CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004808
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
33EEDGIPSKVQRCAVGacetylation[1]
57EIEVDFSKPYVRVTMacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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.
 NP_BIND 168 169 CTP.
 NP_BIND 196 200 CTP.
 REGION 228 287 Amphipathic (Potential).
 REGION 256 288 3 X 11 AA approximate tandem repeats.
 REGION 298 315 Amphipathic (Potential).
 REGION 319 348 3 X repeats.
 BINDING 122 122 CTP.
 BINDING 122 122 Substrate.
 BINDING 151 151 Substrate.
 BINDING 173 173 CTP.
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 8 8 N6-acetyllysine (By similarity).
 MOD_RES 315 315 Phosphoserine; by PKC.
 MOD_RES 319 319 Phosphoserine.
 MOD_RES 321 321 Phosphoserine.
 MOD_RES 322 322 Phosphoserine.
 MOD_RES 323 323 Phosphoserine.
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 331 331 Phosphoserine.
 MOD_RES 333 333 Phosphoserine; by PKC.
 MOD_RES 343 343 Phosphoserine.
 MOD_RES 345 345 Phosphoserine.
 MOD_RES 346 346 Phosphoserine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 350 350 Phosphoserine.
 MOD_RES 352 352 Phosphoserine.
 MOD_RES 362 362 Phosphoserine; by CK2.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; 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
MDAQSSAKVN SRKRRKEVPG PNGATEEDGI PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV 60
RVTMEEACRG 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 SSSPTHERSP SPSFRWPFSG KTSPSSSPAS LSRCKAVTCD 360
ISEDEED 367 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:Compara.
 GO:0019898; C:extrinsic to membrane; NAS:RGD.
 GO:0042587; C:glycogen granule; IEA:Compara.
 GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
 GO:0008289; F:lipid binding; IMP:RGD.
 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