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Reviewed, UniProtKB/Swiss-Prot O95260 (ATE1_HUMAN)

Last modified November 3, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginyl-tRNA--protein transferase 1
      Short name=Arginyltransferase 1
      Short name=R-transferase 1
    EC=2.3.2.8
Alternative name(s):
    Arginine-tRNA--protein transferase 1
Gene names
Name: ATE1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues By similarity.

Catalytic activity

L-arginyl-tRNA + protein = tRNA + L-arginyl-protein.

Subunit structure

Monomer Potential.

Subcellular location

Isoform ATE1-1: Nucleus By similarity. Cytoplasm By similarity.

Isoform ATE1-2: Cytoplasm By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5

Sequence similarities

Belongs to the R-transferase family.

Caution

It is uncertain whether Met-1 or Met-37 is the initiator.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein arginylation Ref.4

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm Ref.4

Inferred from direct assay. Source: UniProtKB

nucleus Ref.4

Inferred from direct assay. Source: UniProtKB

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

arginyltransferase activity Ref.4

Traceable author statement. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform ATE1-1 (identifier: O95260-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform ATE1-2 (identifier: O95260-2)

The sequence of this isoform differs from the canonical sequence as follows:
     274-314: VVRSSPPSSQ...NPPDTPTESQ → LVPVSFEDPE...DPPDECGKTE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Arginyl-tRNA--protein transferase 1
PRO_0000195088

Amino acid modifications

Modified residue1691Phosphoserine Ref.5

Natural variations

Alternative sequence274 – 31441VVRSS…PTESQ → LVPVSFEDPEFKSSFSQSFS LYVKYQVAIHQDPPDECGKT E in isoform ATE1-2.
VSP_000336

Experimental info

Sequence conflict5 – 117AGGSPSV → GGGFAAS in AAD12366. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform ATE1-1 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: BFD1CF8925CF5820

FASTA51859,090
        10         20         30         40         50         60 
MAFWAGGSPS VVDYFPSEDF YRCGYCKNES GSRSNGMWAH SMTVQDYQDL IDRGWRRSGK 

        70         80         90        100        110        120 
YVYKPVMNQT CCPQYTIRCR PLQFQPSKSH KKVLKKMLKF LAKGEVPKGS CEDEPMDSTM 

       130        140        150        160        170        180 
DDAVAGDFAL INKLDIQCDL KTLSDDIKES LESEGKNSKK EEPQELLQSQ DFVGEKLGSG 

       190        200        210        220        230        240 
EPSHSVKVHT VPKPGKGADL SKPPCRKAKE IRKERKRLKL MQQNPAGELE GFQAQGHPPS 

       250        260        270        280        290        300 
LFPPKAKSNQ PKSLEDLIFE SLPENASHKL EVRVVRSSPP SSQFKATLLE SYQVYKRYQM 

       310        320        330        340        350        360 
VIHKNPPDTP TESQFTRFLC SSPLEAETPP NGPDCGYGSF HQQYWLDGKI IAVGVIDILP 

       370        380        390        400        410        420 
NCVSSVYLYY DPDYSFLSLG VYSALREIAF TRQLHEKTSQ LSYYYMGFYI HSCPKMKYKG 

       430        440        450        460        470        480 
QYRPSDLLCP ETYVWVPIEQ CLPSLENSKY CRFNQDPEAV DEDRSTEPDR LQVFHKRAIM 

       490        500        510 
PYGVYKKQQK DPSEEAAVLQ YASLVGQKCS ERMLLFRN 

« Hide

Isoform ATE1-2.

Checksum: D01E1D6024F04565
Show »

FASTA51859,032

References

« Hide 'large scale' references
[1]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ATE1-2).
Tissue: Testis.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway."
Kwon Y.T., Kashina A.S., Varshavsky A.
Mol. Cell. Biol. 19:182-193(1999) [PubMed: 9858543] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-518 (ISOFORMS ATE1-1 AND ATE1-2).
Tissue: Embryonic kidney.
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY.

Cross-references

Sequence databases

BC022026 mRNA. Translation: AAH22026.2.
AL731542, AC025947, AL731566 Genomic DNA. Translation: CAI12918.1.
AL731566, AC025947, AL731542 Genomic DNA. Translation: CAI14813.1.
CH471066 Genomic DNA. Translation: EAW49334.1.
AF079098 mRNA. Translation: AAD12366.1.
AF079099 mRNA. Translation: AAD12367.1.
IPIIPI00029472.
IPI00218377.
RefSeqNP_001001976.1.
NP_008972.2.
UniGeneHs.632080

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO95260. 1 interaction.
STRINGO95260.

PTM databases

PhosphoSiteO95260.

Proteomic databases

PRIDEO95260.

Genome annotation databases

EnsemblENST00000224652; ENSP00000224652; ENSG00000107669; Homo sapiens. [Genome view]
ENST00000369040; ENSP00000358036; ENSG00000107669; Homo sapiens. [Genome view]
ENST00000369043; ENSP00000358039; ENSG00000107669; Homo sapiens. [Genome view]
ENST00000423243; ENSP00000397787; ENSG00000107669; Homo sapiens. [Genome view]
ENST00000455628; ENSP00000405099; ENSG00000107669; Homo sapiens. [Genome view]
GeneID11101.
KEGGhsa:11101.
UCSCuc001lfp.1. human.
uc001lfq.1. human.

Organism-specific databases

CTD11101.
GeneCardsGC10M123492.
H-InvDBHIX0009267.
HGNCHGNC:782. ATE1.
MIM607103. gene.
PharmGKBPA25082.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO95260.
HOVERGENO95260.
OMASIVEYFE.

Enzyme and pathway databases

BRENDA2.3.2.8. 247.

Gene expression databases

ArrayExpressO95260.
BgeeO95260.
CleanExHS_ATE1.
GenevestigatorO95260.
GermOnlineENSG00000107669. Homo sapiens.

Family and domain databases

InterProIPR017137. Arg-tRNA-P_Trfase_1_euk.
IPR007472. Arg-tRNA-P_Trfase_C.
IPR007471. Arg_tRNA_PTrfase_N.
[Graphical view]
PfamPF04377. ATE_C. 1 hit.
PF04376. ATE_N. 1 hit.
[Graphical view]
PIRSFPIRSF037207. ATE1_euk. 1 hit.
ProtoNetSearch...

Other Resources

NextBio42204.
SOURCESearch...

Entry information

Entry nameATE1_HUMAN
AccessionPrimary (citable) accession number: O95260
Secondary accession number(s): O95261, Q5SQQ3, Q8WW04
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 26, 2002
Last modified: November 3, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents