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Protein

Ubiquitin carboxyl-terminal hydrolase calypso

Gene

calypso

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polycomb group (PcG) protein. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-118' (H2AK118ub1). Does not deubiquitinate monoubiquitinated histone H2B. Required to maintain the transcriptionally repressive state of homeotic genes throughout development. The PR-DUB complex has weak or no activity toward 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311NucleophileCurated
Active sitei213 – 2131Proton donorBy similarity
Sitei228 – 2281Important for enzyme activityBy similarity

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  • chromatin silencing Source: UniProtKB
  • monoubiquitinated histone H2A deubiquitination Source: UniProtKB
  • specification of segmental identity, abdomen Source: FlyBase
  • ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC12.A09.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase calypso (EC:3.4.19.12)
Alternative name(s):
BAP1 homolog
Gene namesi
Name:calypso
ORF Names:CG8445
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0262166. calypso.

Subcellular locationi

  • Nucleus

  • Note: Localizes to PcG response elements (PREs).

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nuclear chromatin Source: UniProtKB
  • nucleus Source: FlyBase
  • PR-DUB complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Polycomb phenotype leading to lethality, probably due to misexpression of homeotic genes.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311C → S: Abolishes deubiquitinase activity without affecting the interaction with Asx. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Ubiquitin carboxyl-terminal hydrolase calypsoPRO_0000395823Add
BLAST

Proteomic databases

PaxDbiQ7K5N4.
PRIDEiQ7K5N4.

Expressioni

Gene expression databases

BgeeiQ7K5N4.

Interactioni

Subunit structurei

Component of the PR-DUB complex, at least composed of calypso and Asx.1 Publication

Protein-protein interaction databases

BioGridi62514. 29 interactions.
DIPiDIP-59274N.
STRINGi7227.FBpp0086383.

Structurei

3D structure databases

ProteinModelPortaliQ7K5N4.
SMRiQ7K5N4. Positions 46-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi440 – 4434Poly-Gln
Compositional biasi444 – 4474Poly-Ala

Sequence similaritiesi

Belongs to the peptidase C12 family. BAP1 subfamily.Curated

Phylogenomic databases

eggNOGiNOG249036.
GeneTreeiENSGT00510000046560.
InParanoidiQ7K5N4.
KOiK08588.
OMAiAITHKLK.
OrthoDBiEOG7GN2M2.
PhylomeDBiQ7K5N4.

Family and domain databases

Gene3Di3.40.532.10. 1 hit.
InterProiIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERiPTHR10589. PTHR10589. 1 hit.
PfamiPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSiPR00707. UBCTHYDRLASE.

Sequencei

Sequence statusi: Complete.

Q7K5N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAAGGGSGA QAAAVAAGNN SLSHNALLST ASGATTMPMA QLADGWLELE
60 70 80 90 100
SDPGLFTLLL KDFGCHDVQV EEVYDLQKPI ESPYGFIFLF RWIEERRARR
110 120 130 140 150
KIVETTAEIF VKDEEAISSI FFAQQVVPNS CATHALLSVL LNCNENNLQL
160 170 180 190 200
GDTLSRLKTH TKGMSPENKG LAIGNTPELA CAHNSHAMPQ ARRRLERTGA
210 220 230 240 250
GVSSCRFTGE AFHFVSFVPI NGQLFELDGL KPYPMNHGGW EDSEDWTDKF
260 270 280 290 300
RRVMAERLGI ATGEQDIRFN LMAVVPDRRI AITHKLKMLR TNQAIVSGTL
310 320 330 340 350
QKLLKADEQG ESGNGDSQRP DTPTTLLEPS AFTARDLQSL LKNLDTEIAI
360 370 380 390 400
NEQHLADEND RRHMFKVDAS RRTHNYDKFI CTFLSMLAHQ GVLGELVSQH
410 420 430 440 450
LLPSKKVSGQ GAANRISKQS TTASAGGSTA AGTASTPKTQ QQQAAAAKNG
460 470
KSPSKTPGRR RKGRNKCRKR K
Length:471
Mass (Da):51,507
Last modified:October 3, 2006 - v1
Checksum:iB7C90121EF7716E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58046.1.
AE013599 Genomic DNA. Translation: AAO41384.1.
AY047515 mRNA. Translation: AAK77247.1.
RefSeqiNP_611096.1. NM_137252.3.
NP_788374.1. NM_176194.2.
UniGeneiDm.19939.

Genome annotation databases

EnsemblMetazoaiFBtr0087245; FBpp0086383; FBgn0262166.
FBtr0087246; FBpp0086384; FBgn0262166.
GeneIDi36794.
KEGGidme:Dmel_CG8445.
UCSCiCG8445-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58046.1.
AE013599 Genomic DNA. Translation: AAO41384.1.
AY047515 mRNA. Translation: AAK77247.1.
RefSeqiNP_611096.1. NM_137252.3.
NP_788374.1. NM_176194.2.
UniGeneiDm.19939.

3D structure databases

ProteinModelPortaliQ7K5N4.
SMRiQ7K5N4. Positions 46-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62514. 29 interactions.
DIPiDIP-59274N.
STRINGi7227.FBpp0086383.

Protein family/group databases

MEROPSiC12.A09.

Proteomic databases

PaxDbiQ7K5N4.
PRIDEiQ7K5N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087245; FBpp0086383; FBgn0262166.
FBtr0087246; FBpp0086384; FBgn0262166.
GeneIDi36794.
KEGGidme:Dmel_CG8445.
UCSCiCG8445-RA. d. melanogaster.

Organism-specific databases

CTDi36794.
FlyBaseiFBgn0262166. calypso.

Phylogenomic databases

eggNOGiNOG249036.
GeneTreeiENSGT00510000046560.
InParanoidiQ7K5N4.
KOiK08588.
OMAiAITHKLK.
OrthoDBiEOG7GN2M2.
PhylomeDBiQ7K5N4.

Miscellaneous databases

GenomeRNAii36794.
NextBioi800424.
PROiQ7K5N4.

Gene expression databases

BgeeiQ7K5N4.

Family and domain databases

Gene3Di3.40.532.10. 1 hit.
InterProiIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERiPTHR10589. PTHR10589. 1 hit.
PfamiPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSiPR00707. UBCTHYDRLASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  4. "A genetic screen identifies novel polycomb group genes in Drosophila."
    Gaytan de Ayala Alonso A., Gutierrez L., Fritsch C., Papp B., Beuchle D., Muller J.
    Genetics 176:2099-2108(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB."
    Scheuermann J.C., de Ayala Alonso A.G., Oktaba K., Ly-Hartig N., McGinty R.K., Fraterman S., Wilm M., Muir T.W., Muller J.
    Nature 465:243-247(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, INTERACTION WITH ASX, MUTAGENESIS OF CYS-131, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCALYP_DROME
AccessioniPrimary (citable) accession number: Q7K5N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: October 3, 2006
Last modified: July 22, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.