CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007539
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lamina-associated polypeptide 2, isoform alpha 
Protein Synonyms/Alias
 Thymopoietin isoform alpha; TP alpha; Thymopoietin-related peptide isoform alpha; TPRP isoform alpha; Thymopoietin; TP; Splenin; Thymopentin; TP5 
Gene Name
 TMPO 
Gene Synonyms/Alias
 LAP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
94SRAAVGRKATKKTDKmethylation[1]
269PGRGQLQKLASERNLubiquitination[2, 3]
281RNLFISCKSSHDRCLubiquitination[4]
323ETTTGYYKDIVENICubiquitination[3]
334ENICGREKSGIQPLCubiquitination[2]
356DQSPLSSKRKALEESubiquitination[2, 3]
358SPLSSKRKALEESESubiquitination[2]
416QKRIDQSKFQETEFLubiquitination[4]
435KVPRLSEKSVEERDSacetylation[3]
435KVPRLSEKSVEERDSubiquitination[2, 3, 4]
656GRRYLWLKDCKINLAacetylation[3, 5, 6, 7]
656GRRYLWLKDCKINLAubiquitination[2]
659YLWLKDCKINLASKNubiquitination[2, 4]
667INLASKNKLASTPFKubiquitination[2]
674KLASTPFKGGTLFGGubiquitination[2, 3, 4]
685LFGGEVCKVIKKRGNubiquitination[4]
Reference
 [1] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [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] 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] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
Functional Description
 May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1. 
Sequence Annotation
 DOMAIN 5 48 LEM-like.
 DOMAIN 109 153 LEM.
 REGION 49 108 Linker.
 MOTIF 190 196 Nuclear localization signal (Potential).
 MOD_RES 57 57 Phosphothreonine.
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 74 74 Phosphothreonine.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 154 154 Phosphothreonine.
 MOD_RES 156 156 Phosphoserine.
 MOD_RES 160 160 Phosphothreonine.
 MOD_RES 164 164 Phosphothreonine.
 MOD_RES 184 184 Phosphoserine.
 MOD_RES 351 351 Phosphoserine.
 MOD_RES 354 354 Phosphoserine.
 MOD_RES 370 370 Phosphoserine.
 MOD_RES 424 424 Phosphoserine.
 MOD_RES 656 656 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy; Chromosome; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; DNA-binding; Nucleus; Pharmaceutical; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 694 AA 
Protein Sequence
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK 60
GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL 120
LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS 180
DRYSDNEEGK KKEHKKVKST RDIVPFSELG TTPSGGGFFQ GISFPEISTR PPLGSTELQA 240
AKKVHTSKGD LPREPLVATN LPGRGQLQKL ASERNLFISC KSSHDRCLEK SSSSSSQPEH 300
SAMLVSTAAS PSLIKETTTG YYKDIVENIC GREKSGIQPL CPERSHISDQ SPLSSKRKAL 360
EESESSQLIS PPLAQAIRDY VNSLLVQGGV GSLPGTSNSM PPLDVENIQK RIDQSKFQET 420
EFLSPPRKVP RLSEKSVEER DSGSFVAFQN IPGSELMSSF AKTVVSHSLT TLGLEVAKQS 480
QHDKIDASEL SFPFHESILK VIEEEWQQVD RQLPSLACKY PVSSREATQI LSVPKVDDEI 540
LGFISEATPL GGIQAASTES CNQQLDLALC RAYEAAASAL QIATHTAFVA KAMQADISQA 600
AQILSSDPSR THQALGILSK TYDAASYICE AAFDEVKMAA HTMGNATVGR RYLWLKDCKI 660
NLASKNKLAS TPFKGGTLFG GEVCKVIKKR GNKH 694 
Gene Ontology
 GO:0000785; C:chromatin; IDA:MGI.
 GO:0005635; C:nuclear envelope; TAS:ProtInc.
 GO:0005637; C:nuclear inner membrane; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0005521; F:lamin binding; TAS:ProtInc.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:Compara. 
Interpro
 IPR021623; LAP2alpha.
 IPR013146; LEM-like_dom.
 IPR011015; LEM/LEM-like_dom.
 IPR003887; LEM_dom. 
Pfam
 PF11560; LAP2alpha
 PF03020; LEM
 PF08198; Thymopoietin 
SMART
 SM00540; LEM 
PROSITE
 PS50954; LEM
 PS50955; LEM_LIKE 
PRINTS