C8AP2_HUMAN
ID C8AP2_HUMAN Reviewed; 1982 AA.
AC Q9UKL3; A2RUB7; E1P553; Q6PH76; Q7LCQ7; Q86YD9; Q9NUQ4; Q9NZV9; Q9P2N1;
AC Q9Y563;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=CASP8-associated protein 2;
DE AltName: Full=FLICE-associated huge protein;
GN Name=CASP8AP2 {ECO:0000312|HGNC:HGNC:1510};
GN Synonyms=FLASH, KIAA1315 {ECO:0000312|EMBL:BAA92553.2},
GN RIP25 {ECO:0000312|EMBL:AAD45537.2};
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].
RC TISSUE=T-cell;
RA Kimura T., Imai Y., Yonehara S.;
RT "Reply: searching for FLASH domains.";
RL Nature 401:662-663(1999).
RN [2] {ECO:0000312|EMBL:AAD45537.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood leukocyte {ECO:0000312|EMBL:AAD45537.2};
RA Yan M.D., Sun L.Y., Liu X.Y., Zheng Z.C.;
RT "RIP25, a human homolog of Mus musculus FLASH, is involved in IL-2
RT signaling.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:BAA92553.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAA92553.2};
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6] {ECO:0000312|EMBL:AAD45537.2}
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAH56685.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:AAH42577.1}, and
RC Testis {ECO:0000312|EMBL:AAH56685.1};
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 [8] {ECO:0000305, ECO:0000312|EMBL:BAA92067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1478-1982.
RC TISSUE=Placenta {ECO:0000312|EMBL:BAA92067.1};
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 [9] {ECO:0000312|EMBL:AAF03367.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 714-1982.
RX PubMed=10537104; DOI=10.1038/44317;
RA Koonin E.V., Aravind L., Hofmann K., Tschopp J., Dixit V.M.;
RT "Apoptosis. Searching for FLASH domains.";
RL Nature 401:662-662(1999).
RN [10] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NCOA2, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12477726; DOI=10.1074/jbc.m209234200;
RA Kino T., Chrousos G.P.;
RT "Tumor necrosis factor alpha receptor- and Fas-associated FLASH inhibit
RT transcriptional activity of the glucocorticoid receptor by binding to and
RT interfering with its interaction with p160 type nuclear receptor
RT coactivators.";
RL J. Biol. Chem. 278:3023-3029(2003).
RN [11] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NCOA3.
RX PubMed=15698540; DOI=10.1016/j.jsbmb.2004.09.003;
RA Kino T., Ichijo T., Chrousos G.P.;
RT "FLASH interacts with p160 coactivator subtypes and differentially
RT suppresses transcriptional activity of steroid hormone receptors.";
RL J. Steroid Biochem. Mol. Biol. 92:357-363(2004).
RN [12]
RP FUNCTION, INTERACTION WITH NPAT, AND SUBCELLULAR LOCATION.
RX PubMed=17003125; DOI=10.1073/pnas.0604227103;
RA Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G., Rossi M.,
RA Knight R.A., Matera A.G., Melino G., De Laurenzi V.;
RT "FLASH is required for histone transcription and S-phase progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14808-14812(2006).
RN [13]
RP FUNCTION IN FAS-MEDIATED APOPTOSIS, INTERACTION WITH CASP8 AND SP100, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17245429; DOI=10.1038/sj.emboj.7601504;
RA Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.;
RT "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear
RT bodies.";
RL EMBO J. 26:391-401(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP INTERACTION WITH SRRT.
RX PubMed=19546234; DOI=10.1128/mcb.00289-09;
RA Kiriyama M., Kobayashi Y., Saito M., Ishikawa F., Yonehara S.;
RT "Interaction of FLASH with arsenite resistance protein 2 is involved in
RT cell cycle progression at S phase.";
RL Mol. Cell. Biol. 29:4729-4741(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-20, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, AND INTERACTION WITH SUMO1
RP AND SUMO2.
RX PubMed=23086935; DOI=10.1074/jbc.m112.410985;
RA Sun H., Hunter T.;
RT "PolySUMO-binding proteins identified through a string search.";
RL J. Biol. Chem. 287:42071-42083(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-194; SER-567;
RP SER-658; SER-815; SER-875; SER-940 AND SER-1161, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP STRUCTURE BY NMR OF 1916-1982.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of CASP8-associated protein 2 from Homo sapiens,
RT Northeast structural genomics consortium (NESG) target HR8150A.";
RL Submitted (JUN-2012) to the PDB data bank.
CC -!- FUNCTION: Participates in TNF-alpha-induced blockade of glucocorticoid
CC receptor (GR) transactivation at the nuclear receptor coactivator
CC level, upstream and independently of NF-kappa-B. Suppresses both
CC NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in
CC TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent
CC pathway. Acts as a downstream mediator for CASP8-induced activation of
CC NF-kappa-B. Required for the activation of CASP8 in FAS-mediated
CC apoptosis. Required for histone gene transcription and progression
CC through S phase. {ECO:0000269|PubMed:12477726,
CC ECO:0000269|PubMed:15698540, ECO:0000269|PubMed:17003125,
CC ECO:0000269|PubMed:17245429}.
CC -!- SUBUNIT: Self-associates. Component of the death-inducing signaling
CC complex (DISC) with CASP8, FADD and FAS. Interacts with NCOA2 and
CC NCOA3. Interacts with SRRT. Interacts with TRAF2. Interacts with NPAT.
CC Interacts (via SIM domains) with SUMO1 and SUMO2. Interacts with SP100;
CC may negatively regulate CASP8AP2 export from the nucleus to the
CC cytoplasm. {ECO:0000269|PubMed:12477726, ECO:0000269|PubMed:15698540,
CC ECO:0000269|PubMed:17003125, ECO:0000269|PubMed:17245429,
CC ECO:0000269|PubMed:19546234, ECO:0000269|PubMed:23086935}.
CC -!- INTERACTION:
CC Q9UKL3; Q14790: CASP8; NbExp=3; IntAct=EBI-2339650, EBI-78060;
CC Q9UKL3; O75925: PIAS1; NbExp=4; IntAct=EBI-2339650, EBI-629434;
CC Q9UKL3; P23497: SP100; NbExp=5; IntAct=EBI-2339650, EBI-751145;
CC Q9UKL3; O15350-1: TP73; NbExp=2; IntAct=EBI-2339650, EBI-389619;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body.
CC Mitochondrion. Note=Exported from the nucleus to the mitochondria upon
CC FAS activation.
CC -!- INDUCTION: By TNF which induces strong nuclear localization.
CC {ECO:0000269|PubMed:12477726}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56685.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 364.; Evidence={ECO:0000305};
CC Sequence=BAA92067.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF154415; AAF03367.1; -; mRNA.
DR EMBL; AF164678; AAD45537.2; -; mRNA.
DR EMBL; AB037736; BAA92553.2; -; mRNA.
DR EMBL; AL353692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48540.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48542.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48544.1; -; Genomic_DNA.
DR EMBL; BC042577; AAH42577.1; -; mRNA.
DR EMBL; BC056685; AAH56685.1; ALT_SEQ; mRNA.
DR EMBL; BC132828; AAI32829.1; -; mRNA.
DR EMBL; BC132830; AAI32831.1; -; mRNA.
DR EMBL; AK002070; BAA92067.1; ALT_INIT; mRNA.
DR EMBL; AF165161; AAD45157.1; -; mRNA.
DR RefSeq; NP_001131139.1; NM_001137667.1.
DR RefSeq; NP_001131140.1; NM_001137668.1.
DR RefSeq; NP_036247.1; NM_012115.3.
DR PDB; 2LR8; NMR; -; A=1916-1982.
DR PDB; 6ANO; X-ray; 2.61 A; A/B=51-137.
DR PDB; 6AOZ; X-ray; 2.10 A; A/B/C/D=51-137.
DR PDB; 6AP0; X-ray; 2.58 A; A/B=51-137.
DR PDBsum; 2LR8; -.
DR PDBsum; 6ANO; -.
DR PDBsum; 6AOZ; -.
DR PDBsum; 6AP0; -.
DR AlphaFoldDB; Q9UKL3; -.
DR BMRB; Q9UKL3; -.
DR SMR; Q9UKL3; -.
DR BioGRID; 115315; 38.
DR DIP; DIP-40986N; -.
DR IntAct; Q9UKL3; 18.
DR MINT; Q9UKL3; -.
DR STRING; 9606.ENSP00000478179; -.
DR GlyGen; Q9UKL3; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UKL3; -.
DR PhosphoSitePlus; Q9UKL3; -.
DR BioMuta; CASP8AP2; -.
DR DMDM; 74721007; -.
DR EPD; Q9UKL3; -.
DR jPOST; Q9UKL3; -.
DR MassIVE; Q9UKL3; -.
DR MaxQB; Q9UKL3; -.
DR PeptideAtlas; Q9UKL3; -.
DR PRIDE; Q9UKL3; -.
DR ProteomicsDB; 84816; -.
DR DNASU; 9994; -.
DR GeneID; 9994; -.
DR KEGG; hsa:9994; -.
DR CTD; 9994; -.
DR DisGeNET; 9994; -.
DR GeneCards; CASP8AP2; -.
DR HGNC; HGNC:1510; CASP8AP2.
DR MIM; 606880; gene.
DR neXtProt; NX_Q9UKL3; -.
DR PharmGKB; PA26093; -.
DR eggNOG; ENOG502QQGD; Eukaryota.
DR InParanoid; Q9UKL3; -.
DR OrthoDB; 31356at2759; -.
DR PhylomeDB; Q9UKL3; -.
DR PathwayCommons; Q9UKL3; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR SignaLink; Q9UKL3; -.
DR SIGNOR; Q9UKL3; -.
DR BioGRID-ORCS; 9994; 35 hits in 166 CRISPR screens.
DR ChiTaRS; CASP8AP2; human.
DR GeneWiki; CASP8AP2; -.
DR GenomeRNAi; 9994; -.
DR Pharos; Q9UKL3; Tbio.
DR PRO; PR:Q9UKL3; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9UKL3; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0005123; F:death receptor binding; TAS:ProtInc.
DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0032184; F:SUMO polymer binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR GO; GO:0036337; P:Fas signaling pathway; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR039674; FLASH.
DR InterPro; IPR009057; Homeobox-like_sf.
DR PANTHER; PTHR15489; PTHR15489; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Apoptosis; Cell cycle; Cytoplasm;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..1982
FT /note="CASP8-associated protein 2"
FT /id="PRO_0000076188"
FT REGION 159..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1982
FT /note="NCOA2-binding"
FT /evidence="ECO:0000269|PubMed:12477726"
FT REGION 1803..1909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1683..1687
FT /note="SUMO interaction motif 1 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT MOTIF 1737..1741
FT /note="SUMO interaction motif 2 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT MOTIF 1794..1798
FT /note="SUMO interaction motif 3 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT COMPBIAS 159..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1343
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUF3"
FT VARIANT 1659
FT /note="P -> S (in dbSNP:rs3799896)"
FT /id="VAR_050700"
FT CONFLICT 278
FT /note="L -> S (in Ref. 2; AAD45537)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="D -> E (in Ref. 7; AAH56685)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="L -> P (in Ref. 2; AAD45537)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="M -> T (in Ref. 2; AAD45537)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="N -> S (in Ref. 2; AAD45537)"
FT /evidence="ECO:0000305"
FT CONFLICT 1713
FT /note="C -> Y (in Ref. 2; AAD45537)"
FT /evidence="ECO:0000305"
FT CONFLICT 1754
FT /note="Missing (in Ref. 3; BAA92553)"
FT /evidence="ECO:0000305"
FT CONFLICT 1832
FT /note="S -> P (in Ref. 8; BAA92067)"
FT /evidence="ECO:0000305"
FT HELIX 73..137
FT /evidence="ECO:0007829|PDB:6AOZ"
FT STRAND 1925..1927
FT /evidence="ECO:0007829|PDB:2LR8"
FT HELIX 1931..1943
FT /evidence="ECO:0007829|PDB:2LR8"
FT HELIX 1948..1958
FT /evidence="ECO:0007829|PDB:2LR8"
FT HELIX 1962..1977
FT /evidence="ECO:0007829|PDB:2LR8"
SQ SEQUENCE 1982 AA; 222658 MW; AF2B1A7798C19E39 CRC64;
MAADDDNGDG TSLFDVFSAS PLKNNDEGSL DIYAGLDSAV SDSASKSCVP SRNCLDLYEE
ILTEEGTAKE ATYNDLQVEY GKCQLQMKEL MKKFKEIQTQ NFSLINENQS LKKNISALIK
TARVEINRKD EEISNLHQRL SEFPHFRNNH KTARTFDTVK TKDLKSRSPH LDDCSKTDHR
AKSDVSKDVH HSTSLPNLEK EGKPHSDKRS TSHLPTSVEK HCTNGVWSRS HYQVGEGSSN
EDSRRGRKDI RHSQFNRGTE RVRKDLSTGC GDGEPRILEA SQRLQGHPEK YGKGEPKTES
KSSKFKSNSD SDYKGERINS SWEKETPGER SHSRVDSQSD KKLERQSERS QNINRKEVKS
QDKEERKVDQ KPKSVVKDQD HWRRSERASL PHSKNEITFS HNSSKYHLEE RRGWEDCKRD
KSVNSHSFQD GRCPSSLSNS RTHKNIDSKE VDAMHQWENT PLKAERHRTE DKRKREQESK
EENRHIRNEK RVPTEHLQKT NKETKKTTTD LKKQNEPKTD KGEVLDNGVS EGADNKELAM
KAESGPNETK NKDLKLSFMK KLNLTLSPAK KQPVSQDNQH KITDIPKSSG VCDSESSMQV
KTVAYVPSIS EHILGEAAVS EHTMGETKST LLEPKVALLA VTEPRIGISE TNKEDENSLL
VRSVDNTMHC EEPICGTETS FPSPMEIQQT ESLFPSTGMK QTINNGRAAA PVVMDVLQTD
VSQNFGLELD TKRNDNSDYC GISEGMEMKV ALSTTVSETT ESILQPSIEE ADILPIMLSE
DNNPKFEPSV IVTPLVESKS CHLEPCLPKE TLDSSLQQTE LMDHRMATGE TNSVYHDDDN
SVLSIDLNHL RPIPEAISPL NSPVRPVAKV LRNESPPQVP VYNNSHKDVF LPNSAHSTSK
SQSDLNKENQ KPIYKSDKCT EADTCKNSPL DELEEGEIRS DSETSKPQES FEKNSKRRVS
ADVRKSKTIP RRGKSTVCLD KDSRKTHVRI HQTNNKWNKR PDKSSRSSKT EKKDKVMSTS
SLEKIVPIIA VPSSEQEIMH MLRMIRKHVR KNYMKFKAKF SLIQFHRIIE SAILSFTSLI
KHLNLHKISK SVTTLQKNLC DIIESKLKQV KKNGIVDRLF EQQLPDMKKK LWKFVDDQLD
YLFAKLKKIL VCDSKSFGRD SDEGKLEKTS KQNAQYSNSQ KRSVDNSNRE LLKEKLSKSE
DPVHYKSLVG CKKSEENYQD QNNSSINTVK HDIKKNFNIC FDNIKNSQSE ERSLEVHCPS
TPKSEKNEGS SIEDAQTSQH ATLKPERSFE ILTEQQASSL TFNLVSDAQM GEIFKSLLQG
SDLLDSSVNC TEKSEWELKT PEKQLLETLK CESIPACTTE ELVSGVASPC PKMISDDNWS
LLSSEKGPSL SSGLSLPVHP DVLDESCMFE VSTNLPLSKD NVCSVEKSKP CVSSILLEDL
AVSLTVPSPL KSDGHLSFLK PDMSSSSTPE EVISAHFSED ALLEEEDASE QDIHLALESD
NSSSKSSCSS SWTSRSVAPG FQYHPNLPMH AVIMEKSNDH FIVKIRRATP STSSGLKQSM
MPDELLTSLP RHGKEADEGP EKEYISCQNT VFKSVEELEN SNKNVDGSKS THEEQSSMIQ
TQVPDIYEFL KDASDKMGHS DEVADECFKL HQVWETKVPE SIEELPSMEE ISHSVGEHLP
NTYVDLTKDP VTETKNLGEF IEVTVLHIDQ LGCSGGNLNQ SAQILDNSLQ ADTVGAFIDL
TQDASSEAKS EGNHPALAVE DLGCGVIQVD EDNCKEEKAQ VANRPLKCIV EETYIDLTTE
SPSSCEVKKD ELKSEPGSNC DNSELPGTLH NSHKKRRNIS DLNHPHKKQR KETDLTNKEK
TKKPTQDSCE NTEAHQKKAS KKKAPPVTKD PSSLKATPGI KDSSAALATS TSLSAKNVIK
KKGEIIILWT RNDDREILLE CQKRGPSFKT FAYLAAKLDK NPNQVSERFQ QLMKLFEKSK
CR
