CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011055
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lamin-B2 
Protein Synonyms/Alias
  
Gene Name
 LMNB2 
Gene Synonyms/Alias
 LMN2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57ENDRLLLKISEKEEVubiquitination[1, 2, 3]
61LLLKISEKEEVTTREacetylation[4]
61LLLKISEKEEVTTREubiquitination[2, 5, 6]
73TREVSGIKALYESELubiquitination[2]
103RLQIEIGKLRAELDEubiquitination[1, 3, 5, 7]
113AELDEVNKSAKKREGubiquitination[2, 5, 6]
130TVAQGRVKDLESLFHubiquitination[3, 5, 6, 7]
150LAAALSDKRGLESDVubiquitination[1, 2, 3, 8]
166ELRAQLAKAEDGHAVubiquitination[2, 5, 6, 7]
180VAKKQLEKETLMRVDubiquitination[1, 3, 7]
235RQQEYDFKMAQALEEubiquitination[5, 6]
255DEQVRLYKLELEQTYubiquitination[1, 2, 3, 5, 6, 7]
265LEQTYQAKLDSAKLSubiquitination[1, 2, 3, 5, 6, 7]
270QAKLDSAKLSSDQNDubiquitination[2, 5, 6]
278LSSDQNDKAASAAREubiquitination[1, 2, 3, 5, 6]
288SAAREELKEARMRLEubiquitination[2, 6]
306YQLSGLQKQASAAEDubiquitination[2, 5, 6, 7]
331GERDKFRKMLDAKEQubiquitination[5]
336FRKMLDAKEQEMTEMubiquitination[2]
373MEINAYRKLLEGEEEubiquitination[2, 7]
383EGEEERLKLSPSPSSubiquitination[1, 2, 7]
474QLKNNSDKDQSLGNWubiquitination[2, 5, 7]
496EGEEIAYKFTPKYILubiquitination[1, 2, 3]
500IAYKFTPKYILRAGQacetylation[4]
500IAYKFTPKYILRAGQubiquitination[1, 3, 6, 7]
Reference
 [1] 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]
 [2] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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] 
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 1 28 Head.
 REGION 29 380 Rod.
 REGION 29 63 Coil 1A.
 REGION 64 75 Linker 1.
 REGION 76 209 Coil 1B.
 REGION 210 236 Linker 2.
 REGION 237 380 Coil 2.
 REGION 381 600 Tail.
 MOTIF 415 420 Nuclear localization signal (Potential).
 MOD_RES 14 14 Phosphothreonine.
 MOD_RES 17 17 Phosphoserine.
 MOD_RES 61 61 N6-acetyllysine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 404 404 Phosphoserine.
 MOD_RES 406 406 Phosphoserine.
 MOD_RES 498 498 Phosphothreonine (By similarity).
 MOD_RES 597 597 Cysteine methyl ester (By similarity).
 LIPID 597 597 S-farnesyl cysteine (By similarity).  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Intermediate filament; Lipoprotein; Membrane; Methylation; Nucleus; Phosphoprotein; Polymorphism; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 600 AA 
Protein Sequence
MATPLPGRAG GPATPLSPTR LSRLQEKEEL RELNDRLAHY IDRVRALELE NDRLLLKISE 60
KEEVTTREVS GIKALYESEL ADARRVLDET ARERARLQIE IGKLRAELDE VNKSAKKREG 120
ELTVAQGRVK DLESLFHRSE VELAAALSDK RGLESDVAEL RAQLAKAEDG HAVAKKQLEK 180
ETLMRVDLEN RCQSLQEELD FRKSVFEEEV RETRRRHERR LVEVDSSRQQ EYDFKMAQAL 240
EELRSQHDEQ VRLYKLELEQ TYQAKLDSAK LSSDQNDKAA SAAREELKEA RMRLESLSYQ 300
LSGLQKQASA AEDRIRELEE AMAGERDKFR KMLDAKEQEM TEMRDVMQQQ LAEYQELLDV 360
KLALDMEINA YRKLLEGEEE RLKLSPSPSS RVTVSRATSS SSGSLSATGR LGRSKRKRLE 420
VEEPLGSGPS VLGTGTGGSG GFHLAQQASA SGSVSIEEID LEGKFVQLKN NSDKDQSLGN 480
WRIKRQVLEG EEIAYKFTPK YILRAGQMVT VWAAGAGVAH SPPSTLVWKG QSSWGTGESF 540
RTVLVNADGE EVAMRTVKKS SVMRENENGE EEEEEAEFGE EDLFHQQGDP RTTSRGCYVM 600 
Gene Ontology
 GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0005652; C:nuclear lamina; NAS:UniProtKB.
 GO:0005198; F:structural molecule activity; IEA:InterPro. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR001322; Lamin_tail_dom. 
Pfam
 PF00038; Filament
 PF00932; LTD 
SMART
  
PROSITE
 PS00226; IF 
PRINTS