Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ethanolamine-phosphate phospho-lyase

Gene

ETNPPL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.1 Publication

Catalytic activityi

Ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=680 µM for phosphoethanolamine (at pH 7.4)1 Publication
  1. Vmax=1.46 µmol/min/mg enzyme (at pH 7.4)1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Ethanolamine-phosphate phospho-lyase (EC:4.2.3.2)
Alternative name(s):
Alanine--glyoxylate aminotransferase 2-like 1
Gene namesi
Name:ETNPPL
Synonyms:AGXT2L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:14404. ETNPPL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24635.

Polymorphism and mutation databases

BioMutaiETNPPL.
DMDMi74751376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Ethanolamine-phosphate phospho-lyasePRO_0000287663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei278 – 2781N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiQ8TBG4.
PaxDbiQ8TBG4.
PRIDEiQ8TBG4.

PTM databases

PhosphoSiteiQ8TBG4.

Expressioni

Gene expression databases

BgeeiQ8TBG4.
CleanExiHS_AGXT2L1.
ExpressionAtlasiQ8TBG4. baseline and differential.
GenevestigatoriQ8TBG4.

Organism-specific databases

HPAiHPA044546.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi122323. 3 interactions.
STRINGi9606.ENSP00000296486.

Structurei

3D structure databases

ProteinModelPortaliQ8TBG4.
SMRiQ8TBG4. Positions 15-433.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00530000062907.
HOGENOMiHOG000020206.
HOVERGENiHBG004196.
InParanoidiQ8TBG4.
KOiK14286.
OMAiMPEGFIN.
OrthoDBiEOG79KPF2.
PhylomeDBiQ8TBG4.
TreeFamiTF320468.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TBG4-1) [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
MCELYSKRDT LGLRKKHIGP SCKVFFASDP IKIVRAQRQY MFDENGEQYL
60 70 80 90 100
DCINNVAHVG HCHPGVVKAA LKQMELLNTN SRFLHDNIVE YAKRLSATLP
110 120 130 140 150
EKLSVCYFTN SGSEANDLAL RLARQFRGHQ DVITLDHAYH GHLSSLIEIS
160 170 180 190 200
PYKFQKGKDV KKEFVHVAPT PDTYRGKYRE DHADSASAYA DEVKKIIEDA
210 220 230 240 250
HNSGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEYVHGAG GVFIADEVQV
260 270 280 290 300
GFGRVGKHFW SFQMYGEDFV PDIVTMGKPM GNGHPVACVV TTKEIAEAFS
310 320 330 340 350
SSGMEYFNTY GGNPVSCAVG LAVLDIIENE DLQGNAKRVG NYLTELLKKQ
360 370 380 390 400
KAKHTLIGDI RGIGLFIGID LVKDHLKRTP ATAEAQHIIY KMKEKRVLLS
410 420 430 440 450
ADGPHRNVLK IKPPMCFTEE DAKFMVDQLD RILTVLEEAM GTKTESVTSE
460 470 480 490
NTPCKTKMLK EAHIELLRDS TTDSKENPSR KRNGMCTDTH SLLSKRLKT
Length:499
Mass (Da):55,671
Last modified:June 1, 2002 - v1
Checksum:i3C610898060474B4
GO
Isoform 2 (identifier: Q8TBG4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-64: Missing.

Show »
Length:493
Mass (Da):55,040
Checksum:i550C3D17990588B3
GO
Isoform 3 (identifier: Q8TBG4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MCELYSKRDTLGLRKKHIGPSCKVFFASDPIKIVRAQRQYMFDENGEQYLDCINNVAHV → M

Note: No experimental confirmation available.

Show »
Length:441
Mass (Da):48,942
Checksum:i922846180BD29061
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051V → A in BAH11666 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851S → P.
Corresponds to variant rs1377210 [ dbSNP | Ensembl ].
VAR_032342

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5959MCELY…NVAHV → M in isoform 3. 1 PublicationVSP_046097Add
BLAST
Alternative sequencei59 – 646Missing in isoform 2. 1 PublicationVSP_025583

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298293 mRNA. Translation: CAC22253.1.
AK091888 mRNA. Translation: BAC03766.1.
AK294072 mRNA. Translation: BAH11666.1.
AC097473 Genomic DNA. Translation: AAY40946.1.
BC022526 mRNA. Translation: AAH22526.1.
CCDSiCCDS3682.1. [Q8TBG4-1]
CCDS54792.1. [Q8TBG4-3]
CCDS54793.1. [Q8TBG4-2]
RefSeqiNP_001140062.1. NM_001146590.1. [Q8TBG4-2]
NP_001140099.1. NM_001146627.1. [Q8TBG4-3]
NP_112569.2. NM_031279.3. [Q8TBG4-1]
UniGeneiHs.106576.

Genome annotation databases

EnsembliENST00000296486; ENSP00000296486; ENSG00000164089. [Q8TBG4-1]
ENST00000411864; ENSP00000392269; ENSG00000164089. [Q8TBG4-2]
ENST00000512646; ENSP00000427065; ENSG00000164089. [Q8TBG4-3]
GeneIDi64850.
KEGGihsa:64850.
UCSCiuc003hzc.3. human. [Q8TBG4-1]
uc010imc.3. human. [Q8TBG4-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298293 mRNA. Translation: CAC22253.1.
AK091888 mRNA. Translation: BAC03766.1.
AK294072 mRNA. Translation: BAH11666.1.
AC097473 Genomic DNA. Translation: AAY40946.1.
BC022526 mRNA. Translation: AAH22526.1.
CCDSiCCDS3682.1. [Q8TBG4-1]
CCDS54792.1. [Q8TBG4-3]
CCDS54793.1. [Q8TBG4-2]
RefSeqiNP_001140062.1. NM_001146590.1. [Q8TBG4-2]
NP_001140099.1. NM_001146627.1. [Q8TBG4-3]
NP_112569.2. NM_031279.3. [Q8TBG4-1]
UniGeneiHs.106576.

3D structure databases

ProteinModelPortaliQ8TBG4.
SMRiQ8TBG4. Positions 15-433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122323. 3 interactions.
STRINGi9606.ENSP00000296486.

PTM databases

PhosphoSiteiQ8TBG4.

Polymorphism and mutation databases

BioMutaiETNPPL.
DMDMi74751376.

Proteomic databases

MaxQBiQ8TBG4.
PaxDbiQ8TBG4.
PRIDEiQ8TBG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296486; ENSP00000296486; ENSG00000164089. [Q8TBG4-1]
ENST00000411864; ENSP00000392269; ENSG00000164089. [Q8TBG4-2]
ENST00000512646; ENSP00000427065; ENSG00000164089. [Q8TBG4-3]
GeneIDi64850.
KEGGihsa:64850.
UCSCiuc003hzc.3. human. [Q8TBG4-1]
uc010imc.3. human. [Q8TBG4-2]

Organism-specific databases

CTDi64850.
GeneCardsiGC04M109664.
HGNCiHGNC:14404. ETNPPL.
HPAiHPA044546.
MIMi614682. gene.
neXtProtiNX_Q8TBG4.
PharmGKBiPA24635.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00530000062907.
HOGENOMiHOG000020206.
HOVERGENiHBG004196.
InParanoidiQ8TBG4.
KOiK14286.
OMAiMPEGFIN.
OrthoDBiEOG79KPF2.
PhylomeDBiQ8TBG4.
TreeFamiTF320468.

Miscellaneous databases

GenomeRNAii64850.
NextBioi66972.
PROiQ8TBG4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TBG4.
CleanExiHS_AGXT2L1.
ExpressionAtlasiQ8TBG4. baseline and differential.
GenevestigatoriQ8TBG4.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney."
    Matsui-Lee I.S., Muragaki Y., Ideguchi T., Hase T., Tsuji M., Ooshima A., Okuno E., Kido R.
    J. Biochem. 117:856-862(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain cortex and Kidney.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Brain.
  5. "Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine."
    Veiga-da-Cunha M., Hadi F., Balligand T., Stroobant V., Van Schaftingen E.
    J. Biol. Chem. 287:7246-7255(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiAT2L1_HUMAN
AccessioniPrimary (citable) accession number: Q8TBG4
Secondary accession number(s): B7Z1Y0, E9PBY0, Q9H174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2002
Last modified: April 29, 2015
This is version 106 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

Caution

Does not seem to possess aminotransferase activity.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.