||||||||
| CleanEx | HS_LMNB1. | ||||||||||||||||||||||||||||||
| Genevestigator | P20700. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000113368. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR001322. Lamin_tail_dom. [Graphical view] | ||||||||||||||||||||||||||||||
| PANTHER | PTHR23239. IF. 1 hit. | ||||||||||||||||||||||||||||||
| Pfam | PF00038. Filament. 1 hit. PF00932. LTD. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PROSITE | PS00226. IF. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||
| EvolutionaryTrace | P20700. | ||||||||||||||||||||||||||||||
| NextBio | 15700. | ||||||||||||||||||||||||||||||
| PMAP-CutDB | P20700. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | LMNB1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P20700 Secondary accession number(s): B2R6J6, Q3SYN7, Q96EI6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 5 Human chromosome 5: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with