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   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.
DR   Genevisible; Q9NVF9; HS.
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
//