Reviewed, UniProtKB/Swiss-Prot P28668 (SYEP_DROME)

Names and origin

Protein names

Recommended name:
    Bifunctional aminoacyl-tRNA synthetase
Including the following 2 domains:
    1- Recommended name:
            Glutamyl-tRNA synthetase
              EC=6.1.1.17
        Alternative name(s):
            Glutamate--tRNA ligase
    2- Recommended name:
            Prolyl-tRNA synthetase
              EC=6.1.1.15
        Alternative name(s):
            Proline--tRNA ligase

Gene names

Name:	Aats-glupro
ORF Names:	CG5394

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1714 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
Subunit structure	Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43.
Sequence similarities	In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family. In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family. Contains 6 WHEP-TRS domains.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO binding Inferred from physical interaction. Source: FlyBase glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC proline-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Isoform A (identifier: P28668-1)

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 B (identifier: P28668-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-718: Missing.
     719-732: TSGLKVNAPDAKAT → MLNYLACGSLSSTS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1714	1714	Bifunctional aminoacyl-tRNA synthetase		PRO_0000119741
Regions
	Domain	744 – 800	57	WHEP-TRS 1
	Domain	816 – 872	57	WHEP-TRS 2
	Domain	890 – 946	57	WHEP-TRS 3
	Domain	969 – 1025	57	WHEP-TRS 4
	Domain	1044 – 1100	57	WHEP-TRS 5
	Domain	1118 – 1174	57	WHEP-TRS 6
	Nucleotide binding	438 – 442	5	ATP By similarity
	Region	170 – 754	585	Glutamyl-tRNA synthetase
	Region	1207 – 1714	508	Prolyl-tRNA synthetase
	Motif	209 – 220	12	"HIGH" region
	Motif	438 – 442	5	"KMSKS" region
	Compositional bias	1174 – 1180	7	Poly-Gly
Sites
	Binding site	217	1	ATP By similarity
	Binding site	404	1	ATP By similarity
Amino acid modifications
	Modified residue	1110	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	1 – 718	718	Missing in isoform B.		VSP_009609
	Alternative sequence	719 – 732	14	TSGLK…DAKAT → MLNYLACGSLSSTS in isoform B.		VSP_009610
Experimental info
	Sequence conflict	102 – 106	5	DKSIA → TSPLP Ref.1
	Sequence conflict	102 – 106	5	DKSIA → TSPLP Ref.2
	Sequence conflict	233 – 234	2	AF → VC Ref.1
	Sequence conflict	233 – 234	2	AF → VC Ref.2
	Sequence conflict	341 – 345	5	KYCVR → NTACA Ref.1
	Sequence conflict	341 – 345	5	KYCVR → NTACA Ref.2
	Sequence conflict	583	1	R → K Ref.1
	Sequence conflict	583	1	R → K Ref.2
	Sequence conflict	692	1	A → L Ref.1
	Sequence conflict	692	1	A → L Ref.2
	Sequence conflict	753	1	S → T Ref.1
	Sequence conflict	753	1	S → T Ref.2
	Sequence conflict	802	1	S → T Ref.1
	Sequence conflict	802	1	S → T Ref.2
	Sequence conflict	873	1	T → P Ref.1
	Sequence conflict	873	1	T → P Ref.2
	Sequence conflict	887	1	V → G Ref.1
	Sequence conflict	887	1	V → G Ref.2
	Sequence conflict	1035	1	D → G in AAN71400. Ref.5
	Sequence conflict	1202	1	Missing Ref.1
	Sequence conflict	1202	1	Missing Ref.2
	Sequence conflict	1461	1	E → EK Ref.1
	Sequence conflict	1461	1	E → EK Ref.2
	Sequence conflict	1587	1	V → G Ref.1
	Sequence conflict	1587	1	V → G Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 3F8CF3DB128765A8	FASTA	1,714	189,412
	10 20 30 40 50 60 MSIKLKANLN NPPISGLATA HLINGTVPVE IVWSKEETSL QFPDNRLLVC HSNNDVLRAL 70 80 90 100 110 120 ARAAPDYKLY GETAIERTQI DHWLSFSLTC EDDISWALSF LDKSIAPVTY LVANKLTIAD 130 140 150 160 170 180 FALFNEMHSR YEFLAAKGIP QHVQRWYDLI TAQPLIQKVL QSLPEDAKVK RSPQSSKEQT 190 200 210 220 230 240 PAKTGERKQE GKFVDLPGAE MGKVVVRFPP EASGYLHIGH AKAALLNQYY ALAFQGTLIM 250 260 270 280 290 300 RFDDTNPAKE TVEFENVILG DLEQLQIKPD VFTHTSNYFD LMLDYCVRLI KESKAYVDDT 310 320 330 340 350 360 PPEQMKLERE QRVESANRSN SVEKNLSLWE EMVKGSEKGQ KYCVRAKIDM SSPNGCMRDP 370 380 390 400 410 420 TIYRCKNEPH PRTGTKYKVY PTYDFACPIV DAIENVTHTL RTTEYHDRDD QFYWFIDALK 430 440 450 460 470 480 LRKPYIWSYS RLNMTNTVLS KRKLTWFVDS GLVDGWDDPR FPTVRGIIRR GMTVEGLKEF 490 500 510 520 530 540 IIAQGSSKSV VFMNWDKIWA FNKKVIDPIA PRYTALEKEK RVIVNVAGAK VERIQVSVHP 550 560 570 580 590 600 KDESLGKKTV LLGPRIYIDY VDAEALKEGE NATFINWGNI LIRKVNKDAS GNITSVDAAL 610 620 630 640 650 660 NLENKDFKKT LKLTWLAVED DPSAYPPTFC VYFDNIISKA VLGKDEDFKQ FIGHKTRDEV 670 680 690 700 710 720 PMLGDPELKK CKKGDIIQLQ RRGFFKVDVA YAPPSGYTNV PSPIVLFSIP DGHTKDVPTS 730 740 750 760 770 780 GLKVNAPDAK ATKKASSPVS SSGQASELDS QISQQGDLVR DLKSKKAAKD QIDVAVKKLL 790 800 810 820 830 840 ALKADYKSAT GKDWKPGQTS ASSAPVPAAS SSSANDAVSV NASIVKQGDL VRDLKGKKAS 850 860 870 880 890 900 KPEIDAAVKT LLELKAQYKT LTGQDWKPGT VPTTAAPSAS AAPSVGVNDS VAQILSQITA 910 920 930 940 950 960 QGDKVRELKS AKADKATVDA AVKTLLSLKA DYKAATGSDW KPGTTAPAPA AAPVKVKQEK 970 980 990 1000 1010 1020 NPDPASVLTV NTLLNKIAQQ GDKIRQLKSA KSEKSLVEAE VKLLLALKTD YKSLTGQEWK 1030 1040 1050 1060 1070 1080 PGTVAPAPTT VNVIDLTGGD SGSDVGSVLS KIQAQGDKIR KLKSEKAAKN VIDPEVKTLL 1090 1100 1110 1120 1130 1140 ALKGEYKTLS GKDWTPDAKS EPAVVKKEAS PVSMASPAKD ELTQEINAQG EKVRAAKGNK 1150 1160 1170 1180 1190 1200 AAKEVIDAEV AKLLALKAKY KEVTGTDFPV AGRGGGGGGG SAKKAPKEAQ PKPAKPVKKE 1210 1220 1230 1240 1250 1260 PAADASGAVK KQTRLGLEAT KEDNLPDWYS QVITKGEMIE YYDVSGCYIL RQWSFAIWKA 1270 1280 1290 1300 1310 1320 IKTWFDAEIT RMGVKECYFP IFVSKAVLEK EKTHIADFAP EVAWVTKSGD SDLAEPIAVR 1330 1340 1350 1360 1370 1380 PTSETVMYPA YAKWVQSYRD LPIRLNQWNN VVRWEFKQPT PFLRTREFLW QEGHTAFADK 1390 1400 1410 1420 1430 1440 EEAAKEVLDI LDLYALVYTH LLAIPVVKGR KTEKEKFAGG DYTTTVEAFI SASGRAIQGA 1450 1460 1470 1480 1490 1500 TSHHLGQNFS KMFEIVYEDP ETQQKKYVYQ NSWGITTRTI GVMIMVHADN QGLVLPPHVA 1510 1520 1530 1540 1550 1560 CIQAIVVPCG ITVNTKDDER AQLLDACKAL EKRLVGGGVR CEGDYRDNYS PGWKFNHWEL 1570 1580 1590 1600 1610 1620 KGVPLRLEVG PKDLKAQQLV AVRRDTVEKI TIPLADVEKK IPALLETIHE SMLNKAQEDM 1630 1640 1650 1660 1670 1680 TSHTKKVTNW TDFCGFLEQK NILLAPFCGE ISCEDKIKAD SARGEEAEPG APAMGAKSLC 1690 1700 1710 IPFDQPAPIA ASDKCINPSC TNKPKFYTLF GRSY
	Isoform B. Checksum: 0E0D298DF6D006C9	FASTA	996	107,835
	10 20 30 40 50 60 MLNYLACGSL SSTSKKASSP VSSSGQASEL DSQISQQGDL VRDLKSKKAA KDQIDVAVKK 70 80 90 100 110 120 LLALKADYKS ATGKDWKPGQ TSASSAPVPA ASSSSANDAV SVNASIVKQG DLVRDLKGKK 130 140 150 160 170 180 ASKPEIDAAV KTLLELKAQY KTLTGQDWKP GTVPTTAAPS ASAAPSVGVN DSVAQILSQI 190 200 210 220 230 240 TAQGDKVREL KSAKADKATV DAAVKTLLSL KADYKAATGS DWKPGTTAPA PAAAPVKVKQ 250 260 270 280 290 300 EKNPDPASVL TVNTLLNKIA QQGDKIRQLK SAKSEKSLVE AEVKLLLALK TDYKSLTGQE 310 320 330 340 350 360 WKPGTVAPAP TTVNVIDLTG GDSGSDVGSV LSKIQAQGDK IRKLKSEKAA KNVIDPEVKT 370 380 390 400 410 420 LLALKGEYKT LSGKDWTPDA KSEPAVVKKE ASPVSMASPA KDELTQEINA QGEKVRAAKG 430 440 450 460 470 480 NKAAKEVIDA EVAKLLALKA KYKEVTGTDF PVAGRGGGGG GGSAKKAPKE AQPKPAKPVK 490 500 510 520 530 540 KEPAADASGA VKKQTRLGLE ATKEDNLPDW YSQVITKGEM IEYYDVSGCY ILRQWSFAIW 550 560 570 580 590 600 KAIKTWFDAE ITRMGVKECY FPIFVSKAVL EKEKTHIADF APEVAWVTKS GDSDLAEPIA 610 620 630 640 650 660 VRPTSETVMY PAYAKWVQSY RDLPIRLNQW NNVVRWEFKQ PTPFLRTREF LWQEGHTAFA 670 680 690 700 710 720 DKEEAAKEVL DILDLYALVY THLLAIPVVK GRKTEKEKFA GGDYTTTVEA FISASGRAIQ 730 740 750 760 770 780 GATSHHLGQN FSKMFEIVYE DPETQQKKYV YQNSWGITTR TIGVMIMVHA DNQGLVLPPH 790 800 810 820 830 840 VACIQAIVVP CGITVNTKDD ERAQLLDACK ALEKRLVGGG VRCEGDYRDN YSPGWKFNHW 850 860 870 880 890 900 ELKGVPLRLE VGPKDLKAQQ LVAVRRDTVE KITIPLADVE KKIPALLETI HESMLNKAQE 910 920 930 940 950 960 DMTSHTKKVT NWTDFCGFLE QKNILLAPFC GEISCEDKIK ADSARGEEAE PGAPAMGAKS 970 980 990 LCIPFDQPAP IAASDKCINP SCTNKPKFYT LFGRSY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase." Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M. EMBO J. 10:4267-4277(1991) [PubMed: 1756734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]	"Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex." Cerini C., Semeriva M., Gratecos D. Eur. J. Biochem. 244:176-185(1997) [PubMed: 9063462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A). Strain: Oregon-R.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B). Strain: Berkeley. Tissue: Embryo.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1110, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M74104 mRNA. Translation: AAA28594.1. U59923 Genomic DNA. Translation: AAC47469.1. AE014297 Genomic DNA. Translation: AAF56211.1. AE014297 Genomic DNA. Translation: AAN13964.1. AY058703 mRNA. Translation: AAL13932.1. BT001645 mRNA. Translation: AAN71400.1. Different initiation.
PIR	S18644.
RefSeq	NP_524471.2. NP_732925.1.
UniGene	Dm.1304
3D structure databases
HSSP	HSSP built from PDB template 1FYJ based on UniProtKB P07814.
ModBase	Search...
Protein-protein interaction databases
STRING	P28668.
Genome annotation databases
Ensembl	FBtr0084511; FBpp0083898; FBgn0005674; Drosophila melanogaster. [Genome view]
GeneID	42834.
KEGG	dme:Dmel_CG5394.
NMPDR	fig|7227.3.peg.14325.
Organism-specific databases
CTD	42834.
FlyBase	FBgn0005674. Aats-glupro.
Phylogenomic databases
HOGENOM	P28668.
OMA	MKEVAKH.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-013073-MON.
BRENDA	6.1.1.15. 48. 6.1.1.17. 48.
Gene expression databases
GermOnline	CG5394. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR001412. aa-tRNA-synth_I_CS. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR004526. Glu-tRNA-synth_Ic_arc/euk. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020059. Glu/Gln-tRNA-synth_Ic_codon-bd. IPR020060. Glu/Gln-tRNA-synth_Ic_N. IPR004499. Pro-tRNA-synth_IIa_pro-type. IPR016061. Pro-tRNA_synth_II_C. IPR014729. Rossmann-like_a/b/a_fold. IPR009068. S15_NS1_RNA_bd. IPR000738. WHEP-TRS. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. G3DSA:1.10.287.10. S15_NS1_RNA_bd. 6 hits.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF09180. ProRS-C_1. 1 hit. PF00749. tRNA-synt_1c. 1 hit. PF03950. tRNA-synt_1c_C. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF00458. WHEP-TRS. 6 hits. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
TIGRFAMs	TIGR00463. gltX_arch. 1 hit. TIGR00408. proS_fam_I. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50862. AA_TRNA_LIGASE_II. 1 hit. PS00762. WHEP_TRS_1. 6 hits. PS51185. WHEP_TRS_2. 6 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	830817.

Entry information

Entry name

SYEP_DROME

Accession

Primary (citable) accession number: P28668
Secondary accession number(s): Q8IGR4 , Q8IMX9, Q95TL3, Q9VCF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	March 1, 2004
Last modified:	November 3, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project