ID EKI2_HUMAN Reviewed; 386 AA.
AC Q9NVF9; B7Z7K1; Q5SXX5; Q68CK3; Q96G05;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Ethanolamine kinase 2;
DE Short=EKI 2;
DE EC=2.7.1.82;
DE AltName: Full=Ethanolamine kinase-like protein;
GN Name=ETNK2; Synonyms=EKI2; ORFNames=HMFT1716;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 25-386 (ISOFORM 3).
RC TISSUE=Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-386 (ISOFORM 1), AND VARIANT
RP GLN-227.
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11044454; DOI=10.1074/jbc.m008794200;
RA Lykidis A., Wang J., Karim M.A., Jackowski S.;
RT "Overexpression of a mammalian ethanolamine-specific kinase accelerates the
RT CDP-ethanolamine pathway.";
RL J. Biol. Chem. 276:2174-2179(2001).
CC -!- FUNCTION: Highly specific for ethanolamine phosphorylation. Does not
CC have choline kinase activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC -!- INTERACTION:
CC Q9NVF9; Q86V38: ATN1; NbExp=3; IntAct=EBI-751864, EBI-11954292;
CC Q9NVF9; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-751864, EBI-3867333;
CC Q9NVF9; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-751864, EBI-7060731;
CC Q9NVF9; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-751864, EBI-10176379;
CC Q9NVF9; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-751864, EBI-10172526;
CC Q9NVF9; Q16623: STX1A; NbExp=3; IntAct=EBI-751864, EBI-712466;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NVF9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVF9-2; Sequence=VSP_039098;
CC Name=3;
CC IsoId=Q9NVF9-3; Sequence=VSP_039558;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, ovary, testis and
CC prostate. {ECO:0000269|PubMed:11044454}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH13637.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001623; BAA91793.1; -; mRNA.
DR EMBL; AK302145; BAH13637.1; ALT_INIT; mRNA.
DR EMBL; AL592146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91501.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91502.1; -; Genomic_DNA.
DR EMBL; BC010082; AAH10082.1; -; mRNA.
DR EMBL; AB073608; BAD38645.1; -; mRNA.
DR CCDS; CCDS1442.2; -. [Q9NVF9-1]
DR CCDS; CCDS73006.1; -. [Q9NVF9-2]
DR RefSeq; NP_001284689.1; NM_001297760.1. [Q9NVF9-2]
DR RefSeq; NP_001284690.1; NM_001297761.1.
DR RefSeq; NP_001284691.1; NM_001297762.1. [Q9NVF9-3]
DR RefSeq; NP_060678.2; NM_018208.3. [Q9NVF9-1]
DR AlphaFoldDB; Q9NVF9; -.
DR SMR; Q9NVF9; -.
DR BioGRID; 120519; 19.
DR IntAct; Q9NVF9; 10.
DR STRING; 9606.ENSP00000356169; -.
DR iPTMnet; Q9NVF9; -.
DR PhosphoSitePlus; Q9NVF9; -.
DR BioMuta; ETNK2; -.
DR DMDM; 296439366; -.
DR MassIVE; Q9NVF9; -.
DR MaxQB; Q9NVF9; -.
DR PaxDb; 9606-ENSP00000356169; -.
DR PeptideAtlas; Q9NVF9; -.
DR ProteomicsDB; 82790; -. [Q9NVF9-1]
DR ProteomicsDB; 82791; -. [Q9NVF9-2]
DR ProteomicsDB; 82792; -. [Q9NVF9-3]
DR Pumba; Q9NVF9; -.
DR Antibodypedia; 34553; 195 antibodies from 25 providers.
DR DNASU; 55224; -.
DR Ensembl; ENST00000367201.7; ENSP00000356169.3; ENSG00000143845.15. [Q9NVF9-2]
DR Ensembl; ENST00000367202.9; ENSP00000356170.4; ENSG00000143845.15. [Q9NVF9-1]
DR GeneID; 55224; -.
DR KEGG; hsa:55224; -.
DR MANE-Select; ENST00000367202.9; ENSP00000356170.4; NM_018208.4; NP_060678.2.
DR UCSC; uc001han.5; human. [Q9NVF9-1]
DR AGR; HGNC:25575; -.
DR CTD; 55224; -.
DR GeneCards; ETNK2; -.
DR HGNC; HGNC:25575; ETNK2.
DR HPA; ENSG00000143845; Tissue enhanced (kidney, liver, testis).
DR MIM; 609859; gene.
DR neXtProt; NX_Q9NVF9; -.
DR OpenTargets; ENSG00000143845; -.
DR PharmGKB; PA134888760; -.
DR VEuPathDB; HostDB:ENSG00000143845; -.
DR eggNOG; KOG4720; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_1_0_1; -.
DR InParanoid; Q9NVF9; -.
DR OMA; HNDLIPR; -.
DR OrthoDB; 144299at2759; -.
DR PhylomeDB; Q9NVF9; -.
DR TreeFam; TF313549; -.
DR BRENDA; 2.7.1.82; 2681.
DR PathwayCommons; Q9NVF9; -.
DR Reactome; R-HSA-1483213; Synthesis of PE.
DR SignaLink; Q9NVF9; -.
DR UniPathway; UPA00558; UER00741.
DR BioGRID-ORCS; 55224; 19 hits in 1153 CRISPR screens.
DR ChiTaRS; ETNK2; human.
DR GenomeRNAi; 55224; -.
DR Pharos; Q9NVF9; Tbio.
DR PRO; PR:Q9NVF9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NVF9; Protein.
DR Bgee; ENSG00000143845; Expressed in right testis and 118 other cell types or tissues.
DR ExpressionAtlas; Q9NVF9; baseline and differential.
DR Genevisible; Q9NVF9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004305; F:ethanolamine kinase activity; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR CDD; cd05157; ETNK_euk; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR PANTHER; PTHR22603:SF94; ETHANOLAMINE KINASE 2; 1.
DR Pfam; PF01633; Choline_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="Ethanolamine kinase 2"
FT /id="PRO_0000206229"
FT VAR_SEQ 173..213
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039558"
FT VAR_SEQ 339..386
FT /note="ASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKVKPQASALEMPK ->
FT GPSCVSSTMTASLQCCRVGNRHGEIARLTLSGLFPGVSLLLGSLGPHPEPVLHHRL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039098"
FT VARIANT 227
FT /note="R -> Q (in dbSNP:rs3737657)"
FT /evidence="ECO:0000269|PubMed:15221005"
FT /id="VAR_022145"
FT CONFLICT 10
FT /note="P -> Q (in Ref. 1; BAA91793)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="Q -> R (in Ref. 1; BAH13637)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> F (in Ref. 1; BAH13637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 44781 MW; 341E981AD2B80C15 CRC64;
MAVPPSAPQP RASFHLRRHT PCPQCSWGME EKAAASASCR EPPGPPRAAA VAYFGISVDP
DDILPGALRL IQELRPHWKP EQVRTKRFTD GITNKLVACY VEEDMQDCVL VRVYGERTEL
LVDRENEVRN FQLLRAHSCA PKLYCTFQNG LCYEYMQGVA LEPEHIREPR LFRLIALEMA
KIHTIHANGS LPKPILWHKM HNYFTLVKNE INPSLSADVP KVEVLERELA WLKEHLSQLE
SPVVFCHNDL LCKNIIYDSI KGHVRFIDYE YAGYNYQAFD IGNHFNEFAG VNEVDYCLYP
ARETQLQWLH YYLQAQKGMA VTPREVQRLY VQVNKFALAS HFFWALWALI QNQYSTIDFD
FLRYAVIRFN QYFKVKPQAS ALEMPK
//
