U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

PCYT2 phosphate cytidylyltransferase 2, ethanolamine [ Homo sapiens (human) ]

Gene ID: 5833, updated on 3-Apr-2024

Summary

Go to the top of the page Help
Official Symbol
PCYT2provided by HGNC
Official Full Name
phosphate cytidylyltransferase 2, ethanolamineprovided by HGNC
Primary source
HGNC:HGNC:8756
See related
Ensembl:ENSG00000185813 MIM:602679; AllianceGenome:HGNC:8756
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
ET; SPG82
Summary
This gene encodes an enzyme that catalyzes the formation of CDP-ethanolamine from CTP and phosphoethanolamine in the Kennedy pathway of phospholipid synthesis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2010]
Expression
Broad expression in testis (RPKM 31.9), duodenum (RPKM 10.8) and 22 other tissues See more
Orthologs
mouse all
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Location:
17q25.3
Exon count:
15
Annotation release Status Assembly Chr Location
RS_2023_10 current GRCh38.p14 (GCF_000001405.40) 17 NC_000017.11 (81900958..81911399, complement)
RS_2023_10 current T2T-CHM13v2.0 (GCF_009914755.1) 17 NC_060941.1 (82768118..82778559, complement)
105.20220307 previous assembly GRCh37.p13 (GCF_000001405.25) 17 NC_000017.10 (79858834..79869275, complement)

Chromosome 17 - NC_000017.11Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC124904086 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79825239-79825867 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79825868-79826497 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79826498-79827126 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9158 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12981 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9159 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9160 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12982 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12983 Neighboring gene Rho GDP dissociation inhibitor alpha Neighboring gene CDK7 strongly-dependent group 2 enhancer GRCh37_chr17:79846281-79847480 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9161 Neighboring gene ReSE screen-validated silencer GRCh37_chr17:79850899-79851114 Neighboring gene Aly/REF export factor Neighboring gene anaphase promoting complex subunit 11 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9162 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9163 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9164 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9165 Neighboring gene neuropeptide B Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9166 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9167 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79875237-79876133 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12984 Neighboring gene sirtuin 7 Neighboring gene MED14-independent group 3 enhancer GRCh37_chr17:79880785-79881984 Neighboring gene MAF bZIP transcription factor G Neighboring gene MAFG antisense RNA 1

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help
  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2. Osawa T, et al. Cell Rep, 2019 Oct 1. PMID 31577958
  2. Breast cancer cells adapt to metabolic stress by increasing ethanolamine phospholipid synthesis and CTP:ethanolaminephosphate cytidylyltransferase-Pcyt2 activity. Zhu L, et al. Biochem Cell Biol, 2012 Apr. PMID 22339418
  3. Metabolic and molecular aspects of ethanolamine phospholipid biosynthesis: the role of CTP:phosphoethanolamine cytidylyltransferase (Pcyt2). Bakovic M, et al. Biochem Cell Biol, 2007 Jun. PMID 17612623
  4. Characterization of transcription factors and cis-acting elements that regulate human CTP: phosphoethanolamine cytidylyltransferase (Pcyt2). Johnson CM, et al. Biochim Biophys Acta, 2005 Aug 15. PMID 16023412
  5. CTP:phosphoethanolamine cytidylyltransferase. Bladergroen BA, et al. Biochim Biophys Acta, 1997 Sep 4. PMID 9370320

See all (37) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2.
    Title: Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2.
  2. our data establish PCYT2 as a disease gene for a new complex hereditary spastic paraplegia and confirm that etherlipid homeostasis is important for the development and function of the brain
    Title: Mutations in PCYT2 disrupt etherlipid biosynthesis and cause a complex hereditary spastic paraplegia.
  3. These results suggest that the N-terminal CT domain of hECT contributes to its catalytic reaction, but C-terminal CT domain does not.
    Title: Human CTP:phosphoethanolamine cytidylyltransferase: enzymatic properties and unequal catalytic roles of CTP-binding motifs in two cytidylyltransferase domains.
  4. differences in phosphorylation between Pcyt2 isoforms
    Title: Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation.
  5. Pcyt2 expression is responsive to tumor nutritional micro-environment, up-regulated in response to metabolic stress under conditions of serum deprivation.
    Title: Breast cancer cells adapt to metabolic stress by increasing ethanolamine phospholipid synthesis and CTP:ethanolaminephosphate cytidylyltransferase-Pcyt2 activity.
  6. EGR1 is an important transcriptional stimulator of the human PCYT2 and that conditions that modify EGR1 also affect the function of ECT and consequently PE synthesis
    Title: Stimulation of the human CTP:phosphoethanolamine cytidylyltransferase gene by early growth response protein 1.
  7. The Pcyt2 promoter is driven by a functional CAAT box (-90/-73) and by negative (-385/-255) and positive regulatory elements (-255/-153) in the upstream regions.
    Title: Characterization of transcription factors and cis-acting elements that regulate human CTP: phosphoethanolamine cytidylyltransferase (Pcyt2).
Submit: New GeneRIF Correction

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description Tests
Spastic paraplegia 82, autosomal recessive
MedGen: C5394037 OMIM: 618770 GeneReviews: Not available
Compare labs

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Genotypes

HIV-1 interactions

Go to the top of the page Help

Replication interactions

Interaction Pubs
Knockdown of phosphate cytidylyltransferase 2, ethanolamine (PCYT2) by siRNA inhibits HIV-1 replication in HeLa P4/R5 cells PubMed

Go to the HIV-1, Human Interaction Database

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables ethanolamine-phosphate cytidylyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ethanolamine-phosphate cytidylyltransferase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables ethanolamine-phosphate cytidylyltransferase activity TAS
Traceable Author Statement
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in phosphatidylethanolamine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in phosphatidylethanolamine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in phosphatidylethanolamine biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in phospholipid biosynthetic process TAS
Traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cellular_component ND
No biological Data available
more info
  
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum membrane TAS
Traceable Author Statement
more info
  

General protein information

Go to the top of the page Help
Preferred Names
ethanolamine-phosphate cytidylyltransferase
Names
CTP:phosphoethanolamine cytidylyltransferase
phosphorylethanolamine transferase
NP_001171846.1
NP_001243362.1
NP_001243363.1
NP_001243364.1
NP_001269132.1
NP_001269133.1
NP_001317447.1
NP_002852.1
XP_005256443.1
XP_005256444.1
XP_006722350.1
XP_054172799.1
XP_054172800.1
XP_054172801.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001184917.3 → NP_001171846.1  ethanolamine-phosphate cytidylyltransferase isoform 1

    See identical proteins and their annotated locations for NP_001171846.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (1).
    Source sequence(s)
    AC145207, AK315777, CA411562
    Consensus CDS
    CCDS54178.1
    UniProtKB/TrEMBL
    B7Z4W6
    Related
    ENSP00000442050.2, ENST00000538721.6
    Conserved Domains (1) summary
    cl28626
    Location:14 → 390
    PLN02406; ethanolamine-phosphate cytidylyltransferase

  2. NM_001256433.3 → NP_001243362.1  ethanolamine-phosphate cytidylyltransferase isoform 5

    Status: REVIEWED

    Description
    Transcript Variant: This variant (7) lacks an alternate in-frame exon in both the 5' and central coding regions, compared to variant 1, resulting in an isoform (5) that is shorter than isoform 1.
    Source sequence(s)
    AC145207, BX419403, CA411562, HY042603
    UniProtKB/TrEMBL
    I3L1L9
    Related
    ENSP00000458931.1, ENST00000576343.5
    Conserved Domains (3) summary
    PTZ00308
    Location:14 → 318
    PTZ00308; ethanolamine-phosphate cytidylyltransferase; Provisional
    cd02173
    Location:158 → 310
    ECT; CTP:phosphoethanolamine cytidylyltransferase (ECT)
    cl00015
    Location:21 → 109
    nt_trans; nucleotidyl transferase superfamily

  3. NM_001256434.3 → NP_001243363.1  ethanolamine-phosphate cytidylyltransferase isoform 3

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) uses an alternate splice site in its 5' coding region and uses an alternate downstream start codon, compared to variant 1. The encoded isoform (3) has a distinct and shorter N-terminus, compared to isoform 1.
    Source sequence(s)
    AC145207, AY251539, CA411562, HY042603
    UniProtKB/TrEMBL
    B3KSC8
    Conserved Domains (2) summary
    cd02173
    Location:171 → 323
    ECT; CTP:phosphoethanolamine cytidylyltransferase (ECT)
    cl00015
    Location:2 → 104
    nt_trans; nucleotidyl transferase superfamily

  4. NM_001256435.3 → NP_001243364.1  ethanolamine-phosphate cytidylyltransferase isoform 4

    See identical proteins and their annotated locations for NP_001243364.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (4) uses an alternate splice site in its 5' UTR, uses a downstream in-frame start codon, and lacks an alternate in-frame exon in the central coding region, compared to variant 1. The encoded isoform (4) is shorter at the N-terminus, compared to isoform 1. Both variants 4 and 5 encode the same isoform (4).
    Source sequence(s)
    AC145207, AK301723, CA411562, HY042603
    Consensus CDS
    CCDS58610.1
    UniProtKB/TrEMBL
    B3KSC8
    Related
    ENSP00000458330.1, ENST00000570388.5
    Conserved Domains (1) summary
    PTZ00308
    Location:2 → 294
    PTZ00308; ethanolamine-phosphate cytidylyltransferase; Provisional

  5. NM_001282203.2 → NP_001269132.1  ethanolamine-phosphate cytidylyltransferase isoform 4

    See identical proteins and their annotated locations for NP_001269132.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (5) differs in the 5' UTR and has many differences in the coding region but maintains the reading frame, compared to variant 1. The encoded isoform (4) is shorter at the N-terminus, compared to isoform 1. Both variants 4 and 5 encode the same isoform (4).
    Source sequence(s)
    AC145207, AK093328, CA411562
    Consensus CDS
    CCDS58610.1
    UniProtKB/TrEMBL
    B3KSC8
    Related
    ENSP00000331719.3, ENST00000331285.7
    Conserved Domains (1) summary
    PTZ00308
    Location:2 → 294
    PTZ00308; ethanolamine-phosphate cytidylyltransferase; Provisional

  6. NM_001282204.2 → NP_001269133.1  ethanolamine-phosphate cytidylyltransferase isoform 6

    See identical proteins and their annotated locations for NP_001269133.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (6) differs in the 5' UTR and has many differences in the coding region but maintains the reading frame, compared to variant 1. The encoded isoform (6) is shorter at the N-terminus, compared to isoform 1.
    Source sequence(s)
    AC145207, AK297996, CA411562, HY031003
    Consensus CDS
    CCDS62364.1
    UniProtKB/TrEMBL
    B7Z4W6
    Related
    ENSP00000461190.1, ENST00000570391.5
    Conserved Domains (1) summary
    cl28626
    Location:1 → 340
    PLN02406; ethanolamine-phosphate cytidylyltransferase

  7. NM_001330518.2 → NP_001317447.1  ethanolamine-phosphate cytidylyltransferase isoform 7

    Status: REVIEWED

    Source sequence(s)
    AC145207, BC073815
    Consensus CDS
    CCDS82220.1
    UniProtKB/TrEMBL
    B7Z4W6, I3L1R7
    Related
    ENSP00000459044.1, ENST00000571105.5
    Conserved Domains (1) summary
    cl28626
    Location:14 → 350
    PLN02406; ethanolamine-phosphate cytidylyltransferase

  8. NM_002861.5 → NP_002852.1  ethanolamine-phosphate cytidylyltransferase isoform 2

    See identical proteins and their annotated locations for NP_002852.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) lacks an alternate in-frame exon in the central coding region, compared to variant 1, resulting in an isoform (2) that is shorter than isoform 1.
    Source sequence(s)
    AC145207, BC010075, CA411562
    Consensus CDS
    CCDS11791.1
    UniProtKB/Swiss-Prot
    B7Z7A5, B7ZAS0, F5H8B1, Q6IBM3, Q96G08, Q99447
    UniProtKB/TrEMBL
    B7Z4W6
    Related
    ENSP00000439245.3, ENST00000538936.7
    Conserved Domains (1) summary
    cl28626
    Location:14 → 372
    PLN02406; ethanolamine-phosphate cytidylyltransferase

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000017.11 Reference GRCh38.p14 Primary Assembly

    Range
    81900958..81911399 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_006722287.5 → XP_006722350.1  ethanolamine-phosphate cytidylyltransferase isoform X1

    UniProtKB/TrEMBL
    B7Z4W6
    Conserved Domains (3) summary
    PTZ00308
    Location:14 → 368
    PTZ00308; ethanolamine-phosphate cytidylyltransferase; Provisional
    cd02173
    Location:230 → 360
    ECT; CTP:phosphoethanolamine cytidylyltransferase (ECT)
    cd02174
    Location:21 → 163
    CCT; CTP:phosphocholine cytidylyltransferase

  2. XM_005256387.4 → XP_005256444.1  ethanolamine-phosphate cytidylyltransferase isoform X2

    See identical proteins and their annotated locations for XP_005256444.1

    UniProtKB/TrEMBL
    B7Z4W6
    Conserved Domains (1) summary
    PTZ00308
    Location:1 → 358
    PTZ00308; ethanolamine-phosphate cytidylyltransferase; Provisional

  3. XM_005256386.5 → XP_005256443.1  ethanolamine-phosphate cytidylyltransferase isoform X2

    See identical proteins and their annotated locations for XP_005256443.1

    UniProtKB/TrEMBL
    B7Z4W6
    Conserved Domains (1) summary
    PTZ00308
    Location:1 → 358
    PTZ00308; ethanolamine-phosphate cytidylyltransferase; Provisional

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060941.1 Alternate T2T-CHM13v2.0

    Range
    82768118..82778559 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054316824.1 → XP_054172799.1  ethanolamine-phosphate cytidylyltransferase isoform X1

  2. XM_054316825.1 → XP_054172800.1  ethanolamine-phosphate cytidylyltransferase isoform X2

  3. XM_054316826.1 → XP_054172801.1  ethanolamine-phosphate cytidylyltransferase isoform X2

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q99447.1 GenPept UniProtKB/Swiss-Prot:Q99447

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Chemical Information
Molecular Biology Databases
Research Materials
Tools
Miscellaneous