Q24574 (UBPE_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 64E
EC=3.4.19.12

Alternative name(s):
Ubiquitin thioesterase 64E
Ubiquitin-specific-processing protease 64E
Short name=Deubiquitinating enzyme 64E

Gene names

Name:	Ubp64E
Synonyms:	D-UBP-64E
ORF Names:	CG5486

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1556 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has an effect on position-effect variegation.
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the peptidase C19 family.
Sequence caution	The sequence AAL13901.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	compound eye cone cell differentiation Inferred from mutant phenotype PubMed 18160715. Source: FlyBase protein deubiquitination Inferred from direct assay PubMed 18160715. Source: FlyBase protein stabilization Inferred from direct assay PubMed 18160715. Source: FlyBase regulation of chromatin silencing Inferred from mutant phenotype PubMed 20838586. Source: FlyBase ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 18160715. Source: FlyBase nucleus Inferred from direct assay PubMed 18160715. Source: FlyBase
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1556	1556	Ubiquitin carboxyl-terminal hydrolase 64E		PRO_0000080687
Sites
	Active site	405	1	Nucleophile By similarity
	Active site	720	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	172	1	Phosphoserine Ref.6
	Modified residue	173	1	Phosphoserine Ref.6
	Modified residue	238	1	Phosphoserine Ref.6
	Modified residue	1131	1	Phosphoserine Ref.6
	Modified residue	1132	1	Phosphoserine Ref.6
	Modified residue	1140	1	Phosphoserine Ref.6
	Modified residue	1141	1	Phosphoserine Ref.6
	Modified residue	1199	1	Phosphoserine Ref.6
	Modified residue	1201	1	Phosphoserine Ref.6
	Modified residue	1205	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	437 – 439	3	NIP → KS in CAA67601. Ref.4
	Sequence conflict	513	1	D → A in CAA67601. Ref.4
	Sequence conflict	519	1	E → G in CAA67601. Ref.4
	Sequence conflict	525 – 526	2	TR → NDC in CAA67601. Ref.4
	Sequence conflict	645	1	D → DS in AAL13901. Ref.5
	Sequence conflict	791	1	A → R in CAA67601. Ref.4
	Sequence conflict	910	1	Missing in CAA67601. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q24574 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: F70AE5BB2914E8BE	FASTA	1,556	173,794
	10 20 30 40 50 60 MTDKESEQCT VSVFDQTPGS EQKKINVVVR SHFTVKRVID LIGTQFSYEK FELLLQPHDN 70 80 90 100 110 120 KDLVNLNALE SQLMYEVAGF EPQLKNHLIL LPSGSWDGDV TKRFELPIKR VVVKKVMKSD 130 140 150 160 170 180 GEKAKSPATG EKKKRVVGEK TKKKPASGSS SPSKAKTTSE DSLAKTSISS ESSPEKTSKI 190 200 210 220 230 240 KTTAAKISKP GSEKAPRASP EECPELSTEI NSKNTSSESP VAKKTAKVTS KPTLELLSPI 250 260 270 280 290 300 KPSSPIKELD CEPVDTLSKQ QLSEQLQLYP QGRNLISPVD DAPSDLFISD AEQLSDDDLA 310 320 330 340 350 360 LGASASPTML GPGYDYGAPT GDSDVEGVTG VTDPSTIGTD DGTYPALSNF YRRKYGGDEL 370 380 390 400 410 420 RAWQRVNTTG ADFVSSATTE TEAEARQASL GPRGYVGLVN QAMTCYLNSL LQALFMTPEF 430 440 450 460 470 480 RNALYRWEFD NDNEAKNIPY QLQKLFLNLQ TSPKAAVETT DLTRSFGWDS TEAWQQHDIQ 490 500 510 520 530 540 ELCRVMFDAL EHKFKNTKQA NLISNLYEGK MNDYVKCLEC NTEKTREDTF LDIPLPVRPF 550 560 570 580 590 600 GSSSAYGSIE EALRAFVQPE TLDGNNQYLC EKCKKKCDAH KGLHFKSFPY ILTLHLKRFD 610 620 630 640 650 660 FDYQTMHRIK LNDRVTFPQT LNLNTFINRS GNSGEQNSQL NGTVDDCSTA DSGSAMEDDN 670 680 690 700 710 720 LSSGVVTTAS SSQHENDLND EDEGIDMSSS TSKSAKQGSG PYLYELFAIM IHSGSASGGH 730 740 750 760 770 780 YYAYIKDFDN NEWFCFNDQN VTSITQEDIQ RSFGGPNGSY YSSAYTSSTN AYMLMYRQVD 790 800 810 820 830 840 AKRNELVAKV ADFPEHIKTL LPKLHSEEET RVSRLGRHIT VTDLALPDLY KPRVYFYNPS 850 860 870 880 890 900 LKKMKITRVY VSQSFNINLV LMSAYEMLNV EQFAPLSRCR LVAYNSSMDT IIQSLESCTD 910 920 930 940 950 960 PALTELRAAQ NYSLDFLLEY RAEDQEFEVY PPNGITWYVF KVDLSTMAMD GPFLVYSAAR 970 980 990 1000 1010 1020 EREASDVLRR SIALRLHISE QQFLLATVRA TVPKAFVSYD PHPTPEALQH LQNMANTQFK 1030 1040 1050 1060 1070 1080 SITYFYLNVP NTDAATLEML GVPTVESVEC ASGGDVVDAA MMNGVAPGHM SSSNDYDWRR 1090 1100 1110 1120 1130 1140 YKRDLVEPMS QPSPSHGHES NSEDSSLSDG DRTLVETDNM AHRGGGDSQV SSTSHSPQLS 1150 1160 1170 1180 1190 1200 SPEDEAASHD AMMRVHAYCN GNGSYAAADV VDPLLLPTST NHFFYATKVE CVDVVGTGSS 1210 1220 1230 1240 1250 1260 SGHQSDEEAQ LRKPTRAYKL LVGTHMRMGA FKKHIEQLIQ VPAAHFKLQR KHDNNLSNNQ 1270 1280 1290 1300 1310 1320 NNSLVHLIEG ETLTVELGKT LEPDEFKAKI HFLRLADIDN ETSKLPCVCE WVYNANTTAE 1330 1340 1350 1360 1370 1380 QAKKELVAKL HRIDAKYATL SVQNCRIWLK GGRIPIKILS DDETLYCDMR SSIAAEFIVQ 1390 1400 1410 1420 1430 1440 ECEEEVDPQP KDDSLTLFVR RWCPAKLEFG KFQEITLDQD SEIRLSLSQI SDIPIDKLSY 1450 1460 1470 1480 1490 1500 MKLNSNFPCT SISALSVNES SSWYSVPTTL DKYPLNSTQT GNIYLYKDRT VPARELTLEE 1510 1520 1530 1540 1550 RRLMNAREKA RLDRVGCVST TRYAQRRERA LKIYLDSPEK SSNVTASAPM DVHVNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster." Henchoz S., de Rubertis F., Pauli D., Spierer P. Mol. Cell. Biol. 16:5717-5725(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 318-1556. Tissue: Embryo.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-1556. 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-173; SER-238; SER-1131; SER-1132; SER-1140; SER-1141; SER-1199; SER-1201 AND SER-1205, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014296 Genomic DNA. Translation: AAF50752.2. AE014296 Genomic DNA. Translation: AAN12105.1. AE014296 Genomic DNA. Translation: AAS65076.1. BT003784 mRNA. Translation: AAO41467.1. X99211 mRNA. Translation: CAA67601.1. Sequence problems. AY058672 mRNA. Translation: AAL13901.1. Different initiation.
RefSeq	NP_523937.2. NM_079213.4. NP_729087.1. NM_168129.3. NP_996001.2. NM_206279.3.
UniGene	Dm.3704.
3D structure databases
ProteinModelPortal	Q24574.
SMR	Q24574. Positions 394-812.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q24574. 3 interactions.
MINT	MINT-971166.
Protein family/group databases
MEROPS	C19.A50.
Proteomic databases
PaxDb	Q24574.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077095; FBpp0076802; FBgn0016756. FBtr0077096; FBpp0076803; FBgn0016756.
GeneID	38644.
KEGG	dme:Dmel_CG5486.
Organism-specific databases
CTD	38644.
FlyBase	FBgn0016756. Ubp64E.
Phylogenomic databases
eggNOG	COG5077.
GeneTree	ENSGT00630000089581.
InParanoid	Q24574.
KO	K11857.
OMA	CLECNTE.
OrthoDB	EOG4X69Q3.
PhylomeDB	Q24574.
Gene expression databases
Bgee	Q24574.
GermOnline	CG5486. Drosophila melanogaster.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Ubp64E. drosophila.
GenomeRNAi	38644.
NextBio	809673.

Entry information

Entry name

UBPE_DROME

Accession

Primary (citable) accession number: Q24574
Secondary accession number(s): A4V1I7, Q95TM9, Q9VRP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project