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P49585 (PCY1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytosol 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Choline-phosphate cytidylyltransferase A
PRO_0000208453

Regions

Repeat319 – 32461
Repeat329 – 33352; approximate
Repeat343 – 34863
Nucleotide binding84 – 929CTP By similarity
Nucleotide binding168 – 1692CTP By similarity
Nucleotide binding196 – 2005CTP By similarity
Region228 – 28760Amphipathic Potential
Region256 – 288333 X 11 AA approximate tandem repeats
Region319 – 348303 X repeats

Sites

Binding site1221CTP By similarity
Binding site1221Substrate By similarity
Binding site1511Substrate By similarity
Binding site1731CTP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13 Ref.17
Modified residue81N6-acetyllysine Ref.13
Modified residue3151Phosphoserine Ref.12
Modified residue3191Phosphoserine Ref.12
Modified residue3211Phosphoserine By similarity
Modified residue3221Phosphoserine By similarity
Modified residue3231Phosphoserine By similarity
Modified residue3291Phosphoserine By similarity
Modified residue3311Phosphoserine By similarity
Modified residue3331Phosphoserine By similarity
Modified residue3431Phosphoserine Ref.10 Ref.12
Modified residue3471Phosphoserine Ref.10 Ref.12
Modified residue3521Phosphoserine Ref.10
Modified residue3621Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.16

Experimental info

Mutagenesis371C → S: Abolishes formation of the interchain disulfide that can be observed when the enzyme is treated with copper phenanthrolene (in vitro). Ref.7
Sequence conflict2511K → E in AAA72127. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49585 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 38CE9D5CF2E2AEE2

FASTA36741,731
        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 

« Hide

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] [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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"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-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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.
PIRS50145.
RefSeqNP_005008.2. NM_005017.2.
UniGeneHs.135997.
Hs.732774.

3D structure databases

ProteinModelPortalP49585.
SMRP49585. Positions 40-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111157. 6 interactions.
IntActP49585. 8 interactions.
STRING9606.ENSP00000292823.

Chemistry

DrugBankDB00122. Choline.

PTM databases

PhosphoSiteP49585.

Polymorphism databases

DMDM166214967.

Proteomic databases

PaxDbP49585.
PRIDEP49585.

Protocols and materials databases

DNASU5130.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292823; ENSP00000292823; ENSG00000161217.
ENST00000431016; ENSP00000394617; ENSG00000161217.
GeneID5130.
KEGGhsa:5130.
UCSCuc003fwg.3. human.

Organism-specific databases

CTD5130.
GeneCardsGC03M195941.
H-InvDBHIX0024337.
HGNCHGNC:8754. PCYT1A.
HPAHPA035428.
MIM123695. gene.
neXtProtNX_P49585.
PharmGKBPA33099.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000230945.
HOVERGENHBG053531.
InParanoidP49585.
KOK00968.
PhylomeDBP49585.
TreeFamTF106336.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00753; UER00739.

Gene expression databases

ArrayExpressP49585.
BgeeP49585.
CleanExHS_PCYT1A.
GenevestigatorP49585.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetSearch...

Other

GeneWikiPCYT1A.
GenomeRNAi5130.
NextBio19780.
PMAP-CutDBP49585.
PROP49585.
SOURCESearch...

Entry information

Entry namePCY1A_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM