O95674 (CDS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidate cytidylyltransferase 2
EC=2.7.7.41

Alternative name(s):
CDP-DAG synthase 2
CDP-DG synthase 2
CDP-diacylglycerol synthase 2
Short name=CDS 2
CDP-diglyceride pyrophosphorylase 2
CDP-diglyceride synthase 2
CTP:phosphatidate cytidylyltransferase 2

Gene names

Name:

CDS2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin.
Catalytic activity	CTP + phosphatidate = diphosphate + CDP-diacylglycerol.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side Potential.
Tissue specificity	Widely expressed. Expressed in heart, brain and retina, and to a lesser extent in placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.1
Developmental stage	No expression detected at E10.5 in the developing brain. At E12.5 expression is detected in the developing sentral nervous system and peripheral nervous system. At E17.5 high levels of expression are detected in a number of sites, including the dorsal root ganglia of the peripheral nervous system and the ganglion cell layer of the neural retina in the developing eye. At this stage expression in the brain is restricted to the ventricular zone of the telencephalon, in particular in the basal ganglia and the cerebral cortex. Ref.1
Sequence similarities	Belongs to the CDS family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Non-traceable author statement. Source: UniProtKB
Cellular component	integral to membrane Non-traceable author statement. Source: UniProtKB mitochondrial inner membrane Non-traceable author statement. Source: UniProtKB
Molecular function	phosphatidate cytidylyltransferase activity Non-traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95674-1)

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.

Isoform 2 (identifier: O95674-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
     56-64: NRALSNLSS → MSRLRHPRT
     306-445: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Phosphatidate cytidylyltransferase 2		PRO_0000090716
Regions
	Transmembrane	79 – 99	21	Helical; Potential
	Transmembrane	132 – 152	21	Helical; Potential
	Transmembrane	166 – 186	21	Helical; Potential
	Transmembrane	213 – 233	21	Helical; Potential
	Transmembrane	262 – 282	21	Helical; Potential
	Transmembrane	340 – 360	21	Helical; Potential
Amino acid modifications
	Modified residue	21	1	Phosphoserine Ref.7 Ref.9
	Modified residue	23	1	Phosphoserine Ref.10
	Modified residue	31	1	Phosphothreonine By similarity
	Modified residue	33	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	37	1	Phosphoserine Ref.9 Ref.11 Ref.12
	Modified residue	47	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 55	55	Missing in isoform 2.		VSP_015477
	Alternative sequence	56 – 64	9	NRALSNLSS → MSRLRHPRT in isoform 2.		VSP_015480
	Alternative sequence	306 – 445	140	Missing in isoform 2.		VSP_015482

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 7DAD6A3C1D5587D6	FASTA	445	51,418
	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
	Isoform 2 [UniParc]. Checksum: 5482E813ADA4239C	FASTA	250	29,890
	10 20 30 40 50 60 MSRLRHPRTR WKNWWVRGIL TLAMIAFFFI IIYLGPMVLM IIVMCVQIKC FHEIITIGYN 70 80 90 100 110 120 VYHSYDLPWF RTLSWYFLLC VNYFFYGETV TDYFFTLVQR EEPLRILSKY HRFISFTLYL 130 140 150 160 170 180 IGFCMFVLSL VKKHYRLQFY MFGWTHVTLL IVVTQSHLVI HNLFEGMIWF IVPISCVICN 190 200 210 220 230 240 DIMAYMFGFF FGRTPLIKLS PKKTWEGFIG GFFATVVFGL LLSYVMSGYR CFVCPVEYNN 250 DTNSFTVDCE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene." Volta M., Bulfone A., Gattuso C., Rossi E., Mariani M., Consalez G.G., Zuffardi O., Ballabio A., Banfi S., Franco B. Genomics 55:68-77(1999) [PubMed: 9889000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"The DNA sequence and comparative analysis of human chromosome 20." 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. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[6]	"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: 9806839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-445 (ISOFORM 1). Tissue: Retina.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, MASS SPECTROMETRY. Tissue: Platelet.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-33 AND SER-37, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-33, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y16521 mRNA. Translation: CAA76270.1. AK315489 mRNA. Translation: BAG37873.1. AL121755, AL121924 Genomic DNA. Translation: CAI22376.1. AL121755, AL121924 Genomic DNA. Translation: CAI22378.1. AL121924, AL121755 Genomic DNA. Translation: CAI22631.1. AL121924, AL121755 Genomic DNA. Translation: CAI22633.1. CH471133 Genomic DNA. Translation: EAX10424.1. CH471133 Genomic DNA. Translation: EAX10426.1. BC025751 mRNA. Translation: AAH25751.1. AF069532 mRNA. Translation: AAC78305.1.
IPI	IPI00032150. IPI00646081.
RefSeq	NP_003809.1. NM_003818.3.
UniGene	Hs.126857. Hs.728973.
3D structure databases
ProteinModelPortal	O95674.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95674. 1 interaction.
STRING	O95674.
PTM databases
PhosphoSite	O95674.
Proteomic databases
PRIDE	O95674.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000460006; ENSP00000419879; ENSG00000101290.
GeneID	8760.
KEGG	hsa:8760.
NMPDR	fig|9606.3.peg.19834.
UCSC	uc002wlr.1. human. uc002wls.1. human.
Organism-specific databases
CTD	8760.
GeneCards	GC20P005107.
H-InvDB	HIX0015619.
HGNC	HGNC:1801. CDS2.
HPA	HPA019698.
MIM	603549. gene.
neXtProt	NX_O95674.
PharmGKB	PA26347.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18179.
GeneTree	ENSGT00390000016175.
HOVERGEN	HBG002485.
InParanoid	O95674.
OMA	FNTLRSH.
OrthoDB	EOG4V437K.
PhylomeDB	O95674.
Gene expression databases
ArrayExpress	O95674.
Bgee	O95674.
CleanEx	HS_CDS2.
Genevestigator	O95674.
GermOnline	ENSG00000101290. Homo sapiens.
Family and domain databases
InterPro	IPR000374. PC_trans. IPR016720. PC_Trfase_euk. [Graphical view]
KO	K00981.
Pfam	PF01148. CTP_transf_1. 1 hit. [Graphical view]
PIRSF	PIRSF018269. PC_trans_euk. 1 hit.
PROSITE	PS01315. CDS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	32860.
SOURCE	Search...

Entry information

Entry name

CDS2_HUMAN

Accession

Primary (citable) accession number: O95674
Secondary accession number(s): B2RDC6 , D3DW04, Q5TDY2, Q5TDY3, Q5TDY4, Q5TDY5, Q9BYK5, Q9NTT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.