ATE1_HUMAN
ID ATE1_HUMAN Reviewed; 518 AA.
AC O95260; O95261; Q5SQQ3; Q8WW04;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Arginyl-tRNA--protein transferase 1;
DE Short=Arginyltransferase 1;
DE Short=R-transferase 1;
DE EC=2.3.2.8;
DE AltName: Full=Arginine-tRNA--protein transferase 1;
GN Name=ATE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ATE1-2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-518 (ISOFORMS ATE1-1 AND ATE1-2).
RC TISSUE=Embryonic kidney;
RX PubMed=9858543; DOI=10.1128/mcb.19.1.182;
RA Kwon Y.T., Kashina A.S., Varshavsky A.;
RT "Alternative splicing results in differential expression, activity, and
RT localization of the two forms of arginyl-tRNA-protein transferase, a
RT component of the N-end rule pathway.";
RL Mol. Cell. Biol. 19:182-193(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Involved in the post-translational conjugation of arginine to
CC the N-terminal aspartate or glutamate of a protein. This arginylation
CC is required for degradation of the protein via the ubiquitin pathway.
CC Does not arginylate cysteine residues (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-
CC tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] +
CC tRNA(Arg); Xref=Rhea:RHEA:10208, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10638,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC ChEBI:CHEBI:78597, ChEBI:CHEBI:83562; EC=2.3.2.8;
CC -!- SUBUNIT: Monomer. Interacts with LIAT1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z2A5, ECO:0000305}.
CC -!- INTERACTION:
CC O95260; O43463: SUV39H1; NbExp=2; IntAct=EBI-1043378, EBI-349968;
CC -!- SUBCELLULAR LOCATION: [Isoform ATE1-1]: Nucleus
CC {ECO:0000250|UniProtKB:Q9Z2A5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Z2A5}.
CC -!- SUBCELLULAR LOCATION: [Isoform ATE1-2]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Z2A5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ATE1-1;
CC IsoId=O95260-1; Sequence=Displayed;
CC Name=ATE1-2;
CC IsoId=O95260-2; Sequence=VSP_000336;
CC -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-37 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AC025947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49334.1; -; Genomic_DNA.
DR EMBL; BC022026; AAH22026.2; -; mRNA.
DR EMBL; AF079098; AAD12366.1; -; mRNA.
DR EMBL; AF079099; AAD12367.1; -; mRNA.
DR CCDS; CCDS31299.1; -. [O95260-2]
DR CCDS; CCDS31300.1; -. [O95260-1]
DR RefSeq; NP_001001976.1; NM_001001976.2. [O95260-1]
DR RefSeq; NP_001275663.1; NM_001288734.1.
DR RefSeq; NP_001275664.1; NM_001288735.1.
DR RefSeq; NP_001275665.1; NM_001288736.1.
DR RefSeq; NP_008972.2; NM_007041.3. [O95260-2]
DR AlphaFoldDB; O95260; -.
DR BioGRID; 116282; 97.
DR IntAct; O95260; 29.
DR MINT; O95260; -.
DR STRING; 9606.ENSP00000224652; -.
DR GlyGen; O95260; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O95260; -.
DR PhosphoSitePlus; O95260; -.
DR BioMuta; ATE1; -.
DR EPD; O95260; -.
DR jPOST; O95260; -.
DR MassIVE; O95260; -.
DR MaxQB; O95260; -.
DR PaxDb; O95260; -.
DR PeptideAtlas; O95260; -.
DR PRIDE; O95260; -.
DR ProteomicsDB; 50757; -. [O95260-1]
DR ProteomicsDB; 50758; -. [O95260-2]
DR Antibodypedia; 32214; 188 antibodies from 31 providers.
DR DNASU; 11101; -.
DR Ensembl; ENST00000224652.12; ENSP00000224652.6; ENSG00000107669.19. [O95260-1]
DR Ensembl; ENST00000369043.8; ENSP00000358039.3; ENSG00000107669.19. [O95260-2]
DR Ensembl; ENST00000685007.1; ENSP00000508990.1; ENSG00000107669.19. [O95260-2]
DR GeneID; 11101; -.
DR KEGG; hsa:11101; -.
DR MANE-Select; ENST00000224652.12; ENSP00000224652.6; NM_001001976.3; NP_001001976.1.
DR UCSC; uc001lfp.5; human. [O95260-1]
DR CTD; 11101; -.
DR DisGeNET; 11101; -.
DR GeneCards; ATE1; -.
DR HGNC; HGNC:782; ATE1.
DR HPA; ENSG00000107669; Low tissue specificity.
DR MIM; 607103; gene.
DR neXtProt; NX_O95260; -.
DR OpenTargets; ENSG00000107669; -.
DR PharmGKB; PA25082; -.
DR VEuPathDB; HostDB:ENSG00000107669; -.
DR eggNOG; KOG1193; Eukaryota.
DR GeneTree; ENSGT00500000044926; -.
DR HOGENOM; CLU_020349_1_1_1; -.
DR InParanoid; O95260; -.
DR OMA; SDRMVYS; -.
DR OrthoDB; 1446907at2759; -.
DR PhylomeDB; O95260; -.
DR TreeFam; TF105976; -.
DR BioCyc; MetaCyc:HS03017-MON; -.
DR BRENDA; 2.3.2.8; 2681.
DR PathwayCommons; O95260; -.
DR SignaLink; O95260; -.
DR SIGNOR; O95260; -.
DR BioGRID-ORCS; 11101; 16 hits in 1088 CRISPR screens.
DR ChiTaRS; ATE1; human.
DR GenomeRNAi; 11101; -.
DR Pharos; O95260; Tbio.
DR PRO; PR:O95260; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95260; protein.
DR Bgee; ENSG00000107669; Expressed in tibialis anterior and 193 other tissues.
DR ExpressionAtlas; O95260; baseline and differential.
DR Genevisible; O95260; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004057; F:arginyltransferase activity; IBA:GO_Central.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:MGI.
DR GO; GO:0016598; P:protein arginylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR017137; Arg-tRNA-P_Trfase_1_euk.
DR InterPro; IPR030700; N-end_Aminoacyl_Trfase.
DR InterPro; IPR007472; N-end_Aminoacyl_Trfase_C.
DR InterPro; IPR007471; N-end_Aminoacyl_Trfase_N.
DR PANTHER; PTHR21367; PTHR21367; 1.
DR Pfam; PF04377; ATE_C; 1.
DR Pfam; PF04376; ATE_N; 1.
DR PIRSF; PIRSF037207; ATE1_euk; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..518
FT /note="Arginyl-tRNA--protein transferase 1"
FT /id="PRO_0000195088"
FT REGION 175..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 274..314
FT /note="VVRSSPPSSQFKATLLESYQVYKRYQMVIHKNPPDTPTESQ -> LVPVSFE
FT DPEFKSSFSQSFSLYVKYQVAIHQDPPDECGKTE (in isoform ATE1-2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9858543"
FT /id="VSP_000336"
FT CONFLICT 5..11
FT /note="AGGSPSV -> GGGFAAS (in Ref. 4; AAD12366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 59090 MW; BFD1CF8925CF5820 CRC64;
MAFWAGGSPS VVDYFPSEDF YRCGYCKNES GSRSNGMWAH SMTVQDYQDL IDRGWRRSGK
YVYKPVMNQT CCPQYTIRCR PLQFQPSKSH KKVLKKMLKF LAKGEVPKGS CEDEPMDSTM
DDAVAGDFAL INKLDIQCDL KTLSDDIKES LESEGKNSKK EEPQELLQSQ DFVGEKLGSG
EPSHSVKVHT VPKPGKGADL SKPPCRKAKE IRKERKRLKL MQQNPAGELE GFQAQGHPPS
LFPPKAKSNQ PKSLEDLIFE SLPENASHKL EVRVVRSSPP SSQFKATLLE SYQVYKRYQM
VIHKNPPDTP TESQFTRFLC SSPLEAETPP NGPDCGYGSF HQQYWLDGKI IAVGVIDILP
NCVSSVYLYY DPDYSFLSLG VYSALREIAF TRQLHEKTSQ LSYYYMGFYI HSCPKMKYKG
QYRPSDLLCP ETYVWVPIEQ CLPSLENSKY CRFNQDPEAV DEDRSTEPDR LQVFHKRAIM
PYGVYKKQQK DPSEEAAVLQ YASLVGQKCS ERMLLFRN
