CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004249
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lamin-B1 
Protein Synonyms/Alias
  
Gene Name
 Lmnb1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
80GRELTGLKALYETELubiquitination[1]
103DTARERAKLQIELGKubiquitination[1]
110KLQIELGKFKAEHDQubiquitination[1]
112QIELGKFKAEHDQLLacetylation[2, 3, 4]
112QIELGKFKAEHDQLLubiquitination[1, 5]
135DLSGAQIKLREYEAAubiquitination[1]
158ATALGDKKSLEGDLEubiquitination[1]
183ASLSAAKKQLADETLubiquitination[1, 5]
210TEDLEFRKNMYEEEIubiquitination[1, 5]
242RQIEYEYKLAQALHEacetylation[2]
262DAQVRLYKEELEQTYacetylation[2, 4]
262DAQVRLYKEELEQTYubiquitination[1]
272LEQTYHAKLENARLSacetylation[2, 3, 4]
272LEQTYHAKLENARLSubiquitination[1]
313SQLSNLQKESRACLEubiquitination[1, 5]
331ELEDMLAKERDNSRRacetylation[2, 3, 4]
331ELEDMLAKERDNSRRubiquitination[1]
380MEISAYRKLLEGEEEubiquitination[1]
390EGEEERLKLSPSPSSubiquitination[1]
533EDVKVILKNSQGEEVubiquitination[1]
548AQRSTVFKTTIPEEEubiquitination[1, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144] 
Functional Description
 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. 
Sequence Annotation
 REGION 2 35 Head.
 REGION 36 387 Rod.
 REGION 36 70 Coil 1A.
 REGION 71 82 Linker 1.
 REGION 83 216 Coil 1B.
 REGION 217 244 Linker 2.
 REGION 245 387 Coil 2.
 REGION 388 588 Tail.
 MOTIF 416 421 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 3 3 Phosphothreonine (By similarity).
 MOD_RES 5 5 Phosphothreonine (By similarity).
 MOD_RES 17 17 Phosphoserine.
 MOD_RES 21 21 Phosphothreonine.
 MOD_RES 24 24 Phosphoserine.
 MOD_RES 158 158 N6-acetyllysine (By similarity).
 MOD_RES 272 272 N6-acetyllysine (By similarity).
 MOD_RES 376 376 Phosphoserine (By similarity).
 MOD_RES 392 392 Phosphoserine.
 MOD_RES 394 394 Phosphoserine.
 MOD_RES 484 484 N6-acetyllysine (By similarity).
 MOD_RES 585 585 Cysteine methyl ester (By similarity).
 LIPID 585 585 S-farnesyl cysteine (By similarity).
 DISULFID 318 318 Interchain (By similarity).  
Keyword
 Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; Disulfide bond; Intermediate filament; Lipoprotein; Membrane; Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 588 AA 
Protein Sequence
MATATPVQQQ RAGSRASAPA TPLSPTRLSR LQEKEELREL NDRLAVYIDK VRSLETENSA 60
LQLQVTEREE VRGRELTGLK ALYETELADA RRALDDTARE RAKLQIELGK FKAEHDQLLL 120
NYAKKESDLS GAQIKLREYE AALNSKDAAL ATALGDKKSL EGDLEDLKDQ IAQLEASLSA 180
AKKQLADETL LKVDLENRCQ SLTEDLEFRK NMYEEEINET RRKHETRLVE VDSGRQIEYE 240
YKLAQALHEM REQHDAQVRL YKEELEQTYH AKLENARLSS EMNTSTVNSA REELMESRMR 300
IESLSSQLSN LQKESRACLE RIQELEDMLA KERDNSRRML SDREREMAEI RDQMQQQLSD 360
YEQLLDVKLA LDMEISAYRK LLEGEEERLK LSPSPSSRVT VSRASSSRSV RTTRGKRKRV 420
DVEESEASSS VSISHSASAT GNVCIEEIDV DGKFIRLKNT SEQDQPMGGW EMIRKIGDTS 480
VSYKYTSRYV LKAGQTVTVW AANAGVTASP PTDLIWKNQN SWGTGEDVKV ILKNSQGEEV 540
AQRSTVFKTT IPEEEEEEEE EPIGVAVEEE RFHQQGAPRA SNKSCAIM 588 
Gene Ontology
 GO:0005638; C:lamin filament; IDA:MGI.
 GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
 GO:0008432; F:JUN kinase binding; NAS:BHF-UCL.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0031662; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle; NAS:BHF-UCL.
 GO:0046330; P:positive regulation of JNK cascade; NAS:BHF-UCL. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR001322; Lamin_tail_dom. 
Pfam
 PF00038; Filament
 PF00932; LTD 
SMART
  
PROSITE
 PS00226; IF 
PRINTS