SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8BWU5

- OSGEP_MOUSE

UniProt

Q8BWU5 - OSGEP_MOUSE

(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)

Protein

Probable tRNA N6-adenosine threonylcarbamoyltransferase

Gene
Osgep
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 divalent metal cation per subunit By similarity.

Sites

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

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
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable tRNA N6-adenosine threonylcarbamoyltransferase (EC:2.6.99.4)
Alternative name(s):
N6-L-threonylcarbamoyladenine synthase
Short name:
t(6)A synthase
O-sialoglycoprotein endopeptidase
t(6)A37 threonylcarbamoyladenosine biosynthesis protein Osgep
tRNA threonylcarbamoyladenosine biosynthesis protein Osgep
Gene namesi
Name:Osgep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1913496. Osgep.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Probable tRNA N6-adenosine threonylcarbamoyltransferaseUniRule annotationPRO_0000096985Add
BLAST

Proteomic databases

MaxQBiQ8BWU5.
PaxDbiQ8BWU5.
PRIDEiQ8BWU5.

PTM databases

PhosphoSiteiQ8BWU5.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed at intermediate level in lung. Weakly expressed in testis, skeletal muscle, kidney, liver, spleen, brain and heart.1 Publication

Developmental stagei

Weakly expressed in 7, 11 and 17 day embryos. Expressed at a higher level in 15 day embryos.1 Publication

Gene expression databases

BgeeiQ8BWU5.
CleanExiMM_OSGEP.
GenevestigatoriQ8BWU5.

Interactioni

Subunit structurei

Component of the EKC/KEOPS complex composed of at least TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ8BWU5.
SMRiQ8BWU5. Positions 5-333.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 1345Substrate binding By similarity

Sequence similaritiesi

Belongs to the KAE1 / TsaD family.

Phylogenomic databases

eggNOGiCOG0533.
GeneTreeiENSGT00550000074933.
HOGENOMiHOG000109569.
HOVERGENiHBG051713.
InParanoidiQ8BWU5.
KOiK15900.
OrthoDBiEOG7MD4Q9.
PhylomeDBiQ8BWU5.
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.

Q8BWU5-1 [UniParc]FASTAAdd to Basket

« Hide

MPAVLGFEGS ANKIGVGVVR DGTVLANPRR TYVTAPGTGF LPGDTARHHR    50
AVILDLLQEA LAEAGLTSKD IDCIAFTKGP GMGAPLASVA VVARTVAQLW 100
NKPLLGVNHC IGHIEMGRLI TGAVNPTVLY VSGGNTQVIS YSEHRYRIFG 150
ETIDIAVGNC LDRFARVLKI SNDPSPGYNI EQMAKRGKKL VELPYTVKGM 200
DVSFSGILSF IEDAAQRMLA TGECTPEDLC FSLQETVFAM LVEITERAMA 250
HCGSKEALIV GGVGCNLRLQ EMMGTMCQER GAQLFATDER FCVDNGAMIA 300
QAGWEMFQAG HRTPLKDSAI TQRYRTDEVE VTWRD 335
Length:335
Mass (Da):36,301
Last modified:May 24, 2004 - v2
Checksum:i906F58C5AF53A154
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621A → T in BAC34005. 1 Publication
Sequence conflicti84 – 841A → S in BAC34005. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK049955 mRNA. Translation: BAC34005.1.
BC002296 mRNA. Translation: AAH02296.1.
CCDSiCCDS27026.1.
RefSeqiNP_598437.2. NM_133676.2.
UniGeneiMm.274791.

Genome annotation databases

EnsembliENSMUST00000159292; ENSMUSP00000124039; ENSMUSG00000006289.
ENSMUST00000160393; ENSMUSP00000125155; ENSMUSG00000006289.
GeneIDi66246.
KEGGimmu:66246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK049955 mRNA. Translation: BAC34005.1 .
BC002296 mRNA. Translation: AAH02296.1 .
CCDSi CCDS27026.1.
RefSeqi NP_598437.2. NM_133676.2.
UniGenei Mm.274791.

3D structure databases

ProteinModelPortali Q8BWU5.
SMRi Q8BWU5. Positions 5-333.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BWU5.

Proteomic databases

MaxQBi Q8BWU5.
PaxDbi Q8BWU5.
PRIDEi Q8BWU5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000159292 ; ENSMUSP00000124039 ; ENSMUSG00000006289 .
ENSMUST00000160393 ; ENSMUSP00000125155 ; ENSMUSG00000006289 .
GeneIDi 66246.
KEGGi mmu:66246.

Organism-specific databases

CTDi 55644.
MGIi MGI:1913496. Osgep.

Phylogenomic databases

eggNOGi COG0533.
GeneTreei ENSGT00550000074933.
HOGENOMi HOG000109569.
HOVERGENi HBG051713.
InParanoidi Q8BWU5.
KOi K15900.
OrthoDBi EOG7MD4Q9.
PhylomeDBi Q8BWU5.
TreeFami TF313621.

Miscellaneous databases

NextBioi 321079.
PROi Q8BWU5.
SOURCEi Search...

Gene expression databases

Bgeei Q8BWU5.
CleanExi MM_OSGEP.
Genevestigatori Q8BWU5.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  2. "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: Mammary tumor.
  3. "Identification of the functional elements in the bidirectional promoter of the mouse O-sialoglycoprotein endopeptidase and APEX nuclease genes."
    Ikeda S., Ayabe H., Mori K., Seki Y., Seki S.
    Biochem. Biophys. Res. Commun. 296:785-791(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiOSGEP_MOUSE
AccessioniPrimary (citable) accession number: Q8BWU5
Secondary accession number(s): Q99LN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi