Ubiquitin carboxyl-terminal hydrolase BAP1

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A1L2G3 (BAP1_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 38. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Danio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	755 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Molecular function	Chromatin regulator Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	monoubiquitinated histone H2A deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K48-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell cycle Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	PR-DUB complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 755

755

Ubiquitin carboxyl-terminal hydrolase BAP1

PRO_0000395819

Sites

Active site

Nucleophile By similarity

Active site

169

Proton donor By similarity

Site

184

Important for enzyme activity By similarity

Experimental info

Sequence conflict

E → G in AAI29507. Ref.2

Sequence conflict

111

T → A in AAI29507. Ref.2

Sequence conflict

443

G → D in AAI29507. Ref.2

Sequence conflict

504

S → P in AAI29507. Ref.2

Sequence conflict

617 – 619

VEM → AEI in AAI29507. Ref.2

Sequence conflict

627

S → L in AAI29507. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

A1L2G3 [UniParc].

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

755

83,777

        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' referencesShow 'large scale' references »
[1]	The Danio rerio sequencing project at the Sanger Institute Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases 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.
IPI	IPI00491066.
UniGene	Dr.37720.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	7955.ENSDARP00000086210.
Protein family/group databases
MEROPS	C12.004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
ZFIN	ZDB-GENE-050208-492. bap1.
Phylogenomic databases
eggNOG	NOG249036.
HOGENOM	HOG000013189.
HOVERGEN	HBG054042.
Family and domain databases
Gene3D	3.40.532.10. 1 hit.
InterPro	IPR001578. Peptidase_C12. [Graphical view]
PANTHER	PTHR10589. PTHR10589. 1 hit.
Pfam	PF01088. Peptidase_C12. 1 hit. [Graphical view]
PRINTS	PR00707. UBCTHYDRLASE.
PROSITE	PS00140. UCH_1. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BAP1_DANRE

Accession

Primary (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 3, 2013
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents