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Q9VRP5 (UBP36_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 36

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 36
Protein scrawny
Ubiquitin thioesterase 36
Ubiquitin-specific-processing protease 36
Gene names
Name:scny
Synonyms:Usp36
ORF Names:CG5505
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1038 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). 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

Interacts with atms/PAF1, but not with CycT. Ref.6

Subcellular location

Nucleusnucleolus Ref.6.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform D (identifier: Q9VRP5-3)

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: No experimental confirmation available.
Isoform B (identifier: Q9VRP5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.
     71-110: ESVLENLKSK...TGKLVGANGH → MTVIMVDGFA...KLSTVLFTFA
Note: No experimental confirmation available.
Isoform C (identifier: Q9VRP5-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     91-110: AINGFSGKNNTGKLVGANGH → MLHSPVPRYNKCVPFPTLRT
Note: No experimental confirmation available.
Isoform G (identifier: Q9VRP5-7)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     911-1038: ELLVDAREQR...QPSAQQQQQT → ETFELVCAKR...PDPDRLTDGR
Note: No experimental confirmation available.
Isoform I (identifier: Q9VRP5-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     91-110: AINGFSGKNNTGKLVGANGH → MLHSPVPRYNKCVPFPTLRT
     911-1038: ELLVDAREQR...QPSAQQQQQT → ETFELVCAKR...PDPDRLTDGR
Note: No experimental confirmation available.
Isoform J (identifier: Q9VRP5-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.
     71-110: ESVLENLKSK...TGKLVGANGH → MTVIMVDGFA...KLSTVLFTFA
     911-1038: ELLVDAREQR...QPSAQQQQQT → ETFELVCAKR...PDPDRLTDGR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10381038Ubiquitin carboxyl-terminal hydrolase 36
PRO_0000378498

Regions

Domain172 – 480309USP

Sites

Active site1811Nucleophile
Active site4391Proton acceptor By similarity

Amino acid modifications

Modified residue5131Phosphoserine Ref.5
Modified residue5151Phosphoserine Ref.5
Modified residue6581Phosphothreonine Ref.5
Modified residue6621Phosphothreonine Ref.5
Modified residue6721Phosphoserine Ref.5
Modified residue6741Phosphoserine Ref.5
Modified residue7471Phosphoserine Ref.5
Modified residue7791Phosphoserine Ref.5
Modified residue7821Phosphothreonine Ref.5
Modified residue7851Phosphoserine Ref.5
Modified residue8191Phosphoserine Ref.5
Modified residue8251Phosphothreonine Ref.5
Modified residue8431Phosphoserine Ref.5
Modified residue8461Phosphothreonine Ref.5

Natural variations

Alternative sequence1 – 9090Missing in isoform C and isoform I.
VSP_037590
Alternative sequence1 – 7070Missing in isoform B and isoform J.
VSP_037591
Alternative sequence71 – 11040ESVLE…GANGH → MTVIMVDGFALWLLYKLFLS PCCLLLWHVLKLSTVLFTFA in isoform B and isoform J.
VSP_037592
Alternative sequence91 – 11020AINGF…GANGH → MLHSPVPRYNKCVPFPTLRT in isoform C and isoform I.
VSP_037593
Alternative sequence911 – 1038128ELLVD…QQQQT → ETFELVCAKRIAGHGSVEGS DIVEGSVAVDAAVTSGSDSK DVVVIAVAVTDTTADAPDPD RLTDGR in isoform G, isoform I and isoform J.
VSP_054032

Experimental info

Mutagenesis1811C → S: Loss of H2B deubiquitination. Ref.6
Sequence conflict1151A → T in AAQ22589. Ref.4
Sequence conflict6421N → D in AAQ22589. Ref.4
Sequence conflict6421N → D in AAO42671. Ref.4
Sequence conflict7661P → T in AAQ22589. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform D [UniParc].

Last modified April 16, 2014. Version 3.
Checksum: 98CECD6993333E22

FASTA1,038114,088
        10         20         30         40         50         60 
MPVSMAVCET ANVVNAALRE SLGGNSSAGS STDQAKSGED TNGSLQNHIV ANAKRILMAK 

        70         80         90        100        110        120 
IEYEEVPNYH ESVLENLKSK YIVIKPGNPG AINGFSGKNN TGKLVGANGH DNNGARKQAE 

       130        140        150        160        170        180 
HPNNQSHHIN HHNHQHPTSN PNELPKPKRV LYPRENIRIG WKQSERKWQV GTGMINVGNT 

       190        200        210        220        230        240 
CYLNSTLQAL LHIPALANWL VSEQAHLADC NVAEPGSGCI ICAMTKTLLA TQSNQSAVRP 

       250        260        270        280        290        300 
FLIYSKLKQI CKHMVVGRQE DAHEFLRFLV EAMERAYLMR FRNYKELDQL VKETTPLGQI 

       310        320        330        340        350        360 
FGGYLRSEVR CLSCNHVSIT FQHFQDLLLD IRKADSLEDA FEGHFSRERL EDMGYKCEGC 

       370        380        390        400        410        420 
KKKVSATKQF SLERAPITLC IQLKRFSMIG NKLTKQISFK SRIDLSKYAA RSQAAQAQPL 

       430        440        450        460        470        480 
TYRLVSMVTH LGASQHCGHY TAIGSTDTGS FYNFDDSYVR PIAMHSVCNT NAYIMFFELD 

       490        500        510        520        530        540 
LSQAASPAAN RPNGVRLTNG HSTTPVPAAT VSSPSPTRFI GPQLPAGGAN GYTNGNAQKT 

       550        560        570        580        590        600 
AIQFKQQNQQ SPQNGLQLGT GKFQDTAKPP LVGAHAKGEA TSAPTANGNK SSSPSSNSSS 

       610        620        630        640        650        660 
NHKSINQQQY LPISSDDEDI EDEMKPRPTT AQLPSMPNMT ENHTEPKAKS PVKIQVKTPV 

       670        680        690        700        710        720 
KTPLKSLVPY ESASEEEEAP LPNPRKRPSG EDSSESDQES GQTNGHSKTN GSHTNGSASS 

       730        740        750        760        770        780 
SVHVNNSKQK TDAIDEIFKS LKKSADSDED DDEEEPSIQL TNGWHPQKQS QSQSKAPPSP 

       790        800        810        820        830        840 
KTPPSPAVIK SKTGIWKVTR NDEVDAIEDD VDVVVVEGSP VKIPTPNKNH RNPFSSSKPS 

       850        860        870        880        890        900 
TDSPATPGAK RQKLLNGSAL KSHQQPRVGN GYQSNATSNG STINELLKQS YRGYGSPVLS 

       910        920        930        940        950        960 
WNGKPAELEK ELLVDAREQR QRDIDDDEEN EMDRGRQRKV KSGSAKGNNA SNSTPGYNPF 

       970        980        990       1000       1010       1020 
QEYEGQKRWN KNGGGGGFPR FYNQNYRQNF QQRNKFKFNR FGGPGSAKFQ QQRALQRHLS 

      1030 
AGGGFSRRQP SAQQQQQT 

« Hide

Isoform B [UniParc].

Checksum: 941F6973D4435C8A
Show »

FASTA968107,252
Isoform C [UniParc].

Checksum: 29E5A05BB8761243
Show »

FASTA948104,961
Isoform G (H) [UniParc].

Checksum: 89E02FAC5B5FCC82
Show »

FASTA976105,957
Isoform I [UniParc].

Checksum: 572BE9A8370C7615
Show »

FASTA88696,830
Isoform J [UniParc].

Checksum: 74BBC44F1AB468F4
Show »

FASTA90699,121

References

« Hide '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. 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.
[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. 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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[3]"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] (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., 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. expand/collapse author list , 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 (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D).
Strain: Berkeley.
Tissue: Testis.
[5]"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-513; SER-515; THR-658; THR-662; SER-672; SER-674; SER-747; SER-779; THR-782; SER-785; SER-819; THR-825; SER-843 AND THR-846, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[6]"Drosophila stem cells share a common requirement for the histone H2B ubiquitin protease scrawny."
Buszczak M., Paterno S., Spradling A.C.
Science 323:248-251(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATMS, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-181.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014296 Genomic DNA. Translation: AAN12107.1.
AE014296 Genomic DNA. Translation: AAN12108.1.
AE014296 Genomic DNA. Translation: AAN12109.1.
AE014296 Genomic DNA. Translation: AAN12110.1.
AE014296 Genomic DNA. Translation: AAN12111.1.
AE014296 Genomic DNA. Translation: AFH04310.1.
AE014296 Genomic DNA. Translation: AFH04311.1.
AY051916 mRNA. Translation: AAK93340.1.
BT004507 mRNA. Translation: AAO42671.1.
BT010120 mRNA. Translation: AAQ22589.1.
BT046169 mRNA. Translation: ACI47091.1.
RefSeqNP_647986.3. NM_139729.3.
NP_729092.1. NM_168132.2.
NP_729093.2. NM_168133.2.
NP_729094.1. NM_168134.2.
NP_729095.1. NM_168135.2.
UniGeneDm.6825.

3D structure databases

ProteinModelPortalQ9VRP5.
SMRQ9VRP5. Positions 172-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0076805.

Protein family/group databases

MEROPSC19.097.

Proteomic databases

PaxDbQ9VRP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID38648.
KEGGdme:Dmel_CG5505.

Organism-specific databases

CTD38648.
FlyBaseFBgn0260936. scny.

Phylogenomic databases

eggNOGCOG5533.
InParanoidQ86NM9.
KOK11855.
OMAENEMDRG.
OrthoDBEOG7XDBF6.
PhylomeDBQ9VRP5.

Gene expression databases

BgeeQ9VRP5.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi38648.
NextBio809699.

Entry information

Entry nameUBP36_DROME
AccessionPrimary (citable) accession number: Q9VRP5
Secondary accession number(s): M9NE30 expand/collapse secondary AC list , Q7YTX7, Q86NM9, Q8IQ57, Q8IQ58, Q8IQ59, Q8IQ60, Q960Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: April 16, 2014
Last modified: April 16, 2014
This is version 92 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