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Protein

N-acetylaspartylglutamate synthase A

Gene

RIMKLA

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

Functioni

Catalyzes the synthesis of N-acetyl-L-aspartyl-L-glutamate (NAAG) and N-acetyl-L-aspartyl-L-glutamyl-L-glutamate.By similarity

Catalytic activityi

ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate.By similarity
2 ATP + N-acetyl-L-aspartate + 2 L-glutamate = 2 ADP + 2 phosphate + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541ATPBy similarity
Binding sitei215 – 2151ATPBy similarity
Metal bindingi260 – 2601Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi273 – 2731Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi273 – 2731Magnesium or manganese 2PROSITE-ProRule annotation
Metal bindingi275 – 2751Magnesium or manganese 2PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 19911ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylaspartylglutamate synthase A (EC:6.3.2.41By similarity)
Short name:
NAAG synthetase A
Short name:
NAAGS
Alternative name(s):
N-acetylaspartylglutamylglutamate synthase A (EC:6.3.2.42By similarity)
Ribosomal protein S6 modification-like protein A
Gene namesi
Name:RIMKLA
Synonyms:FAM80A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28725. RIMKLA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164725339.

Polymorphism and mutation databases

BioMutaiRIMKLA.
DMDMi143458650.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391N-acetylaspartylglutamate synthase APRO_0000282568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei319 – 3191PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8IXN7.
PRIDEiQ8IXN7.

PTM databases

iPTMnetiQ8IXN7.
PhosphoSiteiQ8IXN7.

Expressioni

Gene expression databases

BgeeiQ8IXN7.
CleanExiHS_RIMKLA.
ExpressionAtlasiQ8IXN7. baseline and differential.
GenevisibleiQ8IXN7. HS.

Organism-specific databases

HPAiHPA027826.

Interactioni

Protein-protein interaction databases

BioGridi129940. 3 interactions.
STRINGi9606.ENSP00000414330.

Structurei

3D structure databases

ProteinModelPortaliQ8IXN7.
SMRiQ8IXN7. Positions 88-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 300186ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RimK family.Curated
Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IGDC. Eukaryota.
COG0189. LUCA.
GeneTreeiENSGT00390000014577.
HOGENOMiHOG000043112.
HOVERGENiHBG108408.
InParanoidiQ8IXN7.
KOiK18311.
OMAiCHLVRHD.
OrthoDBiEOG7GBFWX.
PhylomeDBiQ8IXN7.
TreeFamiTF332035.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013651. ATP-grasp_RimK-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
[Graphical view]
PfamiPF08443. RimK. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00768. rimK_fam. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IXN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCSQLWFLTD RRIREDYPQV QILRALRQRC SEQDVRFRAV LMDQIAVTIV
60 70 80 90 100
GGHLGLQLNQ KALTTFPDVV LVRVPTPSVQ SDSDITVLRH LEKLGCRLVN
110 120 130 140 150
RPQSILNCIN KFWTFQELAG HGVPMPDTFS YGGHEDFSKM IDEAEPLGYP
160 170 180 190 200
VVVKSTRGHR GKAVFLARDK HHLSDICHLI RHDVPYLFQK YVKESHGKDI
210 220 230 240 250
RVVVVGGQVI GSMLRCSTDG RMQSNCSLGG VGVKCPLTEQ GKQLAIQVSN
260 270 280 290 300
ILGMDFCGID LLIMDDGSFV VCEANANVGF LAFDQACNLD VGGIIADYTM
310 320 330 340 350
SLLPNRQTGK MAVLPGLSSP REKNEPDGCA SAQGVAESVY TINSGSTSSE
360 370 380 390
SEPELGEIRD SSASTMGAPP SMLPEPGYNI NNRIASELKL K
Length:391
Mass (Da):42,864
Last modified:April 3, 2007 - v2
Checksum:i8E78DFA4C0C89592
GO

Sequence cautioni

The sequence AAH39737.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH70661.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513331 Genomic DNA. Translation: CAH70659.2.
AL513331 Genomic DNA. Translation: CAH70661.1. Sequence problems.
BC039737 mRNA. Translation: AAH39737.1. Different initiation.
CCDSiCCDS466.2.
RefSeqiNP_775913.2. NM_173642.3.
UniGeneiHs.420244.

Genome annotation databases

EnsembliENST00000431473; ENSP00000414330; ENSG00000177181.
GeneIDi284716.
KEGGihsa:284716.
UCSCiuc001chi.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513331 Genomic DNA. Translation: CAH70659.2.
AL513331 Genomic DNA. Translation: CAH70661.1. Sequence problems.
BC039737 mRNA. Translation: AAH39737.1. Different initiation.
CCDSiCCDS466.2.
RefSeqiNP_775913.2. NM_173642.3.
UniGeneiHs.420244.

3D structure databases

ProteinModelPortaliQ8IXN7.
SMRiQ8IXN7. Positions 88-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129940. 3 interactions.
STRINGi9606.ENSP00000414330.

PTM databases

iPTMnetiQ8IXN7.
PhosphoSiteiQ8IXN7.

Polymorphism and mutation databases

BioMutaiRIMKLA.
DMDMi143458650.

Proteomic databases

PaxDbiQ8IXN7.
PRIDEiQ8IXN7.

Protocols and materials databases

DNASUi284716.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000431473; ENSP00000414330; ENSG00000177181.
GeneIDi284716.
KEGGihsa:284716.
UCSCiuc001chi.3. human.

Organism-specific databases

CTDi284716.
GeneCardsiRIMKLA.
HGNCiHGNC:28725. RIMKLA.
HPAiHPA027826.
neXtProtiNX_Q8IXN7.
PharmGKBiPA164725339.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGDC. Eukaryota.
COG0189. LUCA.
GeneTreeiENSGT00390000014577.
HOGENOMiHOG000043112.
HOVERGENiHBG108408.
InParanoidiQ8IXN7.
KOiK18311.
OMAiCHLVRHD.
OrthoDBiEOG7GBFWX.
PhylomeDBiQ8IXN7.
TreeFamiTF332035.

Miscellaneous databases

GenomeRNAii284716.
PROiQ8IXN7.

Gene expression databases

BgeeiQ8IXN7.
CleanExiHS_RIMKLA.
ExpressionAtlasiQ8IXN7. baseline and differential.
GenevisibleiQ8IXN7. HS.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013651. ATP-grasp_RimK-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
[Graphical view]
PfamiPF08443. RimK. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00768. rimK_fam. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
    Tissue: Pancreas.

Entry informationi

Entry nameiRIMKA_HUMAN
AccessioniPrimary (citable) accession number: Q8IXN7
Secondary accession number(s): Q5VUS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: June 8, 2016
This is version 124 of the entry and version 2 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

Miscellaneous

N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most abundant dipeptide present in vertebrate central nervous system (CNS).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.