ID   CERK1_HUMAN             Reviewed;         537 AA.
AC   Q8TCT0; A0JNT4; A8K611; Q9BYB3; Q9UGE5;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   19-JAN-2010, entry version 65.
DE   RecName: Full=Ceramide kinase;
DE            Short=hCERK;
DE            EC=2.7.1.138;
DE   AltName: Full=Acylsphingosine kinase;
DE   AltName: Full=Lipid kinase 4;
DE            Short=LK4;
GN   Name=CERK; Synonyms=KIAA1646;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Leukemia;
RX   MEDLINE=22075121; PubMed=11956206; DOI=10.1074/jbc.M201535200;
RA   Sugiura M., Kono K., Liu H., Shimizugawa T., Minekura H., Spiegel S.,
RA   Kohama T.;
RT   "Ceramide kinase, a novel lipid kinase. Molecular cloning and
RT   functional characterization.";
RL   J. Biol. Chem. 277:23294-23300(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Van Veldhoven P.P.;
RT   "A search for lipid kinases.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-537.
RC   TISSUE=Brain;
RX   MEDLINE=21156230; PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA   Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT   "Identification of novel transcribed sequences on human chromosome 22
RT   by expressed sequence tag mapping.";
RL   DNA Res. 8:1-9(2001).
CC   -!- FUNCTION: Catalyzes specifically the phosphorylation of ceramide
CC       to form ceramide 1-phosphate. Acts efficiently on natural and
CC       analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide),
CC       to a lesser extent on C2-ceramide and C6-dihydroceramide, but not
CC       on other lipids, such as various sphingosines.
CC   -!- CATALYTIC ACTIVITY: ATP + ceramide = ADP + ceramide 1-phosphate.
CC   -!- COFACTOR: Calcium.
CC   -!- COFACTOR: Magnesium.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0-7.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: High level expression in heart, brain,
CC       skeletal muscle, kidney and liver; moderate in peripheral blood
CC       leukocytes and thymus; very low in spleen, small intestine,
CC       placenta and lung.
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
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DR   EMBL; AB079066; BAC01154.1; -; mRNA.
DR   EMBL; AJ457828; CAD29884.1; -; mRNA.
DR   EMBL; CR456404; CAG30290.1; -; mRNA.
DR   EMBL; AK291476; BAF84165.1; -; mRNA.
DR   EMBL; AL096766; CAI18819.1; -; Genomic_DNA.
DR   EMBL; AL118516; CAI18819.1; JOINED; Genomic_DNA.
DR   EMBL; AL118516; CAI17953.1; -; Genomic_DNA.
DR   EMBL; AL096766; CAI17953.1; JOINED; Genomic_DNA.
DR   EMBL; BC126940; AAI26941.1; -; mRNA.
DR   EMBL; AB051433; BAB33316.1; -; mRNA.
DR   IPI; IPI00152433; -.
DR   RefSeq; NP_073603.2; -.
DR   UniGene; Hs.200668; -.
DR   SMR; Q8TCT0; 130-526.
DR   STRING; Q8TCT0; -.
DR   PRIDE; Q8TCT0; -.
DR   Ensembl; ENST00000216264; ENSP00000216264; ENSG00000100422; Homo sapiens.
DR   GeneID; 64781; -.
DR   KEGG; hsa:64781; -.
DR   UCSC; uc003bia.1; human.
DR   CTD; 64781; -.
DR   GeneCards; GC22M045400; -.
DR   H-InvDB; HIX0016597; -.
DR   HGNC; HGNC:19256; CERK.
DR   HPA; HPA014700; -.
DR   MIM; 610307; gene.
DR   PharmGKB; PA134958321; -.
DR   eggNOG; prNOG12318; -.
DR   HOGENOM; HBG713689; -.
DR   HOVERGEN; Q8TCT0; -.
DR   InParanoid; Q8TCT0; -.
DR   OMA; RYDFSGL; -.
DR   OrthoDB; EOG9STVQM; -.
DR   PhylomeDB; Q8TCT0; -.
DR   BRENDA; 2.7.1.138; 247.
DR   NextBio; 66814; -.
DR   ArrayExpress; Q8TCT0; -.
DR   Bgee; Q8TCT0; -.
DR   CleanEx; HS_CERK; -.
DR   Genevestigator; Q8TCT0; -.
DR   GermOnline; ENSG00000100422; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000299; C:integral to membrane of membrane fraction; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001729; F:ceramide kinase activity; IDA:UniProtKB.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0007205; P:activation of protein kinase C activity by ...; IEA:InterPro.
DR   GO; GO:0006672; P:ceramide metabolic process; TAS:UniProtKB.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW   Membrane; Nucleotide-binding; Polymorphism; Transferase.
FT   CHAIN         1    537       Ceramide kinase.
FT                                /FTId=PRO_0000181354.
FT   DOMAIN      128    278       DAGKc.
FT   VARIANT     191    191       I -> V (in dbSNP:rs16995615).
FT                                /FTId=VAR_053685.
FT   VARIANT     211    211       T -> M (in dbSNP:rs9306515).
FT                                /FTId=VAR_053686.
FT   VARIANT     306    306       L -> F (in dbSNP:rs13057352).
FT                                /FTId=VAR_053687.
SQ   SEQUENCE   537 AA;  59977 MW;  3DBFC0ED8D679F7F CRC64;
     MGATGAAEPL QSVLWVKQQR CAVSLEPARA LLRWWRSPGP GAGAPGADAC SVPVSEIIAV
     EETDVHGKHQ GSGKWQKMEK PYAFTVHCVK RARRHRWKWA QVTFWCPEEQ LCHLWLQTLR
     EMLEKLTSRP KHLLVFINPF GGKGQGKRIY ERKVAPLFTL ASITTDIIVT EHANQAKETL
     YEINIDKYDG IVCVGGDGMF SEVLHGLIGR TQRSAGVDQN HPRAVLVPSS LRIGIIPAGS
     TDCVCYSTVG TSDAETSALH IVVGDSLAMD VSSVHHNSTL LRYSVSLLGY GFYGDIIKDS
     EKKRWLGLAR YDFSGLKTFL SHHCYEGTVS FLPAQHTVGS PRDRKPCRAG CFVCRQSKQQ
     LEEEQKKALY GLEAAEDVEE WQVVCGKFLA INATNMSCAC RRSPRGLSPA AHLGDGSSDL
     ILIRKCSRFN FLRFLIRHTN QQDQFDFTFV EVYRVKKFQF TSKHMEDEDS DLKEGGKKRF
     GHICSSHPSC CCTVSNSSWN CDGEVLHSPA IEVRVHCQLV RLFARGIEEN PKPDSHS
//