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A1L2G3 (BAP1_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 BAP1

EC=3.4.19.12
Alternative name(s):
BRCA1-associated protein 1
Gene names
Name:bap1
ORF Names:si:dkey-42i9.9
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length755 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) By similarity.

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 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Mainly nuclear. Binds to chromatin By similarity.

Disruption phenotype

Neuronal hyperplasia, suggesting a role in Notch signaling pathway. Ref.3

Sequence similarities

Belongs to the peptidase C12 family. BAP1 subfamily.

Sequence caution

The sequence AAI29507.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence CAK11034.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 755755Ubiquitin carboxyl-terminal hydrolase BAP1
PRO_0000395819

Sites

Active site911Nucleophile By similarity
Active site1691Proton donor By similarity
Site1841Important for enzyme activity By similarity

Experimental info

Sequence conflict541E → G in AAI29507. Ref.2
Sequence conflict1111T → A in AAI29507. Ref.2
Sequence conflict4431G → D in AAI29507. Ref.2
Sequence conflict5041S → P in AAI29507. Ref.2
Sequence conflict617 – 6193VEM → AEI in AAI29507. Ref.2
Sequence conflict6271S → L in AAI29507. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A1L2G3 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 6DE37B40D438B535

FASTA75583,777
        10         20         30         40         50         60 
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ SPVYGFIFLF KWIEERRSRR 

        70         80         90        100        110        120 
KVSTLVDETS VIDDDIVNDM FFAHQLIPNS CATHALLSVL LNCSGVELGM TLSRMKAFTK 

       130        140        150        160        170        180 
GFNPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGIS AVRTMEAFHF VSYVPIKDRL 

       190        200        210        220        230        240 
FELDGLKAYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK 

       250        260        270        280        290        300 
YESKLDILKR NRQIILEGLQ QIREKKVIRM TQQESGQDRK QQDSSSSEDT PPVVKKEEVQ 

       310        320        330        340        350        360 
ETPIPSGAEQ ATPTEAQEGA ASLPSPAGKV RSMAKPALPA GGAPPPAPLP APSTNTIVQR 

       370        380        390        400        410        420 
LPAFLDNHNY AKSPMQEEED LAAGVGRSRP PQPPYSDDED DYDDEEEECS TAGVTNSRVR 

       430        440        450        460        470        480 
RKLGLRTRTM SRTAVGGVAA MEGQLALSVL AEKLKKEVQR KDALATTGST PLNVRTEGRT 

       490        500        510        520        530        540 
GGISITSACQ PSPTPSNEST DTASEIGSAF NSPLRSPARS QATTRPSSPV ASHVGRVLFG 

       550        560        570        580        590        600 
EEEGLPRLDA RHNRAVRDLG VLVSSTQLQL QEDGVIFALP PTEALEGLKK VGGVDKKKKE 

       610        620        630        640        650        660 
EASGPGGEEE VKEGPSVEMK AEDVKESVDV KPEKENLPTT DVENSTKPPG EKYTPKELLA 

       670        680        690        700        710        720 
LLKYVEADIA NYEVYLKEEV EKRKKYKIDD QRRTHNYDEF ICTFISMLAQ EGMLASLVEQ 

       730        740        750 
NISVRRRQGV SIGRLHKQRK PDRRKRSRPY KAKRQ 

« Hide

References

« Hide 'large scale' references
[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-682.
Tissue: Olfactory epithelium.
[3]"Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development."
Tse W.K., Eisenhaber B., Ho S.H., Ng Q., Eisenhaber F., Jiang Y.J.
BMC Genomics 10:637-637(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX465868 Genomic DNA. Translation: CAK11034.1. Sequence problems.
BC129506 mRNA. Translation: AAI29507.1. Sequence problems.
UniGeneDr.37720.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000086210.

Protein family/group databases

MEROPSC12.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ZFINZDB-GENE-050208-492. bap1.

Phylogenomic databases

eggNOGNOG249036.
HOGENOMHOG000013189.
HOVERGENHBG054042.
PhylomeDBA1L2G3.

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

PROA1L2G3.

Entry information

Entry nameBAP1_DANRE
AccessionPrimary (citable) accession number: A1L2G3
Secondary accession number(s): Q1LXB5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries