Tag | Content |
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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 |
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33 | EEDGIPSKVQRCAVG | acetylation | [1] | 57 | EIEVDFSKPYVRVTM | acetylation | [1] |
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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. |
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