RIMKB_HUMAN
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 03-AUG-2022, entry version 142.
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};
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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. [Q9ULI2-2]
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. [Q9ULI2-1]
DR RefSeq; XP_016875173.1; XM_017019684.1. [Q9ULI2-1]
DR RefSeq; XP_016875174.1; XM_017019685.1. [Q9ULI2-1]
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; 2.
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; Q9ULI2; -.
DR PeptideAtlas; Q9ULI2; -.
DR PRIDE; Q9ULI2; -.
DR ProteomicsDB; 85035; -. [Q9ULI2-1]
DR ProteomicsDB; 85036; -. [Q9ULI2-2]
DR Antibodypedia; 23082; 73 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 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; 753616at2759; -.
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; 20 hits in 1075 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 175 other tissues.
DR ExpressionAtlas; Q9ULI2; baseline and differential.
DR Genevisible; Q9ULI2; HS.
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: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 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
