CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022081
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase 
Protein Synonyms/Alias
 4'-phosphopantetheinyl transferase; Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase; AASD-PPT; LYS5 ortholog 
Gene Name
 AASDHPPT 
Gene Synonyms/Alias
 CGI-80; HAH-P; HSPC223; x0005 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45RSIQPEEKERIGQFVubiquitination[1]
58FVFARDAKAAMAGRLubiquitination[1, 2]
74IRKLVAEKLNIPWNHubiquitination[1]
149PEFFHIMKRKFTNKEubiquitination[1, 3, 4]
151FFHIMKRKFTNKEWEubiquitination[1]
155MKRKFTNKEWETIRSubiquitination[1]
164WETIRSFKDEWTQLDubiquitination[1, 2, 3, 4]
180FYRNWALKESFIKAIubiquitination[1, 2, 5]
185ALKESFIKAIGVGLGubiquitination[1]
214LDIGQVYKETRLFLDubiquitination[1, 2, 5, 6]
226FLDGEEEKEWAFEESubiquitination[2]
263VPSQDDSKPTQRQFTubiquitination[1, 2, 5, 7, 8, 9, 10, 11]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] 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]
 [11] 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
Functional Description
 Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'- phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN. 
Sequence Annotation
 REGION 86 91 Coenzyme A binding.
 REGION 108 111 Coenzyme A binding.
 REGION 181 185 Coenzyme A binding.
 METAL 129 129 Magnesium.
 METAL 181 181 Magnesium.
 BINDING 47 47 Coenzyme A.
 MOD_RES 258 258 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 309 AA 
Protein Sequence
MVFPAKRFCL VPSMEGVRWA FSCGTWLPSR AEWLLAVRSI QPEEKERIGQ FVFARDAKAA 60
MAGRLMIRKL VAEKLNIPWN HIRLQRTAKG KPVLAKDSSN PYPNFNFNIS HQGDYAVLAA 120
EPELQVGIDI MKTSFPGRGS IPEFFHIMKR KFTNKEWETI RSFKDEWTQL DMFYRNWALK 180
ESFIKAIGVG LGFELQRLEF DLSPLNLDIG QVYKETRLFL DGEEEKEWAF EESKIDEHHF 240
VAVALRKPDG SRHQDVPSQD DSKPTQRQFT ILNFNDLMSS AVPMTPEDPS FWDCFCFTEE 300
IPIRNGTKS 309 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro.
 GO:0015939; P:pantothenate metabolic process; TAS:Reactome. 
Interpro
 IPR008278; 4-PPantetheinyl_Trfase_SF. 
Pfam
 PF01648; ACPS 
SMART
  
PROSITE
  
PRINTS