CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002786
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tropomyosin alpha-1 chain 
Protein Synonyms/Alias
 Alpha-tropomyosin; Tropomyosin-1 
Gene Name
 TPM1 
Gene Synonyms/Alias
 C15orf13; TMSA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
118QKLEEAEKAADESERubiquitination[1]
149EIQEIQLKEAKHIAEacetylation[2]
213SLEAQAEKYSQKEDRubiquitination[3]
226DRYEEEIKVLSDKLKubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [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
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 1 1 N-acetylmethionine.
 MOD_RES 283 283 Phosphoserine; by DAPK1.
 CROSSLNK 77 77 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Cardiomyopathy; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Isopeptide bond; Muscle protein; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 284 AA 
Protein Sequence
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 60
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 120
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 180
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE 240
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284 
Gene Ontology
 GO:0032059; C:bleb; IMP:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
 GO:0032587; C:ruffle membrane; IDA:BHF-UCL.
 GO:0001725; C:stress fiber; IDA:BHF-UCL.
 GO:0003779; F:actin binding; TAS:BHF-UCL.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
 GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
 GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
 GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0030049; P:muscle filament sliding; ISS:BHF-UCL.
 GO:0030336; P:negative regulation of cell migration; ISS:BHF-UCL.
 GO:0032781; P:positive regulation of ATPase activity; ISS:BHF-UCL.
 GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL.
 GO:0003065; P:positive regulation of heart rate by epinephrine; ISS:BHF-UCL.
 GO:0051496; P:positive regulation of stress fiber assembly; ISS:BHF-UCL.
 GO:0006937; P:regulation of muscle contraction; TAS:ProtInc.
 GO:0031529; P:ruffle organization; ISS:BHF-UCL.
 GO:0045214; P:sarcomere organization; IMP:BHF-UCL.
 GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
 GO:0042060; P:wound healing; ISS:BHF-UCL. 
Interpro
 IPR000533; Tropomyosin. 
Pfam
 PF00261; Tropomyosin 
SMART
  
PROSITE
 PS00326; TROPOMYOSIN 
PRINTS
 PR00194; TROPOMYOSIN.