CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009137
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myotrophin 
Protein Synonyms/Alias
 Protein V-1 
Gene Name
 MTPN 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MCDKEFMWALKacetylation[1]
4****MCDKEFMWALKubiquitination[2, 3]
11KEFMWALKNGDLDEVacetylation[1]
11KEFMWALKNGDLDEVubiquitination[4]
24EVKDYVAKGEDVNRTacetylation[1, 5]
24EVKDYVAKGEDVNRTubiquitination[6]
66ADINAPDKHHITPLLacetylation[5]
66ADINAPDKHHITPLLubiquitination[3]
97KGADKTVKGPDGLTAacetylation[1]
97KGADKTVKGPDGLTAubiquitination[6]
Reference
 [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] 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]
 [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] 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] 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]
 [6] 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
 Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. 
Sequence Annotation
 REPEAT 2 30 ANK 1.
 REPEAT 34 66 ANK 2.
 REPEAT 67 99 ANK 3.
 MOD_RES 2 2 N-acetylcysteine.
 MOD_RES 4 4 N6-acetyllysine.
 MOD_RES 11 11 N6-acetyllysine.
 MOD_RES 24 24 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ANK repeat; Complete proteome; Cytoplasm; Nucleus; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 118 AA 
Protein Sequence
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD 60
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ 118 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0008290; C:F-actin capping protein complex; IDA:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0006584; P:catecholamine metabolic process; IEA:Compara.
 GO:0016049; P:cell growth; IDA:UniProtKB.
 GO:0021707; P:cerebellar granule cell differentiation; IEA:Compara.
 GO:0030182; P:neuron differentiation; NAS:UniProtKB.
 GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
 GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
 GO:0010557; P:positive regulation of macromolecule biosynthetic process; ISS:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
 GO:0051247; P:positive regulation of protein metabolic process; ISS:UniProtKB.
 GO:2000812; P:regulation of barbed-end actin filament capping; IDA:UniProtKB.
 GO:0016202; P:regulation of striated muscle tissue development; NAS:UniProtKB.
 GO:0006417; P:regulation of translation; NAS:UniProtKB.
 GO:0043403; P:skeletal muscle tissue regeneration; IEA:Compara.
 GO:0051146; P:striated muscle cell differentiation; IEA:Compara. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom. 
Pfam
 PF12796; Ank_2 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS
 PR01415; ANKYRIN.