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Q92560 (BAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence 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.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

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.19 Ref.20 Ref.21 Ref.22

Subcellular location

Cytoplasm. Nucleus. Note: Mainly nuclear. Binds to chromatin. Ref.1 Ref.18 Ref.20 Ref.21

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.13 Ref.15

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.14 Ref.15

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Ubiquitin carboxyl-terminal hydrolase BAP1
PRO_0000211069

Regions

Region596 – 721126Interaction with BRCA1
Coiled coil630 – 66132 Potential
Motif363 – 3664HBM-like motif
Motif717 – 7226Nuclear localization signal Ref.18

Sites

Active site911Nucleophile Probable
Active site1691Proton donor By similarity
Site1841Important for enzyme activity By similarity

Natural variations

Natural variant631S → C Found in a malignant pleural mesothelioma sample; somatic mutation. Ref.13
VAR_065976
Natural variant811F → V Found in a malignant pleural mesothelioma sample; somatic mutation. Ref.13
VAR_065977
Natural variant911C → W Found in a malignant pleural mesothelioma sample. Ref.13
VAR_065978
Natural variant951A → D in a lung cancer sample; also found in a malignant pleural mesothelioma cell line; impairs deubiquitinase activity. Ref.13 Ref.16 Ref.18
VAR_063498
Natural variant1781G → V in a lung cancer sample; impairs deubiquitinase activity. Ref.16 Ref.18
VAR_063499
Natural variant3151E → A Found in a malignant pleural mesothelioma sample. Ref.13
Corresponds to variant rs149974450 [ dbSNP | Ensembl ].
VAR_065979
Natural variant6161V → E.
Corresponds to variant rs35353781 [ dbSNP | Ensembl ].
VAR_051517
Natural variant6851E → V Found in a malignant pleural mesothelioma cell line. Ref.13
VAR_065980

Experimental info

Mutagenesis911C → A or S: Abolishes enzymatic activity without affecting its ability to interfere with BRCA1 E3 ligase activity. Ref.1 Ref.18 Ref.19 Ref.20 Ref.21
Mutagenesis363 – 3664NHNY → AAAA: Abolishes interaction with HCFC1. Ref.20 Ref.21
Mutagenesis656 – 6616KRKKFK → AAAAAA: Does not affect nuclear localization. Ref.18
Mutagenesis6911L → P: Abolishes interaction with BRCA1. Ref.1
Mutagenesis717 – 7226RRKRSR → AAAAAA: Abolishes nuclear localization. Ref.18

Sequences

Sequence LengthMass (Da)Tools
Q92560 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: 031DA03AE1841D85

FASTA72980,362
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
[13]"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.
[14]"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. expand/collapse author list , 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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
RefSeqNP_004647.1. NM_004656.3.
UniGeneHs.106674.

3D structure databases

ProteinModelPortalQ92560.
SMRQ92560. Positions 5-284, 630-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113911. 40 interactions.
DIPDIP-47004N.
IntActQ92560. 23 interactions.
STRING9606.ENSP00000417132.

Chemistry

BindingDBQ92560.
ChEMBLCHEMBL1293314.

Protein family/group databases

MEROPSC12.004.

PTM databases

PhosphoSiteQ92560.

Polymorphism databases

DMDM68565074.

Proteomic databases

PaxDbQ92560.
PRIDEQ92560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000460680; ENSP00000417132; ENSG00000163930.
GeneID8314.
KEGGhsa:8314.
UCSCuc003ddx.4. human.

Organism-specific databases

CTD8314.
GeneCardsGC03M052410.
HGNCHGNC:950. BAP1.
HPACAB004322.
HPA028814.
HPA055560.
MIM156240. phenotype.
603089. gene.
614327. phenotype.
neXtProtNX_Q92560.
Orphanet289539. BAP1-related tumor predisposition syndrome.
PharmGKBPA25254.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249036.
HOGENOMHOG000013189.
HOVERGENHBG054042.
InParanoidQ92560.
KOK08588.
OMAPQQYSDD.
OrthoDBEOG7GN2M2.
PhylomeDBQ92560.
TreeFamTF313976.

Gene expression databases

ArrayExpressQ92560.
BgeeQ92560.
CleanExHS_BAP1.
GenevestigatorQ92560.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
ProtoNetSearch...

Other

ChiTaRSBAP1. human.
GeneWikiBAP1.
GenomeRNAi8314.
NextBio31137.
PROQ92560.
SOURCESearch...

Entry information

Entry nameBAP1_HUMAN
AccessionPrimary (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: February 19, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM