CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012385
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lamin-B receptor 
Protein Synonyms/Alias
 Integral nuclear envelope inner membrane protein; LMN2R 
Gene Name
 LBR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MPSRKFADGEVVubiquitination[1]
42QLYTVKYKDGTELELubiquitination[1, 2]
55ELKENDIKPLTSFRQacetylation[3]
107ASHQADIKEARREVEubiquitination[1, 2, 4, 5]
116ARREVEVKLTPLILKubiquitination[1, 6, 7]
123KLTPLILKPFGNSISubiquitination[1, 4, 5, 6, 7, 8]
147ERNDAPHKNTQEKFSubiquitination[2]
178RREEVKLKEIDSKEEubiquitination[1]
183KLKEIDSKEEKYVAKubiquitination[2]
186EIDSKEEKYVAKELAubiquitination[1]
190KEEKYVAKELAVRTFacetylation[3]
190KEEKYVAKELAVRTFubiquitination[1, 2, 4, 5, 6, 7, 8]
508FRGANSQKNAFRKNPubiquitination[2]
524DPKLAHLKTIHTSTGubiquitination[1, 2]
532TIHTSTGKNLLVSGWubiquitination[1]
594DEYHCKKKYGVAWEKacetylation[3]
594DEYHCKKKYGVAWEKubiquitination[1]
601KYGVAWEKYCQRVPYacetylation[3]
601KYGVAWEKYCQRVPYubiquitination[1, 2, 4, 6, 7, 8, 9]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Anchors the lamina and the heterochromatin to the inner nuclear membrane. 
Sequence Annotation
 DOMAIN 1 62 Tudor.
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 71 71 Phosphoserine; by CDK1.
 MOD_RES 86 86 Phosphoserine; by CDK1.
 MOD_RES 97 97 Phosphoserine.
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 118 118 Phosphothreonine.
 MOD_RES 594 594 N6-acetyllysine.
 MOD_RES 601 601 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Disease mutation; DNA-binding; Membrane; Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 615 AA 
Protein Sequence
MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK ENDIKPLTSF 60
RQRKGGSTSS SPSRRRGSRS RSRSRSPGRP PKSARRSASA SHQADIKEAR REVEVKLTPL 120
ILKPFGNSIS RYNGEPEHIE RNDAPHKNTQ EKFSLSQESS YIATQYSLRP RREEVKLKEI 180
DSKEEKYVAK ELAVRTFEVT PIRAKDLEFG GVPGVFLIMF GLPVFLFLLL LMCKQKDPSL 240
LNFPPPLPAL YELWETRVFG VYLLWFLIQV LFYLLPIGKV VEGTPLIDGR RLKYRLNGFY 300
AFILTSAVIG TSLFQGVEFH YVYSHFLQFA LAATVFCVVL SVYLYMRSLK APRNDLSPAS 360
SGNAVYDFFI GRELNPRIGT FDLKYFCELR PGLIGWVVIN LVMLLAEMKI QDRAVPSLAM 420
ILVNSFQLLY VVDALWNEEA LLTTMDIIHD GFGFMLAFGD LVWVPFIYSF QAFYLVSHPN 480
EVSWPMASLI IVLKLCGYVI FRGANSQKNA FRKNPSDPKL AHLKTIHTST GKNLLVSGWW 540
GFVRHPNYLG DLIMALAWSL PCGFNHILPY FYIIYFTMLL VHREARDEYH CKKKYGVAWE 600
KYCQRVPYRI FPYIY 615 
Gene Ontology
 GO:0005639; C:integral to nuclear inner membrane; TAS:ProtInc.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0005521; F:lamin binding; TAS:ProtInc.
 GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
 GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome. 
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