CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009486
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thymosin beta-4 
Protein Synonyms/Alias
 T beta-4; Fx; Hematopoietic system regulatory peptide; Seraspenide 
Gene Name
 TMSB4X 
Gene Synonyms/Alias
 TB4X; THYB4; TMSB4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MSDKPDMAEIEacetylation[1, 2, 3, 4, 5]
4****MSDKPDMAEIEubiquitination[5, 6, 7]
12PDMAEIEKFDKSKLKacetylation[1, 2, 3, 4, 5]
12PDMAEIEKFDKSKLKubiquitination[5, 6, 7, 8, 9]
15AEIEKFDKSKLKKTEacetylation[1, 2]
15AEIEKFDKSKLKKTEubiquitination[6]
17IEKFDKSKLKKTETQacetylation[2]
19KFDKSKLKKTETQEKacetylation[2]
26KKTETQEKNPLPSKEacetylation[1, 3, 5, 10]
26KKTETQEKNPLPSKEubiquitination[5, 7, 11, 12]
32EKNPLPSKETIEQEKacetylation[1, 3, 4, 5]
32EKNPLPSKETIEQEKubiquitination[5, 6, 7, 9, 11, 12]
39KETIEQEKQAGES**acetylation[1, 3, 5]
39KETIEQEKQAGES**ubiquitination[5, 7, 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] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [11] 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]
 [12] 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
Functional Description
 Plays an important role in the organization of the cytoskeleton (By similarity). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization. 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 26 26 N6-acetyllysine.
 MOD_RES 39 39 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 44 AA 
Protein Sequence
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES 44 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005576; C:extracellular region; TAS:Reactome.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO:0001649; P:osteoblast differentiation; IEA:Compara.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0042989; P:sequestering of actin monomers; IEA:InterPro. 
Interpro
 IPR001152; Thymosin_b4.
 IPR016323; Thymosin_b4_chordata. 
Pfam
 PF01290; Thymosin 
SMART
 SM00152; THY 
PROSITE
 PS00500; THYMOSIN_B4 
PRINTS