GenomeNet

Database: UniProt
Entry: Q8IXN7
LinkDB: Q8IXN7
Original site: Q8IXN7 
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   13-FEB-2019, entry version 145.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
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   [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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the synthesis of N-acetyl-L-aspartyl-L-
CC       glutamate (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(+) +
CC         N-acetyl-L-aspartyl-L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:40035, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:76931, 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
CC         H(+) + 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.
CC       {ECO:0000250};
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
CC       (CNS). {ECO:0000250|UniProtKB:Q6PFX8}.
CC   -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH39737.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Hs.420244; -.
DR   ProteinModelPortal; Q8IXN7; -.
DR   SMR; Q8IXN7; -.
DR   BioGrid; 129940; 3.
DR   STRING; 9606.ENSP00000414330; -.
DR   iPTMnet; Q8IXN7; -.
DR   PhosphoSitePlus; Q8IXN7; -.
DR   BioMuta; RIMKLA; -.
DR   DMDM; 143458650; -.
DR   jPOST; Q8IXN7; -.
DR   PaxDb; Q8IXN7; -.
DR   PeptideAtlas; Q8IXN7; -.
DR   PRIDE; Q8IXN7; -.
DR   ProteomicsDB; 71034; -.
DR   DNASU; 284716; -.
DR   Ensembl; ENST00000431473; ENSP00000414330; ENSG00000177181.
DR   GeneID; 284716; -.
DR   KEGG; hsa:284716; -.
DR   UCSC; uc001chi.3; human.
DR   CTD; 284716; -.
DR   EuPathDB; HostDB:ENSG00000177181.14; -.
DR   GeneCards; RIMKLA; -.
DR   HGNC; HGNC:28725; RIMKLA.
DR   HPA; HPA027826; -.
DR   neXtProt; NX_Q8IXN7; -.
DR   OpenTargets; ENSG00000177181; -.
DR   PharmGKB; PA164725339; -.
DR   eggNOG; ENOG410IGDC; Eukaryota.
DR   eggNOG; COG0189; LUCA.
DR   GeneTree; ENSGT00390000014577; -.
DR   HOGENOM; HOG000043112; -.
DR   HOVERGEN; HBG108408; -.
DR   InParanoid; Q8IXN7; -.
DR   KO; K18311; -.
DR   OMA; VYTINNG; -.
DR   OrthoDB; 753616at2759; -.
DR   PhylomeDB; Q8IXN7; -.
DR   TreeFam; TF332035; -.
DR   Reactome; R-HSA-70614; Amino acid synthesis and interconversion (transamination).
DR   GenomeRNAi; 284716; -.
DR   PRO; PR:Q8IXN7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000177181; Expressed in 115 organ(s), highest expression level in secondary oocyte.
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: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:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    391       N-acetylaspartylglutamate synthase A.
FT                                /FTId=PRO_0000282568.
FT   DOMAIN      115    300       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     189    199       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       260    260       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       273    273       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       273    273       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       275    275       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   BINDING     154    154       ATP. {ECO:0000250}.
FT   BINDING     215    215       ATP. {ECO:0000250}.
FT   MOD_RES     319    319       Phosphoserine.
FT                                {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
//
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