CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002377
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tropomyosin alpha-3 chain 
Protein Synonyms/Alias
 Gamma-tropomyosin; Tropomyosin-3; Tropomyosin-5; hTM5 
Gene Name
 TPM3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11ITTIEAVKRKIQVLQubiquitination[1, 2]
13TIEAVKRKIQVLQQQubiquitination[2, 3]
169RLMDQNLKCLSAAEEubiquitination[2]
177CLSAAEEKYSQKEDKacetylation[4]
215RSVAKLEKTIDDLEDacetylation[4]
215RSVAKLEKTIDDLEDubiquitination[2]
223TIDDLEDKLKCTKEEubiquitination[2]
228EDKLKCTKEEHLCTQacetylation[5]
228EDKLKCTKEEHLCTQubiquitination[1, 2, 3]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647] 
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. 
Sequence Annotation
 MOD_RES 284 284 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Muscle protein; Nemaline myopathy; Phosphoprotein; Proto-oncogene; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 285 AA 
Protein Sequence
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA SLNRRIQLVE 60
EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK DEEKMELQEI QLKEAKHIAE 120
EADRKYEEVA RKLVIIEGDL ERTEERAELA ESRCREMDEQ IRLMDQNLKC LSAAEEKYSQ 180
KEDKYEEEIK ILTDKLKEAE TRAEFAERSV AKLEKTIDDL EDKLKCTKEE HLCTQRMLDQ 240
TLLDLNEM 248 
Gene Ontology
 GO:0032154; C:cleavage furrow; IEA:Compara.
 GO:0030863; C:cortical cytoskeleton; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0030426; C:growth cone; IEA:Compara.
 GO:0005862; C:muscle thin filament tropomyosin; TAS:UniProtKB.
 GO:0002102; C:podosome; IEA:Compara.
 GO:0001725; C:stress fiber; IDA:MGI.
 GO:0030049; P:muscle filament sliding; TAS:Reactome.
 GO:0006937; P:regulation of muscle contraction; NAS:UniProtKB. 
Interpro
 IPR000533; Tropomyosin. 
Pfam
 PF00261; Tropomyosin 
SMART
  
PROSITE
 PS00326; TROPOMYOSIN 
PRINTS
 PR00194; TROPOMYOSIN.