P49585 (PCY1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Choline-phosphate cytidylyltransferase A EC=2.7.7.15 Alternative name(s): CCT-alpha CTP:phosphocholine cytidylyltransferase A Short name=CCT A Short name=CT A Phosphorylcholine transferase A | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 367 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Controls phosphatidylcholine synthesis. |
| Catalytic activity | CTP + choline phosphate = diphosphate + CDP-choline. |
| Enzyme regulation | By phosphorylation By similarity. |
| Pathway | |
| Subunit structure | Homodimer; disulfide-linked. Ref.7 |
| Subcellular location | Cytoplasm › cytosol By similarity. Membrane; Peripheral membrane protein By similarity. Note: It can interconvert between an inactive cytosolic form and an active membrane-bound form By similarity. |
| Post-translational modification | The serine residues of the C-terminus are phosphorylated. The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation By similarity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 |
| Sequence similarities | Belongs to the cytidylyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Cytoplasm Membrane |
| Domain | Repeat |
| Molecular function | Nucleotidyltransferase Transferase |
| PTM | Acetylation Disulfide bond Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fractionTraceable author statement. Source: ProtInc |
| Molecular function | choline-phosphate cytidylyltransferase activity Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 367 | 367 | Choline-phosphate cytidylyltransferase A | PRO_0000208453 | |||||
Regions | |||||||||
| Repeat | 319 – 324 | 6 | 1 | ||||||
| Repeat | 329 – 333 | 5 | 2; approximate | ||||||
| Repeat | 343 – 348 | 6 | 3 | ||||||
| Region | 74 – 235 | 162 | Catalytic Potential | ||||||
| Region | 228 – 287 | 60 | Amphipathic Potential | ||||||
| Region | 256 – 288 | 33 | 3 X 11 AA approximate tandem repeats | ||||||
| Region | 319 – 348 | 30 | 3 X repeats | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.16 | ||||||
| Modified residue | 8 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 315 | 1 | Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 | ||||||
| Modified residue | 319 | 1 | Phosphoserine Ref.11 Ref.14 Ref.15 | ||||||
| Modified residue | 321 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 325 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 329 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 331 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 339 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 342 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 343 | 1 | Phosphoserine Ref.13 Ref.14 Ref.15 | ||||||
| Modified residue | 347 | 1 | Phosphoserine Ref.13 Ref.14 Ref.15 | ||||||
| Modified residue | 352 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 362 | 1 | Phosphoserine Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 | ||||||
| Disulfide bond | 37 | Interchain Ref.7 | |||||||
Experimental info | |||||||||
| Sequence conflict | 251 | 1 | K → E in AAA72127. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase." Kalmar G.B., Kay R.J., Lachance A.C., Cornell R.B. Biochim. Biophys. Acta 1219:328-334(1994) [PubMed: 7918629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | SeattleSNPs variation discovery resource Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [5] | "Membrane-binding amphipathic alpha-helical peptide derived from CTP:phosphocholine cytidylyltransferase." Johnson J.E., Cornell R.B. Biochemistry 33:4327-4335(1994) [PubMed: 8155650] [Abstract] Cited for: MECHANISM OF CYTIDYLYLTRANSFERASE ACTIVATION. |
| [6] | "Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase." Dunne S.J., Cornell R.B., Johnson J.E., Glover N.R., Tracey A.S. Biochemistry 35:11975-11984(1996) [PubMed: 8810902] [Abstract] Cited for: CIRCULAR DICHROISM, STRUCTURE BY NMR OF 236-268 AND 267-288. |
| [7] | "Membrane binding modulates the quaternary structure of CTP:phosphocholine cytidylyltransferase." Xie M., Smith J.L., Ding Z., Zhang D., Cornell R.B. J. Biol. Chem. 279:28817-28825(2004) [PubMed: 15069071] [Abstract] Cited for: INTERCHAIN DISULFIDE BOND. |
| [8] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-329; SER-331 AND SER-362, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, MASS SPECTROMETRY. Tissue: Prostate cancer. |
| [11] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-319, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-339; THR-342; SER-343; SER-347; SER-352 AND SER-362, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-321; THR-325; SER-343; SER-347 AND SER-362, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [15] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-343; SER-347 AND SER-362, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [16] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-8, MASS SPECTROMETRY. |
| [17] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
Web resources
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L28957 mRNA. Translation: AAA72127.1. EU280320 Genomic DNA. Translation: ABX44666.1. CH471191 Genomic DNA. Translation: EAW53655.1. CH471191 Genomic DNA. Translation: EAW53662.1. BC046355 mRNA. Translation: AAH46355.1. |
| IPI | IPI00329338. |
| PIR | S50145. |
| RefSeq | NP_005008.2. NM_005017.2. |
| UniGene | Hs.135997. |
3D structure databases | |
| ProteinModelPortal | P49585. |
| SMR | P49585. Positions 40-216. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P49585. 8 interactions. |
| STRING | P49585. |
PTM databases | |
| PhosphoSite | P49585. |
Polymorphism databases | |
| DMDM | 166214967. |
Proteomic databases | |
| PRIDE | P49585. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000292823; ENSP00000292823; ENSG00000161217. ENST00000431016; ENSP00000394617; ENSG00000161217. |
| GeneID | 5130. |
| KEGG | hsa:5130. |
| UCSC | uc003fwg.1. human. |
Organism-specific databases | |
| CTD | 5130. |
| GeneCards | GC03M195941. |
| H-InvDB | HIX0024337. |
| HGNC | HGNC:8754. PCYT1A. |
| HPA | HPA035428. |
| MIM | 123695. gene. |
| neXtProt | NX_P49585. |
| PharmGKB | PA33099. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG12430. |
| GeneTree | ENSGT00390000000269. |
| HOVERGEN | HBG053531. |
| InParanoid | P49585. |
| PhylomeDB | P49585. |
Gene expression databases | |
| ArrayExpress | P49585. |
| Bgee | P49585. |
| CleanEx | HS_PCYT1A. |
| Genevestigator | P49585. |
| GermOnline | ENSG00000161217. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR004821. Cyt_trans-rel. IPR004820. Cytidylyltransf. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| KO | K00968. |
| Pfam | PF01467. CTP_transf_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00125. Cyt_tran_rel. 1 hit. |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00122. Choline. |
| NextBio | 19780. |
| PMAP-CutDB | P49585. |
| SOURCE | Search... |
Entry information
| Entry name | PCY1A_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P49585 Secondary accession number(s): A9LYK9, D3DXB1, Q86Y88 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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