CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002574
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tropomyosin beta chain 
Protein Synonyms/Alias
 Beta-tropomyosin; Tropomyosin-2 
Gene Name
 TPM2 
Gene Synonyms/Alias
 TMSB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30EQAEADKKQAEDRCKubiquitination[1]
37KQAEDRCKQLEEEQQubiquitination[1]
48EEQQALQKKLKGTEDubiquitination[1]
51QALQKKLKGTEDEVEubiquitination[1]
65EKYSESVKEAQEKLEubiquitination[1]
112RLATALQKLEEAEKAubiquitination[1]
118QKLEEAEKAADESERubiquitination[1]
128DESERGMKVIENRAMubiquitination[1]
152EMQLKEAKHIAEDSDubiquitination[1]
168KYEEVARKLVILEGEubiquitination[1]
205RTMDQALKSLMASEEubiquitination[1]
251RSVAKLEKTIDDLEEubiquitination[2]
Reference
 [1] 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]
 [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
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. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 61 61 Phosphoserine; by PIK3CG (By similarity).
 MOD_RES 252 252 Phosphothreonine (By similarity).
 MOD_RES 283 283 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Muscle protein; Nemaline myopathy; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 284 AA 
Protein Sequence
MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY 60
SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 120
DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE 180
ERAEVAESRA RQLEEELRTM DQALKSLMAS EEEYSTKEDK YEEEIKLLEE KLKEAETRAE 240
FAERSVAKLE KTIDDLEETL ASAKEENVEI HQTLDQTLLE LNNL 284 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
 GO:0030049; P:muscle filament sliding; TAS:Reactome.
 GO:0043462; P:regulation of ATPase activity; IDA:UniProtKB. 
Interpro
 IPR000533; Tropomyosin. 
Pfam
 PF00261; Tropomyosin 
SMART
  
PROSITE
 PS00326; TROPOMYOSIN 
PRINTS
 PR00194; TROPOMYOSIN.