TRIA1_HUMAN
ID TRIA1_HUMAN Reviewed; 76 AA.
AC O43715; B2R4Z7; Q5RKS5; Q6LCA7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=TP53-regulated inhibitor of apoptosis 1;
DE AltName: Full=Protein 15E1.1;
DE AltName: Full=WF-1;
DE AltName: Full=p53-inducible cell-survival factor;
DE Short=p53CSV;
GN Name=TRIAP1; Synonyms=15E1.1; ORFNames=HSPC132;
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH ARAF AND HSP70, AND INDUCTION.
RX PubMed=15735003; DOI=10.1158/0008-5472.can-04-3339;
RA Park W.-R., Nakamura Y.;
RT "p53CSV, a novel p53-inducible gene involved in the p53-dependent cell-
RT survival pathway.";
RL Cancer Res. 65:1197-1206(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-76.
RC TISSUE=Heart;
RA Sugihara T., Tanaka M., Mitusi Y.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23931759; DOI=10.1016/j.cmet.2013.07.008;
RA Potting C., Tatsuta T., Konig T., Haag M., Wai T., Aaltonen M.J.,
RA Langer T.;
RT "TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial
RT transport of phosphatidic acid.";
RL Cell Metab. 18:287-295(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-76 IN COMPLEX WITH PRELID3A,
RP NMR, INTERACTION WITH PRELID3A, SUBUNIT, DISULFIDE BOND, FUNCTION, AND
RP MUTAGENESIS OF PHE-27.
RX PubMed=26071602; DOI=10.15252/embr.201540229;
RA Miliara X., Garnett J.A., Tatsuta T., Abid Ali F., Baldie H.,
RA Perez-Dorado I., Simpson P., Yague E., Langer T., Matthews S.;
RT "Structural insight into the TRIAP1/PRELI-like domain family of
RT mitochondrial phospholipid transfer complexes.";
RL EMBO Rep. 16:824-835(2015).
CC -!- FUNCTION: Involved in the modulation of the mitochondrial apoptotic
CC pathway by ensuring the accumulation of cardiolipin (CL) in
CC mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates
CC the transfer of phosphatidic acid (PA) between liposomes and probably
CC functions as a PA transporter across the mitochondrion intermembrane
CC space to provide PA for CL synthesis in the inner membrane
CC (PubMed:23931759). Likewise, the TRIAP1:PRELID3A complex mediates the
CC transfer of phosphatidic acid (PA) between liposomes (in vitro) and
CC probably functions as a PA transporter across the mitochondrion
CC intermembrane space (in vivo) (PubMed:26071602). Mediates cell survival
CC by inhibiting activation of caspase-9 which prevents induction of
CC apoptosis (PubMed:15735003). {ECO:0000269|PubMed:15735003,
CC ECO:0000269|PubMed:23931759, ECO:0000269|PubMed:26071602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000269|PubMed:23931759};
CC -!- SUBUNIT: Monomer (PubMed:26071602). Interacts with APAF1 and HSP70
CC (PubMed:15735003). Forms a complex with PRELID1 in the mitochondrion
CC intermembrane space (PubMed:23931759). Interacts with PRELID3A
CC (PubMed:26071602). {ECO:0000269|PubMed:15735003,
CC ECO:0000269|PubMed:23931759, ECO:0000269|PubMed:26071602}.
CC -!- INTERACTION:
CC O43715; P80188: LCN2; NbExp=3; IntAct=EBI-2820212, EBI-11911016;
CC O43715; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-2820212, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15735003,
CC ECO:0000269|PubMed:23931759}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:23931759}.
CC -!- INDUCTION: In p53/TP53-dependent manner in response to low levels of
CC DNA damage. Not induced when DNA damage is severe.
CC {ECO:0000269|PubMed:15735003}.
CC -!- SIMILARITY: Belongs to the TRIAP1/MDM35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR00584.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRIAP1ID44577ch12q24.html";
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DR EMBL; AF161481; AAF29096.1; -; mRNA.
DR EMBL; AL021546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK312006; BAG34944.1; -; mRNA.
DR EMBL; CH471054; EAW98192.1; -; Genomic_DNA.
DR EMBL; BC002638; AAH02638.1; -; mRNA.
DR EMBL; BC055313; AAH55313.1; -; mRNA.
DR EMBL; U75688; AAR00584.1; ALT_INIT; mRNA.
DR CCDS; CCDS9198.1; -.
DR PIR; T09476; T09476.
DR RefSeq; NP_057483.1; NM_016399.2.
DR PDB; 4XZS; X-ray; 2.12 A; A/B=2-76.
DR PDB; 4XZV; X-ray; 3.58 A; A/C/E/G=2-76.
DR PDB; 6I3V; X-ray; 1.98 A; A/C=1-67.
DR PDB; 6I3Y; X-ray; 2.98 A; A/H=1-76.
DR PDB; 6I4Y; X-ray; 2.91 A; A=4-76.
DR PDBsum; 4XZS; -.
DR PDBsum; 4XZV; -.
DR PDBsum; 6I3V; -.
DR PDBsum; 6I3Y; -.
DR PDBsum; 6I4Y; -.
DR AlphaFoldDB; O43715; -.
DR SMR; O43715; -.
DR BioGRID; 119573; 48.
DR IntAct; O43715; 17.
DR MINT; O43715; -.
DR STRING; 9606.ENSP00000449795; -.
DR SwissLipids; SLP:000000338; -.
DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR iPTMnet; O43715; -.
DR PhosphoSitePlus; O43715; -.
DR BioMuta; TRIAP1; -.
DR EPD; O43715; -.
DR jPOST; O43715; -.
DR MassIVE; O43715; -.
DR MaxQB; O43715; -.
DR PaxDb; O43715; -.
DR PeptideAtlas; O43715; -.
DR PRIDE; O43715; -.
DR ProteomicsDB; 49131; -.
DR Antibodypedia; 53934; 48 antibodies from 17 providers.
DR DNASU; 51499; -.
DR Ensembl; ENST00000546954.2; ENSP00000449795.1; ENSG00000170855.4.
DR GeneID; 51499; -.
DR KEGG; hsa:51499; -.
DR MANE-Select; ENST00000546954.2; ENSP00000449795.1; NM_016399.3; NP_057483.1.
DR UCSC; uc001tyg.3; human.
DR CTD; 51499; -.
DR DisGeNET; 51499; -.
DR GeneCards; TRIAP1; -.
DR HGNC; HGNC:26937; TRIAP1.
DR HPA; ENSG00000170855; Low tissue specificity.
DR MIM; 614943; gene.
DR neXtProt; NX_O43715; -.
DR OpenTargets; ENSG00000170855; -.
DR PharmGKB; PA143485661; -.
DR VEuPathDB; HostDB:ENSG00000170855; -.
DR eggNOG; KOG3481; Eukaryota.
DR GeneTree; ENSGT00940000162087; -.
DR HOGENOM; CLU_101473_4_0_1; -.
DR InParanoid; O43715; -.
DR OMA; KQWYAYT; -.
DR OrthoDB; 1552088at2759; -.
DR PhylomeDB; O43715; -.
DR TreeFam; TF326640; -.
DR PathwayCommons; O43715; -.
DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR SignaLink; O43715; -.
DR BioGRID-ORCS; 51499; 703 hits in 1099 CRISPR screens.
DR ChiTaRS; TRIAP1; human.
DR GenomeRNAi; 51499; -.
DR Pharos; O43715; Tbio.
DR PRO; PR:O43715; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O43715; protein.
DR Bgee; ENSG00000170855; Expressed in tendon of biceps brachii and 211 other tissues.
DR Genevisible; O43715; HS.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; IDA:BHF-UCL.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:HGNC-UCL.
DR GO; GO:0120009; P:intermembrane lipid transfer; IEA:GOC.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0097035; P:regulation of membrane lipid distribution; IMP:UniProtKB.
DR DisProt; DP01835; -.
DR InterPro; IPR007918; MDM35_apoptosis.
DR PANTHER; PTHR46403; PTHR46403; 1.
DR Pfam; PF05254; UPF0203; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Coiled coil; Disulfide bond;
KW Lipid transport; Mitochondrion; Reference proteome; Transport.
FT CHAIN 1..76
FT /note="TP53-regulated inhibitor of apoptosis 1"
FT /id="PRO_0000220523"
FT DOMAIN 5..55
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COILED 1..52
FT /evidence="ECO:0000269|PubMed:26071602"
FT MOTIF 8..18
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 37..47
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT SITE 27
FT /note="Important for interaction with PRELID3A"
FT /evidence="ECO:0000269|PubMed:26071602"
FT SITE 41
FT /note="Important for interaction with PRELID3A"
FT /evidence="ECO:0000269|PubMed:26071602"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT DISULFID 8..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000269|PubMed:26071602, ECO:0007744|PDB:4XZS,
FT ECO:0007744|PDB:4XZV"
FT DISULFID 18..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000269|PubMed:26071602, ECO:0007744|PDB:4XZS,
FT ECO:0007744|PDB:4XZV"
FT MUTAGEN 27
FT /note="F->A: Impairs interaction with PRELID3A."
FT /evidence="ECO:0000269|PubMed:26071602"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:6I3V"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6I4Y"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:6I3V"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6I3V"
SQ SEQUENCE 76 AA; 8786 MW; 00B41AC399D76590 CRC64;
MNSVGEACTD MKREYDQCFN RWFAEKFLKG DSSGDPCTDL FKRYQQCVQK AIKEKEIPIE
GLEFMGHGKE KPENSS
