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Q8BWU5 (OSGEP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Osgep
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03180

Catalytic activity

L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N(6)-L-threonylcarbamoyladenine37 in tRNA. HAMAP-Rule MF_03180

Cofactor

Binds 1 divalent metal cation per subunit By similarity.

Subunit structure

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

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_03180.

Tissue specificity

Widely expressed at low level. Expressed at intermediate level in lung. Weakly expressed in testis, skeletal muscle, kidney, liver, spleen, brain and heart. Ref.3

Developmental stage

Weakly expressed in 7, 11 and 17 day embryos. Expressed at a higher level in 15 day embryos. Ref.3

Sequence similarities

Belongs to the KAE1 / TsaD family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
Nucleus
   LigandMetal-binding
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonylcarbamoyladenosine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transferase activity, transferring acyl groups other than amino-acyl groups

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Probable tRNA N6-adenosine threonylcarbamoyltransferase HAMAP-Rule MF_03180
PRO_0000096985

Regions

Region130 – 1345Substrate binding By similarity

Sites

Metal binding1091Divalent metal cation By similarity
Metal binding1131Divalent metal cation By similarity
Metal binding1301Divalent metal cation By similarity
Metal binding2941Divalent metal cation By similarity
Binding site1621Substrate By similarity
Binding site1771Substrate; via amide nitrogen By similarity
Binding site1811Substrate By similarity
Binding site2661Substrate By similarity

Experimental info

Sequence conflict621A → T in BAC34005. Ref.1
Sequence conflict841A → S in BAC34005. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BWU5 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: 906F58C5AF53A154

FASTA33536,301
        10         20         30         40         50         60 
MPAVLGFEGS ANKIGVGVVR DGTVLANPRR TYVTAPGTGF LPGDTARHHR AVILDLLQEA 

        70         80         90        100        110        120 
LAEAGLTSKD IDCIAFTKGP GMGAPLASVA VVARTVAQLW NKPLLGVNHC IGHIEMGRLI 

       130        140        150        160        170        180 
TGAVNPTVLY VSGGNTQVIS YSEHRYRIFG ETIDIAVGNC LDRFARVLKI SNDPSPGYNI 

       190        200        210        220        230        240 
EQMAKRGKKL VELPYTVKGM DVSFSGILSF IEDAAQRMLA TGECTPEDLC FSLQETVFAM 

       250        260        270        280        290        300 
LVEITERAMA HCGSKEALIV GGVGCNLRLQ EMMGTMCQER GAQLFATDER FCVDNGAMIA 

       310        320        330 
QAGWEMFQAG HRTPLKDSAI TQRYRTDEVE VTWRD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK049955 mRNA. Translation: BAC34005.1.
BC002296 mRNA. Translation: AAH02296.1.
CCDSCCDS27026.1.
RefSeqNP_598437.2. NM_133676.2.
UniGeneMm.274791.

3D structure databases

ProteinModelPortalQ8BWU5.
SMRQ8BWU5. Positions 5-333.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BWU5.

Proteomic databases

MaxQBQ8BWU5.
PaxDbQ8BWU5.
PRIDEQ8BWU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000159292; ENSMUSP00000124039; ENSMUSG00000006289.
ENSMUST00000160393; ENSMUSP00000125155; ENSMUSG00000006289.
GeneID66246.
KEGGmmu:66246.

Organism-specific databases

CTD55644.
MGIMGI:1913496. Osgep.

Phylogenomic databases

eggNOGCOG0533.
GeneTreeENSGT00550000074933.
HOGENOMHOG000109569.
HOVERGENHBG051713.
InParanoidQ8BWU5.
KOK15900.
OrthoDBEOG7MD4Q9.
PhylomeDBQ8BWU5.
TreeFamTF313621.

Gene expression databases

BgeeQ8BWU5.
CleanExMM_OSGEP.
GenevestigatorQ8BWU5.

Family and domain databases

HAMAPMF_01446. Kae1_arch.
InterProIPR000905. Gcp-like_dom.
IPR017861. KAE1/YgjD.
IPR017860. Peptidase_M22_CS.
[Graphical view]
PfamPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSPR00789. OSIALOPTASE.
TIGRFAMsTIGR00329. gcp_kae1. 1 hit.
PROSITEPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio321079.
PROQ8BWU5.
SOURCESearch...

Entry information

Entry nameOSGEP_MOUSE
AccessionPrimary (citable) accession number: Q8BWU5
Secondary accession number(s): Q99LN8
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot