ID RIMKB_HUMAN Reviewed; 386 AA. AC Q9ULI2; B7Z834; D3DUV2; Q8N4P4; Q8WTW6; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 24-JAN-2024, entry version 149. DE RecName: Full=Beta-citrylglutamate synthase B; DE EC=6.3.1.17 {ECO:0000250|UniProtKB:Q80WS1}; DE AltName: Full=N-acetyl-aspartylglutamate synthetase B; DE Short=NAAG synthetase B; DE Short=NAAGS; DE EC=6.3.2.41 {ECO:0000250|UniProtKB:Q80WS1}; DE AltName: Full=Ribosomal protein S6 modification-like protein B; GN Name=RIMKLB; Synonyms=FAM80B, KIAA1238; 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 MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 151-386 (ISOFORM 1). RC TISSUE=Cervix, and Ovary; 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 beta-citryl-L-glutamate and N- CC acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized CC more efficiently than N-acetyl-L-aspartyl-L-glutamate. CC {ECO:0000250|UniProtKB:Q80WS1}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + citrate + L-glutamate = ADP + beta-citrylglutamate + CC H(+) + phosphate; Xref=Rhea:RHEA:40043, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16947, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76942, ChEBI:CHEBI:456216; CC EC=6.3.1.17; Evidence={ECO:0000250|UniProtKB:Q80WS1}; 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:Q80WS1}; 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9ULI2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ULI2-2; Sequence=VSP_024198, VSP_024199; CC -!- MISCELLANEOUS: N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most CC abundant dipeptide present in vertebrate central nervous system (CNS). CC Beta-citryl-L-glutamate, a structural analog of NAAG, is present in CC testis and immature brain. {ECO:0000250|UniProtKB:Q80WS1}. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86552.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB033064; BAA86552.1; ALT_INIT; mRNA. DR EMBL; AK302847; BAH13820.1; -; mRNA. DR EMBL; CH471116; EAW88610.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88611.1; -; Genomic_DNA. DR EMBL; BC021977; AAH21977.2; -; mRNA. DR EMBL; BC033793; AAH33793.1; -; mRNA. DR CCDS; CCDS41748.1; -. [Q9ULI2-1] DR RefSeq; NP_001284705.1; NM_001297776.1. [Q9ULI2-1] DR RefSeq; NP_065785.2; NM_020734.3. [Q9ULI2-1] DR RefSeq; XP_006719181.1; XM_006719118.2. DR RefSeq; XP_006719190.1; XM_006719127.2. DR RefSeq; XP_011519078.1; XM_011520776.1. DR RefSeq; XP_011519079.1; XM_011520777.1. DR RefSeq; XP_011519080.1; XM_011520778.2. DR RefSeq; XP_011519081.1; XM_011520779.2. DR RefSeq; XP_011519082.1; XM_011520780.1. DR RefSeq; XP_011519085.1; XM_011520783.1. DR RefSeq; XP_011519092.1; XM_011520790.1. DR RefSeq; XP_016875166.1; XM_017019677.1. DR RefSeq; XP_016875167.1; XM_017019678.1. DR RefSeq; XP_016875168.1; XM_017019679.1. DR RefSeq; XP_016875169.1; XM_017019680.1. DR RefSeq; XP_016875171.1; XM_017019682.1. DR RefSeq; XP_016875172.1; XM_017019683.1. DR RefSeq; XP_016875173.1; XM_017019684.1. [Q9ULI2-1] DR RefSeq; XP_016875174.1; XM_017019685.1. DR RefSeq; XP_016875175.1; XM_017019686.1. [Q9ULI2-1] DR RefSeq; XP_016875176.1; XM_017019687.1. [Q9ULI2-1] DR RefSeq; XP_016875177.1; XM_017019688.1. DR RefSeq; XP_016875178.1; XM_017019689.1. DR RefSeq; XP_016875179.1; XM_017019690.1. DR RefSeq; XP_016875180.1; XM_017019691.1. DR RefSeq; XP_016875181.1; XM_017019692.1. DR RefSeq; XP_016875182.1; XM_017019693.1. DR RefSeq; XP_016875183.1; XM_017019694.1. DR RefSeq; XP_016875184.1; XM_017019695.1. DR RefSeq; XP_016875185.1; XM_017019696.1. DR RefSeq; XP_016875186.1; XM_017019697.1. DR AlphaFoldDB; Q9ULI2; -. DR SMR; Q9ULI2; -. DR BioGRID; 121561; 7. DR IntAct; Q9ULI2; 3. DR STRING; 9606.ENSP00000350136; -. DR iPTMnet; Q9ULI2; -. DR PhosphoSitePlus; Q9ULI2; -. DR BioMuta; RIMKLB; -. DR DMDM; 143458798; -. DR EPD; Q9ULI2; -. DR jPOST; Q9ULI2; -. DR MassIVE; Q9ULI2; -. DR MaxQB; Q9ULI2; -. DR PaxDb; 9606-ENSP00000350136; -. DR PeptideAtlas; Q9ULI2; -. DR ProteomicsDB; 85035; -. [Q9ULI2-1] DR ProteomicsDB; 85036; -. [Q9ULI2-2] DR Pumba; Q9ULI2; -. DR Antibodypedia; 23082; 88 antibodies from 21 providers. DR DNASU; 57494; -. DR Ensembl; ENST00000357529.7; ENSP00000350136.3; ENSG00000166532.16. [Q9ULI2-1] DR Ensembl; ENST00000535829.6; ENSP00000445863.1; ENSG00000166532.16. [Q9ULI2-1] DR Ensembl; ENST00000538135.5; ENSP00000440943.1; ENSG00000166532.16. [Q9ULI2-1] DR Ensembl; ENST00000544257.5; ENSP00000438004.1; ENSG00000166532.16. [Q9ULI2-2] DR Ensembl; ENST00000619374.4; ENSP00000483871.1; ENSG00000166532.16. [Q9ULI2-2] DR GeneID; 57494; -. DR KEGG; hsa:57494; -. DR MANE-Select; ENST00000535829.6; ENSP00000445863.1; NM_001297776.2; NP_001284705.1. DR UCSC; uc001qux.2; human. [Q9ULI2-1] DR AGR; HGNC:29228; -. DR CTD; 57494; -. DR DisGeNET; 57494; -. DR GeneCards; RIMKLB; -. DR HGNC; HGNC:29228; RIMKLB. DR HPA; ENSG00000166532; Low tissue specificity. DR MIM; 614054; gene. DR neXtProt; NX_Q9ULI2; -. DR OpenTargets; ENSG00000166532; -. DR PharmGKB; PA164725354; -. DR VEuPathDB; HostDB:ENSG00000166532; -. DR eggNOG; ENOG502QT4M; Eukaryota. DR GeneTree; ENSGT00390000014577; -. DR HOGENOM; CLU_054353_3_0_1; -. DR InParanoid; Q9ULI2; -. DR OMA; DAAYNFN; -. DR OrthoDB; 4026633at2759; -. DR PhylomeDB; Q9ULI2; -. DR TreeFam; TF332035; -. DR PathwayCommons; Q9ULI2; -. DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism. DR SignaLink; Q9ULI2; -. DR BioGRID-ORCS; 57494; 22 hits in 1151 CRISPR screens. DR ChiTaRS; RIMKLB; human. DR GenomeRNAi; 57494; -. DR Pharos; Q9ULI2; Tbio. DR PRO; PR:Q9ULI2; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9ULI2; Protein. DR Bgee; ENSG00000166532; Expressed in oviduct epithelium and 177 other cell types or tissues. DR ExpressionAtlas; Q9ULI2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0072591; F:citrate-L-glutamate ligase activity; ISS:UniProtKB. 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 GO; GO:0036211; P:protein modification process; IEA:InterPro. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX. DR NCBIfam; TIGR00768; rimK_fam; 1. DR PANTHER; PTHR21621:SF5; BETA-CITRYLGLUTAMATE SYNTHASE B; 1. DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1. DR Pfam; PF08443; RimK; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR Genevisible; Q9ULI2; HS. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..386 FT /note="Beta-citrylglutamate synthase B" FT /id="PRO_0000282571" FT DOMAIN 119..304 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT REGION 325..359 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 158 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 193..203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 264 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 264 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 277 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 277 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 277 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 277 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 279 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 279 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT VAR_SEQ 282..307 FT /note="VGFIAFDKACNLDVAGIIADYAASLL -> PFQEPKKQIQTNKKIPREKTFL FT LPPS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024198" FT VAR_SEQ 308..386 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024199" SQ SEQUENCE 386 AA; 42464 MW; D9C0D47A831AD9D2 CRC64; MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEVV LTIEQGNLGL RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL SHLIRHEAPY LFQKYVKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA DYAASLLPSG RLTRRMSLLS VVSTASETSE PELGPPASTA VDNMSASSSS VDSDPESTER ELLTKLPGGL FNMNQLLANE IKLLVD //