P49585 (PCY1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	PCYT1A
Synonyms:	CTPCT, PCYT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 + phosphocholine = diphosphate + CDP-choline.
Enzyme regulation	By phosphorylation By similarity.
Pathway	Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
Subunit structure	Homodimer.
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. Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation By similarity.
Sequence similarities	Belongs to the cytidylyltransferase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cytoplasm Membrane
Domain	Repeat
Molecular function	Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to abiotic stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB glycogen granule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	choline-phosphate cytidylyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: Compara
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
	Nucleotide binding	84 – 92	9	CTP By similarity
	Nucleotide binding	168 – 169	2	CTP By similarity
	Nucleotide binding	196 – 200	5	CTP By similarity
	Region	228 – 287	60	Amphipathic Potential
	Region	256 – 288	33	3 X 11 AA approximate tandem repeats
	Region	319 – 348	30	3 X repeats
Sites
	Binding site	122	1	CTP By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	151	1	Substrate By similarity
	Binding site	173	1	CTP By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.12
	Modified residue	8	1	N6-acetyllysine Ref.12
	Modified residue	315	1	Phosphoserine Ref.11 Ref.13 Ref.15
	Modified residue	319	1	Phosphoserine Ref.11
	Modified residue	321	1	Phosphoserine By similarity
	Modified residue	322	1	Phosphoserine By similarity
	Modified residue	323	1	Phosphoserine By similarity
	Modified residue	329	1	Phosphoserine By similarity
	Modified residue	331	1	Phosphoserine By similarity
	Modified residue	333	1	Phosphoserine By similarity
	Modified residue	343	1	Phosphoserine Ref.10 Ref.11
	Modified residue	347	1	Phosphoserine Ref.10 Ref.11
	Modified residue	352	1	Phosphoserine Ref.10
	Modified residue	362	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15
Experimental info
	Mutagenesis	37	1	C → S: Abolishes formation of the interchain disulfide that can be observed when the enzyme is treated with copper phenanthrolene (in vitro). Ref.7
	Sequence conflict	251	1	K → E in AAA72127. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49585 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 38CE9D5CF2E2AEE2	FASTA	367	41,731
	10 20 30 40 50 60 MDAQCSAKVN ARKRRKEAPG PNGATEEDGV PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV 70 80 90 100 110 120 RVTMEEASRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYLIV GVCSDELTHN 130 140 150 160 170 180 FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD 190 200 210 220 230 240 VYKHIKEAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY 250 260 270 280 290 300 HLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK 310 320 330 340 350 360 HMLKEGKGRM LQAISPKQSP SSSPTRERSP SPSFRWPFSG KTSPPCSPAN LSRHKAAAYD ISEDEED

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IN VITRO INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF CYS-37.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-347; SER-352 AND SER-362, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [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.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-8, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-362, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-362, MASS SPECTROMETRY.

Web resources

SeattleSNPs

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.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49585. 8 interactions.
STRING	9606.ENSP00000292823.
PTM databases
PhosphoSite	P49585.
Polymorphism databases
DMDM	166214967.
Proteomic databases
PaxDb	P49585.
PRIDE	P49585.
Protocols and materials databases
DNASU	5130.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000292823; ENSP00000292823; ENSG00000161217. ENST00000431016; ENSP00000394617; ENSG00000161217.
GeneID	5130.
KEGG	hsa:5130.
UCSC	uc003fwg.3. 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	COG0615.
HOGENOM	HOG000230945.
HOVERGEN	HBG053531.
InParanoid	P49585.
KO	K00968.
PhylomeDB	P49585.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00753; UER00739.
Gene expression databases
ArrayExpress	P49585.
Bgee	P49585.
CleanEx	HS_PCYT1A.
Genevestigator	P49585.
GermOnline	ENSG00000161217. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR004821. Cyt_trans-like. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF01467. CTP_transf_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00125. cyt_tran_rel. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00122. Choline.
GenomeRNAi	5130.
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

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

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.