CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022391
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tropomodulin-3 
Protein Synonyms/Alias
 Ubiquitous tropomodulin; U-Tmod 
Gene Name
 TMOD3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13RKDLEKYKDLDEDELubiquitination[1]
101KGKIFIPKQKPVQTFubiquitination[2]
103KIFIPKQKPVQTFTEubiquitination[2, 3]
172SNVVKGEKILPVFDEubiquitination[1, 2, 4, 5]
191TNVEESLKRTKENDAubiquitination[2]
217NIPIPTLKDFAKALEubiquitination[2]
230LETNTHVKCFSLAATubiquitination[2]
252TAFAEMLKVNKTLKSubiquitination[2]
289NETLAELKIDNQRQQubiquitination[2]
317EENTNILKFGYQFTQubiquitination[2]
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] 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] 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]
 [4] 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]
 [5] 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
Functional Description
 Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). 
Sequence Annotation
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 71 71 Phosphoserine (By similarity).  
Keyword
 Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 352 AA 
Protein Sequence
MALPFRKDLE KYKDLDEDEL LGNLSETELK QLETVLDDLD PENALLPAGF RQKNQTSKST 60
TGPFDREHLL SYLEKEALEH KDREDYVPYT GEKKGKIFIP KQKPVQTFTE EKVSLDPELE 120
EALTSASDTE LCDLAAILGM HNLITNTKFC NIMGSSNGVD QEHFSNVVKG EKILPVFDEP 180
PNPTNVEESL KRTKENDAHL VEVNLNNIKN IPIPTLKDFA KALETNTHVK CFSLAATRSN 240
DPVATAFAEM LKVNKTLKSL NVESNFITGV GILALIDALR DNETLAELKI DNQRQQLGTA 300
VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRVEGD HQ 352 
Gene Ontology
 GO:0005865; C:striated muscle thin filament; IEA:Compara.
 GO:0005523; F:tropomyosin binding; TAS:ProtInc. 
Interpro
 IPR004934; Tropomodulin. 
Pfam
 PF03250; Tropomodulin 
SMART
  
PROSITE
  
PRINTS