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GLYL1_HUMAN
ID   GLYL1_HUMAN             Reviewed;         302 AA.
AC   Q969I3; A6NDT0; Q7Z510; Q8NAW8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Glycine N-acyltransferase-like protein 1 {ECO:0000305};
DE            EC=2.3.1.68 {ECO:0000269|PubMed:22475485};
DE   AltName: Full=Acyl-CoA:glycine N-acyltransferase-like protein 1;
DE   AltName: Full=Glutamine N-acyltransferase;
GN   Name=GLYATL1 {ECO:0000312|HGNC:HGNC:30519}; Synonyms=GNAT;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RA   Zhang H., Qu Y., Lang Q., Li J., Zhong Z., Xie F., Ye G., Wan B., Yu L.;
RT   "Molecular cloning and characterization of a novel human glycine-n-
RT   acyltransferase gene GLYATL1, which activates transcriptional activity of
RT   HSE pathway.";
RL   Int. J. Mol. Sci. 8:433-444(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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 [MRNA] OF 1-159.
RA   Cui W.C., Yu L., Gong R.M., Chu J.H., Yu Y.F., Zhao S.Y.;
RT   "Cloning of a new human cDNA homology to human putative glycine-N-
RT   acyltransferase mRNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22475485; DOI=10.1016/j.bbrc.2012.03.099;
RA   Matsuo M., Terai K., Kameda N., Matsumoto A., Kurokawa Y., Funase Y.,
RA   Nishikawa K., Sugaya N., Hiruta N., Kishimoto T.;
RT   "Designation of enzyme activity of glycine-N-acyltransferase family genes
RT   and depression of glycine-N-acyltransferase in human hepatocellular
RT   carcinoma.";
RL   Biochem. Biophys. Res. Commun. 420:901-906(2012).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Acyltransferase which transfers an acyl group to the N-
CC       terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor.
CC       {ECO:0000269|PubMed:22475485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + L-glutamine = an N(2)-acyl-L-glutamine + CoA +
CC         H(+); Xref=Rhea:RHEA:18469, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:58359, ChEBI:CHEBI:87584; EC=2.3.1.68;
CC         Evidence={ECO:0000269|PubMed:22475485};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q969I3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q969I3-2; Sequence=VSP_024076;
CC   -!- TISSUE SPECIFICITY: Expressed in liver and kidney and, at lower levels,
CC       in pancreas, testis, ovary and stomach. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ084381; AAZ31239.1; -; mRNA.
DR   EMBL; AK055818; BAB71023.1; -; mRNA.
DR   EMBL; AK091965; BAC03779.1; -; mRNA.
DR   EMBL; AP001652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC008353; AAH08353.1; -; mRNA.
DR   EMBL; AF087878; AAP97178.1; -; mRNA.
DR   CCDS; CCDS31556.1; -. [Q969I3-2]
DR   CCDS; CCDS55768.1; -. [Q969I3-1]
DR   RefSeq; NP_001207423.1; NM_001220494.2. [Q969I3-1]
DR   RefSeq; NP_001207425.1; NM_001220496.2. [Q969I3-1]
DR   RefSeq; NP_542392.2; NM_080661.4. [Q969I3-2]
DR   AlphaFoldDB; Q969I3; -.
DR   SMR; Q969I3; -.
DR   BioGRID; 124929; 4.
DR   STRING; 9606.ENSP00000300079; -.
DR   DrugBank; DB00145; Glycine.
DR   iPTMnet; Q969I3; -.
DR   PhosphoSitePlus; Q969I3; -.
DR   BioMuta; GLYATL1; -.
DR   DMDM; 74731045; -.
DR   EPD; Q969I3; -.
DR   MassIVE; Q969I3; -.
DR   MaxQB; Q969I3; -.
DR   PaxDb; Q969I3; -.
DR   PeptideAtlas; Q969I3; -.
DR   PRIDE; Q969I3; -.
DR   ProteomicsDB; 75769; -. [Q969I3-1]
DR   ProteomicsDB; 75770; -. [Q969I3-2]
DR   Antibodypedia; 27696; 80 antibodies from 23 providers.
DR   DNASU; 92292; -.
DR   Ensembl; ENST00000300079.9; ENSP00000300079.5; ENSG00000166840.14. [Q969I3-2]
DR   Ensembl; ENST00000317391.8; ENSP00000322223.4; ENSG00000166840.14. [Q969I3-1]
DR   Ensembl; ENST00000532726.6; ENSP00000436116.2; ENSG00000166840.14. [Q969I3-1]
DR   Ensembl; ENST00000612196.1; ENSP00000479741.1; ENSG00000166840.14. [Q969I3-1]
DR   GeneID; 92292; -.
DR   KEGG; hsa:92292; -.
DR   MANE-Select; ENST00000532726.6; ENSP00000436116.2; NM_001389712.2; NP_001376641.1.
DR   UCSC; uc001nnf.4; human. [Q969I3-1]
DR   CTD; 92292; -.
DR   DisGeNET; 92292; -.
DR   GeneCards; GLYATL1; -.
DR   HGNC; HGNC:30519; GLYATL1.
DR   HPA; ENSG00000166840; Tissue enriched (liver).
DR   MIM; 614761; gene.
DR   neXtProt; NX_Q969I3; -.
DR   OpenTargets; ENSG00000166840; -.
DR   PharmGKB; PA142671727; -.
DR   VEuPathDB; HostDB:ENSG00000166840; -.
DR   eggNOG; ENOG502QVT5; Eukaryota.
DR   GeneTree; ENSGT00950000183133; -.
DR   HOGENOM; CLU_060336_0_0_1; -.
DR   InParanoid; Q969I3; -.
DR   OMA; FNAMPCD; -.
DR   OrthoDB; 1221333at2759; -.
DR   PhylomeDB; Q969I3; -.
DR   TreeFam; TF353258; -.
DR   BRENDA; 2.3.1.13; 2681.
DR   BRENDA; 2.3.1.68; 2681.
DR   PathwayCommons; Q969I3; -.
DR   Reactome; R-HSA-177128; Conjugation of salicylate with glycine.
DR   Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 92292; 18 hits in 1067 CRISPR screens.
DR   ChiTaRS; GLYATL1; human.
DR   GenomeRNAi; 92292; -.
DR   Pharos; Q969I3; Tbio.
DR   PRO; PR:Q969I3; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q969I3; protein.
DR   Bgee; ENSG00000166840; Expressed in kidney epithelium and 105 other tissues.
DR   ExpressionAtlas; Q969I3; baseline and differential.
DR   Genevisible; Q969I3; HS.
DR   GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR   GO; GO:0047946; F:glutamine N-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0047961; F:glycine N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IDA:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR010313; Glycine_N-acyltransferase.
DR   InterPro; IPR013652; Glycine_N-acyltransferase_C.
DR   InterPro; IPR015938; Glycine_N-acyltransferase_N.
DR   PANTHER; PTHR15298; PTHR15298; 1.
DR   Pfam; PF08444; Gly_acyl_tr_C; 1.
DR   Pfam; PF06021; Gly_acyl_tr_N; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Reference proteome; Transferase.
FT   CHAIN           1..302
FT                   /note="Glycine N-acyltransferase-like protein 1"
FT                   /id="PRO_0000281874"
FT   VAR_SEQ         1..24
FT                   /note="MILLNNSHKLLALYKSLARSIPES -> MFKLCSNKMVSQEGSEVELLVSPG
FT                   ARSEHGRYLQDPIVSIDLSEWLRIIEFLLQG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_024076"
SQ   SEQUENCE   302 AA;  35101 MW;  D6E7513A9B8769B0 CRC64;
     MILLNNSHKL LALYKSLARS IPESLKVYGS VYHINHGNPF NMEVLVDSWP EYQMVIIRPQ
     KQEMTDDMDS YTNVYRMFSK EPQKSEEVLK NCEIVNWKQR LQIQGLQESL GEGIRVATFS
     KSVKVEHSRA LLLVTEDILK LNASSKSKLG SWAETGHPDD EFESETPNFK YAQLDVSYSG
     LVNDNWKRGK NERSLHYIKR CIEDLPAACM LGPEGVPVSW VTMDPSCEVG MAYSMEKYRR
     TGNMARVMVR YMKYLRQKNI PFYISVLEEN EDSRRFVGQF GFFEASCEWH QWTCYPQNLV
     PF
 
 
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