BIRC7_HUMAN
ID BIRC7_HUMAN Reviewed; 298 AA.
AC Q96CA5; Q9BQV0; Q9H2A8; Q9HAP7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Baculoviral IAP repeat-containing protein 7;
DE EC=2.3.2.27 {ECO:0000269|PubMed:16729033};
DE AltName: Full=Kidney inhibitor of apoptosis protein;
DE Short=KIAP;
DE AltName: Full=Livin;
DE AltName: Full=Melanoma inhibitor of apoptosis protein;
DE Short=ML-IAP;
DE AltName: Full=RING finger protein 50;
DE AltName: Full=RING-type E3 ubiquitin transferase BIRC7 {ECO:0000305};
DE Contains:
DE RecName: Full=Baculoviral IAP repeat-containing protein 7 30kDa subunit;
DE Short=Truncated livin;
DE Short=p30-Livin;
DE Short=tLivin;
GN Name=BIRC7; Synonyms=KIAP, LIVIN, MLIAP, RNF50;
GN ORFNames=UNQ5800/PRO19607/PRO21344;
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 2), AND FUNCTION.
RC TISSUE=Fetal kidney;
RX PubMed=11162435; DOI=10.1006/bbrc.2000.4027;
RA Lin J.-H., Deng G., Huang Q., Morser J.;
RT "KIAP, a novel member of the inhibitor of apoptosis protein family.";
RL Biochem. Biophys. Res. Commun. 279:820-831(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION (ISOFORMS 1 AND 2), ALTERNATIVE
RP SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
RC TISSUE=Melanoma;
RX PubMed=11322947; DOI=10.1016/s0014-5793(01)02366-3;
RA Ashhab Y., Alian A., Polliack A., Panet A., Yehuda D.B.;
RT "Two splicing variants of a new inhibitor of apoptosis gene with different
RT biological properties and tissue distribution pattern.";
RL FEBS Lett. 495:56-60(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=11024045; DOI=10.1074/jbc.m003670200;
RA Kasof G.M., Gomes B.C.;
RT "Livin, a novel inhibitor of apoptosis protein family member.";
RL J. Biol. Chem. 276:3238-3246(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-223.
RC TISSUE=Skin;
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 [7]
RP FUNCTION, AND MUTAGENESIS OF 87-GLU--GLU-88; ASP-120; CYS-124 AND ASP-138.
RX PubMed=11084335; DOI=10.1016/s0960-9822(00)00781-8;
RA Vucic D., Stennicke H.R., Pisabarro M.T., Salvesen G.S., Dixit V.M.;
RT "ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in
RT human melanomas.";
RL Curr. Biol. 10:1359-1366(2000).
RN [8]
RP INTERACTION WITH SMAC.
RX PubMed=11801603; DOI=10.1074/jbc.m112045200;
RA Vucic D., Deshayes K., Ackerly H., Pisabarro M.T., Kadkhodayan S.,
RA Fairbrother W.J., Dixit V.M.;
RT "SMAC negatively regulates the anti-apoptotic activity of melanoma
RT inhibitor of apoptosis (ML-IAP).";
RL J. Biol. Chem. 277:12275-12279(2002).
RN [9]
RP FUNCTION.
RX PubMed=11865055; DOI=10.1128/mcb.22.6.1754-1766.2002;
RA Sanna M.G., da Silva Correia J., Ducrey O., Lee J., Nomoto K., Schrantz N.,
RA Deveraux Q.L., Ulevitch R.J.;
RT "IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1
RT signaling cascade and caspase inhibition.";
RL Mol. Cell. Biol. 22:1754-1766(2002).
RN [10]
RP FUNCTION IN THE UBIQUITINATION OF DIABLO/SMAC, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH DIABLO/SMAC.
RX PubMed=16729033; DOI=10.1038/sj.cdd.4401959;
RA Ma L., Huang Y., Song Z., Feng S., Tian X., Du W., Qiu X., Heese K., Wu M.;
RT "Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathway.";
RL Cell Death Differ. 13:2079-2088(2006).
RN [11]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=17294084; DOI=10.1007/s10495-006-0049-1;
RA Nachmias B., Lazar I., Elmalech M., Abed-El-Rahaman I., Asshab Y.,
RA Mandelboim O., Perlman R., Ben-Yehuda D.;
RT "Subcellular localization determines the delicate balance between the
RT anti- and pro-apoptotic activity of Livin.";
RL Apoptosis 12:1129-1142(2007).
RN [12]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=18034418; DOI=10.1002/eji.200636600;
RA Nachmias B., Mizrahi S., Elmalech M., Lazar I., Ashhab Y., Gazit R.,
RA Markel G., Ben-Yehuda D., Mandelboim O.;
RT "Manipulation of NK cytotoxicity by the IAP family member Livin.";
RL Eur. J. Immunol. 37:3467-3476(2007).
RN [13]
RP REVIEW ON FUNCTION.
RX PubMed=19074843; DOI=10.1158/1535-7163.mct-08-0480;
RA Wang L., Zhang Q., Liu B., Han M., Shan B.;
RT "Challenge and promise: roles for Livin in progression and therapy of
RT cancer.";
RL Mol. Cancer Ther. 7:3661-3669(2008).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=21617971; DOI=10.1007/s11010-011-0873-7;
RA Yan B.;
RT "Research progress on Livin protein: an inhibitor of apoptosis.";
RL Mol. Cell. Biochem. 357:39-45(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 63-179 IN COMPLEX WITH PHAGE-AND
RP SMAC-DERIVED PEPTIDES, AND ZINC-BINDING SITES.
RX PubMed=12846571; DOI=10.1021/bi034227t;
RA Franklin M.C., Kadkhodayan S., Ackerly H., Alexandru D., Distefano M.D.,
RA Elliott L.O., Flygare J.A., Mausisa G., Okawa D.C., Ong D., Vucic D.,
RA Deshayes K., Fairbrother W.J.;
RT "Structure and function analysis of peptide antagonists of melanoma
RT inhibitor of apoptosis (ML-IAP).";
RL Biochemistry 42:8223-8231(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 63-159, AND ZINC-BINDING SITES.
RX PubMed=15485396; DOI=10.1042/bj20041108;
RA Vucic D., Franklin M.C., Wallweber H.J., Das K., Eckelman B.P., Shin H.,
RA Elliott L.O., Kadkhodayan S., Deshayes K., Salvesen G.S., Fairbrother W.J.;
RT "Engineering ML-IAP to produce an extraordinarily potent caspase 9
RT inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-
RT IAP.";
RL Biochem. J. 385:11-20(2005).
CC -!- FUNCTION: Apoptotic regulator capable of exerting proapoptotic and
CC anti-apoptotic activities and plays crucial roles in apoptosis, cell
CC proliferation, and cell cycle control (PubMed:11162435,
CC PubMed:11024045, PubMed:11084335, PubMed:16729033, PubMed:17294084).
CC Its anti-apoptotic activity is mediated through the inhibition of
CC CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase
CC activity (PubMed:11024045, PubMed:16729033). As it is a weak caspase
CC inhibitor, its anti-apoptotic activity is thought to be due to its
CC ability to ubiquitinate DIABLO/SMAC targeting it for degradation
CC thereby promoting cell survival (PubMed:16729033). May contribute to
CC caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt
CC XIAP/BIRC4-caspase interactions (PubMed:16729033). Protects against
CC apoptosis induced by TNF or by chemical agents such as adriamycin,
CC etoposide or staurosporine (PubMed:11162435, PubMed:11084335,
CC PubMed:11865055). Suppression of apoptosis is mediated by activation of
CC MAPK8/JNK1, and possibly also of MAPK9/JNK2 (PubMed:11865055). This
CC activation depends on TAB1 and MAP3K7/TAK1 (PubMed:11865055). In vitro,
CC inhibits CASP3 and proteolytic activation of pro-CASP9
CC (PubMed:11024045). {ECO:0000269|PubMed:11024045,
CC ECO:0000269|PubMed:11084335, ECO:0000269|PubMed:11162435,
CC ECO:0000269|PubMed:11865055, ECO:0000269|PubMed:16729033,
CC ECO:0000269|PubMed:17294084}.
CC -!- FUNCTION: [Isoform 1]: Blocks staurosporine-induced apoptosis
CC (PubMed:11322947). Promotes natural killer (NK) cell-mediated killing
CC (PubMed:18034418). {ECO:0000269|PubMed:11322947,
CC ECO:0000269|PubMed:18034418}.
CC -!- FUNCTION: [Isoform 2]: Blocks etoposide-induced apoptosis
CC (PubMed:11162435, PubMed:11322947). Protects against natural killer
CC (NK) cell-mediated killing (PubMed:18034418).
CC {ECO:0000269|PubMed:11162435, ECO:0000269|PubMed:11322947,
CC ECO:0000269|PubMed:18034418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:16729033};
CC -!- SUBUNIT: Binds to CASP9. Interaction with DIABLO/SMAC via the BIR
CC domain disrupts binding to CASP9 and apoptotic suppressor activity.
CC Interacts with TAB1. In vitro, interacts with CASP3 and CASP7 via its
CC BIR domain. {ECO:0000269|PubMed:11801603, ECO:0000269|PubMed:12846571,
CC ECO:0000269|PubMed:16729033}.
CC -!- INTERACTION:
CC Q96CA5; Q9UQB9: AURKC; NbExp=3; IntAct=EBI-517623, EBI-3926851;
CC Q96CA5; Q13490: BIRC2; NbExp=6; IntAct=EBI-517623, EBI-514538;
CC Q96CA5; Q9Y3E2: BOLA1; NbExp=3; IntAct=EBI-517623, EBI-1049556;
CC Q96CA5; A0A087WZT3: BOLA2B; NbExp=5; IntAct=EBI-517623, EBI-12006120;
CC Q96CA5; P55211: CASP9; NbExp=12; IntAct=EBI-517623, EBI-516799;
CC Q96CA5; P26196: DDX6; NbExp=7; IntAct=EBI-517623, EBI-351257;
CC Q96CA5; Q9NR28: DIABLO; NbExp=6; IntAct=EBI-517623, EBI-517508;
CC Q96CA5; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-517623, EBI-741626;
CC Q96CA5; P52655: GTF2A1; NbExp=3; IntAct=EBI-517623, EBI-389518;
CC Q96CA5; O43464: HTRA2; NbExp=2; IntAct=EBI-517623, EBI-517086;
CC Q96CA5; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-517623, EBI-2556193;
CC Q96CA5; Q96JN0-2: LCOR; NbExp=3; IntAct=EBI-517623, EBI-10961483;
CC Q96CA5; P61968: LMO4; NbExp=3; IntAct=EBI-517623, EBI-2798728;
CC Q96CA5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-517623, EBI-741158;
CC Q96CA5; O43189: PHF1; NbExp=4; IntAct=EBI-517623, EBI-530034;
CC Q96CA5; O15160: POLR1C; NbExp=6; IntAct=EBI-517623, EBI-1055079;
CC Q96CA5; P0CG20: PRR35; NbExp=3; IntAct=EBI-517623, EBI-11986293;
CC Q96CA5; P20618: PSMB1; NbExp=5; IntAct=EBI-517623, EBI-372273;
CC Q96CA5; P47897: QARS1; NbExp=3; IntAct=EBI-517623, EBI-347462;
CC Q96CA5; P35711-4: SOX5; NbExp=3; IntAct=EBI-517623, EBI-11954419;
CC Q96CA5; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-517623, EBI-11139477;
CC Q96CA5; Q08117: TLE5; NbExp=4; IntAct=EBI-517623, EBI-717810;
CC Q96CA5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-517623, EBI-11741437;
CC Q96CA5; O14787-2: TNPO2; NbExp=3; IntAct=EBI-517623, EBI-12076664;
CC Q96CA5; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-517623, EBI-10241197;
CC Q96CA5; P49638: TTPA; NbExp=3; IntAct=EBI-517623, EBI-10210710;
CC Q96CA5; P61086: UBE2K; NbExp=3; IntAct=EBI-517623, EBI-473850;
CC Q96CA5; O75604: USP2; NbExp=3; IntAct=EBI-517623, EBI-743272;
CC Q96CA5; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-517623, EBI-2559305;
CC Q96CA5; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-517623, EBI-2815120;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17294084}. Cytoplasm
CC {ECO:0000269|PubMed:17294084}. Golgi apparatus
CC {ECO:0000269|PubMed:17294084}. Note=Nuclear, and in a filamentous
CC pattern throughout the cytoplasm. Full-length livin is detected
CC exclusively in the cytoplasm, whereas the truncated form (tLivin) is
CC found in the peri-nuclear region with marked localization to the Golgi
CC apparatus; the accumulation of tLivin in the nucleus shows positive
CC correlation with the increase in apoptosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Livin alpha;
CC IsoId=Q96CA5-1; Sequence=Displayed;
CC Name=1; Synonyms=Livin beta;
CC IsoId=Q96CA5-2; Sequence=VSP_002459;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at very low
CC levels or not detectable in most adult tissues. Detected in adult
CC heart, placenta, lung, lymph node, spleen and ovary, and in several
CC carcinoma cell lines. Isoform 2 is detected in fetal kidney, heart and
CC spleen, and at lower levels in adult brain, skeletal muscle and
CC peripheral blood leukocytes.
CC -!- DOMAIN: The RING domain is essential for autoubiquitination.
CC -!- PTM: Autoubiquitinated and undergoes proteasome-mediated degradation.
CC -!- PTM: The truncated protein (tLivin) not only loses its anti-apoptotic
CC effect but also acquires a pro-apoptotic effect.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; AF301009; AAG37878.1; -; mRNA.
DR EMBL; AJ309298; CAC37337.1; -; Genomic_DNA.
DR EMBL; AJ309298; CAC37338.1; -; Genomic_DNA.
DR EMBL; AF311388; AAG33622.1; -; mRNA.
DR EMBL; AY358835; AAQ89194.1; -; mRNA.
DR EMBL; AY358836; AAQ89195.1; -; mRNA.
DR EMBL; AL121827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014475; AAH14475.1; -; mRNA.
DR CCDS; CCDS13512.1; -. [Q96CA5-2]
DR CCDS; CCDS13513.1; -. [Q96CA5-1]
DR PIR; JC7568; JC7568.
DR RefSeq; NP_071444.1; NM_022161.3. [Q96CA5-2]
DR RefSeq; NP_647478.1; NM_139317.2. [Q96CA5-1]
DR PDB; 1OXN; X-ray; 2.20 A; A/B/C/D/E=63-179.
DR PDB; 1OXQ; X-ray; 2.30 A; A/B/C/D/E=63-179.
DR PDB; 1OY7; X-ray; 2.70 A; A/B/C/D/E=63-179.
DR PDB; 1TW6; X-ray; 1.71 A; A/B=63-172.
DR PDB; 2I3H; X-ray; 1.62 A; A/B=63-172.
DR PDB; 2I3I; X-ray; 2.30 A; A/B=63-172.
DR PDB; 3F7G; X-ray; 2.30 A; A/B/C/D/E=63-179.
DR PDB; 3F7H; X-ray; 1.80 A; A/B=63-172.
DR PDB; 3F7I; X-ray; 1.90 A; A/B=63-172.
DR PDB; 3GT9; X-ray; 1.70 A; A/B=63-172.
DR PDB; 3GTA; X-ray; 1.70 A; A/B=63-172.
DR PDB; 3UW5; X-ray; 1.71 A; A/B=63-159.
DR PDB; 4AUQ; X-ray; 2.18 A; B/E=239-298.
DR PDBsum; 1OXN; -.
DR PDBsum; 1OXQ; -.
DR PDBsum; 1OY7; -.
DR PDBsum; 1TW6; -.
DR PDBsum; 2I3H; -.
DR PDBsum; 2I3I; -.
DR PDBsum; 3F7G; -.
DR PDBsum; 3F7H; -.
DR PDBsum; 3F7I; -.
DR PDBsum; 3GT9; -.
DR PDBsum; 3GTA; -.
DR PDBsum; 3UW5; -.
DR PDBsum; 4AUQ; -.
DR AlphaFoldDB; Q96CA5; -.
DR SMR; Q96CA5; -.
DR BioGRID; 122670; 60.
DR DIP; DIP-33486N; -.
DR IntAct; Q96CA5; 43.
DR MINT; Q96CA5; -.
DR STRING; 9606.ENSP00000217169; -.
DR BindingDB; Q96CA5; -.
DR ChEMBL; CHEMBL1075127; -.
DR GuidetoPHARMACOLOGY; 2794; -.
DR MEROPS; I32.007; -.
DR GlyGen; Q96CA5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96CA5; -.
DR PhosphoSitePlus; Q96CA5; -.
DR BioMuta; BIRC7; -.
DR DMDM; 21759008; -.
DR MassIVE; Q96CA5; -.
DR MaxQB; Q96CA5; -.
DR PaxDb; Q96CA5; -.
DR PeptideAtlas; Q96CA5; -.
DR PRIDE; Q96CA5; -.
DR ProteomicsDB; 76171; -. [Q96CA5-1]
DR ProteomicsDB; 76172; -. [Q96CA5-2]
DR Antibodypedia; 15058; 661 antibodies from 44 providers.
DR DNASU; 79444; -.
DR Ensembl; ENST00000217169.8; ENSP00000217169.3; ENSG00000101197.13. [Q96CA5-1]
DR Ensembl; ENST00000342412.10; ENSP00000345213.6; ENSG00000101197.13. [Q96CA5-2]
DR GeneID; 79444; -.
DR KEGG; hsa:79444; -.
DR MANE-Select; ENST00000217169.8; ENSP00000217169.3; NM_139317.3; NP_647478.1.
DR UCSC; uc002yei.5; human. [Q96CA5-1]
DR CTD; 79444; -.
DR DisGeNET; 79444; -.
DR GeneCards; BIRC7; -.
DR HGNC; HGNC:13702; BIRC7.
DR HPA; ENSG00000101197; Tissue enhanced (placenta).
DR MIM; 605737; gene.
DR neXtProt; NX_Q96CA5; -.
DR OpenTargets; ENSG00000101197; -.
DR PharmGKB; PA25364; -.
DR VEuPathDB; HostDB:ENSG00000101197; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000160406; -.
DR HOGENOM; CLU_016347_2_1_1; -.
DR InParanoid; Q96CA5; -.
DR OMA; WWVLEPP; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; Q96CA5; -.
DR TreeFam; TF105356; -.
DR PathwayCommons; Q96CA5; -.
DR SignaLink; Q96CA5; -.
DR SIGNOR; Q96CA5; -.
DR BioGRID-ORCS; 79444; 13 hits in 1115 CRISPR screens.
DR ChiTaRS; BIRC7; human.
DR EvolutionaryTrace; Q96CA5; -.
DR GeneWiki; BIRC7; -.
DR GenomeRNAi; 79444; -.
DR Pharos; Q96CA5; Tchem.
DR PRO; PR:Q96CA5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96CA5; protein.
DR Bgee; ENSG00000101197; Expressed in adrenal tissue and 82 other tissues.
DR ExpressionAtlas; Q96CA5; baseline and differential.
DR Genevisible; Q96CA5; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR GO; GO:0070247; P:regulation of natural killer cell apoptotic process; IDA:UniProtKB.
DR CDD; cd00022; BIR; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00653; BIR; 1.
DR SMART; SM00238; BIR; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Golgi apparatus;
KW Metal-binding; Nucleus; Protease inhibitor; Reference proteome;
KW Thiol protease inhibitor; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..298
FT /note="Baculoviral IAP repeat-containing protein 7"
FT /id="PRO_0000122362"
FT CHAIN 53..298
FT /note="Baculoviral IAP repeat-containing protein 7 30kDa
FT subunit"
FT /id="PRO_0000416092"
FT REPEAT 90..155
FT /note="BIR"
FT ZN_FING 252..286
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 52..53
FT /note="Cleavage; by CASP3 and CASP7"
FT VAR_SEQ 216..233
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11024045,
FT ECO:0000303|PubMed:12975309"
FT /id="VSP_002459"
FT VARIANT 223
FT /note="E -> Q (in dbSNP:rs1077019)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020253"
FT MUTAGEN 87..88
FT /note="EE->AA: No change in SMAC interaction and anti-
FT apoptotic activity."
FT /evidence="ECO:0000269|PubMed:11084335"
FT MUTAGEN 120
FT /note="D->A: Abolishes inhibition of caspases, SMAC binding
FT and anti-apoptotic activity."
FT /evidence="ECO:0000269|PubMed:11084335"
FT MUTAGEN 124
FT /note="C->A: Abolishes inhibition of caspases and anti-
FT apoptotic activity."
FT /evidence="ECO:0000269|PubMed:11084335"
FT MUTAGEN 138
FT /note="D->A: Abolishes inhibition of caspases, SMAC binding
FT and anti-apoptotic activity."
FT /evidence="ECO:0000269|PubMed:11084335"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2I3H"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:2I3H"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:2I3H"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2I3H"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3UW5"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2I3H"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2I3H"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:2I3H"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:4AUQ"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4AUQ"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4AUQ"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4AUQ"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4AUQ"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4AUQ"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4AUQ"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:4AUQ"
SQ SEQUENCE 298 AA; 32798 MW; B2EAAEE531BEC101 CRC64;
MGPKDSAKCL HRGPQPSHWA AGDGPTQERC GPRSLGSPVL GLDTCRAWDH VDGQILGQLR
PLTEEEEEEG AGATLSRGPA FPGMGSEELR LASFYDWPLT AEVPPELLAA AGFFHTGHQD
KVRCFFCYGG LQSWKRGDDP WTEHAKWFPS CQFLLRSKGR DFVHSVQETH SQLLGSWDPW
EEPEDAAPVA PSVPASGYPE LPTPRREVQS ESAQEPGGVS PAEAQRAWWV LEPPGARDVE
AQLRRLQEER TCKVCLDRAV SIVFVPCGHL VCAECAPGLQ LCPICRAPVR SRVRTFLS
