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 27-MAR-2024, entry version 172. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 35. DR CORUM; Q9NZS9; -. DR IntAct; Q9NZS9; 10. DR STRING; 9606.ENSP00000261658; -. DR GlyCosmos; Q9NZS9; 1 site, No reported glycans. 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; 9606-ENSP00000261658; -. DR PeptideAtlas; Q9NZS9; -. DR ProteomicsDB; 5213; -. DR ProteomicsDB; 83505; -. [Q9NZS9-1] DR Pumba; Q9NZS9; -. DR Antibodypedia; 24873; 242 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 AGR; HGNC:17613; -. 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; GNDQMPT; -. DR OrthoDB; 4047619at2759; -. DR PhylomeDB; Q9NZS9; -. DR TreeFam; TF332303; -. DR PathwayCommons; Q9NZS9; -. DR SignaLink; Q9NZS9; -. DR SIGNOR; Q9NZS9; -. DR BioGRID-ORCS; 51283; 20 hits in 1199 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 104 other cell types or tissues. DR ExpressionAtlas; Q9NZS9; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:ParkinsonsUK-UCL. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; NAS:ParkinsonsUK-UCL. 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 CDD; cd16497; RING-HC_BAR; 1. DR CDD; cd09513; SAM_BAR; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR15898:SF21; BIFUNCTIONAL APOPTOSIS REGULATOR; 1. DR PANTHER; PTHR15898; UNCHARACTERIZED; 1. DR Pfam; PF00536; SAM_1; 1. DR Pfam; PF15227; zf-C3HC4_4; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9NZS9; HS. 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 //