CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009831
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tropomyosin alpha-4 chain 
Protein Synonyms/Alias
 TM30p1; Tropomyosin-4 
Gene Name
 TPM4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11LNSLEAVKRKIQALQacetylation[1]
11LNSLEAVKRKIQALQubiquitination[1, 2, 3, 4]
13SLEAVKRKIQALQQQubiquitination[1, 2, 4, 5, 6]
113EIQEMQLKEAKHIAEubiquitination[6]
116EMQLKEAKHIAEEADubiquitination[6]
132KYEEVARKLVILEGEubiquitination[7]
169KNVTNNLKSLEAASEubiquitination[3, 6, 7, 8]
177SLEAASEKYSEKEDKacetylation[9]
177SLEAASEKYSEKEDKubiquitination[5, 6]
184KYSEKEDKYEEEIKLubiquitination[5, 6]
190DKYEEEIKLLSDKLKubiquitination[7, 8]
212FAERTVAKLEKTIDDubiquitination[4]
215RTVAKLEKTIDDLEEacetylation[9]
215RTVAKLEKTIDDLEEubiquitination[4, 5]
228EEKLAQAKEENVGLHubiquitination[6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 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]
 [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] 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]
 [9] 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
Functional Description
 Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 177 177 N6-acetyllysine.
 MOD_RES 215 215 N6-acetyllysine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Calcium; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Metal-binding; Muscle protein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 248 AA 
Protein Sequence
MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE 60
EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE 120
EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE 180
KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ 240
TLNELNCI 248 
Gene Ontology
 GO:0030863; C:cortical cytoskeleton; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
 GO:0002102; C:podosome; IEA:Compara.
 GO:0001725; C:stress fiber; IDA:MGI.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
 GO:0030049; P:muscle filament sliding; TAS:Reactome.
 GO:0006979; P:response to oxidative stress; IEP:BHF-UCL. 
Interpro
 IPR000533; Tropomyosin. 
Pfam
 PF00261; Tropomyosin 
SMART
  
PROSITE
 PS00326; TROPOMYOSIN 
PRINTS
 PR00194; TROPOMYOSIN.