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Ubiquitin carboxyl-terminal hydrolase BAP1 (EC 3.4.19.12) (BRCA1-associated protein 1) (Cerebral protein 6)

 BAP1_HUMAN              Reviewed;         729 AA.
Q92560; A8K993; Q6LEM0; Q7Z5E8;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 2.
27-SEP-2017, entry version 147.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1;
EC=3.4.19.12;
AltName: Full=BRCA1-associated protein 1;
AltName: Full=Cerebral protein 6;
Name=BAP1; Synonyms=KIAA0272; ORFNames=hucep-6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, MUTAGENESIS OF
CYS-91 AND LEU-691, INTERACTION WITH BRCA1, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=B-cell;
PubMed=9528852; DOI=10.1038/sj.onc.1201861;
Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I.,
Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y.,
Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G.,
Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III;
"BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING
finger and enhances BRCA1-mediated cell growth suppression.";
Oncogene 16:1097-1112(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Yoshimoto M., Yazaki M., Takayama K., Matsumoto K.;
"Biological functions of a novel human gene, hucep-6, which is
specifically expressed in the central nervous system.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 164-729.
TISSUE=Medulloblastoma;
PubMed=12800201; DOI=10.1002/ijc.11208;
Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A.,
Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S.,
Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F.,
Asmuss H.-P., Bise K., Mautner J.;
"Novel tumor antigens identified by autologous antibody screening of
childhood medulloblastoma cDNA libraries.";
Int. J. Cancer 106:244-251(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
INVOLVEMENT IN MESOM, AND VARIANTS CYS-63; VAL-81; TRP-91; ASP-95;
ALA-315 AND VAL-685.
PubMed=21642991; DOI=10.1038/ng.855;
Bott M., Brevet M., Taylor B.S., Shimizu S., Ito T., Wang L.,
Creaney J., Lake R.A., Zakowski M.F., Reva B., Sander C., Delsite R.,
Powell S., Zhou Q., Shen R., Olshen A., Rusch V., Ladanyi M.;
"The nuclear deubiquitinase BAP1 is commonly inactivated by somatic
mutations and 3p21.1 losses in malignant pleural mesothelioma.";
Nat. Genet. 43:668-672(2011).
[14]
INVOLVEMENT IN TPDS.
PubMed=21874003; DOI=10.1038/ng.910;
Wiesner T., Obenauf A.C., Murali R., Fried I., Griewank K.G., Ulz P.,
Windpassinger C., Wackernagel W., Loy S., Wolf I., Viale A.,
Lash A.E., Pirun M., Socci N.D., Rutten A., Palmedo G., Abramson D.,
Offit K., Ott A., Becker J.C., Cerroni L., Kutzner H., Bastian B.C.,
Speicher M.R.;
"Germline mutations in BAP1 predispose to melanocytic tumors.";
Nat. Genet. 43:1018-1021(2011).
[15]
INVOLVEMENT IN TPDS AND MESOM.
PubMed=21874000; DOI=10.1038/ng.912;
Testa J.R., Cheung M., Pei J., Below J.E., Tan Y., Sementino E.,
Cox N.J., Dogan A.U., Pass H.I., Trusa S., Hesdorffer M., Nasu M.,
Powers A., Rivera Z., Comertpay S., Tanji M., Gaudino G., Yang H.,
Carbone M.;
"Germline BAP1 mutations predispose to malignant mesothelioma.";
Nat. Genet. 43:1022-1025(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-369; SER-521;
SER-537; SER-585 AND SER-597, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
VARIANTS ASP-95 AND VAL-178.
PubMed=10546591; DOI=10.1016/S0304-3835(99)90004-6;
Jensen D.E., Rauscher F.J. III;
"Defining biochemical functions for the BRCA1 tumor suppressor
protein: analysis of the BRCA1 binding protein BAP1.";
Cancer Lett. 143:S13-S17(1999).
[19]
FUNCTION.
PubMed=12485996; DOI=10.1093/emboj/cdf691;
Mallery D.L., Vandenberg C.J., Hiom K.;
"Activation of the E3 ligase function of the BRCA1/BARD1 complex by
polyubiquitin chains.";
EMBO J. 21:6755-6762(2002).
[20]
FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL,
MUTAGENESIS OF CYS-91; 656-LYS--ARG-661 AND 717-ARG--ARG-722, AND
CHARACTERIZATION OF VARIANTS ASP-95 AND VAL-178.
PubMed=18757409; DOI=10.1158/0008-5472.CAN-08-0365;
Ventii K.H., Devi N.S., Friedrich K.L., Chernova T.A., Tighiouart M.,
Van Meir E.G., Wilkinson K.D.;
"BRCA1-associated protein-1 is a tumor suppressor that requires
deubiquitinating activity and nuclear localization.";
Cancer Res. 68:6953-6962(2008).
[21]
FUNCTION, INTERACTION WITH BARD1 AND BRCA1, AND MUTAGENESIS OF CYS-91.
PubMed=19117993; DOI=10.1158/0008-5472.CAN-08-3355;
Nishikawa H., Wu W., Koike A., Kojima R., Gomi H., Fukuda M., Ohta T.;
"BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING
heterodimer activity.";
Cancer Res. 69:111-119(2009).
[22]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCFC1, AND
MUTAGENESIS OF CYS-91 AND 363-ASN--TYR-366.
PubMed=19815555; DOI=10.1074/jbc.M109.046755;
Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A.;
"The deubiquitinating enzyme BAP1 regulates cell growth via
interaction with HCF-1.";
J. Biol. Chem. 284:34179-34188(2009).
[23]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCFC1, AND
MUTAGENESIS OF CYS-91 AND 363-ASN--TYR-366.
PubMed=19188440; DOI=10.1128/MCB.01517-08;
Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M.,
Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C.;
"Association of C-terminal ubiquitin hydrolase BRCA1-associated
protein 1 with cell cycle regulator host cell factor 1.";
Mol. Cell. Biol. 29:2181-2192(2009).
[24]
FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, AND INTERACTION WITH
ASXL1.
PubMed=20436459; DOI=10.1038/nature08966;
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.;
"Histone H2A deubiquitinase activity of the Polycomb repressive
complex PR-DUB.";
Nature 465:243-247(2010).
[25]
FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, NUCLEAR LOCALIZATION
SIGNAL, AND MUTAGENESIS OF 691-LEU--LYS-711.
PubMed=24703950; DOI=10.1016/j.molcel.2014.03.002;
Mashtalir N., Daou S., Barbour H., Sen N.N., Gagnon J.,
Hammond-Martel I., Dar H.H., Therrien M., Affar E.B.;
"Autodeubiquitination protects the tumor suppressor BAP1 from
cytoplasmic sequestration mediated by the atypical ubiquitin ligase
UBE2O.";
Mol. Cell 54:392-406(2014).
[26]
VARIANT PHE-47.
PubMed=25080371; DOI=10.1111/cge.12472;
de la Fouchardiere A., Cabaret O., Savin L., Combemale P.,
Schvartz H., Penet C., Bonadona V., Soufir N.,
Bressac-de Paillerets B.;
"Germline BAP1 mutations predispose also to multiple basal cell
carcinomas.";
Clin. Genet. 88:273-277(2015).
[27]
CHARACTERIZATION OF VARIANTS PHE-47; VAL-81; ASP-95 AND VAL-178.
PubMed=26680512; DOI=10.1038/srep18462;
Bhattacharya S., Hanpude P., Maiti T.K.;
"Cancer associated missense mutations in BAP1 catalytic domain induce
amyloidogenic aggregation: A new insight in enzymatic inactivation.";
Sci. Rep. 5:18462-18462(2015).
-!- FUNCTION: Deubiquitinating enzyme that plays a key role in
chromatin by mediating deubiquitination of histone H2A and HCFC1.
Catalytic component of the PR-DUB complex, a complex that
specifically mediates deubiquitination of histone H2A
monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not
deubiquitinate monoubiquitinated histone H2B. Acts as a regulator
of cell growth by mediating deubiquitination of HCFC1 N-terminal
and C-terminal chains, with some specificity toward 'Lys-48'-
linked polyubiquitin chains compared to 'Lys-63'-linked
polyubiquitin chains. Deubiquitination of HCFC1 does not lead to
increase stability of HCFC1. Interferes with the BRCA1 and BARD1
heterodimer activity by inhibiting their ability to mediate
ubiquitination and autoubiquitination. It however does not mediate
deubiquitination of BRCA1 and BARD1. Able to mediate
autodeubiquitination via intramolecular interactions to couteract
monoubiquitination at the nuclear localization signal (NLS),
thereby protecting it from cytoplasmic sequestration
(PubMed:24703950). Acts as a tumor suppressor.
{ECO:0000269|PubMed:12485996, ECO:0000269|PubMed:18757409,
ECO:0000269|PubMed:19117993, ECO:0000269|PubMed:19188440,
ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:20436459,
ECO:0000269|PubMed:24703950, ECO:0000269|PubMed:9528852}.
-!- 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).
{ECO:0000269|PubMed:9528852}.
-!- SUBUNIT: Component of the PR-DUB complex, at least composed of
BAP1 and ASXL1. Interacts with BRCA1 (via the RING finger).
Interacts (via HBM-like motif) with HCFC1.
{ECO:0000269|PubMed:19117993, ECO:0000269|PubMed:19188440,
ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:20436459,
ECO:0000269|PubMed:9528852}.
-!- INTERACTION:
Q8IXJ9:ASXL1; NbExp=6; IntAct=EBI-1791447, EBI-1646500;
P38398:BRCA1; NbExp=3; IntAct=EBI-1791447, EBI-349905;
P38398-5:BRCA1; NbExp=2; IntAct=EBI-1791447, EBI-2015072;
P51610:HCFC1; NbExp=4; IntAct=EBI-1791447, EBI-396176;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18757409,
ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555,
ECO:0000269|PubMed:24703950}. Nucleus
{ECO:0000269|PubMed:18757409, ECO:0000269|PubMed:19188440,
ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:24703950,
ECO:0000269|PubMed:9528852}. Note=Mainly nuclear. Binds to
chromatin. Localizes to the cytoplasm when monoubiquitinated by
the E2/E3 hybrid ubiquitin-protein ligase UBE2O (PubMed:24703950).
{ECO:0000269|PubMed:24703950}.
-!- TISSUE SPECIFICITY: Highly expressed in testis, placenta and
ovary. Expressed in breast. {ECO:0000269|PubMed:9528852}.
-!- PTM: Ubiquitinated: monoubiquitinated at multiple site of its
nuclear localization signal (NLS) BY UBE2O, leading to cytoplasmic
retention. Able to mediate autodeubiquitination via intramolecular
interactions to couteract cytoplasmic retention.
{ECO:0000269|PubMed:24703950}.
-!- DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An
aggressive neoplasm of the serosal lining of the chest. It appears
as broad sheets of cells, with some regions containing spindle-
shaped, sarcoma-like cells and other regions showing adenomatous
patterns. Pleural mesotheliomas have been linked to exposure to
asbestos. {ECO:0000269|PubMed:21642991,
ECO:0000269|PubMed:21874000}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Tumor predisposition syndrome (TPDS) [MIM:614327]: A
condition characterized by predisposition to develop a variety of
tumors, including benign melanocytic tumors as well as several
malignant tumors, including uveal melanoma, cutaneous melanoma,
malignant mesothelioma on exposure to asbestos, lung
adenocarcinoma and meningioma. {ECO:0000269|PubMed:21874000,
ECO:0000269|PubMed:21874003}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA13401.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BAP1ID755ch3p21.html";
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EMBL; AF045581; AAC15970.1; -; mRNA.
EMBL; D88812; BAB46921.1; -; mRNA.
EMBL; D87462; BAA13401.2; ALT_INIT; mRNA.
EMBL; AK292608; BAF85297.1; -; mRNA.
EMBL; CH471055; EAW65220.1; -; Genomic_DNA.
EMBL; BC001596; AAH01596.1; -; mRNA.
EMBL; AY130008; AAN05092.1; -; mRNA.
CCDS; CCDS2853.1; -.
RefSeq; NP_004647.1; NM_004656.3.
UniGene; Hs.106674; -.
ProteinModelPortal; Q92560; -.
SMR; Q92560; -.
BioGrid; 113911; 70.
DIP; DIP-47004N; -.
IntAct; Q92560; 55.
STRING; 9606.ENSP00000417132; -.
BindingDB; Q92560; -.
ChEMBL; CHEMBL1293314; -.
MEROPS; C12.004; -.
iPTMnet; Q92560; -.
PhosphoSitePlus; Q92560; -.
BioMuta; BAP1; -.
DMDM; 68565074; -.
EPD; Q92560; -.
MaxQB; Q92560; -.
PaxDb; Q92560; -.
PeptideAtlas; Q92560; -.
PRIDE; Q92560; -.
Ensembl; ENST00000460680; ENSP00000417132; ENSG00000163930.
GeneID; 8314; -.
KEGG; hsa:8314; -.
UCSC; uc003ddx.5; human.
CTD; 8314; -.
DisGeNET; 8314; -.
EuPathDB; HostDB:ENSG00000163930.9; -.
GeneCards; BAP1; -.
HGNC; HGNC:950; BAP1.
HPA; CAB004322; -.
HPA; HPA028814; -.
HPA; HPA028815; -.
HPA; HPA055560; -.
MalaCards; BAP1; -.
MIM; 156240; phenotype.
MIM; 603089; gene.
MIM; 614327; phenotype.
neXtProt; NX_Q92560; -.
OpenTargets; ENSG00000163930; -.
Orphanet; 289539; BAP1-related tumor predisposition syndrome.
PharmGKB; PA25254; -.
eggNOG; KOG2778; Eukaryota.
eggNOG; ENOG410XP0P; LUCA.
GeneTree; ENSGT00510000046560; -.
HOGENOM; HOG000013189; -.
HOVERGEN; HBG054042; -.
InParanoid; Q92560; -.
KO; K08588; -.
OMA; TSHISKV; -.
OrthoDB; EOG091G08R7; -.
PhylomeDB; Q92560; -.
TreeFam; TF313976; -.
BRENDA; 3.4.19.12; 2681.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
SIGNOR; Q92560; -.
ChiTaRS; BAP1; human.
GeneWiki; BAP1; -.
GenomeRNAi; 8314; -.
PRO; PR:Q92560; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163930; -.
CleanEx; HS_BAP1; -.
ExpressionAtlas; Q92560; baseline and differential.
Genevisible; Q92560; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035517; C:PR-DUB complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; NAS:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
GO; GO:0061519; P:macrophage homeostasis; IEA:Ensembl.
GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:UniProtKB.
GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.40.532.10; -; 1.
InterPro; IPR001578; Peptidase_C12_UCH.
PANTHER; PTHR10589; PTHR10589; 1.
Pfam; PF01088; Peptidase_C12; 1.
PRINTS; PR00707; UBCTHYDRLASE.
1: Evidence at protein level;
Chromatin regulator; Coiled coil; Complete proteome; Cytoplasm;
Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 729 Ubiquitin carboxyl-terminal hydrolase
BAP1.
/FTId=PRO_0000211069.
REGION 596 721 Interaction with BRCA1.
COILED 630 661 {ECO:0000255}.
MOTIF 363 366 HBM-like motif.
MOTIF 717 722 Nuclear localization signal.
{ECO:0000269|PubMed:18757409,
ECO:0000269|PubMed:24703950}.
ACT_SITE 91 91 Nucleophile. {ECO:0000305}.
ACT_SITE 169 169 Proton donor. {ECO:0000250}.
SITE 184 184 Important for enzyme activity.
{ECO:0000250}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:Q99PU7}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 597 597 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 47 47 I -> F (found in a primary uveal
melanoma; somatic mutation; induces
cytoplasmic accumulation; loss of
deubiquitinase activity; upregulates heat
shock response; induces formation of
amyloid-beta aggregates).
{ECO:0000269|PubMed:25080371,
ECO:0000269|PubMed:26680512}.
/FTId=VAR_075251.
VARIANT 63 63 S -> C (found in a malignant pleural
mesothelioma sample; somatic mutation).
{ECO:0000269|PubMed:21642991}.
/FTId=VAR_065976.
VARIANT 81 81 F -> V (found in a malignant pleural
mesothelioma sample; somatic mutation;
induces cytoplasmic accumulation; loss of
deubiquitinase activity; upregulates heat
shock response; induces formation of
amyloid-beta aggregates).
{ECO:0000269|PubMed:21642991,
ECO:0000269|PubMed:26680512}.
/FTId=VAR_065977.
VARIANT 91 91 C -> W (found in a malignant pleural
mesothelioma sample).
{ECO:0000269|PubMed:21642991}.
/FTId=VAR_065978.
VARIANT 95 95 A -> D (in a lung cancer sample; also
found in a malignant pleural mesothelioma
cell line; induces cytoplasmic
accumulation; loss of deubiquitinase
activity; upregulates heat shock
response; induces formation of amyloid-
beta aggregates).
{ECO:0000269|PubMed:10546591,
ECO:0000269|PubMed:18757409,
ECO:0000269|PubMed:21642991,
ECO:0000269|PubMed:26680512}.
/FTId=VAR_063498.
VARIANT 178 178 G -> V (in a lung cancer sample; induces
cytoplasmic accumulation; impairs
deubiquitinase activity; upregulates heat
shock response; induces formation of
beta-amyloid aggregates).
{ECO:0000269|PubMed:10546591,
ECO:0000269|PubMed:18757409,
ECO:0000269|PubMed:26680512}.
/FTId=VAR_063499.
VARIANT 315 315 E -> A (found in a malignant pleural
mesothelioma sample; dbSNP:rs149974450).
{ECO:0000269|PubMed:21642991}.
/FTId=VAR_065979.
VARIANT 616 616 V -> E (in dbSNP:rs35353781).
/FTId=VAR_051517.
VARIANT 685 685 E -> V (found in a malignant pleural
mesothelioma cell line).
{ECO:0000269|PubMed:21642991}.
/FTId=VAR_065980.
MUTAGEN 91 91 C->A,S: Abolishes enzymatic activity
without affecting its ability to
interfere with BRCA1 E3 ligase activity.
{ECO:0000269|PubMed:18757409,
ECO:0000269|PubMed:19117993,
ECO:0000269|PubMed:19188440,
ECO:0000269|PubMed:19815555,
ECO:0000269|PubMed:9528852}.
MUTAGEN 363 366 NHNY->AAAA: Abolishes interaction with
HCFC1. {ECO:0000269|PubMed:19188440,
ECO:0000269|PubMed:19815555}.
MUTAGEN 656 661 KRKKFK->AAAAAA: Does not affect nuclear
localization.
{ECO:0000269|PubMed:18757409}.
MUTAGEN 691 711 Missing: Abolishes ubiquitination by
UBE2O. {ECO:0000269|PubMed:24703950}.
MUTAGEN 691 691 L->P: Abolishes interaction with BRCA1.
{ECO:0000269|PubMed:9528852}.
MUTAGEN 717 722 RRKRSR->AAAAAA: Abolishes nuclear
localization.
{ECO:0000269|PubMed:18757409}.
SEQUENCE 729 AA; 80362 MW; 031DA03AE1841D85 CRC64;
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEERRSRR
KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL LNCSSVDLGP TLSRMKDFTK
GFSPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGLS AVRTMEAFHF VSYVPITGRL
FELDGLKVYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK
YEARLHVLKV NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKSASN KSPLVLEANR
APAASEGNHT DGAEEAAGSC AQAPSHSPPN KPKLVVKPPG SSLNGVHPNP TPIVQRLPAF
LDNHNYAKSP MQEEEDLAAG VGRSRVPVRP PQQYSDDEDD YEDDEEDDVQ NTNSALRYKG
KGTGKPGALS GSADGQLSVL QPNTINVLAE KLKESQKDLS IPLSIKTSSG AGSPAVAVPT
HSQPSPTPSN ESTDTASEIG SAFNSPLRSP IRSANPTRPS SPVTSHISKV LFGEDDSLLR
VDCIRYNRAV RDLGPVISTG LLHLAEDGVL SPLALTEGGK GSSPSIRPIQ GSQGSSSPVE
KEVVEATDSR EKTGMVRPGE PLSGEKYSPK ELLALLKCVE AEIANYEACL KEEVEKRKKF
KIDDQRRTHN YDEFICTFIS MLAQEGMLAN LVEQNISVRR RQGVSIGRLH KQRKPDRRKR
SRPYKAKRQ


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