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Q9VVR1 (NOT_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase nonstop

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme nonstop
Ubiquitin thioesterase nonstop
Ubiquitin-specific-processing protease nonstop
Gene names
Name:not
ORF Names:CG4166
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length735 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of histone H2B, thereby acting as a coactivator in a large subset of genes. Required to counteract heterochromatin silencing. Controls the development of neuronal connectivity in visual system by being required for accurate axon targeting in the optic lobe. Required for expression of ecdysone-induced genes such as br/broad. Ref.1 Ref.5 Ref.6

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).

Subunit structure

Component of the SAGA transcription coactivator-HAT complex, at least composed of Ada2b, not/nonstop, Pcaf/Gcn5, Sgf11 and Spt3. Ref.5

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in the optic lobe and central brain. Highly expressed in the lamina precursor cells but not in differentiated lamina neurons. Also expressed in marginal, epithelial and medulla glial cells adjacent to the lamina plexus. Ref.1

Disruption phenotype

Defects in the number and migration of glial cells located within the lamina plexus of the developing eye; the lack of glial cells causing mistargeting of the R1-R6 axons in the optic lobe. Lamina neuron development is normal. Ref.1 Ref.5

Sequence similarities

Belongs to the peptidase C19 family. UBP8 subfamily.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence caution

The sequence AAF49249.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAL13936.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Hydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from mutant phenotype PubMed 18516287. Source: FlyBase

axon target recognition

Inferred from mutant phenotype Ref.5PubMed 7857635. Source: FlyBase

chromatin modification

Inferred from mutant phenotype Ref.6. Source: UniProtKB

chromatin organization

Inferred from mutant phenotype Ref.6. Source: FlyBase

glial cell development

Inferred from mutant phenotype Ref.1. Source: FlyBase

glial cell migration

Inferred from mutant phenotype Ref.1. Source: FlyBase

histone deubiquitination

Inferred from mutant phenotype Ref.5. Source: FlyBase

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.6. Source: UniProtKB

protein deubiquitination

Inferred from mutant phenotype Ref.1. Source: FlyBase

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.5. Source: FlyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from genetic interaction Ref.1. Source: FlyBase

   Cellular_componentSAGA complex

Inferred from direct assay Ref.5PubMed 21764853. Source: FlyBase

nucleus

Inferred from direct assay PubMed 21764853. Source: FlyBase

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.5. Source: FlyBase

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 735735Ubiquitin carboxyl-terminal hydrolase nonstop
PRO_0000367514

Regions

Domain397 – 730334USP
Zinc finger283 – 34260UBP-type

Sites

Active site4061Nucleophile By similarity
Active site6891Proton acceptor By similarity

Experimental info

Sequence conflict1901A → T in AAD53181. Ref.1
Sequence conflict1991H → N in AAD53181. Ref.1
Sequence conflict2351A → D in AAD53181. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VVR1 [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: EAE3F4B1DBFF850F

FASTA73582,458
        10         20         30         40         50         60 
MFQYSYIRKI PMPTSEYDFA TGHTDSCLLP THMRACVCVC VQCEIETRKA SEKSQKFTKK 

        70         80         90        100        110        120 
KPNYFQNWAA RRRTAKVAKI RRKQRKCDKA FVPLQSSAKR AKTKENSVDS NTSVFSSSSS 

       130        140        150        160        170        180 
SSSGRSFGRG TERWAVGAEA GRGTAENETL AVAAAAATTT NAGRFITADL IKTVNSDKQR 

       190        200        210        220        230        240 
DRVAKGHRDA KNPLDATKHL RLSDCLRTVQ KLAIELESAD AGSDASAQAN ASADASSAVM 

       250        260        270        280        290        300 
SETGCRHYQS YVKEHSYDTF RVIDAYFAAC VNRDARERKA IHCNCFECGS YGIQLYACLH 

       310        320        330        340        350        360 
CIYFGCRGAH ITSHLRSKKH NVALELSHGT LYCYACRDFI YDARSREYAL INRKLEAKDL 

       370        380        390        400        410        420 
QKSIGWVPWV PTTKETNLLL ANARRRLVRP NQTIGLRGLL NLGATCFMNC IVQALVHTPL 

       430        440        450        460        470        480 
LSDYFMSDRH DCGSKSSHKC LVCEVSRLFQ EFYSGSRSPL SLHRLLHLIW NHAKHLAGYE 

       490        500        510        520        530        540 
QQDAHEFFIA TLDVLHRHCV KAKAEHESKS NSSGSGSGTN SSNSSSSHCY GQCNCIIDQI 

       550        560        570        580        590        600 
FTGMLQSDVV CQACNGVSTT YDPFWDISLD LGETTTHGGV TPKTLIDCLE RYTRAEHLGS 

       610        620        630        640        650        660 
AAKIKCSTCK SYQESTKQFS LRTLPSVVSF HLKRFEHSAL IDRKISSFIQ FPVEFDMTPF 

       670        680        690        700        710        720 
MSEKKNAYGD FRFSLYAVVN HVGTIDTGHY TAYVRHQKDT WVKCDDHVIT MASLKQVLDS 

       730 
EGYLLFYHKN VLEYE 

« Hide

References

« Hide 'large scale' references
[1]"Glial cells mediate target layer selection of retinal axons in the developing visual system of Drosophila."
Poeck B., Fischer S., Gunning D., Zipursky S.L., Salecker I.
Neuron 29:99-113(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[2]"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. expand/collapse author list , 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.
[3]"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. expand/collapse author list , 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.
[4]"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 27-735.
Strain: Berkeley.
Tissue: Embryo.
[5]"SAGA-mediated H2B deubiquitination controls the development of neuronal connectivity in the Drosophila visual system."
Weake V.M., Lee K.K., Guelman S., Lin C.-H., Seidel C., Abmayr S.M., Workman J.L.
EMBO J. 27:394-405(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN THE SAGA COMPLEX, INTERACTION WITH SGF11.
[6]"A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF179590 Genomic DNA. Translation: AAD53181.1.
AE014296 Genomic DNA. Translation: AAF49249.2. Sequence problems.
AY058707 mRNA. Translation: AAL13936.1. Different initiation.
RefSeqNP_524140.2. NM_079416.4.
UniGeneDm.2731.

3D structure databases

ProteinModelPortalQ9VVR1.
SMRQ9VVR1. Positions 296-727.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65311. 5 interactions.
IntActQ9VVR1. 4 interactions.
MINTMINT-6179419.
STRING7227.FBpp0288698.

Protein family/group databases

MEROPSC19.095.

Proteomic databases

PaxDbQ9VVR1.
PRIDEQ9VVR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID40030.
KEGGdme:Dmel_CG4166.
UCSCCG4166-RB. d. melanogaster.

Organism-specific databases

CTD40030.
FlyBaseFBgn0013717. not.

Phylogenomic databases

eggNOGCOG5533.
InParanoidQ9U6Q9.
KOK11366.
OrthoDBEOG7FR7G7.
PhylomeDBQ9VVR1.

Gene expression databases

BgeeQ9VVR1.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR015880. Znf_C2H2-like.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40030.
NextBio816633.

Entry information

Entry nameNOT_DROME
AccessionPrimary (citable) accession number: Q9VVR1
Secondary accession number(s): Q95TK9, Q9U6Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase