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Protein

Ethanolamine-phosphate cytidylyltransferase

Gene

PCYT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine.

Catalytic activityi

CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei259 – 2591CTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 2222CTP
Nucleotide bindingi229 – 2324CTP
Nucleotide bindingi307 – 3104CTP
Nucleotide bindingi336 – 3405CTP

GO - Molecular functioni

  1. ethanolamine-phosphate cytidylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. glycerophospholipid biosynthetic process Source: Reactome
  2. phosphatidylethanolamine biosynthetic process Source: Reactome
  3. phospholipid biosynthetic process Source: UniProtKB
  4. phospholipid metabolic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_120919. Synthesis of PE.
UniPathwayiUPA00558; UER00742.

Names & Taxonomyi

Protein namesi
Recommended name:
Ethanolamine-phosphate cytidylyltransferase (EC:2.7.7.14)
Alternative name(s):
CTP:phosphoethanolamine cytidylyltransferase
Phosphorylethanolamine transferase
Gene namesi
Name:PCYT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:8756. PCYT2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33101.

Chemistry

DrugBankiDB00709. Lamivudine.

Polymorphism and mutation databases

DMDMi12585314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Ethanolamine-phosphate cytidylyltransferasePRO_0000208461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei338 – 3381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99447.
PaxDbiQ99447.
PRIDEiQ99447.

2D gel databases

UCD-2DPAGEQ99447.

PTM databases

PhosphoSiteiQ99447.

Expressioni

Tissue specificityi

Strongest expression in liver, heart, and skeletal muscle.

Gene expression databases

BgeeiQ99447.
CleanExiHS_PCYT2.
ExpressionAtlasiQ99447. baseline and differential.
GenevestigatoriQ99447.

Organism-specific databases

HPAiHPA023033.
HPA023034.

Interactioni

Protein-protein interaction databases

BioGridi111791. 21 interactions.
IntActiQ99447. 7 interactions.
MINTiMINT-3059003.
STRINGi9606.ENSP00000331719.

Structurei

Secondary structure

1
389
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 296Combined sources
Helixi36 – 4712Combined sources
Beta strandi49 – 568Combined sources
Helixi59 – 657Combined sources
Helixi73 – 8210Combined sources
Beta strandi88 – 914Combined sources
Helixi99 – 1046Combined sources
Beta strandi108 – 1125Combined sources
Helixi127 – 1315Combined sources
Beta strandi135 – 1373Combined sources
Helixi146 – 1549Combined sources
Helixi197 – 2037Combined sources
Beta strandi214 – 2207Combined sources
Helixi227 – 23711Combined sources
Beta strandi240 – 25011Combined sources
Helixi252 – 2598Combined sources
Helixi268 – 2769Combined sources
Beta strandi283 – 2886Combined sources
Helixi294 – 2996Combined sources
Beta strandi303 – 3075Combined sources
Helixi323 – 3286Combined sources
Beta strandi331 – 3333Combined sources
Helixi342 – 3509Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ELBX-ray2.00A18-356[»]
SMRiQ99447. Positions 19-351.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99447.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

eggNOGiCOG0615.
GeneTreeiENSGT00550000075065.
HOGENOMiHOG000187618.
HOVERGENiHBG000865.
InParanoidiQ99447.
KOiK00967.
OMAiSEGSSQC.
OrthoDBiEOG7CRTPS.
PhylomeDBiQ99447.
TreeFamiTF106337.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99447-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MIRNGRGAAG GAEQPGPGGR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD
60 70 80 90 100
YLIVGVHTDE EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE
110 120 130 140 150
TLDKYNCDFC VHGNDITLTV DGRDTYEEVK QAGRYRECKR TQGVSTTDLV
160 170 180 190 200
GRMLLVTKAH HSSQEMSSEY REYADSFGKC PGGRNPWTGV SQFLQTSQKI
210 220 230 240 250
IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVHRLA ERPYIIAGLH
260 270 280 290 300
FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY AVTAELLSHF
310 320 330 340 350
KVDLVCHGKT EIIPDRDGSD PYQEPKRRGI FRQIDSGSNL TTDLIVQRII
360 370 380
TNRLEYEARN QKKEAKELAF LEAARQQAAQ PLGERDGDF
Length:389
Mass (Da):43,835
Last modified:May 1, 1997 - v1
Checksum:i13FE8EAEB7FFAF7F
GO
Isoform 2 (identifier: Q99447-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Show »
Length:311
Mass (Da):35,200
Checksum:iAE4851C05A3B403C
GO
Isoform 3 (identifier: Q99447-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-179: K → KPPHPIPAGDILSSEGCSQ

Note: No experimental confirmation available. Gene prediction based on cDNA data.

Show »
Length:407
Mass (Da):45,622
Checksum:i8BA20CC46F0F06C9
GO
Isoform 4 (identifier: Q99447-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: No experimental confirmation available.

Show »
Length:357
Mass (Da):40,520
Checksum:iF246E5C6A87F55CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441Y → H in AAH10075 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7878Missing in isoform 2. 1 PublicationVSP_045131Add
BLAST
Alternative sequencei1 – 3232Missing in isoform 4. 1 PublicationVSP_054615Add
BLAST
Alternative sequencei179 – 1791K → KPPHPIPAGDILSSEGCSQ in isoform 3. CuratedVSP_046844

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84307 mRNA. Translation: BAA12311.1.
CR456779 mRNA. Translation: CAG33060.1.
AK301723 mRNA. Translation: BAH13541.1.
AK316385 mRNA. Translation: BAH14756.1.
AC145207 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89705.1.
BC000351 mRNA. Translation: AAH00351.1.
BC010075 mRNA. Translation: AAH10075.1.
CCDSiCCDS11791.1. [Q99447-1]
CCDS54178.1. [Q99447-3]
CCDS58610.1. [Q99447-2]
CCDS62364.1. [Q99447-4]
RefSeqiNP_001171846.1. NM_001184917.2. [Q99447-3]
NP_001243364.1. NM_001256435.2. [Q99447-2]
NP_001269132.1. NM_001282203.1. [Q99447-2]
NP_001269133.1. NM_001282204.1. [Q99447-4]
NP_002852.1. NM_002861.4. [Q99447-1]
UniGeneiHs.569843.

Genome annotation databases

EnsembliENST00000331285; ENSP00000331719; ENSG00000185813. [Q99447-2]
ENST00000538721; ENSP00000442050; ENSG00000185813. [Q99447-3]
ENST00000538936; ENSP00000439245; ENSG00000185813. [Q99447-1]
ENST00000570388; ENSP00000458330; ENSG00000185813. [Q99447-2]
ENST00000570391; ENSP00000461190; ENSG00000185813. [Q99447-4]
GeneIDi5833.
KEGGihsa:5833.
UCSCiuc002kce.2. human. [Q99447-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84307 mRNA. Translation: BAA12311.1.
CR456779 mRNA. Translation: CAG33060.1.
AK301723 mRNA. Translation: BAH13541.1.
AK316385 mRNA. Translation: BAH14756.1.
AC145207 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89705.1.
BC000351 mRNA. Translation: AAH00351.1.
BC010075 mRNA. Translation: AAH10075.1.
CCDSiCCDS11791.1. [Q99447-1]
CCDS54178.1. [Q99447-3]
CCDS58610.1. [Q99447-2]
CCDS62364.1. [Q99447-4]
RefSeqiNP_001171846.1. NM_001184917.2. [Q99447-3]
NP_001243364.1. NM_001256435.2. [Q99447-2]
NP_001269132.1. NM_001282203.1. [Q99447-2]
NP_001269133.1. NM_001282204.1. [Q99447-4]
NP_002852.1. NM_002861.4. [Q99447-1]
UniGeneiHs.569843.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ELBX-ray2.00A18-356[»]
SMRiQ99447. Positions 19-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111791. 21 interactions.
IntActiQ99447. 7 interactions.
MINTiMINT-3059003.
STRINGi9606.ENSP00000331719.

Chemistry

DrugBankiDB00709. Lamivudine.

PTM databases

PhosphoSiteiQ99447.

Polymorphism and mutation databases

DMDMi12585314.

2D gel databases

UCD-2DPAGEQ99447.

Proteomic databases

MaxQBiQ99447.
PaxDbiQ99447.
PRIDEiQ99447.

Protocols and materials databases

DNASUi5833.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331285; ENSP00000331719; ENSG00000185813. [Q99447-2]
ENST00000538721; ENSP00000442050; ENSG00000185813. [Q99447-3]
ENST00000538936; ENSP00000439245; ENSG00000185813. [Q99447-1]
ENST00000570388; ENSP00000458330; ENSG00000185813. [Q99447-2]
ENST00000570391; ENSP00000461190; ENSG00000185813. [Q99447-4]
GeneIDi5833.
KEGGihsa:5833.
UCSCiuc002kce.2. human. [Q99447-1]

Organism-specific databases

CTDi5833.
GeneCardsiGC17M079862.
HGNCiHGNC:8756. PCYT2.
HPAiHPA023033.
HPA023034.
MIMi602679. gene.
neXtProtiNX_Q99447.
PharmGKBiPA33101.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0615.
GeneTreeiENSGT00550000075065.
HOGENOMiHOG000187618.
HOVERGENiHBG000865.
InParanoidiQ99447.
KOiK00967.
OMAiSEGSSQC.
OrthoDBiEOG7CRTPS.
PhylomeDBiQ99447.
TreeFamiTF106337.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00742.
ReactomeiREACT_120919. Synthesis of PE.

Miscellaneous databases

EvolutionaryTraceiQ99447.
GenomeRNAii5833.
NextBioi22732.
PROiQ99447.
SOURCEiSearch...

Gene expression databases

BgeeiQ99447.
CleanExiHS_PCYT2.
ExpressionAtlasiQ99447. baseline and differential.
GenevestigatoriQ99447.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant."
    Nakashima A., Hosaka K., Nikawa J.
    J. Biol. Chem. 272:9567-9572(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
    Tissue: Testis.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Muscle.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Human CTP:phosphoethanolamine cytidylyltransferase."
    Structural genomics consortium (SGC)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-356 IN COMPLEX WITH CYTIDINE-5'-MONOPHOSPHATE.

Entry informationi

Entry nameiPCY2_HUMAN
AccessioniPrimary (citable) accession number: Q99447
Secondary accession number(s): B7Z7A5
, B7ZAS0, F5H8B1, Q6IBM3, Q96G08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1997
Last modified: April 1, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.