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UniProtKB/Swiss-Prot entry O95674


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDS2_HUMAN
Primary accession number O95674
Secondary accession numbers Q5TDY2 Q5TDY3 Q5TDY4 Q5TDY5 Q9BYK5 Q9NTT2
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 67)
Name and origin of the protein
Protein name Phosphatidate cytidylyltransferase 2
Synonyms EC 2.7.7.41
CDP-diglyceride pyrophosphorylase 2
CDP-diglyceride synthetase 2
CDP-diacylglycerol synthase 2
CDS 2
CTP:phosphatidate cytidylyltransferase 2
CDP-DG synthetase 2
CDP-DAG synthase 2
Gene name
Name: CDS2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1006/geno.1998.5610; PubMed=9889000 [NCBI, ExPASy, EBI, Israel, Japan]
Volta M., Bulfone A., Gattuso C., Rossi E., Mariani M., Consalez G.G., Zuffardi O., Ballabio A., Banfi S., Franco B.;
"Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene.";
Genomics 55:68-77(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-445 (ISOFORM 1).
TISSUE=Retina;
DOI=10.1006/geno.1998.5547; PubMed=9806839 [NCBI, ExPASy, EBI, Israel, Japan]
Halford S., Dulai K.S., Daw S.C.M., Fitzgibbon J., Hunt D.M.;
"Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes.";
Genomics 54:140-144(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-33, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y16521; CAA76270.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121755; CAI22376.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121924; CAI22376.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121755; CAI22378.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121924; CAI22378.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121924; CAI22631.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121755; CAI22631.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121924; CAI22633.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121755; CAI22633.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025751; AAH25751.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF069532; AAC78305.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003809.1; -.
UniGene Hs.472027
3D structure databases
ModBase O95674.
PTM databases
PhosphoSite O95674; -.
Organism-specific databases
HGNC HGNC:1801; CDS2.
GenAtlas CDS2.
HPA HPA019698; -.
MIM 603549; gene. [NCBI / EBI]
PharmGKB PA26347; -.
GeneCards O95674.
Gene expression databases
ArrayExpress O95674; -.
CleanEx HS_CDS2; -.
GermOnline ENSG00000101290; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005743; Cellular component: mitochondrial inner membrane (non-traceable author statement from UniProtKB).
GO:0004605; Molecular function: phosphatidate cytidylyltransferase activity (non-traceable author statement from UniProtKB).
GO:0008654; Biological process: phospholipid biosynthetic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000374; PC_trans.
IPR016720; PC_Trfase_euk.
Graphical view of domain structure.
Pfam PF01148; CTP_transf_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF018269; PC_trans_euk; 1.
PROSITE PS01315; CDS; 1.
ProtoNet O95674.
Genome annotation databases
Ensembl ENSG00000101290; Homo sapiens. [Contig view]
GeneID 8760; -.
KEGG hsa:8760; -.
NMPDR fig|9606.3.peg.19834; -.
Phylogenomic databases
HOVERGEN O95674; -.
Other
NextBio 32860; -.
SOURCE CDS2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotidyltransferase; Phospholipid biosynthesis; Phosphoprotein; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   445  445     Phosphatidate cytidylyltransferase 2. PRO_0000090716
TRANSMEM   79    99  21     Potential. 
TRANSMEM   132   152  21     Potential. 
TRANSMEM   166   186  21     Potential. 
TRANSMEM   213   233  21     Potential. 
TRANSMEM   262   282  21     Potential. 
TRANSMEM   340   360  21     Potential. 
MOD_RES   21    21        Phosphoserine. 
MOD_RES   23    23        Phosphoserine. 
MOD_RES   31    31        Phosphothreonine (By similarity). 
MOD_RES   33    33        Phosphoserine. 
MOD_RES   47    47        Phosphoserine (By similarity). 
VAR_SEQ   1    55        Missing (in isoform 2). VSP_015477
VAR_SEQ   56    64        NRALSNLSS -> MSRLRHPRT (in isoform 2). VSP_015480
VAR_SEQ   306   445        Missing (in isoform 2). VSP_015482
Sequence information
Length: 445 AA [This is the length of the unprocessed precursor] Molecular weight: 51418 Da [This is the MW of the unprocessed precursor] CRC64: 7DAD6A3C1D5587D6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTELRQRVAH EPVAPPEDKE SESEAKVDGE TASDSESRAE SAPLPVSADD TPEVLNRALS 

        70         80         90        100        110        120 
NLSSRWKNWW VRGILTLAMI AFFFIIIYLG PMVLMIIVMC VQIKCFHEII TIGYNVYHSY 

       130        140        150        160        170        180 
DLPWFRTLSW YFLLCVNYFF YGETVTDYFF TLVQREEPLR ILSKYHRFIS FTLYLIGFCM 

       190        200        210        220        230        240 
FVLSLVKKHY RLQFYMFGWT HVTLLIVVTQ SHLVIHNLFE GMIWFIVPIS CVICNDIMAY 

       250        260        270        280        290        300 
MFGFFFGRTP LIKLSPKKTW EGFIGGFFAT VVFGLLLSYV MSGYRCFVCP VEYNNDTNSF 

       310        320        330        340        350        360 
TVDCEPSDLF RLQEYNIPGV IQSVIGWKTV RMYPFQIHSI ALSTFASLIG PFGGFFASGF 

       370        380        390        400        410        420 
KRAFKIKDFA NTIPGHGGIM DRFDCQYLMA TFVNVYIASF IRGPNPSKLI QQFLTLRPDQ 

       430        440 
QLHIFNTLRS HLIDKGMLTS TTEDE 

O95674 in FASTA format

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View entry in raw text format (no links)
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