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P20700 (LMNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lamin-B1
Gene names
Name:LMNB1
Synonyms:LMN2, LMNB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Homodimer. Interacts with lamin-associated polypeptides IA, IB and 2. Ref.21

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.

Involvement in disease

Leukodystrophy, demyelinating, autosomal dominant, adult-onset (ADLD) [MIM:169500]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

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 Ref.6
Chain2 – 583582Lamin-B1
PRO_0000063816
Propeptide584 – 5863Removed in mature form Probable
PRO_0000393945

Regions

Region2 – 3433Head
Region35 – 386352Rod
Region35 – 6935Coil 1A
Region70 – 8112Linker 1
Region82 – 215134Coil 1B
Region216 – 24328Linker 2
Region244 – 386143Coil 2
Region387 – 586200Tail
Motif415 – 4206Nuclear localization signal Potential
Compositional bias552 – 5598Glu-rich (highly acidic; could be involved in chromatin binding)

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.14 Ref.17 Ref.20
Modified residue31Phosphothreonine Ref.17
Modified residue51Phosphothreonine Ref.17
Modified residue201Phosphothreonine Ref.10 Ref.13
Modified residue231Phosphoserine Ref.10 Ref.13 Ref.17 Ref.19
Modified residue1111N6-acetyllysine By similarity
Modified residue1571N6-acetyllysine Ref.16
Modified residue2101Phosphoserine Ref.19
Modified residue2711N6-acetyllysine Ref.16
Modified residue3301N6-acetyllysine By similarity
Modified residue3751Phosphoserine Ref.15 Ref.17
Modified residue4831N6-acetyllysine Ref.16
Modified residue5751Phosphothreonine Ref.9 Ref.13 Ref.17 Ref.19
Modified residue5831Cysteine methyl ester Probable
Lipidation5831S-farnesyl cysteine Ref.8
Disulfide bond317Interchain Ref.21

Natural variations

Natural variant5011A → V.
Corresponds to variant rs36105360 [ dbSNP | Ensembl ].
VAR_031646

Experimental info

Sequence conflict3821E → Q in AAH12295. Ref.5

Secondary structure

........................ 586
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20700 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 73292877745722C4

FASTA58666,408
        10         20         30         40         50         60 
MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL 

        70         80         90        100        110        120 
QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKC KAEHDQLLLN 

       130        140        150        160        170        180 
YAKKESDLNG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLAAA 

       190        200        210        220        230        240 
KKQLADETLL KVDLENRCQS LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY 

       250        260        270        280        290        300 
KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI 

       310        320        330        340        350        360 
ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR DQMQQQLNDY 

       370        380        390        400        410        420 
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD 

       430        440        450        460        470        480 
VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV 

       490        500        510        520        530        540 
SYKYTSRYVL KAGQTVTIWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA 

       550        560        570        580 
QRSTVFKTTI PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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, IDENTIFICATION BY 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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-583.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ADLD.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-271 AND LYS-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; THR-5; SER-23; SER-375 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-210 AND THR-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1."
Ruan J., Xu C., Bian C., Lam R., Wang J.P., Kania J., Min J., Zang J.
FEBS Lett. 586:314-318(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 311-388, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 428-550, DISULFIDE BOND, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34458 mRNA. Translation: AAA36162.1.
L37747 expand/collapse EMBL AC list , L37737, L37738, L37739, L37740, L37741, L37742, L37743, L37744, L37745, 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.
PIRVEHULB. A34707.
RefSeqNP_005564.1. NM_005573.3.
UniGeneHs.89497.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KPWNMR-A439-549[»]
3JT0X-ray2.39A/B426-558[»]
3TYYX-ray2.40A/B311-388[»]
3UMNX-ray2.00A/B/C428-550[»]
ProteinModelPortalP20700.
SMRP20700. Positions 28-121, 290-385, 431-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110187. 57 interactions.
DIPDIP-34897N.
IntActP20700. 25 interactions.
MINTMINT-3009331.
STRING9606.ENSP00000261366.

PTM databases

PhosphoSiteP20700.

Polymorphism databases

DMDM125953.

2D gel databases

SWISS-2DPAGEP20700.

Proteomic databases

PaxDbP20700.
PeptideAtlasP20700.
PRIDEP20700.

Protocols and materials databases

DNASU4001.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261366; ENSP00000261366; ENSG00000113368.
GeneID4001.
KEGGhsa:4001.
UCSCuc003kud.2. human.

Organism-specific databases

CTD4001.
GeneCardsGC05P126112.
HGNCHGNC:6637. LMNB1.
HPACAB005269.
HPA050524.
MIM150340. gene.
169500. phenotype.
neXtProtNX_P20700.
Orphanet99027. Adult-onset autosomal dominant leukodystrophy.
PharmGKBPA30403.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325506.
HOGENOMHOG000007711.
HOVERGENHBG013015.
InParanoidP20700.
KOK07611.
OMAQKESRAC.
OrthoDBEOG7MD4PW.
PhylomeDBP20700.
TreeFamTF101181.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP20700.
BgeeP20700.
CleanExHS_LMNB1.
GenevestigatorP20700.

Family and domain databases

Gene3D2.60.40.1260. 1 hit.
InterProIPR001664. 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]
SUPFAMSSF74853. SSF74853. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLMNB1. human.
EvolutionaryTraceP20700.
GeneWikiLMNB1.
GenomeRNAi4001.
NextBio15700.
PMAP-CutDBP20700.
PROP20700.
SOURCESearch...

Entry information

Entry nameLMNB1_HUMAN
AccessionPrimary (citable) accession number: P20700
Secondary accession number(s): B2R6J6, Q3SYN7, Q96EI6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM