Q8TCT0 (CERK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ceramide kinase
Short name=hCERK
EC=2.7.1.138

Alternative name(s):
Acylsphingosine kinase
Lipid kinase 4
Short name=LK4

Gene names

Name:	CERK
Synonyms:	KIAA1646

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Binds phosphoinositides. Ref.8
Catalytic activity	ATP + ceramide = ADP + ceramide 1-phosphate.
Cofactor	Calcium. Magnesium.
Enzyme regulation	Inhibited by sulfatide. Ref.8
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein Ref.8.
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.
Sequence similarities	Contains 1 DAGKc domain.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0-7.5.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Calcium Magnesium Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ceramide metabolic process Inferred from direct assay PubMed 19501188. Source: UniProtKB glycosphingolipid metabolic process Traceable author statement. Source: Reactome phospholipid metabolic process Traceable author statement. Source: Reactome protein kinase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA integral to membrane Inferred from direct assay Ref.1. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA plasma membrane Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ceramide kinase activity Inferred from direct assay Ref.1PubMed 19501188. Source: UniProtKB diacylglycerol kinase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from direct assay PubMed 10947957. Source: UniProtKB phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 537	537	Ceramide kinase		PRO_0000181354
Regions
	Domain	128 – 278	151	DAGKc
	Region	1 – 125	125	Required for binding to sulfatide and phosphoinositides
Natural variations
	Natural variant	191	1	I → V. Corresponds to variant rs16995615 [ dbSNP | Ensembl ].		VAR_053685
	Natural variant	211	1	T → M. Corresponds to variant rs9306515 [ dbSNP | Ensembl ].		VAR_053686
	Natural variant	306	1	L → F. Corresponds to variant rs13057352 [ dbSNP | Ensembl ].		VAR_053687

Sequences

	Sequence		Length	Mass (Da)
	Q8TCT0 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3DBFC0ED8D679F7F	FASTA	537	59,977
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization." Sugiura M., Kono K., Liu H., Shimizugawa T., Minekura H., Spiegel S., Kohama T. J. Biol. Chem. 277:23294-23300(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Leukemia.
[2]	"A search for lipid kinases." Van Veldhoven P.P. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"A genome annotation-driven approach to cloning the human ORFeome." 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. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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]. Tissue: Brain.
[5]	"The DNA sequence of human chromosome 22." 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. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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].
[7]	"Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping." Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O. DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-537. Tissue: Brain.
[8]	"A lipid binding domain in sphingosine kinase 2." Don A.S., Rosen H. Biochem. Biophys. Res. Commun. 380:87-92(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, REGION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB079066 mRNA. Translation: BAC01154.1. AJ457828 mRNA. Translation: CAD29884.1. CR456404 mRNA. Translation: CAG30290.1. AK291476 mRNA. Translation: BAF84165.1. AL096766, AL118516 Genomic DNA. Translation: CAI18819.1. AL118516, AL096766 Genomic DNA. Translation: CAI17953.1. BC126940 mRNA. Translation: AAI26941.1. AB051433 mRNA. Translation: BAB33316.1.
IPI	IPI00152433.
RefSeq	NP_073603.2. NM_022766.5.
UniGene	Hs.200668.
3D structure databases
ProteinModelPortal	Q8TCT0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000216264.
PTM databases
PhosphoSite	Q8TCT0.
Polymorphism databases
DMDM	30172885.
Proteomic databases
PaxDb	Q8TCT0.
PRIDE	Q8TCT0.
Protocols and materials databases
DNASU	64781.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216264; ENSP00000216264; ENSG00000100422.
GeneID	64781.
KEGG	hsa:64781.
UCSC	uc003bia.3. human.
Organism-specific databases
CTD	64781.
GeneCards	GC22M047080.
HGNC	HGNC:19256. CERK.
HPA	HPA014700.
MIM	610307. gene.
neXtProt	NX_Q8TCT0.
PharmGKB	PA134958321.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1597.
HOGENOM	HOG000111551.
HOVERGEN	HBG050903.
InParanoid	Q8TCT0.
KO	K04715.
OMA	VSSVHHN.
OrthoDB	EOG4J1181.
PhylomeDB	Q8TCT0.
Enzyme and pathway databases
BRENDA	2.7.1.138. 2681.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q8TCT0.
Gene expression databases
ArrayExpress	Q8TCT0.
Bgee	Q8TCT0.
CleanEx	HS_CERK.
Genevestigator	Q8TCT0.
GermOnline	ENSG00000100422. Homo sapiens.
Family and domain databases
InterPro	IPR001206. Diacylglycerol_kinase_cat_dom. IPR001849. Pleckstrin_homology. [Graphical view]
Pfam	PF00781. DAGK_cat. 1 hit. [Graphical view]
SMART	SM00046. DAGKc. 1 hit. SM00233. PH. 1 hit. [Graphical view]
PROSITE	PS50146. DAGK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q8TCT0.
ChEMBL	CHEMBL1764936.
ChiTaRS	CERK. human.
GenomeRNAi	64781.
NextBio	66814.
SOURCE	Search...

Entry information

Entry name

CERK1_HUMAN

Accession

Primary (citable) accession number: Q8TCT0
Secondary accession number(s): A0JNT4 , A8K611, Q9BYB3, Q9UGE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	June 1, 2002
Last modified:	April 3, 2013
This is version 92 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.