API5_HUMAN
ID API5_HUMAN Reviewed; 524 AA.
AC Q9BZZ5; B4DGR0; B4DRJ2; B4E283; D3DR21; G3V1C3; O15441; Q9Y4J7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Apoptosis inhibitor 5 {ECO:0000305};
DE Short=API-5;
DE AltName: Full=Antiapoptosis clone 11 protein;
DE Short=AAC-11;
DE AltName: Full=Cell migration-inducing gene 8 protein;
DE AltName: Full=Fibroblast growth factor 2-interacting factor;
DE Short=FIF;
DE AltName: Full=Protein XAGL;
GN Name=API5 {ECO:0000312|HGNC:HGNC:594}; ORFNames=MIG8;
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 4).
RX PubMed=9307294;
RA Tewari M., Yu M., Ross B., Dean C., Giordano A., Rubin R.;
RT "AAC-11, a novel cDNA that inhibits apoptosis after growth factor
RT withdrawal.";
RL Cancer Res. 57:4063-4069(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10393420; DOI=10.1159/000015247;
RA Gianfrancesco F., Esposito T., Ciccodicola A., D'Esposito M.,
RA Mazzarella R., D'Urso M., Forabosco A.;
RT "Molecular cloning and fine mapping of API5L1, a novel human gene strongly
RT related to an antiapoptotic gene.";
RL Cytogenet. Cell Genet. 84:164-166(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 72-524 (ISOFORM 1), IDENTIFICATION OF ISOFORM 3, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH FGF2.
RC TISSUE=Liver;
RX PubMed=11075807; DOI=10.1210/mend.14.11.0556;
RA Van den Berghe L., Laurell H., Huez I., Zanibellato C., Prats H.,
RA Bugler B.;
RT "FIF [fibroblast growth factor-2 (FGF-2)-interacting-factor], a nuclear
RT putatively antiapoptotic factor, interacts specifically with FGF-2.";
RL Mol. Endocrinol. 14:1709-1724(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kim J.W.;
RT "Identification of a human cell migration gene.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-276; VAL-300 AND
RP SER-493.
RG NIEHS SNPs program;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Brain, and Trachea;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph;
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 [11]
RP PROTEIN SEQUENCE OF 2-9; 26-36; 131-148; 161-169; 244-251 AND 427-436,
RP CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-524 (ISOFORM 3).
RX PubMed=8889549; DOI=10.1101/gr.6.9.807;
RA Hillier L.D., Lennon G., Becker M., Bonaldo M.F., Chiapelli B., Chissoe S.,
RA Dietrich N., DuBuque T., Favello A., Gish W., Hawkins M., Hultman M.,
RA Kucaba T., Lacy M., Le M., Le N., Mardis E., Moore B., Morris M.,
RA Parsons J., Prange C., Rifkin L., Rohlfing T., Schellenberg K.,
RA Bento Soares M., Tan F., Thierry-Meg J., Trevaskis E., Underwood K.,
RA Wohldman P., Waterston R., Wilson R., Marra M.;
RT "Generation and analysis of 280,000 human expressed sequence tags.";
RL Genome Res. 6:807-828(1996).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10780674; DOI=10.1038/labinvest.3780063;
RA Kim J.W., Cho H.S., Kim J.H., Hur S.Y., Kim T.E., Lee J.M., Kim I.K.,
RA Namkoong S.E.;
RT "AAC-11 overexpression induces invasion and protects cervical cancer cells
RT from apoptosis.";
RL Lab. Invest. 80:587-594(2000).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=11557113; DOI=10.1016/s0169-5002(01)00213-6;
RA Sasaki H., Moriyama S., Yukiue H., Kobayashi Y., Nakashima Y., Kaji M.,
RA Fukai I., Kiriyama M., Yamakawa Y., Fujii Y.;
RT "Expression of the antiapoptosis gene, AAC-11, as a prognosis marker in
RT non-small cell lung cancer.";
RL Lung Cancer 34:53-57(2001).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP FUNCTION.
RX PubMed=17112319; DOI=10.1371/journal.pgen.0020196;
RA Morris E.J., Michaud W.A., Ji J.Y., Moon N.S., Rocco J.W., Dyson N.J.;
RT "Functional identification of Api5 as a suppressor of E2F-dependent
RT apoptosis in vivo.";
RL PLoS Genet. 2:E196-E196(2006).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=17827341; DOI=10.1189/jlb.0607425;
RA Krejci P., Pejchalova K., Rosenbloom B.E., Rosenfelt F.P., Tran E.L.,
RA Laurell H., Wilcox W.R.;
RT "The antiapoptotic protein Api5 and its partner, high molecular weight
RT FGF2, are up-regulated in B cell chronic lymphoid leukemia.";
RL J. Leukoc. Biol. 82:1363-1364(2007).
RN [18]
RP FUNCTION, INTERACTION WITH ACIN1, AND TISSUE SPECIFICITY.
RX PubMed=19387494; DOI=10.1038/emboj.2009.106;
RA Rigou P., Piddubnyak V., Faye A., Rain J.-C., Michel L., Calvo F.,
RA Poyet J.-L.;
RT "The antiapoptotic protein AAC-11 interacts with and regulates Acinus-
RT mediated DNA fragmentation.";
RL EMBO J. 28:1576-1588(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462 AND SER-464, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP IDENTIFICATION BY MASS 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, AND IDENTIFICATION BY
RP MASS 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP 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 [25]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-500, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-498 OF WILD-TYPE AND MUTANT
RP GLN-251, NUCLEAR LOCALIZATION SIGNAL, ACETYLATION AT LYS-251, REPEATS, AND
RP SUBUNIT.
RX PubMed=22334682; DOI=10.1074/jbc.m111.317594;
RA Han B.G., Kim K.H., Lee S.J., Jeong K.C., Cho J.W., Noh K.H., Kim T.W.,
RA Kim S.J., Yoon H.J., Suh S.W., Lee S., Lee B.I.;
RT "Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein
RT interaction modules.";
RL J. Biol. Chem. 287:10727-10737(2012).
CC -!- FUNCTION: Antiapoptotic factor that may have a role in protein
CC assembly. Negatively regulates ACIN1. By binding to ACIN1, it
CC suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA
CC fragmentation. Also known to efficiently suppress E2F1-induced
CC apoptosis. Its depletion enhances the cytotoxic action of the
CC chemotherapeutic drugs. {ECO:0000269|PubMed:10780674,
CC ECO:0000269|PubMed:17112319, ECO:0000269|PubMed:19387494}.
CC -!- SUBUNIT: Monomer. Interacts with FGF2 and ACIN1.
CC {ECO:0000269|PubMed:11075807, ECO:0000269|PubMed:19387494,
CC ECO:0000269|PubMed:22334682}.
CC -!- INTERACTION:
CC Q9BZZ5; Q9UKV3-3: ACIN1; NbExp=2; IntAct=EBI-1048422, EBI-6976596;
CC Q9BZZ5-2; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-10989614, EBI-702390;
CC Q9BZZ5-2; A1A5D9: BICDL2; NbExp=3; IntAct=EBI-10989614, EBI-10171799;
CC Q9BZZ5-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-10989614, EBI-713665;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11075807}. Cytoplasm
CC {ECO:0000269|PubMed:11075807}. Note=Mainly nuclear. Can also be
CC cytoplasmic.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=4;
CC IsoId=Q9BZZ5-4; Sequence=Displayed;
CC Name=1; Synonyms=FIF-510;
CC IsoId=Q9BZZ5-1; Sequence=VSP_041969, VSP_041972;
CC Name=2; Synonyms=FIF-504;
CC IsoId=Q9BZZ5-2; Sequence=VSP_041970, VSP_041971;
CC Name=3; Synonyms=FIF C1;
CC IsoId=Q9BZZ5-3; Sequence=VSP_039761, VSP_039762;
CC Name=5;
CC IsoId=Q9BZZ5-5; Sequence=VSP_043289, VSP_041970, VSP_041971;
CC Name=6;
CC IsoId=Q9BZZ5-6; Sequence=VSP_057412;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including heart,
CC brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC Highest levels in heart, pancreas and placenta. Highly expressed in
CC several cancers. Preferentially expressed in squamous cell carcinoma
CC versus adenocarcinoma in non-small cell lung cancer.
CC {ECO:0000269|PubMed:10780674, ECO:0000269|PubMed:11075807,
CC ECO:0000269|PubMed:11557113, ECO:0000269|PubMed:17827341,
CC ECO:0000269|PubMed:19387494}.
CC -!- DOMAIN: Two regions, an N-terminal (aa 96-107) and a C-terminal (aa
CC 274-311) are required for binding FGF2.
CC -!- PTM: Acetylation at Lys-251 impairs antiapoptotic function.
CC {ECO:0000269|PubMed:22334682}.
CC -!- SIMILARITY: Belongs to the API5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB86528.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB86528.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/api5/";
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DR EMBL; U83857; AAB86528.1; ALT_SEQ; mRNA.
DR EMBL; Y15906; CAA75867.1; -; mRNA.
DR EMBL; AF229253; AAK00737.1; -; mRNA.
DR EMBL; AF229254; AAK00738.1; -; mRNA.
DR EMBL; AY311389; AAQ76714.1; -; mRNA.
DR EMBL; BT007093; AAP35756.1; -; mRNA.
DR EMBL; AY265973; AAO89077.1; -; Genomic_DNA.
DR EMBL; AK294724; BAG57871.1; -; mRNA.
DR EMBL; AK299288; BAG61304.1; -; mRNA.
DR EMBL; AK304157; BAG65045.1; -; mRNA.
DR EMBL; AC087276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68098.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68099.1; -; Genomic_DNA.
DR EMBL; BC017709; AAH17709.1; -; mRNA.
DR EMBL; W40304; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS31465.1; -. [Q9BZZ5-2]
DR CCDS; CCDS44572.1; -. [Q9BZZ5-4]
DR CCDS; CCDS44573.1; -. [Q9BZZ5-5]
DR RefSeq; NP_001136402.1; NM_001142930.1. [Q9BZZ5-4]
DR RefSeq; NP_001136403.1; NM_001142931.1. [Q9BZZ5-5]
DR RefSeq; NP_001230676.1; NM_001243747.1.
DR RefSeq; NP_006586.1; NM_006595.3. [Q9BZZ5-2]
DR PDB; 3U0R; X-ray; 2.50 A; A=1-498.
DR PDB; 3V6A; X-ray; 2.60 A; A=1-454.
DR PDB; 6L4O; X-ray; 2.60 A; A=1-524.
DR PDBsum; 3U0R; -.
DR PDBsum; 3V6A; -.
DR PDBsum; 6L4O; -.
DR AlphaFoldDB; Q9BZZ5; -.
DR SMR; Q9BZZ5; -.
DR BioGRID; 114109; 151.
DR CORUM; Q9BZZ5; -.
DR IntAct; Q9BZZ5; 34.
DR MINT; Q9BZZ5; -.
DR STRING; 9606.ENSP00000431391; -.
DR GlyGen; Q9BZZ5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BZZ5; -.
DR PhosphoSitePlus; Q9BZZ5; -.
DR SwissPalm; Q9BZZ5; -.
DR BioMuta; API5; -.
DR DMDM; 353526346; -.
DR EPD; Q9BZZ5; -.
DR jPOST; Q9BZZ5; -.
DR MassIVE; Q9BZZ5; -.
DR MaxQB; Q9BZZ5; -.
DR PaxDb; Q9BZZ5; -.
DR PeptideAtlas; Q9BZZ5; -.
DR PRIDE; Q9BZZ5; -.
DR ProteomicsDB; 79926; -. [Q9BZZ5-4]
DR ProteomicsDB; 79927; -. [Q9BZZ5-1]
DR ProteomicsDB; 79928; -. [Q9BZZ5-2]
DR ProteomicsDB; 79929; -. [Q9BZZ5-3]
DR ProteomicsDB; 79930; -. [Q9BZZ5-5]
DR Antibodypedia; 13145; 292 antibodies from 33 providers.
DR DNASU; 8539; -.
DR Ensembl; ENST00000378852.7; ENSP00000368129.3; ENSG00000166181.13. [Q9BZZ5-2]
DR Ensembl; ENST00000420461.6; ENSP00000402540.2; ENSG00000166181.13. [Q9BZZ5-5]
DR Ensembl; ENST00000455725.6; ENSP00000399341.2; ENSG00000166181.13. [Q9BZZ5-6]
DR Ensembl; ENST00000531273.6; ENSP00000431391.1; ENSG00000166181.13. [Q9BZZ5-4]
DR GeneID; 8539; -.
DR KEGG; hsa:8539; -.
DR MANE-Select; ENST00000531273.6; ENSP00000431391.1; NM_001142930.2; NP_001136402.1.
DR UCSC; uc001mxf.3; human. [Q9BZZ5-4]
DR UCSC; uc010rfg.2; human.
DR CTD; 8539; -.
DR DisGeNET; 8539; -.
DR GeneCards; API5; -.
DR HGNC; HGNC:594; API5.
DR HPA; ENSG00000166181; Low tissue specificity.
DR MIM; 609774; gene.
DR neXtProt; NX_Q9BZZ5; -.
DR OpenTargets; ENSG00000166181; -.
DR PharmGKB; PA24881; -.
DR VEuPathDB; HostDB:ENSG00000166181; -.
DR eggNOG; KOG2213; Eukaryota.
DR GeneTree; ENSGT00390000010991; -.
DR HOGENOM; CLU_037809_1_0_1; -.
DR InParanoid; Q9BZZ5; -.
DR OMA; FIQCATA; -.
DR OrthoDB; 1385954at2759; -.
DR PhylomeDB; Q9BZZ5; -.
DR TreeFam; TF324283; -.
DR PathwayCommons; Q9BZZ5; -.
DR SignaLink; Q9BZZ5; -.
DR BioGRID-ORCS; 8539; 64 hits in 1076 CRISPR screens.
DR ChiTaRS; API5; human.
DR GeneWiki; API5; -.
DR GenomeRNAi; 8539; -.
DR Pharos; Q9BZZ5; Tbio.
DR PRO; PR:Q9BZZ5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BZZ5; protein.
DR Bgee; ENSG00000166181; Expressed in islet of Langerhans and 216 other tissues.
DR ExpressionAtlas; Q9BZZ5; baseline and differential.
DR Genevisible; Q9BZZ5; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
DR DisProt; DP02894; -. [Q9BZZ5-2]
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR008383; API5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR PANTHER; PTHR12758; PTHR12758; 1.
DR Pfam; PF05918; API5; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.11"
FT CHAIN 2..524
FT /note="Apoptosis inhibitor 5"
FT /id="PRO_0000064634"
FT REGION 2..360
FT /note="ARM-like and Heat-like helical repeats"
FT REGION 370..391
FT /note="Leucine-zipper"
FT REGION 452..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 454..475
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22334682"
FT COMPBIAS 483..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22334682"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35841"
FT MOD_RES 500
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..23
FT /note="MPTVEELYRNYGILADATEQVGQ -> MKQRWRENGIGK (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057412"
FT VAR_SEQ 24..77
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043289"
FT VAR_SEQ 427..431
FT /note="DLFHI -> AKESQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8889549"
FT /id="VSP_039761"
FT VAR_SEQ 432..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8889549"
FT /id="VSP_039762"
FT VAR_SEQ 498..510
FT /note="EQRGAFRGSRGGR -> GERFRLGTRNMRD (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11075807"
FT /id="VSP_041969"
FT VAR_SEQ 499..504
FT /note="QRGAFR -> RSLQGK (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10393420,
FT ECO:0000303|PubMed:11075807, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5"
FT /id="VSP_041970"
FT VAR_SEQ 505..524
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10393420,
FT ECO:0000303|PubMed:11075807, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5"
FT /id="VSP_041971"
FT VAR_SEQ 511..524
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11075807"
FT /id="VSP_041972"
FT VARIANT 276
FT /note="P -> S"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021519"
FT VARIANT 300
FT /note="M -> V (in dbSNP:rs5743240)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021520"
FT VARIANT 493
FT /note="G -> S (in dbSNP:rs2862934)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021521"
FT CONFLICT 371..373
FT /note="KDF -> HES (in Ref. 1; AAB86528)"
FT /evidence="ECO:0000305"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6L4O"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3U0R"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6L4O"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 207..221
FT /evidence="ECO:0007829|PDB:3U0R"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:3U0R"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3V6A"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3U0R"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6L4O"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:3U0R"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3V6A"
FT HELIX 371..395
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3U0R"
FT HELIX 406..427
FT /evidence="ECO:0007829|PDB:3U0R"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6L4O"
SQ SEQUENCE 524 AA; 59005 MW; A2EA6BE4D8318BB9 CRC64;
MPTVEELYRN YGILADATEQ VGQHKDAYQV ILDGVKGGTK EKRLAAQFIP KFFKHFPELA
DSAINAQLDL CEDEDVSIRR QAIKELPQFA TGENLPRVAD ILTQLLQTDD SAEFNLVNNA
LLSIFKMDAK GTLGGLFSQI LQGEDIVRER AIKFLSTKLK TLPDEVLTKE VEELILTESK
KVLEDVTGEE FVLFMKILSG LKSLQTVSGR QQLVELVAEQ ADLEQTFNPS DPDCVDRLLQ
CTRQAVPLFS KNVHSTRFVT YFCEQVLPNL GTLTTPVEGL DIQLEVLKLL AEMSSFCGDM
EKLETNLRKL FDKLLEYMPL PPEEAENGEN AGNEEPKLQF SYVECLLYSF HQLGRKLPDF
LTAKLNAEKL KDFKIRLQYF ARGLQVYIRQ LRLALQGKTG EALKTEENKI KVVALKITNN
INVLIKDLFH IPPSYKSTVT LSWKPVQKVE IGQKRASEDT TSGSPPKKSS AGPKRDARQI
YNPPSGKYSS NLGNFNYEQR GAFRGSRGGR GWGTRGNRSR GRLY
