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Q9NPF4 (OSGEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Short name=hOSGEP
t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP
tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP
Gene names
Name:OSGEP
Synonyms:GCPL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Interacts with PRAME. Ref.7

Subcellular location

Cytoplasm By similarity. Nucleus Ref.7.

Tissue specificity

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

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_0000096984

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

Sequences

Sequence LengthMass (Da)Tools
Q9NPF4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 54DCBBB26C03E8FB

FASTA33536,427
        10         20         30         40         50         60 
MPAVLGFEGS ANKIGVGVVR DGKVLANPRR TYVTPPGTGF LPGDTARHHR AVILDLLQEA 

        70         80         90        100        110        120 
LTESGLTSQD IDCIAYTKGP GMGAPLVSVA VVARTVAQLW NKPLVGVNHC IGHIEMGRLI 

       130        140        150        160        170        180 
TGATSPTVLY VSGGNTQVIA YSEHRYRIFG ETIDIAVGNC LDRFARVLKI SNDPSPGYNI 

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

       250        260        270        280        290        300 
LVEITERAMA HCGSQEALIV GGVGCNVRLQ EMMATMCQER GARLFATDER FCIDNGAMIA 

       310        320        330 
QAGWEMFRAG HRTPLSDSGV TQRYRTDEVE VTWRD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9549.1.
RefSeqNP_060277.1. NM_017807.3.
UniGeneHs.525196.

3D structure databases

ProteinModelPortalQ9NPF4.
SMRQ9NPF4. Positions 5-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120779. 59 interactions.
IntActQ9NPF4. 21 interactions.
MINTMINT-3071750.
STRING9606.ENSP00000206542.

PTM databases

PhosphoSiteQ9NPF4.

Polymorphism databases

DMDM47605574.

Proteomic databases

MaxQBQ9NPF4.
PaxDbQ9NPF4.
PeptideAtlasQ9NPF4.
PRIDEQ9NPF4.

Protocols and materials databases

DNASU55644.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000206542; ENSP00000206542; ENSG00000092094.
GeneID55644.
KEGGhsa:55644.
UCSCuc001vxf.3. human.

Organism-specific databases

CTD55644.
GeneCardsGC14M020915.
HGNCHGNC:18028. OSGEP.
HPAHPA039751.
MIM610107. gene.
neXtProtNX_Q9NPF4.
PharmGKBPA32834.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0533.
HOGENOMHOG000109569.
HOVERGENHBG051713.
InParanoidQ9NPF4.
KOK15900.
OMAVIGFEGS.
PhylomeDBQ9NPF4.
TreeFamTF313621.

Gene expression databases

ArrayExpressQ9NPF4.
BgeeQ9NPF4.
CleanExHS_OSGEP.
GenevestigatorQ9NPF4.

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

ChiTaRSOSGEP. human.
GeneWikiOSGEP.
GenomeRNAi55644.
NextBio60334.
PROQ9NPF4.
SOURCESearch...

Entry information

Entry nameOSGEP_HUMAN
AccessionPrimary (citable) accession number: Q9NPF4
Secondary accession number(s): Q6IAC3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM