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Q9ULI2

- RIMKB_HUMAN

UniProt

Q9ULI2 - RIMKB_HUMAN

Protein

Beta-citrylglutamate synthase B

Gene

RIMKLB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate By similarity.By similarity

    Catalytic activityi

    ATP + citrate + L-glutamate = ADP + phosphate + beta-citryl-L-glutamate.
    ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate.

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei158 – 1581ATPBy similarity
    Binding sitei219 – 2191ATPBy similarity
    Metal bindingi264 – 2641Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi277 – 2771Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi277 – 2771Magnesium or manganese 2PROSITE-ProRule annotation
    Metal bindingi279 – 2791Magnesium or manganese 2PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 20311ATPPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. citrate-L-glutamate ligase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. N-acetyl-L-aspartate-L-glutamate ligase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-citrylglutamate synthase B (EC:6.3.1.17)
    Alternative name(s):
    N-acetyl-aspartylglutamate synthetase B (EC:6.3.2.41)
    Short name:
    NAAG synthetase B
    Short name:
    NAAGS
    Ribosomal protein S6 modification-like protein B
    Gene namesi
    Name:RIMKLB
    Synonyms:FAM80B, KIAA1238
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:29228. RIMKLB.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164725354.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386Beta-citrylglutamate synthase BPRO_0000282571Add
    BLAST

    Proteomic databases

    MaxQBiQ9ULI2.
    PaxDbiQ9ULI2.
    PRIDEiQ9ULI2.

    PTM databases

    PhosphoSiteiQ9ULI2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ULI2.
    BgeeiQ9ULI2.
    CleanExiHS_RIMKLB.
    GenevestigatoriQ9ULI2.

    Organism-specific databases

    HPAiHPA056344.
    HPA059552.

    Interactioni

    Protein-protein interaction databases

    BioGridi121561. 2 interactions.
    IntActiQ9ULI2. 1 interaction.
    STRINGi9606.ENSP00000350136.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULI2.
    SMRiQ9ULI2. Positions 92-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini119 – 304186ATP-graspPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0189.
    HOGENOMiHOG000043112.
    HOVERGENiHBG108408.
    InParanoidiQ9ULI2.
    KOiK18310.
    OMAiTSYPQVV.
    OrthoDBiEOG7GBFWX.
    PhylomeDBiQ9ULI2.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ULI2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEVV    50
    LTIEQGNLGL RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC 100
    RLMNRPQAIL NCVNKFWTFQ ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV 150
    LEFPMVVKNT RGHRGKAVFL ARDKHHLADL SHLIRHEAPY LFQKYVKESH 200
    GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS LSEQGKQLAI 250
    QVSNILGMDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA 300
    DYAASLLPSG RLTRRMSLLS VVSTASETSE PELGPPASTA VDNMSASSSS 350
    VDSDPESTER ELLTKLPGGL FNMNQLLANE IKLLVD 386
    Length:386
    Mass (Da):42,464
    Last modified:April 3, 2007 - v2
    Checksum:iD9C0D47A831AD9D2
    GO
    Isoform 2 (identifier: Q9ULI2-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:307
    Mass (Da):34,557
    Checksum:i2725103A1A5D627B
    GO

    Sequence cautioni

    The sequence BAA86552.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei282 – 30726VGFIA…AASLL → PFQEPKKQIQTNKKIPREKT FLLPPS in isoform 2. 1 PublicationVSP_024198Add
    BLAST
    Alternative sequencei308 – 38679Missing in isoform 2. 1 PublicationVSP_024199Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41748.1. [Q9ULI2-1]
    RefSeqiNP_065785.2. NM_020734.2. [Q9ULI2-1]
    XP_006719179.1. XM_006719116.1. [Q9ULI2-1]
    XP_006719180.1. XM_006719117.1. [Q9ULI2-1]
    XP_006719181.1. XM_006719118.1. [Q9ULI2-1]
    XP_006719182.1. XM_006719119.1. [Q9ULI2-1]
    XP_006719183.1. XM_006719120.1. [Q9ULI2-1]
    XP_006719184.1. XM_006719121.1. [Q9ULI2-1]
    XP_006719185.1. XM_006719122.1. [Q9ULI2-1]
    XP_006719186.1. XM_006719123.1. [Q9ULI2-1]
    XP_006719187.1. XM_006719124.1. [Q9ULI2-1]
    XP_006719188.1. XM_006719125.1. [Q9ULI2-2]
    XP_006719189.1. XM_006719126.1. [Q9ULI2-2]
    XP_006719190.1. XM_006719127.1. [Q9ULI2-2]
    UniGeneiHs.504670.

    Genome annotation databases

    EnsembliENST00000357529; ENSP00000350136; ENSG00000166532. [Q9ULI2-1]
    ENST00000535829; ENSP00000445863; ENSG00000166532. [Q9ULI2-1]
    ENST00000538135; ENSP00000440943; ENSG00000166532. [Q9ULI2-1]
    ENST00000544257; ENSP00000438004; ENSG00000166532. [Q9ULI2-2]
    GeneIDi57494.
    KEGGihsa:57494.
    UCSCiuc001quw.2. human. [Q9ULI2-2]
    uc001qux.2. human. [Q9ULI2-1]

    Polymorphism databases

    DMDMi143458798.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41748.1. [Q9ULI2-1 ]
    RefSeqi NP_065785.2. NM_020734.2. [Q9ULI2-1 ]
    XP_006719179.1. XM_006719116.1. [Q9ULI2-1 ]
    XP_006719180.1. XM_006719117.1. [Q9ULI2-1 ]
    XP_006719181.1. XM_006719118.1. [Q9ULI2-1 ]
    XP_006719182.1. XM_006719119.1. [Q9ULI2-1 ]
    XP_006719183.1. XM_006719120.1. [Q9ULI2-1 ]
    XP_006719184.1. XM_006719121.1. [Q9ULI2-1 ]
    XP_006719185.1. XM_006719122.1. [Q9ULI2-1 ]
    XP_006719186.1. XM_006719123.1. [Q9ULI2-1 ]
    XP_006719187.1. XM_006719124.1. [Q9ULI2-1 ]
    XP_006719188.1. XM_006719125.1. [Q9ULI2-2 ]
    XP_006719189.1. XM_006719126.1. [Q9ULI2-2 ]
    XP_006719190.1. XM_006719127.1. [Q9ULI2-2 ]
    UniGenei Hs.504670.

    3D structure databases

    ProteinModelPortali Q9ULI2.
    SMRi Q9ULI2. Positions 92-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121561. 2 interactions.
    IntActi Q9ULI2. 1 interaction.
    STRINGi 9606.ENSP00000350136.

    PTM databases

    PhosphoSitei Q9ULI2.

    Polymorphism databases

    DMDMi 143458798.

    Proteomic databases

    MaxQBi Q9ULI2.
    PaxDbi Q9ULI2.
    PRIDEi Q9ULI2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357529 ; ENSP00000350136 ; ENSG00000166532 . [Q9ULI2-1 ]
    ENST00000535829 ; ENSP00000445863 ; ENSG00000166532 . [Q9ULI2-1 ]
    ENST00000538135 ; ENSP00000440943 ; ENSG00000166532 . [Q9ULI2-1 ]
    ENST00000544257 ; ENSP00000438004 ; ENSG00000166532 . [Q9ULI2-2 ]
    GeneIDi 57494.
    KEGGi hsa:57494.
    UCSCi uc001quw.2. human. [Q9ULI2-2 ]
    uc001qux.2. human. [Q9ULI2-1 ]

    Organism-specific databases

    CTDi 57494.
    GeneCardsi GC12P008851.
    HGNCi HGNC:29228. RIMKLB.
    HPAi HPA056344.
    HPA059552.
    MIMi 614054. gene.
    neXtProti NX_Q9ULI2.
    PharmGKBi PA164725354.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0189.
    HOGENOMi HOG000043112.
    HOVERGENi HBG108408.
    InParanoidi Q9ULI2.
    KOi K18310.
    OMAi TSYPQVV.
    OrthoDBi EOG7GBFWX.
    PhylomeDBi Q9ULI2.
    TreeFami TF332035.

    Miscellaneous databases

    ChiTaRSi RIMKLB. human.
    GenomeRNAii 57494.
    NextBioi 63798.
    PROi Q9ULI2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULI2.
    Bgeei Q9ULI2.
    CleanExi HS_RIMKLB.
    Genevestigatori Q9ULI2.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProi 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 ]
    Pfami PF08443. RimK. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00768. rimK_fam. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiRIMKB_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULI2
    Secondary accession number(s): B7Z834
    , D3DUV2, Q8N4P4, Q8WTW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 92 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). Beta-citryl-L-glutamate, a structural analog of NAAG, is present in testis and immature brain By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3