UniProt Accession

 LBR_MOUSE; Q3U9G9; Q3TSW2; Q811V8; Q811V9; Q8BST3; Q8K2Y8; Q8VDM0; Q91YS5; Q91Z27 

Genbank Protein ID

 AK030606; AK028426; AK033459; AK151798; AK161762; AK166850; AK167157; BC010261; BC014835; BC021516; BC029171; BC042522; AY148158; AY148158 

Genbank Nucleotide ID

 BAC27042.1; BAE20442.1; BAE20487.1; BAE30698.1; BAE36563.1; BAE39069.1; BAE39298.1; AAH10261.1; AAH14835.1; AAH21516.1; AAH29171.1; AAH42522.1; AAN76314.1; AAN76315.1 

Protein Name

 Lamin-B receptor 

Protein Synonyms/Alias

 Integral nuclear envelope inner membrane protein 

Gene Name

 Lbr 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
5	***MPSRKFVEGEVV	acetylation	[1, 2]
5	***MPSRKFVEGEVV	ubiquitination	[3]
42	QLYTVKYKDGTELEL	ubiquitination	[3]
133	KLTPLVLKPFGNSVS	ubiquitination	[3]
151	GEPEHMEKNATPYKD	ubiquitination	[3]
188	RREEVKAKEIESEEQ	acetylation	[2]
188	RREEVKAKEIESEEQ	ubiquitination	[3]
612	KYGLAWEKYCQRVPY	acetylation	[1, 2, 4]
612	KYGLAWEKYCQRVPY	ubiquitination	[3]

Reference

 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). 

Sequence Annotation

 DOMAIN 1 62 Tudor.
 MOD_RES 55 55 N6-acetyllysine (By similarity).
 MOD_RES 71 71 Phosphoserine; by CDK1 (By similarity).
 MOD_RES 86 86 Phosphoserine; by CDK1 (By similarity).
 MOD_RES 90 90 Phosphoserine (By similarity).
 MOD_RES 101 101 Phosphoserine.
 MOD_RES 103 103 Phosphoserine.
 MOD_RES 128 128 Phosphothreonine (By similarity).
 MOD_RES 605 605 N6-acetyllysine (By similarity).
 MOD_RES 612 612 N6-acetyllysine (By similarity).
 CARBOHYD 98 98 O-linked (GlcNAc) (By similarity).  

Keyword

 Acetylation; Complete proteome; DNA-binding; Glycoprotein; Membrane; Nucleus; Phosphoprotein; Receptor; Reference proteome; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 626 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; ISO:MGI.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005637; C:nuclear inner membrane; TAS:MGI.
 GO:0005652; C:nuclear lamina; TAS:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro. 

Interpro

 IPR001171; Ergosterol_biosynth_ERG4_ERG24.
 IPR019023; Lamin-B_rcpt_of_tudor.
 IPR018083; Sterol_reductase_CS.
 IPR002999; Tudor. 

Pfam

 PF01222; ERG4_ERG24
 PF09465; LBR_tudor 

SMART

 SM00333; TUDOR 

PROSITE

 PS01017; STEROL_REDUCT_1
 PS01018; STEROL_REDUCT_2
 PS50304; TUDOR 

PRINTS