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BIRC8_HUMAN
ID   BIRC8_HUMAN             Reviewed;         236 AA.
AC   Q96P09; Q6IPY1; Q96RW5;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Baculoviral IAP repeat-containing protein 8;
DE   AltName: Full=Inhibitor of apoptosis-like protein 2;
DE            Short=IAP-like protein 2;
DE            Short=ILP-2;
DE   AltName: Full=Testis-specific inhibitor of apoptosis;
GN   Name=BIRC8; Synonyms=ILP2;
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], AND VARIANT TYR-196.
RC   TISSUE=Testis;
RX   PubMed=11597143; DOI=10.1006/geno.2001.6635;
RA   Lagace M., Xuan J.-Y., Young S.S., McRoberts C., Maier J.,
RA   Rajcan-Separovic E., Korneluk R.G.;
RT   "Genomic organization of the X-linked inhibitor of apoptosis and
RT   identification of a novel testis-specific transcript.";
RL   Genomics 77:181-188(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11390657; DOI=10.1128/mcb.21.13.4292-4301.2001;
RA   Richter B.W.M., Mir S.S., Eiben L.J., Lewis J., Reffey S.B., Frattini A.,
RA   Tian L., Frank S., Youle R.J., Nelson D.L., Notarangelo L.D., Vezzoni P.,
RA   Fearnhead H.O., Duckett C.S.;
RT   "Molecular cloning of ILP-2, a novel member of the inhibitor of apoptosis
RT   protein family.";
RL   Mol. Cell. Biol. 21:4292-4301(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-196.
RC   TISSUE=Brain;
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   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-95.
RX   PubMed=15485395; DOI=10.1042/bj20041107;
RA   Shin H., Renatus M., Eckelman B.P., Nunes V.A., Sampaio C.A.,
RA   Salvesen G.S.;
RT   "The BIR domain of IAP-like protein 2 is conformationally unstable:
RT   implications for caspase inhibition.";
RL   Biochem. J. 385:1-10(2005).
CC   -!- FUNCTION: Protects against apoptosis mediated by BAX.
CC   -!- SUBUNIT: Binds to caspase-9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis specific in normal tissues.
CC   -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR   EMBL; AF420440; AAL30369.1; -; mRNA.
DR   EMBL; AF164682; AAK81892.1; -; Genomic_DNA.
DR   EMBL; AC092070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC071665; AAH71665.2; -; mRNA.
DR   RefSeq; NP_203127.3; NM_033341.4.
DR   PDB; 1XB0; X-ray; 2.20 A; A/B/C/D/E/F=1-95.
DR   PDB; 1XB1; X-ray; 2.70 A; A/B/C/D/E/F=1-95.
DR   PDBsum; 1XB0; -.
DR   PDBsum; 1XB1; -.
DR   AlphaFoldDB; Q96P09; -.
DR   SMR; Q96P09; -.
DR   BioGRID; 125186; 32.
DR   IntAct; Q96P09; 16.
DR   MINT; Q96P09; -.
DR   STRING; 9606.ENSP00000412957; -.
DR   BindingDB; Q96P09; -.
DR   ChEMBL; CHEMBL5851; -.
DR   MEROPS; I32.008; -.
DR   iPTMnet; Q96P09; -.
DR   PhosphoSitePlus; Q96P09; -.
DR   BioMuta; BIRC8; -.
DR   DMDM; 311033354; -.
DR   MassIVE; Q96P09; -.
DR   PaxDb; Q96P09; -.
DR   PeptideAtlas; Q96P09; -.
DR   PRIDE; Q96P09; -.
DR   DNASU; 112401; -.
DR   UCSC; uc002qbk.4; human.
DR   GeneCards; BIRC8; -.
DR   HGNC; HGNC:14878; BIRC8.
DR   neXtProt; NX_Q96P09; -.
DR   PharmGKB; PA25365; -.
DR   eggNOG; KOG1101; Eukaryota.
DR   HOGENOM; CLU_016347_2_0_1; -.
DR   InParanoid; Q96P09; -.
DR   OrthoDB; 1340284at2759; -.
DR   PhylomeDB; Q96P09; -.
DR   TreeFam; TF105356; -.
DR   PathwayCommons; Q96P09; -.
DR   SignaLink; Q96P09; -.
DR   BioGRID-ORCS; 112401; 9 hits in 1102 CRISPR screens.
DR   EvolutionaryTrace; Q96P09; -.
DR   GenomeRNAi; 112401; -.
DR   Pharos; Q96P09; Tchem.
DR   PRO; PR:Q96P09; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q96P09; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
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:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   CDD; cd00022; BIR; 1.
DR   CDD; cd14395; UBA_BIRC4_8; 1.
DR   Gene3D; 1.10.533.10; -; 1.
DR   InterPro; IPR001370; BIR_rpt.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR042579; XIAP/BIRC8_UBA.
DR   InterPro; IPR001841; Znf_RING.
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; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytoplasm; Metal-binding; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..236
FT                   /note="Baculoviral IAP repeat-containing protein 8"
FT                   /id="PRO_0000122363"
FT   REPEAT          7..70
FT                   /note="BIR"
FT   ZN_FING         189..224
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   VARIANT         156
FT                   /note="A -> T (in dbSNP:rs35880972)"
FT                   /id="VAR_055944"
FT   VARIANT         165
FT                   /note="L -> S (in dbSNP:rs34092035)"
FT                   /id="VAR_055945"
FT   VARIANT         196
FT                   /note="H -> Y (in dbSNP:rs8109165)"
FT                   /evidence="ECO:0000269|PubMed:11597143,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028282"
FT   VARIANT         225
FT                   /note="A -> T (in dbSNP:rs35700345)"
FT                   /id="VAR_055946"
FT   VARIANT         225
FT                   /note="A -> V (in dbSNP:rs34683072)"
FT                   /id="VAR_055947"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   HELIX           20..25
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   HELIX           55..62
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   HELIX           67..73
FT                   /evidence="ECO:0007829|PDB:1XB0"
FT   HELIX           75..81
FT                   /evidence="ECO:0007829|PDB:1XB0"
SQ   SEQUENCE   236 AA;  27089 MW;  DF3A170E0DDFAD9D CRC64;
     MTGYEARLIT FGTWMYSVNK EQLARAGFYA IGQEDKVQCF HCGGGLANWK PKEDPWEQHA
     KWYPGCKYLL EEKGHEYINN IHLTRSLEGA LVQTTKKTPS LTKRISDTIF PNPMLQEAIR
     MGFDFKDVKK IMEERIQTSG SNYKTLEVLV ADLVSAQKDT TENELNQTSL QREISPEEPL
     RRLQEEKLCK ICMDRHIAVV FIPCGHLVTC KQCAEAVDRC PMCSAVIDFK QRVFMS
 
 
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