Q9Z2A5 (ATE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1
Catalytic activity	L-arginyl-tRNA + protein = tRNA + L-arginyl-protein.
Subunit structure	Monomer Potential. Ref.1
Subcellular location	Isoform ATE1-1: Nucleus. Cytoplasm Ref.1. Isoform ATE1-2: Cytoplasm Ref.1.
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Belongs to the R-transferase family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein arginylation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI
Molecular function	arginyltransferase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform ATE1-1 (identifier: Q9Z2A5-1)

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.

Note: Shows significantly higher activity than isoform ATE1-2.

Isoform ATE1-2 (identifier: Q9Z2A5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     272-312: VVRSSPPSPQ...DPPDKPTVSQ → LVPASFEDPE...EAPEICEKSE

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 516	516	Arginyl-tRNA--protein transferase 1		PRO_0000195089
Natural variations
	Alternative sequence	272 – 312	41	VVRSS…PTVSQ → LVPASFEDPEFNSSFNQSFS LYTKYQVAIHQEAPEICEKS E in isoform ATE1-2.		VSP_000337
Experimental info
	Sequence conflict	362	1	S → F in AAD12364. Ref.1
	Sequence conflict	362	1	S → F in AAD12365. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform ATE1-1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 40CCC7756C75858A	FASTA	516	59,146
	10 20 30 40 50 60 MASWSAPSPS LVEYFEGQTS FQCGYCKNKL GSRSYGMWAH SMTVQDYQDL IDRGWRRSGK 70 80 90 100 110 120 YVYKPVMDQT CCPQYTIRCH PLQFQPSKSH KKVLKKMLKF LAKGEISKGN CEDEPMDSTV 130 140 150 160 170 180 EDAVDGDFAL INKLDIKCDL KTLSDLKGSI ESEEKEKEKS IKKEGSKEFI HPQSIEEKLG 190 200 210 220 230 240 SGEPSHPIKV HIGPKPGKGA DLSKPPCRKA REMRKERQRL KRMQQASAAA SEAQGQPVCL 250 260 270 280 290 300 LPKAKSNQPK SLEDLIFQSL PENASHKLEV RVVRSSPPSP QFRATFQESY QVYKRYQMVV 310 320 330 340 350 360 HKDPPDKPTV SQFTRFLCSS PLEAEHPADG PECGYGSFHQ QYWLDGKIIA VGVLDILPYC 370 380 390 400 410 420 VSSVYLYYDP DYSFLSLGVY SALREIAFTR QLHEKTSQLS YYYMGFYIHS CPKMRYKGQY 430 440 450 460 470 480 RPSDLLCPET YVWVPIEQCL PSLDNSKYCR FNQDPEAEDE GRSKELDRLR VFHRRSAMPY 490 500 510 GVYKNHQEDP SEEAGVLEYA NLVGQKCSER MLLFRH
	Isoform ATE1-2 [UniParc]. Checksum: F7C19A086881067B	FASTA	516	59,048
	10 20 30 40 50 60 MASWSAPSPS LVEYFEGQTS FQCGYCKNKL GSRSYGMWAH SMTVQDYQDL IDRGWRRSGK 70 80 90 100 110 120 YVYKPVMDQT CCPQYTIRCH PLQFQPSKSH KKVLKKMLKF LAKGEISKGN CEDEPMDSTV 130 140 150 160 170 180 EDAVDGDFAL INKLDIKCDL KTLSDLKGSI ESEEKEKEKS IKKEGSKEFI HPQSIEEKLG 190 200 210 220 230 240 SGEPSHPIKV HIGPKPGKGA DLSKPPCRKA REMRKERQRL KRMQQASAAA SEAQGQPVCL 250 260 270 280 290 300 LPKAKSNQPK SLEDLIFQSL PENASHKLEV RLVPASFEDP EFNSSFNQSF SLYTKYQVAI 310 320 330 340 350 360 HQEAPEICEK SEFTRFLCSS PLEAEHPADG PECGYGSFHQ QYWLDGKIIA VGVLDILPYC 370 380 390 400 410 420 VSSVYLYYDP DYSFLSLGVY SALREIAFTR QLHEKTSQLS YYYMGFYIHS CPKMRYKGQY 430 440 450 460 470 480 RPSDLLCPET YVWVPIEQCL PSLDNSKYCR FNQDPEAEDE GRSKELDRLR VFHRRSAMPY 490 500 510 GVYKNHQEDP SEEAGVLEYA NLVGQKCSER MLLFRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORMS ATE1-1 AND ATE1-2), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Erythroleukemia.
[2]	"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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ATE1-1). Strain: C57BL/6J. Tissue: Placenta.
[3]	"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 ATE1-1). Tissue: Eye.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF079096 mRNA. Translation: AAD12364.1. AF079097 mRNA. Translation: AAD12365.1. AK148442 mRNA. Translation: BAE28555.1. AK167591 mRNA. Translation: BAE39649.1. BC042601 mRNA. Translation: AAH42601.1.
IPI	IPI00130961. IPI00230466.
RefSeq	NP_038827.2. NM_013799.2.
UniGene	Mm.216321.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z2A5.
PTM databases
PhosphoSite	Q9Z2A5.
Proteomic databases
PRIDE	Q9Z2A5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033139; ENSMUSP00000033139; ENSMUSG00000030850. ENSMUST00000035458; ENSMUSP00000043365; ENSMUSG00000030850.
GeneID	11907.
KEGG	mmu:11907.
Organism-specific databases
CTD	11101.
MGI	MGI:1333870. Ate1.
Phylogenomic databases
GeneTree	ENSGT00500000044926.
HOGENOM	HBG714174.
HOVERGEN	HBG004299.
InParanoid	Q9Z2A5.
Gene expression databases
ArrayExpress	Q9Z2A5.
Bgee	Q9Z2A5.
CleanEx	MM_ATE1.
Genevestigator	Q9Z2A5.
GermOnline	ENSMUSG00000030850. Mus musculus.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR017137. Arg-tRNA-P_Trfase_1_euk. IPR007472. Arg-tRNA-P_Trfase_C. IPR007471. Arg_tRNA_PTrfase_N. [Graphical view]
KO	K00685.
Pfam	PF04377. ATE_C. 1 hit. PF04376. ATE_N. 1 hit. [Graphical view]
PIRSF	PIRSF037207. ATE1_euk. 1 hit.
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

ATE1_MOUSE

Accession

Primary (citable) accession number: Q9Z2A5
Secondary accession number(s): Q8CFP7, Q9Z2A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program