Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NPF4

- OSGEP_HUMAN

UniProt

Q9NPF4 - OSGEP_HUMAN

Protein

Probable tRNA N6-adenosine threonylcarbamoyltransferase

Gene

OSGEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.UniRule annotation

    Catalytic activityi

    L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.

    Cofactori

    Binds 1 divalent metal cation per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi109 – 1091Divalent metal cationUniRule annotation
    Metal bindingi113 – 1131Divalent metal cationUniRule annotation
    Metal bindingi130 – 1301Divalent metal cationUniRule annotation
    Binding sitei162 – 1621SubstrateUniRule annotation
    Binding sitei177 – 1771Substrate; via amide nitrogenUniRule annotation
    Binding sitei181 – 1811SubstrateUniRule annotation
    Binding sitei266 – 2661SubstrateUniRule annotation
    Metal bindingi294 – 2941Divalent metal cationUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. transferase activity, transferring acyl groups other than amino-acyl groups Source: UniProtKB-HAMAP

    GO - Biological processi

    1. threonylcarbamoyladenosine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable tRNA N6-adenosine threonylcarbamoyltransferaseUniRule annotation (EC:2.6.99.4)
    Alternative name(s):
    N6-L-threonylcarbamoyladenine synthase
    Short name:
    t(6)A synthase
    O-sialoglycoprotein endopeptidaseUniRule annotation
    Short name:
    hOSGEP
    t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEPUniRule annotation
    tRNA threonylcarbamoyladenosine biosynthesis protein OSGEPUniRule annotation
    Gene namesi
    Name:OSGEPUniRule annotation
    Synonyms:GCPL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:18028. OSGEP.

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32834.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Probable tRNA N6-adenosine threonylcarbamoyltransferasePRO_0000096984Add
    BLAST

    Proteomic databases

    MaxQBiQ9NPF4.
    PaxDbiQ9NPF4.
    PeptideAtlasiQ9NPF4.
    PRIDEiQ9NPF4.

    PTM databases

    PhosphoSiteiQ9NPF4.

    Expressioni

    Tissue specificityi

    Widely expressed at low level. Expressed in heart, placenta, liver, kidney, lung, brain, skeletal muscle and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9NPF4.
    BgeeiQ9NPF4.
    CleanExiHS_OSGEP.
    GenevestigatoriQ9NPF4.

    Organism-specific databases

    HPAiHPA039751.

    Interactioni

    Subunit structurei

    Component of the EKC/KEOPS complex composed of at least TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. Interacts with PRAME.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi120779. 59 interactions.
    IntActiQ9NPF4. 21 interactions.
    MINTiMINT-3071750.
    STRINGi9606.ENSP00000206542.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NPF4.
    SMRiQ9NPF4. Positions 5-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni130 – 1345Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the KAE1 / TsaD family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0533.
    HOGENOMiHOG000109569.
    HOVERGENiHBG051713.
    InParanoidiQ9NPF4.
    KOiK15900.
    OMAiVIGFEGS.
    PhylomeDBiQ9NPF4.
    TreeFamiTF313621.

    Family and domain databases

    HAMAPiMF_01446. Kae1_arch.
    InterProiIPR000905. Gcp-like_dom.
    IPR017861. KAE1/YgjD.
    IPR017860. Peptidase_M22_CS.
    [Graphical view]
    PfamiPF00814. Peptidase_M22. 1 hit.
    [Graphical view]
    PRINTSiPR00789. OSIALOPTASE.
    TIGRFAMsiTIGR00329. gcp_kae1. 1 hit.
    PROSITEiPS01016. GLYCOPROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NPF4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAVLGFEGS ANKIGVGVVR DGKVLANPRR TYVTPPGTGF LPGDTARHHR    50
    AVILDLLQEA LTESGLTSQD IDCIAYTKGP GMGAPLVSVA VVARTVAQLW 100
    NKPLVGVNHC IGHIEMGRLI TGATSPTVLY VSGGNTQVIA YSEHRYRIFG 150
    ETIDIAVGNC LDRFARVLKI SNDPSPGYNI EQMAKRGKKL VELPYTVKGM 200
    DVSFSGILSF IEDVAHRMLA TGECTPEDLC FSLQETVFAM LVEITERAMA 250
    HCGSQEALIV GGVGCNVRLQ EMMATMCQER GARLFATDER FCIDNGAMIA 300
    QAGWEMFRAG HRTPLSDSGV TQRYRTDEVE VTWRD 335
    Length:335
    Mass (Da):36,427
    Last modified:October 1, 2000 - v1
    Checksum:i54DCBBB26C03E8FB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047823 Genomic DNA. Translation: BAB33147.1.
    AB050442 mRNA. Translation: BAB33172.1.
    AJ271669 mRNA. Translation: CAB71031.1.
    AK000418 mRNA. Translation: BAA91150.1.
    CR457232 mRNA. Translation: CAG33513.1.
    BC032310 mRNA. Translation: AAH32310.1.
    CCDSiCCDS9549.1.
    RefSeqiNP_060277.1. NM_017807.3.
    UniGeneiHs.525196.

    Genome annotation databases

    EnsembliENST00000206542; ENSP00000206542; ENSG00000092094.
    GeneIDi55644.
    KEGGihsa:55644.
    UCSCiuc001vxf.3. human.

    Polymorphism databases

    DMDMi47605574.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047823 Genomic DNA. Translation: BAB33147.1 .
    AB050442 mRNA. Translation: BAB33172.1 .
    AJ271669 mRNA. Translation: CAB71031.1 .
    AK000418 mRNA. Translation: BAA91150.1 .
    CR457232 mRNA. Translation: CAG33513.1 .
    BC032310 mRNA. Translation: AAH32310.1 .
    CCDSi CCDS9549.1.
    RefSeqi NP_060277.1. NM_017807.3.
    UniGenei Hs.525196.

    3D structure databases

    ProteinModelPortali Q9NPF4.
    SMRi Q9NPF4. Positions 5-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120779. 59 interactions.
    IntActi Q9NPF4. 21 interactions.
    MINTi MINT-3071750.
    STRINGi 9606.ENSP00000206542.

    PTM databases

    PhosphoSitei Q9NPF4.

    Polymorphism databases

    DMDMi 47605574.

    Proteomic databases

    MaxQBi Q9NPF4.
    PaxDbi Q9NPF4.
    PeptideAtlasi Q9NPF4.
    PRIDEi Q9NPF4.

    Protocols and materials databases

    DNASUi 55644.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000206542 ; ENSP00000206542 ; ENSG00000092094 .
    GeneIDi 55644.
    KEGGi hsa:55644.
    UCSCi uc001vxf.3. human.

    Organism-specific databases

    CTDi 55644.
    GeneCardsi GC14M020915.
    HGNCi HGNC:18028. OSGEP.
    HPAi HPA039751.
    MIMi 610107. gene.
    neXtProti NX_Q9NPF4.
    PharmGKBi PA32834.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0533.
    HOGENOMi HOG000109569.
    HOVERGENi HBG051713.
    InParanoidi Q9NPF4.
    KOi K15900.
    OMAi VIGFEGS.
    PhylomeDBi Q9NPF4.
    TreeFami TF313621.

    Miscellaneous databases

    ChiTaRSi OSGEP. human.
    GeneWikii OSGEP.
    GenomeRNAii 55644.
    NextBioi 60334.
    PROi Q9NPF4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPF4.
    Bgeei Q9NPF4.
    CleanExi HS_OSGEP.
    Genevestigatori Q9NPF4.

    Family and domain databases

    HAMAPi MF_01446. Kae1_arch.
    InterProi IPR000905. Gcp-like_dom.
    IPR017861. KAE1/YgjD.
    IPR017860. Peptidase_M22_CS.
    [Graphical view ]
    Pfami PF00814. Peptidase_M22. 1 hit.
    [Graphical view ]
    PRINTSi PR00789. OSIALOPTASE.
    TIGRFAMsi TIGR00329. gcp_kae1. 1 hit.
    PROSITEi PS01016. GLYCOPROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing analysis of a putative human O-sialoglycoprotein endopeptidase gene (OSGEP) and analysis of a bidirectional promoter between the OSGEP and APEX genes."
      Seki Y., Ikeda S., Kiyohara H., Ayabe H., Seki T., Matsui H.
      Gene 285:101-108(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "Cloning and sequencing of putative human sialoglycoprotease."
      Wigelsworth D.J., Coadwell J., Rawlings N.D., Barrett A.J.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "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].
      Tissue: Carcinoma.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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: Blood.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by the human tumour antigen PRAME."
      Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., Tijchon E., Conaway J.W., Conaway R.C., Stunnenberg H.G.
      PLoS ONE 7:E42822-E42822(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EKC/KEOPS COMPLEX, INTERACTION WITH PRAME, SUBCELLULAR LOCATION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiOSGEP_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPF4
    Secondary accession number(s): Q6IAC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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