BNIPL_HUMAN
ID BNIPL_HUMAN Reviewed; 357 AA.
AC Q7Z465; Q6DK43; Q8TCY7; Q8WYG2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein;
GN Name=BNIPL;
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] (ISOFORMS 2 AND 3).
RX PubMed=11741952; DOI=10.1074/jbc.m109459200;
RA Zhou Y.T., Soh U.J.K., Shang X., Guy G.R., Low B.C.;
RT "The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a
RT novel apoptosis-inducing sequence.";
RL J. Biol. Chem. 277:7483-7492(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BCL2 AND ARHGAP1,
RP AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=12901880; DOI=10.1016/s0006-291x(03)01387-1;
RA Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P.,
RA Shen L., Wan D., Gu J.;
RT "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 308:379-385(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP INTERACTION WITH GIF AND GFER, AND TISSUE SPECIFICITY.
RX PubMed=12681488; DOI=10.1016/s0014-5793(03)00229-1;
RA Shen L., Hu J., Lu H., Wu M., Qin W., Wan D., Li Y.-Y., Gu J.;
RT "The apoptosis-associated protein BNIPL interacts with two cell
RT proliferation-related proteins, MIF and GFER.";
RL FEBS Lett. 540:86-90(2003).
CC -!- FUNCTION: May be a bridge molecule between BCL2 and ARHGAP1/CDC42 in
CC promoting cell death. {ECO:0000269|PubMed:12901880}.
CC -!- SUBUNIT: Homodimer. Interacts with BCL2, ARHGAP1, MIF and GFER.
CC {ECO:0000269|PubMed:12681488, ECO:0000269|PubMed:12901880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=BNIPL-2;
CC IsoId=Q7Z465-1; Sequence=Displayed;
CC Name=2; Synonyms=BNIPL-1, BNIP-Salpha;
CC IsoId=Q7Z465-2; Sequence=VSP_012448;
CC Name=3; Synonyms=BNIP-Sbeta;
CC IsoId=Q7Z465-3; Sequence=VSP_012448, VSP_012449;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in placenta and lung.
CC {ECO:0000269|PubMed:12681488}.
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DR EMBL; AF193056; AAG22484.1; -; mRNA.
DR EMBL; AY078983; AAL85483.1; -; mRNA.
DR EMBL; AY078984; AAL85484.1; -; mRNA.
DR EMBL; AY033000; AAK54348.1; -; mRNA.
DR EMBL; AL590133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027868; AAH27868.2; -; mRNA.
DR EMBL; BC074779; AAH74779.3; -; mRNA.
DR EMBL; BC074780; AAH74780.3; -; mRNA.
DR CCDS; CCDS53362.1; -. [Q7Z465-2]
DR CCDS; CCDS978.2; -. [Q7Z465-1]
DR RefSeq; NP_001153114.1; NM_001159642.1. [Q7Z465-2]
DR RefSeq; NP_612122.2; NM_138278.3. [Q7Z465-1]
DR AlphaFoldDB; Q7Z465; -.
DR BioGRID; 127211; 14.
DR ELM; Q7Z465; -.
DR IntAct; Q7Z465; 8.
DR STRING; 9606.ENSP00000357927; -.
DR iPTMnet; Q7Z465; -.
DR PhosphoSitePlus; Q7Z465; -.
DR BioMuta; BNIPL; -.
DR DMDM; 57012595; -.
DR MassIVE; Q7Z465; -.
DR PaxDb; Q7Z465; -.
DR PeptideAtlas; Q7Z465; -.
DR PRIDE; Q7Z465; -.
DR ProteomicsDB; 69155; -. [Q7Z465-1]
DR ProteomicsDB; 69156; -. [Q7Z465-2]
DR ProteomicsDB; 69157; -. [Q7Z465-3]
DR Antibodypedia; 20308; 102 antibodies from 23 providers.
DR DNASU; 149428; -.
DR Ensembl; ENST00000295294.11; ENSP00000295294.7; ENSG00000163141.20. [Q7Z465-2]
DR Ensembl; ENST00000368931.8; ENSP00000357927.3; ENSG00000163141.20. [Q7Z465-1]
DR Ensembl; ENST00000485855.1; ENSP00000435072.1; ENSG00000163141.20. [Q7Z465-3]
DR Ensembl; ENST00000650563.1; ENSP00000497659.1; ENSG00000163141.20. [Q7Z465-2]
DR GeneID; 149428; -.
DR KEGG; hsa:149428; -.
DR MANE-Select; ENST00000368931.8; ENSP00000357927.3; NM_138278.4; NP_612122.2.
DR UCSC; uc001ewl.3; human. [Q7Z465-1]
DR CTD; 149428; -.
DR DisGeNET; 149428; -.
DR GeneCards; BNIPL; -.
DR HGNC; HGNC:16976; BNIPL.
DR HPA; ENSG00000163141; Group enriched (esophagus, skin, vagina).
DR MIM; 611275; gene.
DR neXtProt; NX_Q7Z465; -.
DR OpenTargets; ENSG00000163141; -.
DR PharmGKB; PA38196; -.
DR VEuPathDB; HostDB:ENSG00000163141; -.
DR eggNOG; ENOG502QUPS; Eukaryota.
DR GeneTree; ENSGT00940000161723; -.
DR HOGENOM; CLU_039135_1_0_1; -.
DR InParanoid; Q7Z465; -.
DR OMA; KEDWQDE; -.
DR OrthoDB; 755773at2759; -.
DR PhylomeDB; Q7Z465; -.
DR TreeFam; TF324164; -.
DR PathwayCommons; Q7Z465; -.
DR SignaLink; Q7Z465; -.
DR BioGRID-ORCS; 149428; 14 hits in 1074 CRISPR screens.
DR GeneWiki; BNIPL; -.
DR GenomeRNAi; 149428; -.
DR Pharos; Q7Z465; Tbio.
DR PRO; PR:Q7Z465; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z465; protein.
DR Bgee; ENSG00000163141; Expressed in lower esophagus mucosa and 118 other tissues.
DR ExpressionAtlas; Q7Z465; baseline and differential.
DR Genevisible; Q7Z465; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0040009; P:regulation of growth rate; IDA:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR Pfam; PF12496; BNIP2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Reference proteome.
FT CHAIN 1..357
FT /note="Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-
FT like protein"
FT /id="PRO_0000210770"
FT DOMAIN 191..352
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 32..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11741952,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012448"
FT VAR_SEQ 285..357
FT /note="LRKNLRALVVVHATWYVKAFLALLRPFISSKFTRKIRFLDSLGELAQLISLD
FT QVHIPEAVRQLDRDLHGSGGT -> VL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11741952"
FT /id="VSP_012449"
FT VARIANT 65
FT /note="S -> N (in dbSNP:rs12068365)"
FT /id="VAR_051917"
FT VARIANT 226
FT /note="S -> N (in dbSNP:rs12068365)"
FT /id="VAR_051918"
SQ SEQUENCE 357 AA; 39713 MW; C0BCF92BACE9DE4F CRC64;
MGTIQEAGKK TDVGVREIAE APELGAALRH GELELKEEWQ DEEFPRLLPE EAGTSEDPED
PKGDSQAAAG TPSTLALCGQ RPMRKRLSAP ELRLSLTKGP GNDGASPTQS APSSPDGSSD
LEIDELETPS DSEQLDSGHE FEWEDELPRA EGLGTSETAE RLGRGCMWDV TGEDGHHWRV
FRMGPREQRV DMTVIEPYKK VLSHGGYHGD GLNAVILFAS CYLPRSSIPN YTYVMEHLFR
YMVGTLELLV AENYLLVHLS GGTSRAQVPP LSWIRQCYRT LDRRLRKNLR ALVVVHATWY
VKAFLALLRP FISSKFTRKI RFLDSLGELA QLISLDQVHI PEAVRQLDRD LHGSGGT
