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Protein

Ethanolamine kinase 1

Gene

ETNK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis.

Catalytic activityi

ATP + ethanolamine = ADP + O-phosphoethanolamine.

Pathway:iphosphatidylethanolamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphatidylethanolamine from ethanolamine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Choline/ethanolamine kinase (CHKB), Ethanolamine kinase 2 (ETNK2), Choline kinase alpha (CHKA), Ethanolamine kinase 1 (ETNK1)
  2. Ethanolamine-phosphate cytidylyltransferase (PCYT2)
  3. Ethanolaminephosphotransferase 1 (EPT1), Choline/ethanolaminephosphotransferase 1 (CEPT1)
This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from ethanolamine, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ethanolamine kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.82. 2681.
ReactomeiREACT_120919. Synthesis of PE.
UniPathwayiUPA00558; UER00741.

Names & Taxonomyi

Protein namesi
Recommended name:
Ethanolamine kinase 1 (EC:2.7.1.82)
Short name:
EKI 1
Gene namesi
Name:ETNK1
Synonyms:EKI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24649. ETNK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134921265.

Polymorphism and mutation databases

BioMutaiETNK1.
DMDMi14194724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Ethanolamine kinase 1PRO_0000206227Add
BLAST

Proteomic databases

MaxQBiQ9HBU6.
PaxDbiQ9HBU6.
PRIDEiQ9HBU6.

PTM databases

PhosphoSiteiQ9HBU6.

Expressioni

Tissue specificityi

Expressed in kidney, liver, placenta, heart, leukocyte, ovary and testis.

Gene expression databases

BgeeiQ9HBU6.
CleanExiHS_ETNK1.
ExpressionAtlasiQ9HBU6. baseline and differential.
GenevisibleiQ9HBU6. HS.

Organism-specific databases

HPAiHPA010712.
HPA029407.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
UBQLN1Q9UMX03EBI-2834493,EBI-741480
UBQLN1Q9UMX0-23EBI-2834493,EBI-10173939

Protein-protein interaction databases

BioGridi120680. 3 interactions.
IntActiQ9HBU6. 2 interactions.
STRINGi9606.ENSP00000266517.

Structurei

3D structure databases

ProteinModelPortaliQ9HBU6.
SMRiQ9HBU6. Positions 146-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi73 – 8311Poly-ValAdd
BLAST

Sequence similaritiesi

Belongs to the choline/ethanolamine kinase family.Curated

Phylogenomic databases

eggNOGiCOG0510.
GeneTreeiENSGT00530000062991.
HOGENOMiHOG000004856.
HOVERGENiHBG018981.
InParanoidiQ9HBU6.
KOiK00894.
OMAiQEEMAWM.
OrthoDBiEOG72NRQH.
PhylomeDBiQ9HBU6.
TreeFamiTF313549.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HBU6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLCGRPRSSS DNRNFLRERA GLSSAAVQTR IGNSAASRRS PAARPPVPAP
60 70 80 90 100
PALPRGRPGT EGSTSLSAPA VLVVAVAVVV VVVSAVAWAM ANYIHVPPGS
110 120 130 140 150
PEVPKLNVTV QDQEEHRCRE GALSLLQHLR PHWDPQEVTL QLFTDGITNK
160 170 180 190 200
LIGCYVGNTM EDVVLVRIYG NKTELLVDRD EEVKSFRVLQ AHGCAPQLYC
210 220 230 240 250
TFNNGLCYEF IQGEALDPKH VCNPAIFRLI ARQLAKIHAI HAHNGWIPKS
260 270 280 290 300
NLWLKMGKYF SLIPTGFADE DINKRFLSDI PSSQILQEEM TWMKEILSNL
310 320 330 340 350
GSPVVLCHND LLCKNIIYNE KQGDVQFIDY EYSGYNYLAY DIGNHFNEFA
360 370 380 390 400
GVSDVDYSLY PDRELQSQWL RAYLEAYKEF KGFGTEVTEK EVEILFIQVN
410 420 430 440 450
QFALASHFFW GLWALIQAKY STIEFDFLGY AIVRFNQYFK MKPEVTALKV

PE
Length:452
Mass (Da):50,968
Last modified:March 1, 2001 - v1
Checksum:i9AF29EAC556ED91F
GO
Isoform 2 (identifier: Q9HBU6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-452: RLIARQLAKI...PEVTALKVPE → SLSSLTLCKGKTTRCFGLTGCRGSRLLLSFF

Note: No experimental confirmation available.
Show »
Length:258
Mass (Da):27,995
Checksum:iED3BD93928986C4A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei228 – 452225RLIAR…LKVPE → SLSSLTLCKGKTTRCFGLTG CRGSRLLLSFF in isoform 2. 1 PublicationVSP_047191Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207600 mRNA. Translation: AAF71220.2.
AC087241 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96479.1.
BC006111 mRNA. Translation: AAH06111.2.
BC066907 mRNA. Translation: AAH66907.1.
CCDSiCCDS41760.1. [Q9HBU6-2]
CCDS8698.1. [Q9HBU6-1]
RefSeqiNP_001034570.1. NM_001039481.1. [Q9HBU6-2]
NP_061108.2. NM_018638.4. [Q9HBU6-1]
UniGeneiHs.29464.

Genome annotation databases

EnsembliENST00000266517; ENSP00000266517; ENSG00000139163.
ENST00000335148; ENSP00000334041; ENSG00000139163. [Q9HBU6-2]
GeneIDi55500.
KEGGihsa:55500.
UCSCiuc001rfs.3. human.
uc001rft.3. human. [Q9HBU6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207600 mRNA. Translation: AAF71220.2.
AC087241 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96479.1.
BC006111 mRNA. Translation: AAH06111.2.
BC066907 mRNA. Translation: AAH66907.1.
CCDSiCCDS41760.1. [Q9HBU6-2]
CCDS8698.1. [Q9HBU6-1]
RefSeqiNP_001034570.1. NM_001039481.1. [Q9HBU6-2]
NP_061108.2. NM_018638.4. [Q9HBU6-1]
UniGeneiHs.29464.

3D structure databases

ProteinModelPortaliQ9HBU6.
SMRiQ9HBU6. Positions 146-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120680. 3 interactions.
IntActiQ9HBU6. 2 interactions.
STRINGi9606.ENSP00000266517.

PTM databases

PhosphoSiteiQ9HBU6.

Polymorphism and mutation databases

BioMutaiETNK1.
DMDMi14194724.

Proteomic databases

MaxQBiQ9HBU6.
PaxDbiQ9HBU6.
PRIDEiQ9HBU6.

Protocols and materials databases

DNASUi55500.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266517; ENSP00000266517; ENSG00000139163.
ENST00000335148; ENSP00000334041; ENSG00000139163. [Q9HBU6-2]
GeneIDi55500.
KEGGihsa:55500.
UCSCiuc001rfs.3. human.
uc001rft.3. human. [Q9HBU6-1]

Organism-specific databases

CTDi55500.
GeneCardsiGC12P022778.
HGNCiHGNC:24649. ETNK1.
HPAiHPA010712.
HPA029407.
MIMi609858. gene.
neXtProtiNX_Q9HBU6.
PharmGKBiPA134921265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0510.
GeneTreeiENSGT00530000062991.
HOGENOMiHOG000004856.
HOVERGENiHBG018981.
InParanoidiQ9HBU6.
KOiK00894.
OMAiQEEMAWM.
OrthoDBiEOG72NRQH.
PhylomeDBiQ9HBU6.
TreeFamiTF313549.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00741.
BRENDAi2.7.1.82. 2681.
ReactomeiREACT_120919. Synthesis of PE.

Miscellaneous databases

ChiTaRSiETNK1. human.
GenomeRNAii55500.
NextBioi59873.
PROiQ9HBU6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBU6.
CleanExiHS_ETNK1.
ExpressionAtlasiQ9HBU6. baseline and differential.
GenevisibleiQ9HBU6. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway."
    Lykidis A., Wang J., Karim M.A., Jackowski S.
    J. Biol. Chem. 276:2174-2179(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEKI1_HUMAN
AccessioniPrimary (citable) accession number: Q9HBU6
Secondary accession number(s): G5E969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.