RIMKA_HUMAN
ID RIMKA_HUMAN Reviewed; 391 AA.
AC Q8IXN7; Q5VUS5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=N-acetylaspartylglutamate synthase A;
DE Short=NAAG synthetase A;
DE Short=NAAGS;
DE EC=6.3.2.41 {ECO:0000250|UniProtKB:Q6PFX8};
DE AltName: Full=N-acetylaspartylglutamylglutamate synthase A;
DE EC=6.3.2.42 {ECO:0000250|UniProtKB:Q6PFX8};
DE AltName: Full=Ribosomal protein S6 modification-like protein A;
GN Name=RIMKLA; Synonyms=FAM80A;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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).
CC -!- FUNCTION: Catalyzes the synthesis of N-acetyl-L-aspartyl-L-glutamate
CC (NAAG) and N-acetyl-L-aspartyl-L-glutamyl-L-glutamate.
CC {ECO:0000250|UniProtKB:Q6PFX8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-
CC acetyl-L-aspartyl-L-glutamate + phosphate; Xref=Rhea:RHEA:40035,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931,
CC ChEBI:CHEBI:456216; EC=6.3.2.41;
CC Evidence={ECO:0000250|UniProtKB:Q6PFX8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 L-glutamate + N-acetyl-L-aspartate = 2 ADP + 2 H(+)
CC + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate + 2 phosphate;
CC Xref=Rhea:RHEA:40039, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:76935, ChEBI:CHEBI:456216; EC=6.3.2.42;
CC Evidence={ECO:0000250|UniProtKB:Q6PFX8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q8IXN7; P22607: FGFR3; NbExp=3; IntAct=EBI-21890191, EBI-348399;
CC Q8IXN7; P06396: GSN; NbExp=3; IntAct=EBI-21890191, EBI-351506;
CC Q8IXN7; P01112: HRAS; NbExp=3; IntAct=EBI-21890191, EBI-350145;
CC Q8IXN7; P42858: HTT; NbExp=3; IntAct=EBI-21890191, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most
CC abundant dipeptide present in vertebrate central nervous system (CNS).
CC {ECO:0000250|UniProtKB:Q6PFX8}.
CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39737.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL513331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039737; AAH39737.1; ALT_INIT; mRNA.
DR CCDS; CCDS466.2; -.
DR RefSeq; NP_775913.2; NM_173642.3.
DR AlphaFoldDB; Q8IXN7; -.
DR SMR; Q8IXN7; -.
DR BioGRID; 129940; 122.
DR IntAct; Q8IXN7; 7.
DR STRING; 9606.ENSP00000414330; -.
DR iPTMnet; Q8IXN7; -.
DR PhosphoSitePlus; Q8IXN7; -.
DR BioMuta; RIMKLA; -.
DR DMDM; 143458650; -.
DR jPOST; Q8IXN7; -.
DR MassIVE; Q8IXN7; -.
DR PaxDb; Q8IXN7; -.
DR PeptideAtlas; Q8IXN7; -.
DR PRIDE; Q8IXN7; -.
DR ProteomicsDB; 71034; -.
DR Antibodypedia; 32199; 95 antibodies from 20 providers.
DR DNASU; 284716; -.
DR Ensembl; ENST00000431473.4; ENSP00000414330.2; ENSG00000177181.15.
DR GeneID; 284716; -.
DR KEGG; hsa:284716; -.
DR MANE-Select; ENST00000431473.4; ENSP00000414330.2; NM_173642.4; NP_775913.2.
DR UCSC; uc001chi.3; human.
DR CTD; 284716; -.
DR GeneCards; RIMKLA; -.
DR HGNC; HGNC:28725; RIMKLA.
DR HPA; ENSG00000177181; Group enriched (brain, retina).
DR MIM; 618949; gene.
DR neXtProt; NX_Q8IXN7; -.
DR OpenTargets; ENSG00000177181; -.
DR PharmGKB; PA164725339; -.
DR VEuPathDB; HostDB:ENSG00000177181; -.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_1_1; -.
DR InParanoid; Q8IXN7; -.
DR OMA; TRGHQGK; -.
DR OrthoDB; 753616at2759; -.
DR PhylomeDB; Q8IXN7; -.
DR TreeFam; TF332035; -.
DR PathwayCommons; Q8IXN7; -.
DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
DR SignaLink; Q8IXN7; -.
DR BioGRID-ORCS; 284716; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; RIMKLA; human.
DR GenomeRNAi; 284716; -.
DR Pharos; Q8IXN7; Tdark.
DR PRO; PR:Q8IXN7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IXN7; protein.
DR Bgee; ENSG00000177181; Expressed in secondary oocyte and 130 other tissues.
DR ExpressionAtlas; Q8IXN7; baseline and differential.
DR Genevisible; Q8IXN7; HS.
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:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072590; F:N-acetyl-L-aspartate-L-glutamate ligase activity; ISS:UniProtKB.
DR GO; GO:0009064; P:glutamine family amino acid metabolic process; TAS:Reactome.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..391
FT /note="N-acetylaspartylglutamate synthase A"
FT /id="PRO_0000282568"
FT DOMAIN 115..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 341..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 189..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFX8"
SQ SEQUENCE 391 AA; 42864 MW; 8E78DFA4C0C89592 CRC64;
MCSQLWFLTD RRIREDYPQV QILRALRQRC SEQDVRFRAV LMDQIAVTIV GGHLGLQLNQ
KALTTFPDVV LVRVPTPSVQ SDSDITVLRH LEKLGCRLVN RPQSILNCIN KFWTFQELAG
HGVPMPDTFS YGGHEDFSKM IDEAEPLGYP VVVKSTRGHR GKAVFLARDK HHLSDICHLI
RHDVPYLFQK YVKESHGKDI RVVVVGGQVI GSMLRCSTDG RMQSNCSLGG VGVKCPLTEQ
GKQLAIQVSN ILGMDFCGID LLIMDDGSFV VCEANANVGF LAFDQACNLD VGGIIADYTM
SLLPNRQTGK MAVLPGLSSP REKNEPDGCA SAQGVAESVY TINSGSTSSE SEPELGEIRD
SSASTMGAPP SMLPEPGYNI NNRIASELKL K
