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Protein

CTP-dependent diacylglycerol kinase 1

Gene

ptp4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of ned1. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus (By similarity). Involved in pre-tRNA splicing.By similarity1 Publication

Catalytic activityi

CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate.

Cofactori

Ca2+By similarity, Mg2+By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

ER-Golgi transport, Transport

Keywords - Ligandi

Calcium, Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
CTP-dependent diacylglycerol kinase 1 (EC:2.7.1.174)
Alternative name(s):
Diglyceride kinase 1By similarity
Short name:
DAG kinase 1By similarity
Gene namesi
Name:ptp4
Synonyms:dgk1By similarity
ORF Names:SPBC3D6.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC3D6.05.
PomBaseiSPBC3D6.05. ptp4.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Golgi apparatus membrane By similarity; Multi-pass membrane protein By similarity
  • Nucleus membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 3718HelicalSequence analysisAdd
BLAST
Transmembranei39 – 5921HelicalSequence analysisAdd
BLAST
Transmembranei89 – 10921HelicalSequence analysisAdd
BLAST
Transmembranei143 – 16321HelicalSequence analysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218CTP-dependent diacylglycerol kinase 1PRO_0000371716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP87170.

Interactioni

Protein-protein interaction databases

BioGridi277514. 36 interactions.
MINTiMINT-4692748.

Family & Domainsi

Sequence similaritiesi

Belongs to the DGK1 family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000198978.
InParanoidiP87170.
KOiK16368.
OMAiFMRESER.
OrthoDBiEOG7VX96V.
PhylomeDBiP87170.

Sequencei

Sequence statusi: Complete.

P87170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKLTWSQW SKKHEIPRKA LHTSIGFFAL LLQGCGYHAA QIIPVIEIGF
60 70 80 90 100
IPAFTGDVIR FNWPAFSRLY NRVIGPLMRE SEKNAWNGVI FYMIGVWIVL
110 120 130 140 150
KVFPEEIAVM SVLLLSWCDT TASTVGRKWG KYTPKIAKNK SLAGSLGAFV
160 170 180 190 200
CGVFCCYVYW GLFRTGPDSL AAQSRIPFPW LCLINGFIGA FAEAMDVWGL
210
DDNLVIPVVS ACLLYLIM
Length:218
Mass (Da):24,397
Last modified:July 1, 1997 - v1
Checksum:iD934354CE978A667
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB09125.1.
PIRiT40365.
RefSeqiNP_595517.1. NM_001021426.2.

Genome annotation databases

EnsemblFungiiSPBC3D6.05.1; SPBC3D6.05.1:pep; SPBC3D6.05.
GeneIDi2540998.
KEGGispo:SPBC3D6.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB09125.1.
PIRiT40365.
RefSeqiNP_595517.1. NM_001021426.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277514. 36 interactions.
MINTiMINT-4692748.

Proteomic databases

MaxQBiP87170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3D6.05.1; SPBC3D6.05.1:pep; SPBC3D6.05.
GeneIDi2540998.
KEGGispo:SPBC3D6.05.

Organism-specific databases

EuPathDBiFungiDB:SPBC3D6.05.
PomBaseiSPBC3D6.05. ptp4.

Phylogenomic databases

HOGENOMiHOG000198978.
InParanoidiP87170.
KOiK16368.
OMAiFMRESER.
OrthoDBiEOG7VX96V.
PhylomeDBiP87170.

Miscellaneous databases

PROiP87170.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A potential membrane protein involved in pre-tRNA splicing of Schizosaccharomyces pombe."
    Kim M., Hwang K., Lim C.-J., Kim D.
    Biochim. Biophys. Acta 1574:210-214(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TRANSMEMBRANE DOMAINS.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDGK1_SCHPO
AccessioniPrimary (citable) accession number: P87170
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.