CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004890
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lamin-B1 
Protein Synonyms/Alias
  
Gene Name
 LMNB1 
Gene Synonyms/Alias
 LMN2; LMNB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33RLSRLQEKEELRELNacetylation[1]
33RLSRLQEKEELRELNubiquitination[2]
49RLAVYIDKVRSLETEubiquitination[2, 3, 4, 5, 6]
79GRELTGLKALYETELubiquitination[2, 3, 5, 6, 7]
102DTARERAKLQIELGKubiquitination[2, 5, 6, 7]
109KLQIELGKCKAEHDQubiquitination[2, 5, 6]
111QIELGKCKAEHDQLLubiquitination[2, 4, 5, 6]
123QLLLNYAKKESDLNGacetylation[1]
123QLLLNYAKKESDLNGubiquitination[3, 6, 7]
124LLLNYAKKESDLNGAubiquitination[2]
134DLNGAQIKLREYEAAubiquitination[2, 3, 4, 5, 6, 7]
145YEAALNSKDAALATAubiquitination[3, 7]
157ATALGDKKSLEGDLEacetylation[1]
157ATALGDKKSLEGDLEubiquitination[2, 3, 5, 6, 7]
167EGDLEDLKDQIAQLEubiquitination[6]
181EASLAAAKKQLADETacetylation[1]
181EASLAAAKKQLADETubiquitination[6, 8]
182ASLAAAKKQLADETLubiquitination[2, 3, 4, 5, 6, 7]
209TEDLEFRKSMYEEEIubiquitination[2, 3, 5, 6, 7]
222EINETRRKHETRLVEubiquitination[7]
241RQIEYEYKLAQALHEubiquitination[2, 3, 5, 6, 7]
261DAQVRLYKEELEQTYubiquitination[2, 3, 5]
271LEQTYHAKLENARLSacetylation[1]
271LEQTYHAKLENARLSubiquitination[2, 3, 4, 5, 6, 7, 9]
312SQLSNLQKESRACLEubiquitination[2, 3, 4, 5, 6, 7]
330ELEDLLAKEKDNSRRubiquitination[2, 6, 7]
379MEISAYRKLLEGEEEubiquitination[2, 4, 5]
389EGEEERLKLSPSPSSubiquitination[2, 4, 5, 6, 7]
457DGKFIRLKNTSEQDQubiquitination[2]
474GGWEMIRKIGDTSVSubiquitination[10]
483GDTSVSYKYTSRYVLacetylation[1, 10, 11, 12]
483GDTSVSYKYTSRYVLubiquitination[2, 3, 4, 5, 10]
528WGTGEDVKVILKNSQubiquitination[3]
532EDVKVILKNSQGEEVubiquitination[2, 3, 5, 6, 7, 10, 13]
547AQRSTVFKTTIPEEEubiquitination[6, 7, 13]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [11] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [12] 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]
 [13] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
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 34 Head.
 REGION 35 386 Rod.
 REGION 35 69 Coil 1A.
 REGION 70 81 Linker 1.
 REGION 82 215 Coil 1B.
 REGION 216 243 Linker 2.
 REGION 244 386 Coil 2.
 REGION 387 586 Tail.
 MOTIF 415 420 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 Phosphothreonine.
 MOD_RES 5 5 Phosphothreonine.
 MOD_RES 20 20 Phosphothreonine.
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 157 157 N6-acetyllysine.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 271 271 N6-acetyllysine.
 MOD_RES 375 375 Phosphoserine.
 MOD_RES 391 391 Phosphoserine (By similarity).
 MOD_RES 393 393 Phosphoserine (By similarity).
 MOD_RES 483 483 N6-acetyllysine.
 MOD_RES 575 575 Phosphothreonine.
 MOD_RES 583 583 Cysteine methyl ester (Probable).
 LIPID 583 583 S-farnesyl cysteine.
 DISULFID 317 317 Interchain.  
Keyword
 3D-structure; Acetylation; Chromosomal rearrangement; Coiled coil; Complete proteome; Direct protein sequencing; Disulfide bond; Intermediate filament; Leukodystrophy; Lipoprotein; Membrane; Methylation; Nucleus; Phosphoprotein; Polymorphism; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 586 AA 
Protein Sequence
MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL 60
QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKC KAEHDQLLLN 120
YAKKESDLNG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLAAA 180
KKQLADETLL KVDLENRCQS LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY 240
KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI 300
ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR DQMQQQLNDY 360
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD 420
VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV 480
SYKYTSRYVL KAGQTVTIWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA 540
QRSTVFKTTI PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM 586 
Gene Ontology
 GO:0005638; C:lamin filament; TAS:ProtInc.
 GO:0005635; C:nuclear envelope; TAS:Reactome.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR001322; Lamin_tail_dom. 
Pfam
 PF00038; Filament
 PF00932; LTD 
SMART
  
PROSITE
 PS00226; IF 
PRINTS