CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037277
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33RLSRLQEKEELRELNacetylation[1, 2, 3]
33RLSRLQEKEELRELNubiquitination[4]
49RLAVYIDKVRSLETEacetylation[3]
49RLAVYIDKVRSLETEubiquitination[4, 5, 6, 7, 8]
79GRELTGLKALYETELubiquitination[3, 4, 5, 8, 9]
102DTARERAKLQIELGKubiquitination[3, 4, 8, 9]
109KLQIELGKCKAEHDQubiquitination[3, 4, 8]
111QIELGKCKAEHDQLLacetylation[2]
111QIELGKCKAEHDQLLubiquitination[3, 4, 7, 8]
123QLLLNYAKKESDLNGubiquitination[5, 8, 9]
124LLLNYAKKESDLNGAubiquitination[3, 4]
134DLNGAQIKLREYEAAubiquitination[3, 4, 5, 7, 8, 9]
145YEAALNSKDAALATAubiquitination[5, 9]
157ATALGDKKSLEGDLEubiquitination[4, 5, 8, 9]
167EGDLEDLKDQIAQLEubiquitination[8]
181EASLAAAKKQLADETubiquitination[8]
182ASLAAAKKQLADETLubiquitination[3, 4, 5, 6, 7, 8, 9]
209TEDLEFRKSMYEEEIubiquitination[3, 4, 5, 8, 9]
241RQIEYEYKLAQALHEubiquitination[3, 4, 5, 8, 9]
261DAQVRLYKEELEQTYubiquitination[3, 4, 5]
271LEQTYHAKLENARLSacetylation[1, 2, 3]
271LEQTYHAKLENARLSubiquitination[3, 4, 5, 7, 8, 9, 10]
312SQLSNLQKESRACLEubiquitination[3, 4, 5, 7, 8, 9]
330ELEDLLAKEKDNSRRubiquitination[4, 8, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Coiled coil; Complete proteome; Intermediate filament; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 387 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 LEGEEER 387 
Gene Ontology
 GO:0005638; C:lamin filament; IEA:Compara.
 GO:0005635; C:nuclear envelope; IEA:Compara.
 GO:0005654; C:nucleoplasm; IEA:Compara.
 GO:0005198; F:structural molecule activity; IEA:InterPro. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS. 
Pfam
 PF00038; Filament 
SMART
  
PROSITE
 PS00226; IF 
PRINTS