BFAR_HUMAN
ID BFAR_HUMAN Reviewed; 450 AA.
AC Q9NZS9; A8K4Z9; B4DUT0; D3DUG8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Bifunctional apoptosis regulator;
DE AltName: Full=RING finger protein 47;
GN Name=BFAR; Synonyms=BAR, RNF47;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CASP8; BCL2 AND
RP BCL2L1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=10716992; DOI=10.1073/pnas.97.6.2597;
RA Zhang H., Xu Q., Krajewski S., Krajewska M., Xie Z., Fuess S., Kitada S.,
RA Pawlowski K., Godzik A., Reed J.C.;
RT "BAR: an apoptosis regulator at the intersection of caspases and Bcl-2
RT family proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2597-2602(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IFT57; HIP1; ESRRBL1 AND
RP BCAP31, AND TISSUE SPECIFICITY.
RX PubMed=14502241; DOI=10.1038/sj.cdd.4401287;
RA Roth W., Kermer P., Krajewska M., Welsh K., Davis S., Krajewski S.,
RA Reed J.C.;
RT "Bifunctional apoptosis inhibitor (BAR) protects neurons from diverse cell
RT death pathways.";
RL Cell Death Differ. 10:1178-1187(2003).
CC -!- FUNCTION: Apoptosis regulator. Has anti-apoptotic activity, both for
CC apoptosis triggered via death-receptors and via mitochondrial factors.
CC {ECO:0000269|PubMed:14502241}.
CC -!- SUBUNIT: Interacts with CASP8, BCL2 and BCL2L1 through SAM domain and
CC also with HIP1, IFT57, ESRRBL1 and BCAP31.
CC {ECO:0000269|PubMed:10716992, ECO:0000269|PubMed:14502241}.
CC -!- INTERACTION:
CC Q9NZS9; P61086: UBE2K; NbExp=6; IntAct=EBI-2130199, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10716992, ECO:0000269|PubMed:14502241}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10716992,
CC ECO:0000269|PubMed:14502241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZS9-2; Sequence=VSP_055879, VSP_055880;
CC -!- TISSUE SPECIFICITY: Expressed highly in brain, moderately in small
CC intestine, weakly in testes and only faintly in liver and skeletal
CC muscle. Not expressed in heart, kidney, lung and spleen.
CC {ECO:0000269|PubMed:10716992, ECO:0000269|PubMed:14502241}.
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DR EMBL; AF173003; AAF59975.1; -; mRNA.
DR EMBL; AK291114; BAF83803.1; -; mRNA.
DR EMBL; AK300778; BAG62442.1; -; mRNA.
DR EMBL; AC009167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85105.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85108.1; -; Genomic_DNA.
DR EMBL; BC003054; AAH03054.1; -; mRNA.
DR CCDS; CCDS10554.1; -. [Q9NZS9-1]
DR RefSeq; NP_057645.1; NM_016561.2. [Q9NZS9-1]
DR RefSeq; XP_005255407.1; XM_005255350.2. [Q9NZS9-2]
DR AlphaFoldDB; Q9NZS9; -.
DR SMR; Q9NZS9; -.
DR BioGRID; 119435; 34.
DR CORUM; Q9NZS9; -.
DR IntAct; Q9NZS9; 10.
DR STRING; 9606.ENSP00000261658; -.
DR GlyGen; Q9NZS9; 1 site.
DR iPTMnet; Q9NZS9; -.
DR PhosphoSitePlus; Q9NZS9; -.
DR BioMuta; BFAR; -.
DR DMDM; 74753089; -.
DR EPD; Q9NZS9; -.
DR jPOST; Q9NZS9; -.
DR MassIVE; Q9NZS9; -.
DR MaxQB; Q9NZS9; -.
DR PaxDb; Q9NZS9; -.
DR PeptideAtlas; Q9NZS9; -.
DR PRIDE; Q9NZS9; -.
DR ProteomicsDB; 5213; -.
DR ProteomicsDB; 83505; -. [Q9NZS9-1]
DR Antibodypedia; 24873; 220 antibodies from 28 providers.
DR DNASU; 51283; -.
DR Ensembl; ENST00000261658.7; ENSP00000261658.2; ENSG00000103429.11. [Q9NZS9-1]
DR Ensembl; ENST00000619034.2; ENSP00000478190.1; ENSG00000275618.2. [Q9NZS9-1]
DR GeneID; 51283; -.
DR KEGG; hsa:51283; -.
DR MANE-Select; ENST00000261658.7; ENSP00000261658.2; NM_016561.3; NP_057645.1.
DR UCSC; uc002dco.4; human. [Q9NZS9-1]
DR CTD; 51283; -.
DR DisGeNET; 51283; -.
DR GeneCards; BFAR; -.
DR HGNC; HGNC:17613; BFAR.
DR HPA; ENSG00000103429; Low tissue specificity.
DR MIM; 619516; gene.
DR neXtProt; NX_Q9NZS9; -.
DR OpenTargets; ENSG00000103429; -.
DR PharmGKB; PA38460; -.
DR VEuPathDB; HostDB:ENSG00000103429; -.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00390000005386; -.
DR InParanoid; Q9NZS9; -.
DR OMA; FWRLWSR; -.
DR OrthoDB; 1332799at2759; -.
DR PhylomeDB; Q9NZS9; -.
DR TreeFam; TF332303; -.
DR PathwayCommons; Q9NZS9; -.
DR SignaLink; Q9NZS9; -.
DR SIGNOR; Q9NZS9; -.
DR BioGRID-ORCS; 51283; 18 hits in 1121 CRISPR screens.
DR ChiTaRS; BFAR; human.
DR GenomeRNAi; 51283; -.
DR Pharos; Q9NZS9; Tbio.
DR PRO; PR:Q9NZS9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NZS9; protein.
DR Bgee; ENSG00000103429; Expressed in islet of Langerhans and 102 other tissues.
DR ExpressionAtlas; Q9NZS9; baseline and differential.
DR Genevisible; Q9NZS9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:ParkinsonsUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:ParkinsonsUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0089720; F:caspase binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..450
FT /note="Bifunctional apoptosis regulator"
FT /id="PRO_0000055822"
FT TOPO_DOM 1..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..331
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..404
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 182..249
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 34..74
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..28
FT /note="MEEPQKSYVNTMDLERDEPLKSTGPQIS -> MVGIFKENRMSRMQRKMGRF
FT PQSQYSPQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055879"
FT VAR_SEQ 29..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055880"
FT VARIANT 140
FT /note="M -> R (in dbSNP:rs11546303)"
FT /id="VAR_052075"
FT VARIANT 245
FT /note="R -> H (in dbSNP:rs35377618)"
FT /id="VAR_052076"
SQ SEQUENCE 450 AA; 52738 MW; A662454FC2806CE6 CRC64;
MEEPQKSYVN TMDLERDEPL KSTGPQISVS EFSCHCCYDI LVNPTTLNCG HSFCRHCLAL
WWASSKKTEC PECREKWEGF PKVSILLRDA IEKLFPDAIR LRFEDIQQNN DIVQSLAAFQ
KYGNDQIPLA PNTGRANQQM GGGFFSGVLT ALTGVAVVLL VYHWSSRESE HDLLVHKAVA
KWTAEEVVLW LEQLGPWASL YRERFLSERV NGRLLLTLTE EEFSKTPYTI ENSSHRRAIL
MELERVKALG VKPPQNLWEY KAVNPGRSLF LLYALKSSPR LSLLYLYLFD YTDTFLPFIH
TICPLQEDSS GEDIVTKLLD LKEPTWKQWR EFLVKYSFLP YQLIAEFAWD WLEVHYWTSR
FLIINAMLLS VLELFSFWRI WSRSELKTVP QRMWSHFWKV STQGLFVAMF WPLIPQFVCN
CLFYWALYFN PIINIDLVVK ELRRLETQVL
