Q92560 (BAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase BAP1
EC=3.4.19.12

Alternative name(s):
BRCA1-associated protein 1
Cerebral protein 6

Gene names

Name:	BAP1
Synonyms:	KIAA0272
ORF Names:	hucep-6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Acts as a tumor suppressor. Ref.1 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
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). Ref.1
Subunit structure	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. Ref.1 Ref.18 Ref.19 Ref.20 Ref.21
Subcellular location	Cytoplasm. Nucleus. Note: Mainly nuclear. Binds to chromatin. Ref.1 Ref.17 Ref.19 Ref.20
Tissue specificity	Highly expressed in testis, placenta and ovary. Expressed in breast. Ref.1
Involvement in 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. Note: The gene represented in this entry is involved in disease pathogenesis. Ref.12 Ref.14 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14
Sequence similarities	Belongs to the peptidase C12 family. BAP1 subfamily.
Sequence caution	The sequence BAA13401.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
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 direct assay Ref.21. Source: UniProtKB negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc protein K48-linked deubiquitination Inferred from mutant phenotype Ref.20. Source: UniProtKB regulation of cell cycle Inferred from mutant phenotype Ref.20. Source: UniProtKB regulation of cell growth Inferred from mutant phenotype Ref.19. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	PR-DUB complex Inferred from direct assay Ref.21. Source: UniProtKB cytoplasm Inferred from direct assay Ref.17Ref.20. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular_function	chromatin binding Inferred from direct assay Ref.19. Source: UniProtKB ubiquitin thiolesterase activity Inferred from mutant phenotype Ref.17Ref.20Ref.19. Source: UniProtKB ubiquitin-specific protease activity Inferred from direct assay Ref.17Ref.20Ref.19Ref.21. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASXL1	Q8IXJ9	4	EBI-1791447,EBI-1646500
BRCA1	P38398	3	EBI-1791447,EBI-349905
BRCA1	P38398-5	2	EBI-1791447,EBI-2015072

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 729	729	Ubiquitin carboxyl-terminal hydrolase BAP1		PRO_0000211069
Regions
	Region	596 – 721	126	Interaction with BRCA1
	Coiled coil	630 – 661	32	Potential
	Motif	363 – 366	4	HBM-like motif
	Motif	717 – 722	6	Nuclear localization signal Ref.17
Sites
	Active site	91	1	Nucleophile Probable
	Active site	169	1	Proton donor By similarity
	Site	184	1	Important for enzyme activity By similarity
Natural variations
	Natural variant	63	1	S → C Found in a malignant pleural mesothelioma sample; somatic mutation. Ref.12		VAR_065976
	Natural variant	81	1	F → V Found in a malignant pleural mesothelioma sample; somatic mutation. Ref.12		VAR_065977
	Natural variant	91	1	C → W Found in a malignant pleural mesothelioma sample. Ref.12		VAR_065978
	Natural variant	95	1	A → D in a lung cancer sample; also found in a malignant pleural mesothelioma cell line; impairs deubiquitinase activity. Ref.12 Ref.15 Ref.17		VAR_063498
	Natural variant	178	1	G → V in a lung cancer sample; impairs deubiquitinase activity. Ref.15 Ref.17		VAR_063499
	Natural variant	315	1	E → A Found in a malignant pleural mesothelioma sample. Ref.12		VAR_065979
	Natural variant	616	1	V → E. Corresponds to variant rs35353781 [ dbSNP | Ensembl ].		VAR_051517
	Natural variant	685	1	E → V Found in a malignant pleural mesothelioma cell line. Ref.12		VAR_065980
Experimental info
	Mutagenesis	91	1	C → A or S: Abolishes enzymatic activity without affecting its ability to interfere with BRCA1 E3 ligase activity. Ref.1 Ref.17 Ref.18 Ref.19 Ref.20
	Mutagenesis	363 – 366	4	NHNY → AAAA: Abolishes interaction with HCFC1. Ref.19 Ref.20
	Mutagenesis	656 – 661	6	KRKKFK → AAAAAA: Does not affect nuclear localization. Ref.17
	Mutagenesis	691	1	L → P: Abolishes interaction with BRCA1. Ref.1
	Mutagenesis	717 – 722	6	RRKRSR → AAAAAA: Abolishes nuclear localization. Ref.17

Sequences

	Sequence		Length	Mass (Da)
	Q92560 [UniParc]. Last modified November 1, 1998. Version 2. Checksum: 031DA03AE1841D85	FASTA	729	80,362
	10 20 30 40 50 60 MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEERRSRR 70 80 90 100 110 120 KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL LNCSSVDLGP TLSRMKDFTK 130 140 150 160 170 180 GFSPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGLS AVRTMEAFHF VSYVPITGRL 190 200 210 220 230 240 FELDGLKVYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK 250 260 270 280 290 300 YEARLHVLKV NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKSASN KSPLVLEANR 310 320 330 340 350 360 APAASEGNHT DGAEEAAGSC AQAPSHSPPN KPKLVVKPPG SSLNGVHPNP TPIVQRLPAF 370 380 390 400 410 420 LDNHNYAKSP MQEEEDLAAG VGRSRVPVRP PQQYSDDEDD YEDDEEDDVQ NTNSALRYKG 430 440 450 460 470 480 KGTGKPGALS GSADGQLSVL QPNTINVLAE KLKESQKDLS IPLSIKTSSG AGSPAVAVPT 490 500 510 520 530 540 HSQPSPTPSN ESTDTASEIG SAFNSPLRSP IRSANPTRPS SPVTSHISKV LFGEDDSLLR 550 560 570 580 590 600 VDCIRYNRAV RDLGPVISTG LLHLAEDGVL SPLALTEGGK GSSPSIRPIQ GSQGSSSPVE 610 620 630 640 650 660 KEVVEATDSR EKTGMVRPGE PLSGEKYSPK ELLALLKCVE AEIANYEACL KEEVEKRKKF 670 680 690 700 710 720 KIDDQRRTHN YDEFICTFIS MLAQEGMLAN LVEQNISVRR RQGVSIGRLH KQRKPDRRKR SRPYKAKRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression." 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 Oncogene 16:1097-1112(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, MUTAGENESIS OF CYS-91 AND LEU-691, INTERACTION WITH BRCA1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: B-cell.
[2]	"Biological functions of a novel human gene, hucep-6, which is specifically expressed in the central nervous system." Yoshimoto M., Yazaki M., Takayama K., Matsumoto K. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"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." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[8]	"Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries." 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. Int. J. Cancer 106:244-251(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-729. Tissue: Medulloblastoma.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"The nuclear deubiquitinase BAP1 is commonly inactivated by somatic mutations and 3p21.1 losses in malignant pleural mesothelioma." 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. Nat. Genet. 43:668-672(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MESOM, VARIANTS CYS-63; VAL-81; TRP-91; ASP-95; ALA-315 AND VAL-685.
[13]	"Germline mutations in BAP1 predispose to melanocytic tumors." 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. Nat. Genet. 43:1018-1021(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN TPDS.
[14]	"Germline BAP1 mutations predispose to malignant mesothelioma." 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. Nat. Genet. 43:1022-1025(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN TPDS AND MESOM.
[15]	"Defining biochemical functions for the BRCA1 tumor suppressor protein: analysis of the BRCA1 binding protein BAP1." Jensen D.E., Rauscher F.J. III Cancer Lett. 143:S13-S17(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-95 AND VAL-178.
[16]	"Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains." Mallery D.L., Vandenberg C.J., Hiom K. EMBO J. 21:6755-6762(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization." Ventii K.H., Devi N.S., Friedrich K.L., Chernova T.A., Tighiouart M., Van Meir E.G., Wilkinson K.D. Cancer Res. 68:6953-6962(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF CYS-91; 656-LYS--ARG-661 AND 717-ARG--ARG-722, CHARACTERIZATION OF VARIANTS ASP-95 AND VAL-178.
[18]	"BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity." Nishikawa H., Wu W., Koike A., Kojima R., Gomi H., Fukuda M., Ohta T. Cancer Res. 69:111-119(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BARD1 AND BRCA1, MUTAGENESIS OF CYS-91.
[19]	"The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1." Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A. J. Biol. Chem. 284:34179-34188(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCFC1, MUTAGENESIS OF CYS-91 AND 363-ASN--TYR-366.
[20]	"Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1." Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M., Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C. Mol. Cell. Biol. 29:2181-2192(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCFC1, MUTAGENESIS OF CYS-91 AND 363-ASN--TYR-366.
[21]	"Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB." 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. Nature 465:243-247(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, INTERACTION WITH ASXL1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF045581 mRNA. Translation: AAC15970.1. D88812 mRNA. Translation: BAB46921.1. D87462 mRNA. Translation: BAA13401.2. Different initiation. AK292608 mRNA. Translation: BAF85297.1. CH471055 Genomic DNA. Translation: EAW65220.1. BC001596 mRNA. Translation: AAH01596.1. AY130008 mRNA. Translation: AAN05092.1.
IPI	IPI00465087.
RefSeq	NP_004647.1. NM_004656.2.
UniGene	Hs.106674.
3D structure databases
ProteinModelPortal	Q92560.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47004N.
IntAct	Q92560. 23 interactions.
STRING	9606.ENSP00000417132.
Protein family/group databases
MEROPS	C12.004.
PTM databases
PhosphoSite	Q92560.
Polymorphism databases
DMDM	68565074.
Proteomic databases
PaxDb	Q92560.
PRIDE	Q92560.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000460680; ENSP00000417132; ENSG00000163930.
GeneID	8314.
KEGG	hsa:8314.
UCSC	uc003ddx.3. human.
Organism-specific databases
CTD	8314.
GeneCards	GC03M052410.
HGNC	HGNC:950. BAP1.
HPA	CAB004322. HPA028814.
MIM	156240. phenotype. 603089. gene. 614327. phenotype.
neXtProt	NX_Q92560.
Orphanet	289539. BAP1-related tumor predisposition syndrome.
PharmGKB	PA25254.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG249036.
HOGENOM	HOG000013189.
HOVERGEN	HBG054042.
InParanoid	Q92560.
KO	K08588.
OMA	PQQYSDD.
OrthoDB	EOG4XPQFC.
PhylomeDB	Q92560.
Gene expression databases
ArrayExpress	Q92560.
Bgee	Q92560.
CleanEx	HS_BAP1.
Genevestigator	Q92560.
GermOnline	ENSG00000163930. Homo sapiens.
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...
Other
BindingDB	Q92560.
ChEMBL	CHEMBL1293314.
ChiTaRS	BAP1. human.
GenomeRNAi	8314.
NextBio	31137.
SOURCE	Search...

Entry information

Entry name

BAP1_HUMAN

Accession

Primary (citable) accession number: Q92560
Secondary accession number(s): A8K993, Q6LEM0, Q7Z5E8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.