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Protein

Phosphatidate cytidylyltransferase 1

Gene

CDS1

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

Functioni

Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells.

Catalytic activityi

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Cofactori

Mg2+By similarity

Pathway:iCDP-diacylglycerol biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 2, mitochondrial (GPAT2), Glycerol-3-phosphate acyltransferase 4 (AGPAT6), Glycerol-3-phosphate acyltransferase 3 (AGPAT9), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (AGPAT2), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (AGPAT4), 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (AGPAT3), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (AGPAT5), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (AGPAT1), Lysocardiolipin acyltransferase 1 (LCLAT1)
  3. Phosphatidate cytidylyltransferase 1 (CDS1), Phosphatidate cytidylyltransferase 2 (CDS2), Phosphatidate cytidylyltransferase, mitochondrial (TAMM41), Phosphatidate cytidylyltransferase (CDS1), Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • diacylglycerol cholinephosphotransferase activity Source: UniProtKB
  • phosphatidate cytidylyltransferase activity Source: UniProtKB

GO - Biological processi

  • CDP-choline pathway Source: GOC
  • CDP-diacylglycerol biosynthetic process Source: UniProtKB
  • glycerophospholipid biosynthetic process Source: Reactome
  • phosphatidylglycerol biosynthetic process Source: GO_Central
  • phosphatidylinositol biosynthetic process Source: UniProtKB
  • phospholipid metabolic process Source: Reactome
  • phototransduction Source: UniProtKB
  • signal transduction Source: UniProtKB
  • 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

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BRENDAi2.7.7.41. 2681.
ReactomeiREACT_121000. Synthesis of PI.
UniPathwayiUPA00557; UER00614.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate cytidylyltransferase 1 (EC:2.7.7.41)
Alternative name(s):
CDP-DAG synthase 1
CDP-DG synthase 1
CDP-diacylglycerol synthase 1
Short name:
CDS 1
CDP-diglyceride pyrophosphorylase 1
CDP-diglyceride synthase 1
CTP:phosphatidate cytidylyltransferase 1
Gene namesi
Name:CDS1
Synonyms:CDS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1800. CDS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei96 – 11621HelicalSequence AnalysisAdd
BLAST
Transmembranei149 – 16921HelicalSequence AnalysisAdd
BLAST
Transmembranei183 – 20321HelicalSequence AnalysisAdd
BLAST
Transmembranei230 – 25021HelicalSequence AnalysisAdd
BLAST
Transmembranei279 – 29921HelicalSequence AnalysisAdd
BLAST
Transmembranei357 – 37721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26346.

Polymorphism and mutation databases

BioMutaiCDS1.
DMDMi3123204.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Phosphatidate cytidylyltransferase 1PRO_0000090713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92903.
PaxDbiQ92903.
PRIDEiQ92903.

PTM databases

PhosphoSiteiQ92903.

Expressioni

Tissue specificityi

Expressed in adult tissues such as placenta, brain, small intestine, ovary, testis and prostate. Highly expressed in fetal kidney, lung and brain. Lower level in fetal liver.

Gene expression databases

BgeeiQ92903.
CleanExiHS_CDS1.
ExpressionAtlasiQ92903. baseline and differential.
GenevisibleiQ92903. HS.

Organism-specific databases

HPAiHPA036187.

Interactioni

Subunit structurei

Interacts with FOS; this interaction may enhance catalytic activity.By similarity

Protein-protein interaction databases

BioGridi107471. 4 interactions.
STRINGi9606.ENSP00000295887.

Structurei

3D structure databases

ProteinModelPortaliQ92903.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
HOGENOMiHOG000209582.
HOVERGENiHBG002485.
InParanoidiQ92903.
KOiK00981.
OMAiGHYLRNQ.
OrthoDBiEOG7M98G5.
PhylomeDBiQ92903.
TreeFamiTF313464.

Family and domain databases

InterProiIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
PROSITEiPS01315. CDS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLELRHRGSC PGPREAVSPP HREGEAAGGD HETESTSDKE TDIDDRYGDL
60 70 80 90 100
DSRTDSDIPE IPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF
110 120 130 140 150
FLIIYMGSFM LMLLVLGIQV KCFHEIITIG YRVYHSYDLP WFRTLSWYFL
160 170 180 190 200
LCVNYFFYGE TVADYFATFV QREEQLQFLI RYHRFISFAL YLAGFCMFVL
210 220 230 240 250
SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI WFLVPISSVI
260 270 280 290 300
CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVVF GFIAAYVLSK
310 320 330 340 350
YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ TYSLPPFLKA VLRQERVSLY
360 370 380 390 400
PFQIHSIALS TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF
410 420 430 440 450
DCQYLMATFV HVYITSFIRG PNPSKVLQQL LVLQPEQQLN IYKTLKTHLI
460
EKGILQPTLK V
Length:461
Mass (Da):53,304
Last modified:July 15, 1998 - v2
Checksum:iE9D761BA285A5AB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti444 – 46118TLKTH…PTLKV → P in AAC50735 (PubMed:8863531).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991L → F.
Corresponds to variant rs36068434 [ dbSNP | Ensembl ].
VAR_048736
Natural varianti204 – 2041K → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_036129

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65887 mRNA. Translation: AAC50735.1.
U60808 mRNA. Translation: AAC51184.1.
AK314245 mRNA. Translation: BAG36912.1.
CH471057 Genomic DNA. Translation: EAX05950.1.
BC074833 mRNA. Translation: AAH74833.1.
BC074881 mRNA. Translation: AAH74881.1.
CCDSiCCDS3608.1.
RefSeqiNP_001254.2. NM_001263.3.
UniGeneiHs.654899.
Hs.708641.

Genome annotation databases

EnsembliENST00000295887; ENSP00000295887; ENSG00000163624.
GeneIDi1040.
KEGGihsa:1040.
UCSCiuc011ccv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65887 mRNA. Translation: AAC50735.1.
U60808 mRNA. Translation: AAC51184.1.
AK314245 mRNA. Translation: BAG36912.1.
CH471057 Genomic DNA. Translation: EAX05950.1.
BC074833 mRNA. Translation: AAH74833.1.
BC074881 mRNA. Translation: AAH74881.1.
CCDSiCCDS3608.1.
RefSeqiNP_001254.2. NM_001263.3.
UniGeneiHs.654899.
Hs.708641.

3D structure databases

ProteinModelPortaliQ92903.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107471. 4 interactions.
STRINGi9606.ENSP00000295887.

PTM databases

PhosphoSiteiQ92903.

Polymorphism and mutation databases

BioMutaiCDS1.
DMDMi3123204.

Proteomic databases

MaxQBiQ92903.
PaxDbiQ92903.
PRIDEiQ92903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295887; ENSP00000295887; ENSG00000163624.
GeneIDi1040.
KEGGihsa:1040.
UCSCiuc011ccv.2. human.

Organism-specific databases

CTDi1040.
GeneCardsiGC04P085428.
HGNCiHGNC:1800. CDS1.
HPAiHPA036187.
MIMi603548. gene.
neXtProtiNX_Q92903.
PharmGKBiPA26346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
HOGENOMiHOG000209582.
HOVERGENiHBG002485.
InParanoidiQ92903.
KOiK00981.
OMAiGHYLRNQ.
OrthoDBiEOG7M98G5.
PhylomeDBiQ92903.
TreeFamiTF313464.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00614.
BRENDAi2.7.7.41. 2681.
ReactomeiREACT_121000. Synthesis of PI.

Miscellaneous databases

ChiTaRSiCDS1. human.
GeneWikiiCDS1_(gene).
GenomeRNAii1040.
NextBioi4365.
PROiQ92903.
SOURCEiSearch...

Gene expression databases

BgeeiQ92903.
CleanExiHS_CDS1.
ExpressionAtlasiQ92903. baseline and differential.
GenevisibleiQ92903. HS.

Family and domain databases

InterProiIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
PROSITEiPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of CDP-diacylglycerol synthase from a human neuronal cell line."
    Heacock A.M., Uhler M.D., Agranoff B.W.
    J. Neurochem. 67:2200-2203(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Neuron.
  2. "Isolation and expression of an isoform of human CDP-diacylglycerol synthase cDNA."
    Weeks R., Dowhan W., Shen H., Balantac N., Meengs B., Nudelman E., Leung D.W.
    DNA Cell Biol. 16:281-289(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leukocyte and Placenta.
  3. "The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content."
    Lykidis A., Jackson P.D., Rock C.O., Jackowski S.
    J. Biol. Chem. 272:33402-33409(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  4. "Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes."
    Halford S., Dulai K.S., Daw S.C.M., Fitzgibbon J., Hunt D.M.
    Genomics 54:140-144(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  5. "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].
    Tissue: Ovary.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-204.

Entry informationi

Entry nameiCDS1_HUMAN
AccessioniPrimary (citable) accession number: Q92903
Secondary accession number(s): B2RAL5, O00163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: July 22, 2015
This is version 126 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.