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Q7K5N4 (CALYP_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. 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 calypso

EC=3.4.19.12
Alternative name(s):
BAP1 homolog
Gene names
Name:calypso
ORF Names:CG8445
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

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 PR-DUB complex, at least composed of calypso and Asx. Ref.5

Subcellular location

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

Disruption phenotype

Polycomb phenotype leading to lethality, probably due to misexpression of homeotic genes. Ref.4 Ref.5

Sequence similarities

Belongs to the peptidase C12 family. BAP1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Ubiquitin carboxyl-terminal hydrolase calypso
PRO_0000395823

Regions

Compositional bias440 – 4434Poly-Gln
Compositional bias444 – 4474Poly-Ala

Sites

Active site1311Nucleophile Probable
Active site2131Proton donor By similarity
Site2281Important for enzyme activity By similarity

Experimental info

Mutagenesis1311C → S: Abolishes deubiquitinase activity without affecting the interaction with Asx. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q7K5N4 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: B7C90121EF7716E5

FASTA47151,507
        10         20         30         40         50         60 
MNAAGGGSGA QAAAVAAGNN SLSHNALLST ASGATTMPMA QLADGWLELE SDPGLFTLLL 

        70         80         90        100        110        120 
KDFGCHDVQV EEVYDLQKPI ESPYGFIFLF RWIEERRARR KIVETTAEIF VKDEEAISSI 

       130        140        150        160        170        180 
FFAQQVVPNS CATHALLSVL LNCNENNLQL GDTLSRLKTH TKGMSPENKG LAIGNTPELA 

       190        200        210        220        230        240 
CAHNSHAMPQ ARRRLERTGA GVSSCRFTGE AFHFVSFVPI NGQLFELDGL KPYPMNHGGW 

       250        260        270        280        290        300 
EDSEDWTDKF RRVMAERLGI ATGEQDIRFN LMAVVPDRRI AITHKLKMLR TNQAIVSGTL 

       310        320        330        340        350        360 
QKLLKADEQG ESGNGDSQRP DTPTTLLEPS AFTARDLQSL LKNLDTEIAI NEQHLADEND 

       370        380        390        400        410        420 
RRHMFKVDAS RRTHNYDKFI CTFLSMLAHQ GVLGELVSQH LLPSKKVSGQ GAANRISKQS 

       430        440        450        460        470 
TTASAGGSTA AGTASTPKTQ QQQAAAAKNG KSPSKTPGRR RKGRNKCRKR K 

« Hide

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.
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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013599 Genomic DNA. Translation: AAF58046.1.
AE013599 Genomic DNA. Translation: AAO41384.1.
AY047515 mRNA. Translation: AAK77247.1.
RefSeqNP_611096.1. NM_137252.2.
NP_788374.1. NM_176194.1.
UniGeneDm.19939.

3D structure databases

ProteinModelPortalQ7K5N4.
SMRQ7K5N4. Positions 46-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59274N.
STRING7227.FBpp0086383.

Protein family/group databases

MEROPSC12.A09.

Proteomic databases

PaxDbQ7K5N4.
PRIDEQ7K5N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087245; FBpp0086383; FBgn0262166.
FBtr0087246; FBpp0086384; FBgn0262166.
GeneID36794.
KEGGdme:Dmel_CG8445.
UCSCCG8445-RA. d. melanogaster.

Organism-specific databases

CTD36794.
FlyBaseFBgn0262166. calypso.

Phylogenomic databases

eggNOGNOG249036.
GeneTreeENSGT00510000046560.
InParanoidQ7K5N4.
KOK08588.
OMATDKFRRV.
OrthoDBEOG7GN2M2.
PhylomeDBQ7K5N4.

Gene expression databases

BgeeQ7K5N4.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
ProtoNetSearch...

Other

GenomeRNAi36794.
NextBio800424.
PROQ7K5N4.

Entry information

Entry nameCALYP_DROME
AccessionPrimary (citable) accession number: Q7K5N4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 61 of the entry and version 1 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