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Q9NPF4

- OSGEP_HUMAN

UniProt

Q9NPF4 - OSGEP_HUMAN

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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

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

a divalent metal cationUniRule annotationNote: 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
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 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-HAMAP
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ9NPF4.
CleanExiHS_OSGEP.
ExpressionAtlasiQ9NPF4. baseline and differential.
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. 62 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.
GeneTreeiENSGT00550000074933.
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

        10         20         30         40         50
MPAVLGFEGS ANKIGVGVVR DGKVLANPRR TYVTPPGTGF LPGDTARHHR
60 70 80 90 100
AVILDLLQEA LTESGLTSQD IDCIAYTKGP GMGAPLVSVA VVARTVAQLW
110 120 130 140 150
NKPLVGVNHC IGHIEMGRLI TGATSPTVLY VSGGNTQVIA YSEHRYRIFG
160 170 180 190 200
ETIDIAVGNC LDRFARVLKI SNDPSPGYNI EQMAKRGKKL VELPYTVKGM
210 220 230 240 250
DVSFSGILSF IEDVAHRMLA TGECTPEDLC FSLQETVFAM LVEITERAMA
260 270 280 290 300
HCGSQEALIV GGVGCNVRLQ EMMATMCQER GARLFATDER FCIDNGAMIA
310 320 330
QAGWEMFRAG HRTPLSDSGV TQRYRTDEVE VTWRD
Length:335
Mass (Da):36,427
Last modified:October 1, 2000 - v1
Checksum:i54DCBBB26C03E8FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 62 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.
GeneTreei ENSGT00550000074933.
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

Bgeei Q9NPF4.
CleanExi HS_OSGEP.
ExpressionAtlasi Q9NPF4. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 113 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