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A1L2G3

- BAP1_DANRE

UniProt

A1L2G3 - BAP1_DANRE

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Protein

Ubiquitin carboxyl-terminal hydrolase BAP1

Gene

bap1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

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 sitei91 – 911NucleophileBy similarity
Active sitei169 – 1691Proton donorBy similarity
Sitei184 – 1841Important for enzyme activityBy similarity

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. ubiquitin-specific protease activity Source: UniProtKB
  3. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
  2. protein deubiquitination Source: UniProtKB
  3. protein K48-linked deubiquitination Source: UniProtKB
  4. regulation of cell cycle Source: UniProtKB
  5. regulation of cell growth Source: UniProtKB
  6. 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

MEROPSiC12.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase BAP1 (EC:3.4.19.12)
Alternative name(s):
BRCA1-associated protein 1
Gene namesi
Name:bap1
ORF Names:si:dkey-42i9.9
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

Organism-specific databases

ZFINiZDB-GENE-050208-492. bap1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. PR-DUB complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Neuronal hyperplasia, suggesting a role in Notch signaling pathway.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 755755Ubiquitin carboxyl-terminal hydrolase BAP1PRO_0000395819Add
BLAST

Interactioni

Subunit structurei

Component of the PR-DUB complex.By similarity

Protein-protein interaction databases

STRINGi7955.ENSDARP00000086210.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C12 family. BAP1 subfamily.Curated

Phylogenomic databases

eggNOGiNOG249036.
HOGENOMiHOG000013189.
HOVERGENiHBG054042.
InParanoidiA1L2G3.
PhylomeDBiA1L2G3.

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.

A1L2G3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ SPVYGFIFLF
60 70 80 90 100
KWIEERRSRR KVSTLVDETS VIDDDIVNDM FFAHQLIPNS CATHALLSVL
110 120 130 140 150
LNCSGVELGM TLSRMKAFTK GFNPESKGYA IGNAPELAKA HNSHARPEPR
160 170 180 190 200
HLPEKQNGIS AVRTMEAFHF VSYVPIKDRL FELDGLKAYP IDHGPWGEDE
210 220 230 240 250
EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YESKLDILKR
260 270 280 290 300
NRQIILEGLQ QIREKKVIRM TQQESGQDRK QQDSSSSEDT PPVVKKEEVQ
310 320 330 340 350
ETPIPSGAEQ ATPTEAQEGA ASLPSPAGKV RSMAKPALPA GGAPPPAPLP
360 370 380 390 400
APSTNTIVQR LPAFLDNHNY AKSPMQEEED LAAGVGRSRP PQPPYSDDED
410 420 430 440 450
DYDDEEEECS TAGVTNSRVR RKLGLRTRTM SRTAVGGVAA MEGQLALSVL
460 470 480 490 500
AEKLKKEVQR KDALATTGST PLNVRTEGRT GGISITSACQ PSPTPSNEST
510 520 530 540 550
DTASEIGSAF NSPLRSPARS QATTRPSSPV ASHVGRVLFG EEEGLPRLDA
560 570 580 590 600
RHNRAVRDLG VLVSSTQLQL QEDGVIFALP PTEALEGLKK VGGVDKKKKE
610 620 630 640 650
EASGPGGEEE VKEGPSVEMK AEDVKESVDV KPEKENLPTT DVENSTKPPG
660 670 680 690 700
EKYTPKELLA LLKYVEADIA NYEVYLKEEV EKRKKYKIDD QRRTHNYDEF
710 720 730 740 750
ICTFISMLAQ EGMLASLVEQ NISVRRRQGV SIGRLHKQRK PDRRKRSRPY

KAKRQ
Length:755
Mass (Da):83,777
Last modified:July 13, 2010 - v2
Checksum:i6DE37B40D438B535
GO

Sequence cautioni

The sequence AAI29507.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAK11034.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541E → G in AAI29507. 1 PublicationCurated
Sequence conflicti111 – 1111T → A in AAI29507. 1 PublicationCurated
Sequence conflicti443 – 4431G → D in AAI29507. 1 PublicationCurated
Sequence conflicti504 – 5041S → P in AAI29507. 1 PublicationCurated
Sequence conflicti617 – 6193VEM → AEI in AAI29507. 1 PublicationCurated
Sequence conflicti627 – 6271S → L in AAI29507. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX465868 Genomic DNA. Translation: CAK11034.1. Sequence problems.
BC129506 mRNA. Translation: AAI29507.1. Sequence problems.
UniGeneiDr.37720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX465868 Genomic DNA. Translation: CAK11034.1 . Sequence problems.
BC129506 mRNA. Translation: AAI29507.1 . Sequence problems.
UniGenei Dr.37720.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000086210.

Protein family/group databases

MEROPSi C12.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ZFINi ZDB-GENE-050208-492. bap1.

Phylogenomic databases

eggNOGi NOG249036.
HOGENOMi HOG000013189.
HOVERGENi HBG054042.
InParanoidi A1L2G3.
PhylomeDBi A1L2G3.

Miscellaneous databases

PROi A1L2G3.

Family and domain databases

Gene3Di 3.40.532.10. 1 hit.
InterProi IPR001578. Peptidase_C12_UCH.
[Graphical view ]
PANTHERi PTHR10589. PTHR10589. 1 hit.
Pfami PF01088. Peptidase_C12. 1 hit.
[Graphical view ]
PRINTSi PR00707. UBCTHYDRLASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBAP1_DANRE
AccessioniPrimary (citable) accession number: A1L2G3
Secondary accession number(s): Q1LXB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: October 29, 2014
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3