Q9ULI2 (RIMKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-citryl-glutamate synthase B
EC=6.3.2.n6

Alternative name(s):
N-acetyl-aspartyl-glutamate synthetase B
Short name=NAAG synthetase B
Short name=NAAGS
EC=6.3.2.n6
Ribosomal protein S6 modification-like protein B

Gene names

Name:	RIMKLB
Synonyms:	FAM80B, KIAA1238

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the synthesis of beta-citryl-glutamate and N-acetyl-aspartyl-glutamate. Beta-citryl-glutamate is synthesized more efficiently than N-acetyl-aspartyl-glutamate By similarity.
Catalytic activity	ATP + citrate + L-glutamate = ADP + phosphate + beta-citryl-L-glutamate. ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetylaspartyl-glutamate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	N-acetylaspartyl-glutamate (NAAG) is the most abundant dipeptide present in vertebrate central nervous system (CNS). Beta-citryl-L-glutamate, a structural analog of NAAG, is present in testis and immature brain By similarity.
Sequence similarities	Belongs to the RimK family. Contains 1 ATP-grasp domain.
Sequence caution	The sequence BAA86552.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyl-L-aspartate-L-glutamate ligase activity Inferred from sequence or structural similarity. Source: UniProtKB acid-amino acid ligase activity Inferred from electronic annotation. Source: EC citrate-L-glutamate ligase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9ULI2-1)

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.

Isoform 2 (identifier: Q9ULI2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     282-307: VGFIAFDKACNLDVAGIIADYAASLL → PFQEPKKQIQTNKKIPREKTFLLPPS
     308-386: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 386	386	Beta-citryl-glutamate synthase B		PRO_0000282571
Regions
	Domain	119 – 304	186	ATP-grasp
	Nucleotide binding	193 – 203	11	ATP By similarity
Sites
	Metal binding	264	1	Magnesium or manganese 1 By similarity
	Metal binding	277	1	Magnesium or manganese 1 By similarity
	Metal binding	277	1	Magnesium or manganese 2 By similarity
	Metal binding	279	1	Magnesium or manganese 2 By similarity
	Binding site	158	1	ATP By similarity
	Binding site	219	1	ATP By similarity
Natural variations
	Alternative sequence	282 – 307	26	VGFIA…AASLL → PFQEPKKQIQTNKKIPREKT FLLPPS in isoform 2.		VSP_024198
	Alternative sequence	308 – 386	79	Missing in isoform 2.		VSP_024199

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: D9C0D47A831AD9D2	FASTA	386	42,464
	10 20 30 40 50 60 MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEVV LTIEQGNLGL 70 80 90 100 110 120 RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ 130 140 150 160 170 180 ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL 190 200 210 220 230 240 SHLIRHEAPY LFQKYVKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS 250 260 270 280 290 300 LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA 310 320 330 340 350 360 DYAASLLPSG RLTRRMSLLS VVSTASETSE PELGPPASTA VDNMSASSSS VDSDPESTER 370 380 ELLTKLPGGL FNMNQLLANE IKLLVD
	Isoform 2 [UniParc]. Checksum: 2725103A1A5D627B	FASTA	307	34,557
	10 20 30 40 50 60 MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEVV LTIEQGNLGL 70 80 90 100 110 120 RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ 130 140 150 160 170 180 ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL 190 200 210 220 230 240 SHLIRHEAPY LFQKYVKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS 250 260 270 280 290 300 LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFCVCEANA NPFQEPKKQI QTNKKIPREK TFLLPPS

References

[1]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[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] (ISOFORM 1). Tissue: Testis.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-386 (ISOFORM 1). Tissue: Cervix and Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB033064 mRNA. Translation: BAA86552.1. Different initiation. AK302847 mRNA. Translation: BAH13820.1. CH471116 Genomic DNA. Translation: EAW88610.1. CH471116 Genomic DNA. Translation: EAW88611.1. BC021977 mRNA. Translation: AAH21977.2. BC033793 mRNA. Translation: AAH33793.1.
IPI	IPI00008121. IPI00166734.
RefSeq	NP_065785.2. NM_020734.2.
UniGene	Hs.504670.
3D structure databases
ProteinModelPortal	Q9ULI2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ULI2. 1 interaction.
STRING	9606.ENSP00000350136.
PTM databases
PhosphoSite	Q9ULI2.
Polymorphism databases
DMDM	143458798.
Proteomic databases
PaxDb	Q9ULI2.
PRIDE	Q9ULI2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357529; ENSP00000350136; ENSG00000166532. ENST00000535829; ENSP00000445863; ENSG00000166532. ENST00000538135; ENSP00000440943; ENSG00000166532. ENST00000544257; ENSP00000438004; ENSG00000166532.
GeneID	57494.
KEGG	hsa:57494.
UCSC	uc001quw.2. human. uc001qux.2. human.
Organism-specific databases
CTD	57494.
GeneCards	GC12P008851.
HGNC	HGNC:29228. RIMKLB.
MIM	614054. gene.
neXtProt	NX_Q9ULI2.
PharmGKB	PA164725354.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0189.
HOGENOM	HOG000043112.
HOVERGEN	HBG108408.
InParanoid	Q9ULI2.
OMA	IAFDQAC.
OrthoDB	EOG49S66M.
PhylomeDB	Q9ULI2.
Gene expression databases
ArrayExpress	Q9ULI2.
Bgee	Q9ULI2.
CleanEx	HS_RIMKLB.
Genevestigator	Q9ULI2.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit.
InterPro	IPR011761. 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]
Pfam	PF08443. RimK. 1 hit. [Graphical view]
TIGRFAMs	TIGR00768. rimK_fam. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RIMKLB. human.
GenomeRNAi	57494.
NextBio	63798.
SOURCE	Search...

Entry information

Entry name

RIMKB_HUMAN

Accession

Primary (citable) accession number: Q9ULI2
Secondary accession number(s): B7Z834 , D3DUV2, Q8N4P4, Q8WTW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.