CPLM-002376

Genbank Nucleotide ID

Tropomyosin alpha-3 chain

Protein Synonyms/Alias

Gamma-tropomyosin; Tropomyosin-3; Tropomyosin-5; hTM5

Homo sapiens (Human)

Position	Peptide	Type	References
13	KKKMQMLKLDKENAL	acetylation	[1]
13	KKKMQMLKLDKENAL	ubiquitination	[2]
16	MQMLKLDKENALDRA	ubiquitination	[3]
60	GTEDELDKYSEALKD	ubiquitination	[4]
113	RLATALQKLEEAEKA	acetylation	[1]
119	QKLEEAEKAADESER	acetylation	[5]
137	VIENRALKDEEKMEL	ubiquitination	[3]
141	RALKDEEKMELQEIQ	acetylation	[5]
150	ELQEIQLKEAKHIAE	ubiquitination	[2, 4]
153	EIQLKEAKHIAEEAD	ubiquitination	[3]
162	IAEEADRKYEEVARK	acetylation	[1]
169	KYEEVARKLVIIEGD	ubiquitination	[6]
214	SLEAQAEKYSQKEDK	ubiquitination	[4]
218	QAEKYSQKEDKYEEE	ubiquitination	[2, 3]
221	KYSQKEDKYEEEIKI	acetylation	[1]
252	RSVAKLEKTIDDLED	ubiquitination	[2]

[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] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]

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.

MOD_RES 284 284 Phosphoserine (By similarity).

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

IPR000533; Tropomyosin.

PF00261; Tropomyosin

PS00326; TROPOMYOSIN

PR00194; TROPOMYOSIN.