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Protein

Lamin-B2

Gene

LMNB2

Organism
Homo sapiens (Human)
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
Synonyms:LMN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6638. LMNB2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Partial acquired lipodystrophy (APLD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare childhood disease characterized by loss of subcutaneous fat from the face and trunk. Fat deposition on the pelvic girdle and lower limbs is normal or excessive. Most frequently, onset between 5 and 15 years of age. Most affected subjects are females and some show no other abnormality, but many develop glomerulonephritis, diabetes mellitus, hyperlipidemia, and complement deficiency. Mental retardation in some cases. APLD is a sporadic disorder of unknown etiology.
See also OMIM:608709
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti235 – 2351R → Q in APLD. 1 Publication
Corresponds to variant rs61726481 [ dbSNP | Ensembl ].
VAR_031063
Natural varianti252 – 2521Y → H in APLD. 1 Publication
VAR_074171
Natural varianti427 – 4271A → T in APLD. 1 Publication
Corresponds to variant rs57521499 [ dbSNP | Ensembl ].
VAR_031064
Epilepsy, progressive myoclonic 9 (EPM9)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive form of progressive myoclonic epilepsy, a rare disease initially responsive to antiepileptic drugs which over time becomes refractory and can be associated with cognitive decline. EPM9 features include myoclonus, tonic-clonic seizures, ataxia, and psychomotor development.
See also OMIM:616540
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571H → Y in EPM9; disrupts fibrillar formation. 1 Publication
VAR_074170

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MalaCardsiLMNB2.
MIMi608709. phenotype.
616540. phenotype.
Orphaneti79087. Partial acquired lipodystrophy.
PharmGKBiPA30404.

Polymorphism and mutation databases

BioMutaiLMNB2.
DMDMi23503078.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617Lamin-B2PRO_0000063820Add
BLAST
Propeptidei618 – 6203Removed in mature formBy similarityPRO_0000403470

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341PhosphothreonineCombined sources
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei81 – 811N6-acetyllysineCombined sources
Modified residuei420 – 4201PhosphoserineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources
Modified residuei424 – 4241PhosphoserineCombined sources
Modified residuei426 – 4261PhosphoserineCombined sources
Modified residuei617 – 6171Cysteine methyl esterBy similarity
Lipidationi617 – 6171S-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, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ03252.
PaxDbiQ03252.
PRIDEiQ03252.

2D gel databases

REPRODUCTION-2DPAGEIPI00009771.

PTM databases

iPTMnetiQ03252.
PhosphoSiteiQ03252.

Expressioni

Gene expression databases

BgeeiQ03252.
CleanExiHS_LMNB2.

Organism-specific databases

HPAiCAB022593.

Interactioni

Subunit structurei

Interacts with TMEM43.By similarity

Protein-protein interaction databases

BioGridi124281. 23 interactions.
DIPiDIP-57724N.
IntActiQ03252. 12 interactions.
MINTiMINT-3024955.
STRINGi9606.ENSP00000462730.

Structurei

Secondary structure

1
620
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi473 – 4797Combined sources
Beta strandi484 – 4907Combined sources
Beta strandi492 – 4943Combined sources
Beta strandi502 – 5076Combined sources
Beta strandi512 – 5165Combined sources
Beta strandi528 – 5336Combined sources
Helixi534 – 5363Combined sources
Turni542 – 5443Combined sources
Beta strandi545 – 5484Combined sources
Beta strandi552 – 5554Combined sources
Beta strandi558 – 5658Combined sources
Beta strandi571 – 58010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLLNMR-A469-589[»]
5BNWX-ray2.40D383-395[»]
ProteinModelPortaliQ03252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini465 – 578114LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4848HeadAdd
BLAST
Regioni49 – 400352RodAdd
BLAST
Regioni49 – 8335Coil 1AAdd
BLAST
Regioni84 – 9512Linker 1Add
BLAST
Regioni96 – 229134Coil 1BAdd
BLAST
Regioni230 – 25627Linker 2Add
BLAST
Regioni257 – 400144Coil 2Add
BLAST
Regioni401 – 620220TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi435 – 4406Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi590 – 60213Asp/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.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiQ03252.
KOiK07611.
PhylomeDBiQ03252.
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]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPPSPGRRR EQRRPRAAAT MATPLPGRAG GPATPLSPTR LSRLQEKEEL
60 70 80 90 100
RELNDRLAHY IDRVRALELE NDRLLLKISE KEEVTTREVS GIKALYESEL
110 120 130 140 150
ADARRVLDET ARERARLQIE IGKLRAELDE VNKSAKKREG ELTVAQGRVK
160 170 180 190 200
DLESLFHRSE VELAAALSDK RGLESDVAEL RAQLAKAEDG HAVAKKQLEK
210 220 230 240 250
ETLMRVDLEN RCQSLQEELD FRKSVFEEEV RETRRRHERR LVEVDSSRQQ
260 270 280 290 300
EYDFKMAQAL EELRSQHDEQ VRLYKLELEQ TYQAKLDSAK LSSDQNDKAA
310 320 330 340 350
SAAREELKEA RMRLESLSYQ LSGLQKQASA AEDRIRELEE AMAGERDKFR
360 370 380 390 400
KMLDAKEQEM TEMRDVMQQQ LAEYQELLDV KLALDMEINA YRKLLEGEEE
410 420 430 440 450
RLKLSPSPSS RVTVSRATSS SSGSLSATGR LGRSKRKRLE VEEPLGSGPS
460 470 480 490 500
VLGTGTGGSG GFHLAQQASA SGSVSIEEID LEGKFVQLKN NSDKDQSLGN
510 520 530 540 550
WRIKRQVLEG EEIAYKFTPK YILRAGQMVT VWAAGAGVAH SPPSTLVWKG
560 570 580 590 600
QSSWGTGESF RTVLVNADGE EVAMRTVKKS SVMRENENGE EEEEEAEFGE
610 620
EDLFHQQGDP RTTSRGCYVM
Length:620
Mass (Da):69,948
Last modified:November 11, 2015 - v4
Checksum:iA8799BB12B6242B9
GO

Sequence cautioni

The sequence AAH06551.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011R → S in AAA80979 (PubMed:1630457).Curated
Sequence conflicti439 – 47537LEVEE…SGSVS → WRWRSPWQRPKRPGHGHGWQ RWLPPGPAGLGLGQRH in AAA80979 (PubMed:1630457).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571H → Y in EPM9; disrupts fibrillar formation. 1 Publication
VAR_074170
Natural varianti235 – 2351R → Q in APLD. 1 Publication
Corresponds to variant rs61726481 [ dbSNP | Ensembl ].
VAR_031063
Natural varianti236 – 2361R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036370
Natural varianti252 – 2521Y → H in APLD. 1 Publication
VAR_074171
Natural varianti427 – 4271A → T in APLD. 1 Publication
Corresponds to variant rs57521499 [ dbSNP | Ensembl ].
VAR_031064

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT007441 mRNA. Translation: AAP36109.1.
AC011522 Genomic DNA. No translation available.
AC005624 Genomic DNA. Translation: AAC34573.1.
BC006551 mRNA. Translation: AAH06551.1. Different initiation.
M94362 mRNA. Translation: AAA80979.1.
M94363 Genomic DNA. Translation: AAB00873.1. Sequence problems.
CCDSiCCDS12090.2.
RefSeqiNP_116126.3. NM_032737.3.
UniGeneiHs.538286.

Genome annotation databases

EnsembliENST00000325327; ENSP00000327054; ENSG00000176619.
GeneIDi84823.
KEGGihsa:84823.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT007441 mRNA. Translation: AAP36109.1.
AC011522 Genomic DNA. No translation available.
AC005624 Genomic DNA. Translation: AAC34573.1.
BC006551 mRNA. Translation: AAH06551.1. Different initiation.
M94362 mRNA. Translation: AAA80979.1.
M94363 Genomic DNA. Translation: AAB00873.1. Sequence problems.
CCDSiCCDS12090.2.
RefSeqiNP_116126.3. NM_032737.3.
UniGeneiHs.538286.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLLNMR-A469-589[»]
5BNWX-ray2.40D383-395[»]
ProteinModelPortaliQ03252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124281. 23 interactions.
DIPiDIP-57724N.
IntActiQ03252. 12 interactions.
MINTiMINT-3024955.
STRINGi9606.ENSP00000462730.

PTM databases

iPTMnetiQ03252.
PhosphoSiteiQ03252.

Polymorphism and mutation databases

BioMutaiLMNB2.
DMDMi23503078.

2D gel databases

REPRODUCTION-2DPAGEIPI00009771.

Proteomic databases

MaxQBiQ03252.
PaxDbiQ03252.
PRIDEiQ03252.

Protocols and materials databases

DNASUi84823.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325327; ENSP00000327054; ENSG00000176619.
GeneIDi84823.
KEGGihsa:84823.

Organism-specific databases

CTDi84823.
GeneCardsiLMNB2.
HGNCiHGNC:6638. LMNB2.
HPAiCAB022593.
MalaCardsiLMNB2.
MIMi150341. gene.
608709. phenotype.
616540. phenotype.
neXtProtiNX_Q03252.
Orphaneti79087. Partial acquired lipodystrophy.
PharmGKBiPA30404.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiQ03252.
KOiK07611.
PhylomeDBiQ03252.
TreeFamiTF101181.

Miscellaneous databases

ChiTaRSiLMNB2. human.
GenomeRNAii84823.
NextBioi75028.
PROiQ03252.
SOURCEiSearch...

Gene expression databases

BgeeiQ03252.
CleanExiHS_LMNB2.

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]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Muscle.
  4. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 94-104; 131-150; 152-161; 192-202; 236-244; 294-306; 345-372; 486-496 AND 530-555, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  5. "The gene for a novel human lamin maps at a highly transcribed locus of chromosome 19 which replicates at the onset of S-phase."
    Biamonti G., Giacca M., Perini G., Contreas G., Zentilin L., Weighardt F., Guerra M., Valle G.D., Saccone S., Riva S., Falaschi A.
    Mol. Cell. Biol. 12:3499-3506(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-620, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 531-620.
  6. "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-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34; SER-37; SER-422; SER-424 AND SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 THR-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-420; SER-422; SER-424 AND SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy."
    Hegele R.A., Cao H., Liu D.M., Costain G.A., Charlton-Menys V., Rodger N.W., Durrington P.N.
    Am. J. Hum. Genet. 79:383-389(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS APLD GLN-235 AND THR-427.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-236.
  21. "A Chinese patient with acquired partial lipodystrophy caused by a novel mutation with LMNB2 gene."
    Gao J., Li Y., Fu X., Luo X.
    J. Pediatr. Endocrinol. Metab. 25:375-377(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT APLD HIS-252.
  22. Cited for: VARIANT EPM9 TYR-157, CHARACTERIZATION OF VARIANT EPM9 TYR-157.

Entry informationi

Entry nameiLMNB2_HUMAN
AccessioniPrimary (citable) accession number: Q03252
Secondary accession number(s): O75292, Q14734, Q96DF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 11, 2015
Last modified: January 20, 2016
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.