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Protein

Phosphatidate cytidylyltransferase 2

Gene

CDS2

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

Functioni

Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin.

Catalytic activityi

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway: CDP-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

  • phosphatidate cytidylyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_121280. Synthesis of PG.
UniPathwayiUPA00557; UER00614.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CDS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:1801. CDS2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei79 – 9921HelicalSequence AnalysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence AnalysisAdd
BLAST
Transmembranei166 – 18621HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei262 – 28221HelicalSequence AnalysisAdd
BLAST
Transmembranei340 – 36021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26347.

Polymorphism and mutation databases

BioMutaiCDS2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Phosphatidate cytidylyltransferase 2PRO_0000090716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei31 – 311Phosphothreonine1 Publication
Modified residuei33 – 331Phosphoserine2 Publications
Modified residuei35 – 351Phosphoserine1 Publication
Modified residuei37 – 371Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95674.
PaxDbiO95674.
PRIDEiO95674.

PTM databases

PhosphoSiteiO95674.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain and retina, and to a lesser extent in placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiO95674.
CleanExiHS_CDS2.
GenevisibleiO95674. HS.

Organism-specific databases

HPAiHPA019698.

Interactioni

Protein-protein interaction databases

BioGridi114295. 4 interactions.
IntActiO95674. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliO95674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
HOVERGENiHBG002485.
InParanoidiO95674.
KOiK00981.
OMAiQRVAHEP.
OrthoDBiEOG7M98G5.
PhylomeDBiO95674.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95674-1) [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
MTELRQRVAH EPVAPPEDKE SESEAKVDGE TASDSESRAE SAPLPVSADD
60 70 80 90 100
TPEVLNRALS NLSSRWKNWW VRGILTLAMI AFFFIIIYLG PMVLMIIVMC
110 120 130 140 150
VQIKCFHEII TIGYNVYHSY DLPWFRTLSW YFLLCVNYFF YGETVTDYFF
160 170 180 190 200
TLVQREEPLR ILSKYHRFIS FTLYLIGFCM FVLSLVKKHY RLQFYMFGWT
210 220 230 240 250
HVTLLIVVTQ SHLVIHNLFE GMIWFIVPIS CVICNDIMAY MFGFFFGRTP
260 270 280 290 300
LIKLSPKKTW EGFIGGFFAT VVFGLLLSYV MSGYRCFVCP VEYNNDTNSF
310 320 330 340 350
TVDCEPSDLF RLQEYNIPGV IQSVIGWKTV RMYPFQIHSI ALSTFASLIG
360 370 380 390 400
PFGGFFASGF KRAFKIKDFA NTIPGHGGIM DRFDCQYLMA TFVNVYIASF
410 420 430 440
IRGPNPSKLI QQFLTLRPDQ QLHIFNTLRS HLIDKGMLTS TTEDE
Length:445
Mass (Da):51,418
Last modified:May 1, 1999 - v1
Checksum:i7DAD6A3C1D5587D6
GO
Isoform 2 (identifier: O95674-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:250
Mass (Da):29,890
Checksum:i5482E813ADA4239C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5555Missing in isoform 2. CuratedVSP_015477Add
BLAST
Alternative sequencei56 – 649NRALSNLSS → MSRLRHPRT in isoform 2. CuratedVSP_015480
Alternative sequencei306 – 445140Missing in isoform 2. CuratedVSP_015482Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13088.1. [O95674-1]
RefSeqiNP_003809.1. NM_003818.3. [O95674-1]
UniGeneiHs.126857.

Genome annotation databases

EnsembliENST00000450570; ENSP00000403205; ENSG00000101290. [O95674-2]
ENST00000460006; ENSP00000419879; ENSG00000101290. [O95674-1]
GeneIDi8760.
KEGGihsa:8760.
UCSCiuc002wlr.2. human. [O95674-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13088.1. [O95674-1]
RefSeqiNP_003809.1. NM_003818.3. [O95674-1]
UniGeneiHs.126857.

3D structure databases

ProteinModelPortaliO95674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114295. 4 interactions.
IntActiO95674. 2 interactions.

PTM databases

PhosphoSiteiO95674.

Polymorphism and mutation databases

BioMutaiCDS2.

Proteomic databases

MaxQBiO95674.
PaxDbiO95674.
PRIDEiO95674.

Protocols and materials databases

DNASUi8760.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000450570; ENSP00000403205; ENSG00000101290. [O95674-2]
ENST00000460006; ENSP00000419879; ENSG00000101290. [O95674-1]
GeneIDi8760.
KEGGihsa:8760.
UCSCiuc002wlr.2. human. [O95674-1]

Organism-specific databases

CTDi8760.
GeneCardsiGC20P005107.
HGNCiHGNC:1801. CDS2.
HPAiHPA019698.
MIMi603549. gene.
neXtProtiNX_O95674.
PharmGKBiPA26347.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
HOVERGENiHBG002485.
InParanoidiO95674.
KOiK00981.
OMAiQRVAHEP.
OrthoDBiEOG7M98G5.
PhylomeDBiO95674.
TreeFamiTF313464.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00614.
ReactomeiREACT_121280. Synthesis of PG.

Miscellaneous databases

ChiTaRSiCDS2. human.
GeneWikiiCDS2.
GenomeRNAii8760.
NextBioi32860.
PROiO95674.
SOURCEiSearch...

Gene expression databases

BgeeiO95674.
CleanExiHS_CDS2.
GenevisibleiO95674. 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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-33 AND SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 THR-31 AND SER-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCDS2_HUMAN
AccessioniPrimary (citable) accession number: O95674
Secondary accession number(s): B2RDC6
, D3DW04, Q5TDY2, Q5TDY3, Q5TDY4, Q5TDY5, Q9BYK5, Q9NTT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. 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.