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UniProtKB/Swiss-Prot entry Q8TCT0


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

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Entry information
Entry name CERK1_HUMAN
Primary accession number Q8TCT0
Secondary accession numbers A0JNT4 A8K611 Q9BYB3 Q9UGE5
Integrated into Swiss-Prot on April 23, 2003
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 56)
Name and origin of the protein
Protein name Ceramide kinase
Synonyms hCERK
EC 2.7.1.138
Acylsphingosine kinase
Lipid kinase 4
LK4
Gene name
Name: CERK
Synonyms: KIAA1646
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], AND CHARACTERIZATION.
TISSUE=Leukemia;
DOI=10.1074/jbc.M201535200; PubMed=11956206 [NCBI, ExPASy, EBI, Israel, Japan]
Sugiura M., Kono K., Liu H., Shimizugawa T., Minekura H., Spiegel S., Kohama T.;
"Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization.";
J. Biol. Chem. 277:23294-23300(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Van Veldhoven P.P.;
"A search for lipid kinases.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-537.
TISSUE=Brain;
DOI=10.1093/dnares/8.1.1; PubMed=11258795 [NCBI, ExPASy, EBI, Israel, Japan]
Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
"Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping.";
DNA Res. 8:1-9(2001).
Comments
  • FUNCTION: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines.
  • CATALYTIC ACTIVITY: ATP + ceramide = ADP + ceramide 1-phosphate.
  • COFACTOR: Calcium.
  • COFACTOR: Magnesium.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    pH dependence:   Optimum pH is 6.0-7.5;
  • SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
  • TISSUE SPECIFICITY: High level expression in heart, brain, skeletal muscle, kidney and liver; moderate in peripheral blood leukocytes and thymus; very low in spleen, small intestine, placenta and lung.
  • SIMILARITY: Contains 1 DAGKc domain.
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
AB079066; BAC01154.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ457828; CAD29884.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456404; CAG30290.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291476; BAF84165.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096766; CAI18819.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL118516; CAI18819.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL118516; CAI17953.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096766; CAI17953.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126940; AAI26941.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB051433; BAB33316.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00152433; -.
RefSeq NP_073603.2; -.
UniGene Hs.200668
3D structure databases
ModBase Q8TCT0.
Enzyme and pathway databases
BRENDA 2.7.1.138; 247.
Organism-specific databases
GeneCards GC22M045400; -.
H-InvDB HIX0016597; -.
HGNC HGNC:19256; CERK.
GenAtlas CERK.
HPA HPA014700; -.
MIM 610307; gene. [NCBI / EBI]
PharmGKB PA134958321; -.
HUGE KIAA1646.
Gene expression databases
ArrayExpress Q8TCT0; -.
Bgee Q8TCT0; -.
CleanEx HS_CERK; -.
GermOnline ENSG00000100422; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000299; Cellular component: integral to membrane of membrane fraction (inferred from direct assay from UniProtKB).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0001729; Molecular function: ceramide kinase activity (inferred from direct assay from UniProtKB).
GO:0004143; Molecular function: diacylglycerol kinase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from direct assay from UniProtKB).
GO:0007205; Biological process: activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway (inferred from electronic annotation from InterPro).
GO:0006672; Biological process: ceramide metabolic process (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001206; Diacylglycerol_kinase_cat.
IPR001849; Pleckstrin_homology.
Graphical view of domain structure.
Pfam PF00781; DAGK_cat; 1.
Pfam graphical view of domain structure.
ProDom PD005043; DAGKc; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00046; DAGKc; 1.
SM00233; PH; 1.
SMART graphical view of domain structure.
Proteomic databases
PRIDE Q8TCT0; -.
Genome annotation databases
Ensembl ENSG00000100422; Homo sapiens. [Contig view]
GeneID 64781; -.
KEGG hsa:64781; -.
Phylogenomic databases
HOGENOM Q8TCT0; -.
HOVERGEN Q8TCT0; -.
OMA Q8TCT0; RYDFSGL.
Other
NextBio 66814; -.
SOURCE CERK; Homo sapiens.
ProtoNet Q8TCT0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Calcium; Cytoplasm; Kinase; Magnesium; Membrane; Nucleotide-binding; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   537  537     Ceramide kinase. PRO_0000181354
DOMAIN   132   278  147     DAGKc. 
VARIANT   191   191  1     I -> V (in dbSNP:rs16995615 [NCBI]). VAR_053685 
VARIANT   211   211  1     T -> M (in dbSNP:rs9306515 [NCBI]). VAR_053686 
VARIANT   306   306  1     L -> F (in dbSNP:rs13057352 [NCBI]). VAR_053687 
Sequence information
Length: 537 AA [This is the length of the unprocessed precursor] Molecular weight: 59977 Da [This is the MW of the unprocessed precursor] CRC64: 3DBFC0ED8D679F7F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGATGAAEPL QSVLWVKQQR CAVSLEPARA LLRWWRSPGP GAGAPGADAC SVPVSEIIAV 

        70         80         90        100        110        120 
EETDVHGKHQ GSGKWQKMEK PYAFTVHCVK RARRHRWKWA QVTFWCPEEQ LCHLWLQTLR 

       130        140        150        160        170        180 
EMLEKLTSRP KHLLVFINPF GGKGQGKRIY ERKVAPLFTL ASITTDIIVT EHANQAKETL 

       190        200        210        220        230        240 
YEINIDKYDG IVCVGGDGMF SEVLHGLIGR TQRSAGVDQN HPRAVLVPSS LRIGIIPAGS 

       250        260        270        280        290        300 
TDCVCYSTVG TSDAETSALH IVVGDSLAMD VSSVHHNSTL LRYSVSLLGY GFYGDIIKDS 

       310        320        330        340        350        360 
EKKRWLGLAR YDFSGLKTFL SHHCYEGTVS FLPAQHTVGS PRDRKPCRAG CFVCRQSKQQ 

       370        380        390        400        410        420 
LEEEQKKALY GLEAAEDVEE WQVVCGKFLA INATNMSCAC RRSPRGLSPA AHLGDGSSDL 

       430        440        450        460        470        480 
ILIRKCSRFN FLRFLIRHTN QQDQFDFTFV EVYRVKKFQF TSKHMEDEDS DLKEGGKKRF 

       490        500        510        520        530 
GHICSSHPSC CCTVSNSSWN CDGEVLHSPA IEVRVHCQLV RLFARGIEEN PKPDSHS 

Q8TCT0 in FASTA format

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