Full text data of ETNK2
ETNK2
(EKI2)
[Confidence: low (only semi-automatic identification from reviews)]
Ethanolamine kinase 2; EKI 2; 2.7.1.82 (Ethanolamine kinase-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ethanolamine kinase 2; EKI 2; 2.7.1.82 (Ethanolamine kinase-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NVF9
ID EKI2_HUMAN Reviewed; 386 AA.
AC Q9NVF9; B7Z7K1; Q5SXX5; Q68CK3; Q96G05;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 102.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [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.,
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 [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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP VARIANT 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.,
RA Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
RA Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
RA Nakagawara A.;
RT "Expression profiling and differential screening between
RT hepatoblastomas and the corresponding normal livers: identification of
RT high expression of the PLK1 oncogene as a poor-prognostic indicator of
RT 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
RT accelerates the CDP-ethanolamine pathway.";
RL J. Biol. Chem. 276:2174-2179(2001).
CC -!- FUNCTION: Highly specific for ethanolamine phosphorylation. Does
CC not have choline kinase activity (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + ethanolamine = ADP + O-
CC phosphoethanolamine.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step
CC 1/3.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, ovary, testis and
CC prostate.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH13637.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AK001623; BAA91793.1; -; mRNA.
DR EMBL; AK302145; BAH13637.1; ALT_INIT; mRNA.
DR EMBL; AL592146; CAI16602.1; -; Genomic_DNA.
DR EMBL; AL592146; CAI16603.1; -; 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 RefSeq; NP_060678.2; NM_018208.2.
DR RefSeq; XP_005245359.1; XM_005245302.1.
DR RefSeq; XP_005245361.1; XM_005245304.1.
DR UniGene; Hs.497469; -.
DR ProteinModelPortal; Q9NVF9; -.
DR SMR; Q9NVF9; 62-381.
DR IntAct; Q9NVF9; 3.
DR STRING; 9606.ENSP00000356170; -.
DR DMDM; 296439366; -.
DR PaxDb; Q9NVF9; -.
DR PRIDE; Q9NVF9; -.
DR DNASU; 55224; -.
DR Ensembl; ENST00000367201; ENSP00000356169; ENSG00000143845.
DR Ensembl; ENST00000367202; ENSP00000356170; ENSG00000143845.
DR GeneID; 55224; -.
DR KEGG; hsa:55224; -.
DR UCSC; uc001hao.4; human.
DR CTD; 55224; -.
DR GeneCards; GC01M204100; -.
DR H-InvDB; HIX0001494; -.
DR HGNC; HGNC:25575; ETNK2.
DR HPA; HPA057167; -.
DR MIM; 609859; gene.
DR neXtProt; NX_Q9NVF9; -.
DR PharmGKB; PA134888760; -.
DR eggNOG; COG0510; -.
DR HOGENOM; HOG000004856; -.
DR HOVERGEN; HBG018981; -.
DR InParanoid; Q9NVF9; -.
DR KO; K00894; -.
DR OMA; SLGPHPE; -.
DR OrthoDB; EOG72NRQH; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00558; UER00741.
DR ChiTaRS; ETNK2; human.
DR GenomeRNAi; 55224; -.
DR NextBio; 59212; -.
DR PRO; PR:Q9NVF9; -.
DR ArrayExpress; Q9NVF9; -.
DR Bgee; Q9NVF9; -.
DR CleanEx; HS_ETNK2; -.
DR Genevestigator; Q9NVF9; -.
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; IEA:UniProtKB-EC.
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; TAS:Reactome.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR011009; Kinase-like_dom.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Complete proteome; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 386 Ethanolamine kinase 2.
FT /FTId=PRO_0000206229.
FT VAR_SEQ 173 213 Missing (in isoform 3).
FT /FTId=VSP_039558.
FT VAR_SEQ 339 386 ASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKVKPQA
FT SALEMPK -> GPSCVSSTMTASLQCCRVGNRHGEIARLTL
FT SGLFPGVSLLLGSLGPHPEPVLHHRL (in isoform
FT 2).
FT /FTId=VSP_039098.
FT VARIANT 227 227 R -> Q (in dbSNP:rs3737657).
FT /FTId=VAR_022145.
FT CONFLICT 10 10 P -> Q (in Ref. 1; BAA91793).
FT CONFLICT 148 148 Q -> R (in Ref. 1; BAH13637).
FT CONFLICT 241 241 S -> F (in Ref. 1; BAH13637).
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
//
ID EKI2_HUMAN Reviewed; 386 AA.
AC Q9NVF9; B7Z7K1; Q5SXX5; Q68CK3; Q96G05;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 102.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [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.,
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 [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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP VARIANT 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.,
RA Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
RA Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
RA Nakagawara A.;
RT "Expression profiling and differential screening between
RT hepatoblastomas and the corresponding normal livers: identification of
RT high expression of the PLK1 oncogene as a poor-prognostic indicator of
RT 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
RT accelerates the CDP-ethanolamine pathway.";
RL J. Biol. Chem. 276:2174-2179(2001).
CC -!- FUNCTION: Highly specific for ethanolamine phosphorylation. Does
CC not have choline kinase activity (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + ethanolamine = ADP + O-
CC phosphoethanolamine.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step
CC 1/3.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, ovary, testis and
CC prostate.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH13637.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AK001623; BAA91793.1; -; mRNA.
DR EMBL; AK302145; BAH13637.1; ALT_INIT; mRNA.
DR EMBL; AL592146; CAI16602.1; -; Genomic_DNA.
DR EMBL; AL592146; CAI16603.1; -; 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 RefSeq; NP_060678.2; NM_018208.2.
DR RefSeq; XP_005245359.1; XM_005245302.1.
DR RefSeq; XP_005245361.1; XM_005245304.1.
DR UniGene; Hs.497469; -.
DR ProteinModelPortal; Q9NVF9; -.
DR SMR; Q9NVF9; 62-381.
DR IntAct; Q9NVF9; 3.
DR STRING; 9606.ENSP00000356170; -.
DR DMDM; 296439366; -.
DR PaxDb; Q9NVF9; -.
DR PRIDE; Q9NVF9; -.
DR DNASU; 55224; -.
DR Ensembl; ENST00000367201; ENSP00000356169; ENSG00000143845.
DR Ensembl; ENST00000367202; ENSP00000356170; ENSG00000143845.
DR GeneID; 55224; -.
DR KEGG; hsa:55224; -.
DR UCSC; uc001hao.4; human.
DR CTD; 55224; -.
DR GeneCards; GC01M204100; -.
DR H-InvDB; HIX0001494; -.
DR HGNC; HGNC:25575; ETNK2.
DR HPA; HPA057167; -.
DR MIM; 609859; gene.
DR neXtProt; NX_Q9NVF9; -.
DR PharmGKB; PA134888760; -.
DR eggNOG; COG0510; -.
DR HOGENOM; HOG000004856; -.
DR HOVERGEN; HBG018981; -.
DR InParanoid; Q9NVF9; -.
DR KO; K00894; -.
DR OMA; SLGPHPE; -.
DR OrthoDB; EOG72NRQH; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00558; UER00741.
DR ChiTaRS; ETNK2; human.
DR GenomeRNAi; 55224; -.
DR NextBio; 59212; -.
DR PRO; PR:Q9NVF9; -.
DR ArrayExpress; Q9NVF9; -.
DR Bgee; Q9NVF9; -.
DR CleanEx; HS_ETNK2; -.
DR Genevestigator; Q9NVF9; -.
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; IEA:UniProtKB-EC.
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; TAS:Reactome.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR011009; Kinase-like_dom.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Complete proteome; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 386 Ethanolamine kinase 2.
FT /FTId=PRO_0000206229.
FT VAR_SEQ 173 213 Missing (in isoform 3).
FT /FTId=VSP_039558.
FT VAR_SEQ 339 386 ASHFFWALWALIQNQYSTIDFDFLRYAVIRFNQYFKVKPQA
FT SALEMPK -> GPSCVSSTMTASLQCCRVGNRHGEIARLTL
FT SGLFPGVSLLLGSLGPHPEPVLHHRL (in isoform
FT 2).
FT /FTId=VSP_039098.
FT VARIANT 227 227 R -> Q (in dbSNP:rs3737657).
FT /FTId=VAR_022145.
FT CONFLICT 10 10 P -> Q (in Ref. 1; BAA91793).
FT CONFLICT 148 148 Q -> R (in Ref. 1; BAH13637).
FT CONFLICT 241 241 S -> F (in Ref. 1; BAH13637).
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
//
MIM
609859
*RECORD*
*FIELD* NO
609859
*FIELD* TI
*609859 ETHANOLAMINE KINASE 2; ETNK2
;;EKI2
*FIELD* TX
DESCRIPTION
Ethanolamine kinase (ATP:ethanolamine O-phosphotransferase; EC 2.7.1.82)
read morecatalyzes the first step of phosphatidylethanolamine (PtdEtn)
biosynthesis via the CDP-Etn pathway (Lykidis et al., 2001).
CLONING
By searching for sequences similar to ETNK1 (609858), Lykidis et al.
(2001) identified 2 splice variants of ETNK2, which they called
EKI2-alpha and EKI2-beta. The deduced proteins contain 477 and 394 amino
acids, respectively, and are identical in the first 338 amino acids.
Northern blot analysis detected EKI2 transcripts of 3.0 and 2.5 kb in
kidney, liver, ovary, testis, and prostate only.
Hurley et al. (2004) found that expression of mouse Eki2 was restricted
to the gonads of both sexes at 10.5 days postcoitum. Expression in ovary
was substantially reduced compared with testis at 12.5 days postcoitum
and was absent by 13.5 days postcoitum. Expression in testis persisted
into adulthood, and the main site of expression was Sertoli cells.
MAPPING
By genomic sequence analysis, Lykidis et al. (2001) mapped the ETNK2
gene to chromosome 1 in both human and mouse.
*FIELD* RF
1. Hurley, T. M.; McClive, P. J.; Sarraj, M. A.; Sinclair, A. H.:
Eki2 is upregulated specifically in the testis during mouse sex determination. Gene
Expr. Patterns 4: 135-140, 2004.
2. Lykidis, A.; Wang, J.; Karim, M. A.; Jackowski, S.: Overexpression
of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine
pathway. J. Biol. Chem. 276: 2174-2179, 2001.
*FIELD* CD
Patricia A. Hartz: 1/30/2006
*FIELD* ED
mgross: 01/30/2006
*RECORD*
*FIELD* NO
609859
*FIELD* TI
*609859 ETHANOLAMINE KINASE 2; ETNK2
;;EKI2
*FIELD* TX
DESCRIPTION
Ethanolamine kinase (ATP:ethanolamine O-phosphotransferase; EC 2.7.1.82)
read morecatalyzes the first step of phosphatidylethanolamine (PtdEtn)
biosynthesis via the CDP-Etn pathway (Lykidis et al., 2001).
CLONING
By searching for sequences similar to ETNK1 (609858), Lykidis et al.
(2001) identified 2 splice variants of ETNK2, which they called
EKI2-alpha and EKI2-beta. The deduced proteins contain 477 and 394 amino
acids, respectively, and are identical in the first 338 amino acids.
Northern blot analysis detected EKI2 transcripts of 3.0 and 2.5 kb in
kidney, liver, ovary, testis, and prostate only.
Hurley et al. (2004) found that expression of mouse Eki2 was restricted
to the gonads of both sexes at 10.5 days postcoitum. Expression in ovary
was substantially reduced compared with testis at 12.5 days postcoitum
and was absent by 13.5 days postcoitum. Expression in testis persisted
into adulthood, and the main site of expression was Sertoli cells.
MAPPING
By genomic sequence analysis, Lykidis et al. (2001) mapped the ETNK2
gene to chromosome 1 in both human and mouse.
*FIELD* RF
1. Hurley, T. M.; McClive, P. J.; Sarraj, M. A.; Sinclair, A. H.:
Eki2 is upregulated specifically in the testis during mouse sex determination. Gene
Expr. Patterns 4: 135-140, 2004.
2. Lykidis, A.; Wang, J.; Karim, M. A.; Jackowski, S.: Overexpression
of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine
pathway. J. Biol. Chem. 276: 2174-2179, 2001.
*FIELD* CD
Patricia A. Hartz: 1/30/2006
*FIELD* ED
mgross: 01/30/2006