BAP1_BRAFL
ID BAP1_BRAFL Reviewed; 694 AA.
AC C4A0D9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q92560};
DE AltName: Full=BRCA1-associated protein 1;
GN Name=BAP1; ORFNames=BRAFLDRAFT_277645;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by
CC mediating deubiquitination of histone H2A. Catalytic component of the
CC PR-DUB complex, a complex that specifically mediates deubiquitination
CC of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By
CC similarity). {ECO:0000250|UniProtKB:Q92560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560};
CC -!- SUBUNIT: Component of the PR-DUB complex.
CC {ECO:0000250|UniProtKB:Q92560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus
CC {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to
CC chromatin. {ECO:0000250|UniProtKB:Q92560}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; GG666800; EEN41742.1; -; Genomic_DNA.
DR RefSeq; XP_002585731.1; XM_002585685.1.
DR AlphaFoldDB; C4A0D9; -.
DR SMR; C4A0D9; -.
DR STRING; 7739.XP_002585731.1; -.
DR MEROPS; C12.004; -.
DR PRIDE; C4A0D9; -.
DR eggNOG; KOG2778; Eukaryota.
DR InParanoid; C4A0D9; -.
DR OrthoDB; 1363547at2759; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Cytoplasm; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..694
FT /note="Ubiquitin carboxyl-terminal hydrolase BAP1"
FT /id="PRO_0000395822"
FT REGION 392..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 678..683
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT COMPBIAS 396..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 184
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
SQ SEQUENCE 694 AA; 77164 MW; 6A4B1902DE067B3D CRC64;
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLSKPIE GPVYGFIFLF KWSEERRSRR
KVGPSMEESF VVDEDIVNDM FFAQQLIPNS CATHALLSVL LNCPQISLGS TLTRLKYFTR
GMGPESKGWA IGNVPEIARA HNSHARPEPR HLPEKQTGIS SVRTAEAFHF VSYVTTNDRL
FELDGLKPYP IDHGPWGEKE DWTEKFRRVI SERIGNATGG ENGHDIRFNL MAVVADRRQQ
YETKLNTLKT NRQIVLEALQ QVGGVNTKKS IQYAEVSHVC LHPPKFVPCS DDCAIWDALR
YSSALRCSLI QHGCEHPSIP RSDGSTLVSW PSCVTSVNIV VSGHLKYVLL CFSIILDHKL
EKLVPARLDP IKVNEPHLTS LIPSAFGRES HHKSKASSTV TSSSAAASSS AAGTDGVQPA
EMKPDEFLHP DASRRVGFLE MPWRSDEARP LSIHTGYSKI PSPAPSNEST DTASEIGSAF
NSPVRSANRS ALQTIPEGSI TKQEGDTKTD ANIITVCLKR SLSGEGGGPP AKRLHIGDPD
MALQRLGSGD SVEGDPMALQ GGSGTGDAQQ DQHALQAGGA RPNMAHAFAP KDLLALLKNV
ETEIQICEQH LKDEIEKRKK YKVDDCRRTH NYDDFIRTFL RMLAEQGQLS KLVDQHVLVR
RRQGVSVGRL HKQRKPDRRR KRARVSDKYR RKKQ
