CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008161
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Choline-phosphate cytidylyltransferase A 
Protein Synonyms/Alias
 CCT-alpha; CTP:phosphocholine cytidylyltransferase A; CCT A; CT A; Phosphorylcholine transferase A 
Gene Name
 PCYT1A 
Gene Synonyms/Alias
 CTPCT; PCYT1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MDAQCSAKVNARKRRacetylation[1]
33EEDGVPSKVQRCAVGubiquitination[2, 3]
57EIEVDFSKPYVRVTMubiquitination[2]
183AGSDDVYKHIKEAGMubiquitination[2]
186DDVYKHIKEAGMFAPubiquitination[2, 3]
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] 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] 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
Functional Description
 Controls phosphatidylcholine synthesis. 
Sequence Annotation
 REPEAT 319 324 1.
 REPEAT 329 333 2; approximate.
 REPEAT 343 348 3.
 NP_BIND 84 92 CTP (By similarity).
 NP_BIND 168 169 CTP (By similarity).
 NP_BIND 196 200 CTP (By similarity).
 REGION 228 287 Amphipathic (Potential).
 REGION 256 288 3 X 11 AA approximate tandem repeats.
 REGION 319 348 3 X repeats.
 BINDING 122 122 CTP (By similarity).
 BINDING 122 122 Substrate (By similarity).
 BINDING 151 151 Substrate (By similarity).
 BINDING 173 173 CTP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 8 8 N6-acetyllysine.
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 319 319 Phosphoserine.
 MOD_RES 321 321 Phosphoserine (By similarity).
 MOD_RES 322 322 Phosphoserine (By similarity).
 MOD_RES 323 323 Phosphoserine (By similarity).
 MOD_RES 329 329 Phosphoserine (By similarity).
 MOD_RES 331 331 Phosphoserine (By similarity).
 MOD_RES 333 333 Phosphoserine (By similarity).
 MOD_RES 343 343 Phosphoserine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 352 352 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Membrane; Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 367 AA 
Protein Sequence
MDAQCSAKVN ARKRRKEAPG PNGATEEDGV PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV 60
RVTMEEASRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYLIV GVCSDELTHN 120
FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD 180
VYKHIKEAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY 240
HLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK 300
HMLKEGKGRM LQAISPKQSP SSSPTRERSP SPSFRWPFSG KTSPPCSPAN LSRHKAAAYD 360
ISEDEED 367 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
 GO:0042587; C:glycogen granule; ISS:UniProtKB.
 GO:0004105; F:choline-phosphate cytidylyltransferase activity; ISS:UniProtKB.
 GO:0008289; F:lipid binding; IEA:Compara.
 GO:0009628; P:response to abiotic stimulus; IEA:Compara. 
Interpro
 IPR004821; Cyt_trans-like.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF01467; CTP_transf_2 
SMART
  
PROSITE
  
PRINTS