CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006799
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transgelin-2 
Protein Synonyms/Alias
 Epididymis tissue protein Li 7e; SM22-alpha homolog 
Gene Name
 TAGLN2 
Gene Synonyms/Alias
 KIAA0120; CDABP0035 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17LSREVQQKIEKQYDAacetylation[1, 2, 3, 4]
17LSREVQQKIEKQYDAubiquitination[5, 6]
20EVQQKIEKQYDADLEacetylation[1]
78PEGQAPVKKIQASTMubiquitination[5]
79EGQAPVKKIQASTMAubiquitination[6, 7, 8]
88QASTMAFKQMEQISQacetylation[3]
88QASTMAFKQMEQISQubiquitination[5]
120TVDLWEGKNMACVQRacetylation[3]
120TVDLWEGKNMACVQRubiquitination[9]
153GDPNWFPKKSKENPRacetylation[3]
153GDPNWFPKKSKENPRubiquitination[10]
154DPNWFPKKSKENPRNubiquitination[6]
171DNQLQEGKNVIGLQMacetylation[3]
171DNQLQEGKNVIGLQMubiquitination[4, 5, 6, 7, 8, 9, 10, 11, 12]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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
Functional Description
  
Sequence Annotation
 DOMAIN 24 136 CH.
 REPEAT 174 199 Calponin-like.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 17 17 N6-acetyllysine.
 MOD_RES 20 20 N6-acetyllysine.
 MOD_RES 163 163 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 199 AA 
Protein Sequence
MANRGPAYGL SREVQQKIEK QYDADLEQIL IQWITTQCRK DVGRPQPGRE NFQNWLKDGT 60
VLCELINALY PEGQAPVKKI QASTMAFKQM EQISQFLQAA ERYGINTTDI FQTVDLWEGK 120
NMACVQRTLM NLGGLAVARD DGLFSGDPNW FPKKSKENPR NFSDNQLQEG KNVIGLQMGT 180
NRGASQAGMT GYGMPRQIL 199 
Gene Ontology
 GO:0007517; P:muscle organ development; IEA:InterPro. 
Interpro
 IPR000557; Calponin_repeat.
 IPR001715; CH-domain.
 IPR003096; SM22_calponin.
 IPR001061; TAGLN. 
Pfam
 PF00402; Calponin
 PF00307; CH 
SMART
 SM00033; CH 
PROSITE
 PS01052; CALPONIN_1
 PS51122; CALPONIN_2
 PS50021; CH 
PRINTS
 PR00888; SM22CALPONIN.