ID PDC6I_HUMAN Reviewed; 868 AA. AC Q8WUM4; C5MQH7; E9PFU1; Q6NUS1; Q9BX86; Q9NUN0; Q9P2H2; Q9UKL5; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 28-JAN-2026, entry version 218. DE RecName: Full=Programmed cell death 6-interacting protein {ECO:0000305}; DE Short=PDCD6-interacting protein; DE AltName: Full=ALG-2-interacting protein 1; DE AltName: Full=ALG-2-interacting protein X; DE AltName: Full=Hp95; GN Name=PDCD6IP {ECO:0000312|HGNC:HGNC:8766}; GN Synonyms=AIP1, ALIX, KIAA1375; 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 1), AND VARIANT SER-550. RX PubMed=11683497; DOI=10.1046/j.1432-0436.2001.670406.x; RA Wu Y., Pan S., Che S., He G., Nelman-Gonzalez M., Weil M.M., Kuang J.; RT "Overexpression of Hp95 induces G1 phase arrest in confluent HeLa cells."; RL Differentiation 67:139-153(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=19906316; DOI=10.1186/1471-2164-10-518; RA Wang P., Yu P., Gao P., Shi T., Ma D.; RT "Discovery of novel human transcript variants by analysis of intronic RT single-block EST with polyadenylation site."; RL BMC Genomics 10:518-518(2009). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-309 AND LEU-730. RA Li H., Shioda T., Isselbacher K.J.; RT "Molecular cloning of human ALG-2 interacting protein 1 (AIP1)."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP MET-7 AND ILE-378. RC TISSUE=Lymph, and Testis; 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 PROTEIN SEQUENCE OF 2-23; 111-120; 216-229; 439-446; 457-469 AND 542-553, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Osteosarcoma; RA Bienvenut W.V., Glen H., Frame M.C.; RL Submitted (MAR-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-868 (ISOFORM 1), AND VARIANT RP ILE-378. RC TISSUE=Placenta; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-868 (ISOFORM 1), AND VARIANT RP SER-550. RC TISSUE=Brain; 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 [10] RP INTERACTION WITH CHMP4A AND CHMP4B. RX PubMed=12860994; DOI=10.1074/jbc.m301604200; RA Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E., RA Yoshimori T., Maki M.; RT "The ALG-2-interacting protein Alix associates with CHMP4b, a human RT homologue of yeast Snf7 that is involved in multivesicular body sorting."; RL J. Biol. Chem. 278:39104-39113(2003). RN [11] RP FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), INTERACTION WITH CHMP4A; RP CHMP4B AND CHMP4C, AND INTERACTION WITH HIV-1 P6 AND EIAV P9 (MICROBIAL RP INFECTION). RX PubMed=14505569; DOI=10.1016/s0092-8674(03)00653-6; RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.; RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in RT virus budding."; RL Cell 114:689-699(2003). RN [12] RP FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), SELF-ASSOCIATION, RP INTERACTION WITH TSG101; CHMP4A; CHMP4B CHMP4C, AND SUBCELLULAR LOCATION. RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1; RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.; RT "The protein network of HIV budding."; RL Cell 114:701-713(2003). RN [13] RP SELF-ASSOCIATION, INTERACTION WITH TSG101; CHMP4A; CHMP4B AND CHMP4C, AND RP INTERACTION WITH EIAV P9 (MICROBIAL INFECTION). RX PubMed=14519844; DOI=10.1073/pnas.2133846100; RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; RT "Divergent retroviral late-budding domains recruit vacuolar protein sorting RT factors by using alternative adaptor proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003). RN [14] RP ERRATUM OF PUBMED:14519844. RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003). RN [15] RP INTERACTION WITH CHMP4A; CHMP4B AND CHMP4C. RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038; RA Katoh K., Shibata H., Hatta K., Maki M.; RT "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix RT among the three CHMP4 isoforms."; RL Arch. Biochem. Biophys. 421:159-165(2004). RN [16] RP INTERACTION WITH CHMP4A; CHMP4B AND CHMP4C. RX PubMed=14583093; DOI=10.1042/bj20031347; RA Peck J.W., Bowden E.T., Burbelo P.D.; RT "Structure and function of human Vps20 and Snf7 proteins."; RL Biochem. J. 377:693-700(2004). RN [17] RP FUNCTION IN ENDOSOME ORGANIZATION. RX PubMed=14739459; DOI=10.1126/science.1092425; RA Matsuo H., Chevallier J., Mayran N., Le Blanc I., Ferguson C., Faure J., RA Blanc N.S., Matile S., Dubochet J., Sadoul R., Parton R.G., Vilbois F., RA Gruenberg J.; RT "Role of LBPA and Alix in multivesicular liposome formation and endosome RT organization."; RL Science 303:531-534(2004). RN [18] RP INTERACTION WITH SGSM3, AND SUBCELLULAR LOCATION. RX PubMed=15849434; DOI=10.1271/bbb.69.861; RA Ichioka F., Horii M., Katoh K., Terasawa Y., Shibata H., Maki M.; RT "Identification of Rab GTPase-activating protein-like protein (RabGAPLP) as RT a novel Alix/AIP1-interacting protein."; RL Biosci. Biotechnol. Biochem. 69:861-865(2005). RN [19] RP INTERACTION WITH MURINE LEUKEMIA VIRUS GAG POLYPROTEIN. RX PubMed=15908698; DOI=10.1074/jbc.m413735200; RA Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., RA Basyuk E.; RT "Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with RT Nedd4 ubiquitin ligases during budding."; RL J. Biol. Chem. 280:27004-27012(2005). RN [20] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PDCD6. RX PubMed=16957052; DOI=10.1091/mbc.e06-05-0444; RA Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.; RT "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit RT sites by Sec31A and stabilizes the localization of Sec31A."; RL Mol. Biol. Cell 17:4876-4887(2006). RN [22] RP FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55 AND RP CD2AP, AND MUTAGENESIS OF ILE-212; PHE-676 AND 800-GLY--PRO-802. RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850; RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., RA Sundquist W.I.; RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and RT function in cytokinesis."; RL EMBO J. 26:4215-4227(2007). RN [23] RP FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), INTERACTION WITH CHMP4B, RP AND MUTAGENESIS OF PHE-199; LEU-216; PHE-317; ILE-318 AND TYR-319. RX PubMed=17428861; DOI=10.1128/jvi.00314-07; RA Usami Y., Popov S., Goettlinger H.G.; RT "Potent rescue of human immunodeficiency virus type 1 late domain mutants RT by ALIX/AIP1 depends on its CHMP4 binding site."; RL J. Virol. 81:6614-6622(2007). RN [24] RP FUNCTION IN CYTOKINESIS AND HIV1 RELEASE, SUBCELLULAR LOCATION, AND RP INTERACTION WITH CEP55. RX PubMed=17556548; DOI=10.1126/science.1143422; RA Carlton J.G., Martin-Serrano J.; RT "Parallels between cytokinesis and retroviral budding: a role for the ESCRT RT machinery."; RL Science 316:1908-1912(2007). RN [25] RP INTERACTION WITH PDCD6. RX PubMed=18256029; DOI=10.1074/jbc.m800717200; RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., RA Maki M.; RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human RT phospholipid scramblase 3: differential binding to an alternatively spliced RT isoform and amino acid-substituted mutants."; RL J. Biol. Chem. 283:9623-9632(2008). RN [26] RP FUNCTION IN CYTOKINESIS AND HIV1 RELEASE, INTERACTION WITH CEP55 AND RP TSG101, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-199; ILE-212; PHE-676; RP 717-PRO--PRO-720; 744-PRO-ARG-745; 757-ARG--PRO-759; 794-PRO--CYS-813; RP 801-PRO-PRO-802; 803-TYR-PRO-804; 805-THR-TYR-806; 852-PRO--PRO-855 AND RP 864-TYR-TYR-865. RX PubMed=18641129; DOI=10.1073/pnas.0802008105; RA Carlton J.G., Agromayor M., Martin-Serrano J.; RT "Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 RT release."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10541-10546(2008). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730; THR-738 AND THR-741, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [29] RP INTERACTION WITH TSG101. RX PubMed=19520058; DOI=10.1016/j.bbrc.2009.06.015; RA Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H., Shibata H., RA Maki M.; RT "Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that RT bridges Alix and TSG101."; RL Biochem. Biophys. Res. Commun. 386:237-241(2009). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [31] RP PHOSPHORYLATION, AND INTERACTION WITH PDGFRB. RX PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004; RA Wardega P., Heldin C.H., Lennartsson J.; RT "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell RT proliferation but not migration."; RL Cell. Signal. 22:1363-1368(2010). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-738 AND THR-741, AND RP 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 [33] 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 [34] RP INTERACTION WITH ARRDC1. RX PubMed=21191027; DOI=10.1128/jvi.02045-10; RA Rauch S., Martin-Serrano J.; RT "Multiple interactions between the ESCRT machinery and arrestin-related RT proteins: implications for PPXY-dependent budding."; RL J. Virol. 85:3546-3556(2011). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [36] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SDCBP AND SDC2, AND RP MUTAGENESIS OF PHE-676. RX PubMed=22660413; DOI=10.1038/ncb2502; RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A., RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P., RA David G.; RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes."; RL Nat. Cell Biol. 14:677-685(2012). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479 AND SER-481, AND RP IDENTIFICATION BY 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 [38] 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 [39] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-745, 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 [40] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [41] RP INTERACTION WITH EBOLA VIRUS PROTEIN VP40 (MICROBIAL INFECTION). RX PubMed=25786915; DOI=10.1093/infdis/jiu838; RA Han Z., Madara J.J., Liu Y., Liu W., Ruthel G., Freedman B.D., Harty R.N.; RT "ALIX Rescues Budding of a Double PTAP/PPEY L-Domain Deletion Mutant of RT Ebola VP40: A Role for ALIX in Ebola Virus Egress."; RL J. Infect. Dis. 212:S138-S145(2015). RN [42] RP INTERACTION WITH ATG3. RX PubMed=25686249; DOI=10.1038/ncb3112; RA Murrow L., Malhotra R., Debnath J.; RT "ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late RT endosome function."; RL Nat. Cell Biol. 17:300-310(2015). RN [43] RP INVOLVEMENT IN MCPH29. RX PubMed=32286682; DOI=10.1111/cge.13756; RA Khan A., Alaamery M., Massadeh S., Obaid A., Kashgari A.A., Walsh C.A., RA Eyaid W.; RT "PDCD6IP, encoding a regulator of the ESCRT complex, is mutated in RT microcephaly."; RL Clin. Genet. 98:80-85(2020). RN [44] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 1-698, INTERACTION WITH CHMP4A; RP HIV-1 P6; EIAV P9; TSG101; SH3GL1 AND SH3GL2, AND MUTAGENESIS OF ILE-212; RP TYR-319; PHE-495; VAL-498; VAL-509; PHE-676; LEU-680; ILE-683; PRO-720 AND RP 757-ARG-PRO-758. RX PubMed=17350572; DOI=10.1016/j.cell.2007.01.035; RA Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., Hill C.P.; RT "Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus RT budding."; RL Cell 128:841-852(2007). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 360-702, INTERACTION WITH HIV-1 RP P6, AND MUTAGENESIS OF VAL-498; VAL-509; CYS-512; PHE-676 AND ILE-683. RX PubMed=17277784; DOI=10.1038/nsmb1203; RA Lee S., Joshi A., Nagashima K., Freed E.O., Hurley J.H.; RT "Structural basis for viral late-domain binding to Alix."; RL Nat. Struct. Mol. Biol. 14:194-199(2007). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 2-698 IN COMPLEX WITH HIV-1 P6, RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 2-698 IN COMPLEX WITH HIV-1 P9, RP AND INTERACTION WITH EIAV P9. RX PubMed=18066081; DOI=10.1038/nsmb1319; RA Zhai Q., Fisher R.D., Chung H.Y., Myszka D.G., Sundquist W.I., Hill C.P.; RT "Structural and functional studies of ALIX interactions with YPX(n)L late RT domains of HIV-1 and EIAV."; RL Nat. Struct. Mol. Biol. 15:43-49(2008). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-359 IN COMPLEX WITH CHMP4A, RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-359 IN COMPLEX WITH CHMP4B, AND RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 1-359 IN COMPLEX WITH CHMP4C. RX PubMed=18511562; DOI=10.1073/pnas.0801567105; RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.; RT "ALIX-CHMP4 interactions in the human ESCRT pathway."; RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008). RN [48] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 797-809 IN COMPLEX WITH CEP55, RP AND MUTAGENESIS OF PRO-801; PRO-802 AND TYR-806. RX PubMed=18948538; DOI=10.1126/science.1162042; RA Lee H.H., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J.H.; RT "Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in RT CEP55."; RL Science 322:576-580(2008). RN [49] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 799-812 IN COMPLEX WITH PDCD6. RX PubMed=18940611; DOI=10.1016/j.str.2008.07.012; RA Suzuki H., Kawasaki M., Inuzuka T., Okumura M., Kakiuchi T., Shibata H., RA Wakatsuki S., Maki M.; RT "Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide RT complex: Ca2+/EF3-driven arginine switch mechanism."; RL Structure 16:1562-1573(2008). RN [50] RP VARIANT SER-429. RX PubMed=22073189; DOI=10.1371/journal.pone.0026741; RA Benitez B.A., Alvarado D., Cai Y., Mayo K., Chakraverty S., Norton J., RA Morris J.C., Sands M.S., Goate A., Cruchaga C.; RT "Exome-sequencing confirms DNAJC5 mutations as cause of adult neuronal RT ceroid-lipofuscinosis."; RL PLoS ONE 6:E26741-E26741(2011). CC -!- FUNCTION: Multifunctional protein involved in endocytosis, CC multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis CC and maintenance of tight junction integrity. Class E VPS protein CC involved in concentration and sorting of cargo proteins of the CC multivesicular body (MVB) for incorporation into intralumenal vesicles CC (ILVs) that are generated by invagination and scission from the CC limiting membrane of the endosome. Binds to the phospholipid CC lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal CC membranes. The MVB pathway requires the sequential function of ESCRT-O, CC -I,-II and -III complexes (PubMed:14739459). The ESCRT machinery also CC functions in topologically equivalent membrane fission events, such as CC the terminal stages of cytokinesis (PubMed:17556548, PubMed:17853893). CC Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function CC at distinct membranes. Required for completion of cytokinesis CC (PubMed:17556548, PubMed:17853893, PubMed:18641129). May play a role in CC the regulation of both apoptosis and cell proliferation. Regulates CC exosome biogenesis in concert with SDC1/4 and SDCBP (PubMed:22660413). CC By interacting with F-actin, PARD3 and TJP1 secures the proper assembly CC and positioning of actomyosin-tight junction complex at the apical CC sides of adjacent epithelial cells that defines a spatial membrane CC domain essential for the maintenance of epithelial cell polarity and CC barrier (By similarity). {ECO:0000250|UniProtKB:Q9WU78, CC ECO:0000269|PubMed:14739459, ECO:0000269|PubMed:17556548, CC ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129, CC ECO:0000269|PubMed:22660413}. CC -!- FUNCTION: (Microbial infection) Involved in HIV-1 virus budding. Can CC replace TSG101 it its role of supporting HIV-1 release; this function CC requires the interaction with CHMP4B. The ESCRT machinery also CC functions in topologically equivalent membrane fission events, such as CC enveloped virus budding (HIV-1 and other lentiviruses). CC {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:17556548, CC ECO:0000269|PubMed:18641129}. CC -!- SUBUNIT: Self-associates (PubMed:14505570, PubMed:14519844). Interacts CC with SH3KBP1/CIN85 (By similarity). Interacts with PDCD6 in a calcium CC -dependent manner (PubMed:16957052, PubMed:18256029, PubMed:18940611). CC Interacts with TSG101 in a calcium-dependent manner; PDCD6IP CC homooligomerization may be required for TSG101-binding CC (PubMed:14505570, PubMed:14519844, PubMed:17350572, PubMed:18641129, CC PubMed:19520058). Interacts with SGSM3 (PubMed:15849434). Directly CC interacts with CHMP4A, CHMP4B and CHMP4C (PubMed:12860994, CC PubMed:14505569, PubMed:14505570, PubMed:14519844, PubMed:14583093, CC PubMed:14678797, PubMed:17350572, PubMed:17428861, PubMed:18511562). CC Directly interacts with CEP55 in a 1:2 stoechiometry (PubMed:17556548, CC PubMed:17853893, PubMed:18641129, PubMed:18948538). The interaction CC with CEP55 is required for PDCD6IP targeting to the midbody CC (PubMed:18641129). May interact with PDGFRB (PubMed:20494825). CC Interacts with SH3GL1 and SH3GL2/endophilin-1 (PubMed:17350572). Forms CC a complex with SDCBP and SDC2 (PubMed:22660413). Found in a complex CC with F-actin, TJP1/ZO-1 and PARD3 (By similarity). Interacts with CD2AP CC (PubMed:17853893). Interacts with ARRDC1 (PubMed:21191027). Interacts CC (via BRO1 domain) with the ATG12-ATG3 conjugate; this interaction is CC bridged by ATG12 and promotes multiple PDCD6IP-mediated functions such CC as endolysosomal trafficking, macroautophagy and exosome biogenesis CC (PubMed:25686249). {ECO:0000250|UniProtKB:Q9QZA2, CC ECO:0000250|UniProtKB:Q9WU78, ECO:0000269|PubMed:12860994, CC ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093, CC ECO:0000269|PubMed:14678797, ECO:0000269|PubMed:15849434, CC ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:17350572, CC ECO:0000269|PubMed:17428861, ECO:0000269|PubMed:17556548, CC ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18256029, CC ECO:0000269|PubMed:18511562, ECO:0000269|PubMed:18641129, CC ECO:0000269|PubMed:18940611, ECO:0000269|PubMed:18948538, CC ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:20494825, CC ECO:0000269|PubMed:21191027, ECO:0000269|PubMed:22660413, CC ECO:0000269|PubMed:25686249}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 p6 CC (PubMed:14505569, PubMed:17277784, PubMed:17350572, PubMed:18066081). CC Interacts with HIV-1 p9 (PubMed:18066081). CC {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14519844, CC ECO:0000269|PubMed:17277784, ECO:0000269|PubMed:17350572, CC ECO:0000269|PubMed:18066081}. CC -!- SUBUNIT: (Microbial infection) Interacts with EIAV p9. CC {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14519844, CC ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:18066081}. CC -!- SUBUNIT: (Microbial infection) Interacts with Murine leukemia virus Gag CC polyprotein (via LYPX(n)L motif). {ECO:0000269|PubMed:15908698}. CC -!- SUBUNIT: (Microbial infection) Interacts with ebola virus protein VP40 CC (via YPx(n)L/I motif). {ECO:0000269|PubMed:15908698}. CC -!- INTERACTION: CC Q8WUM4; Q9Y5K6: CD2AP; NbExp=3; IntAct=EBI-310624, EBI-298152; CC Q8WUM4; Q53EZ4: CEP55; NbExp=22; IntAct=EBI-310624, EBI-747776; CC Q8WUM4; Q9BY43: CHMP4A; NbExp=3; IntAct=EBI-310624, EBI-747981; CC Q8WUM4; Q9H444: CHMP4B; NbExp=6; IntAct=EBI-310624, EBI-749627; CC Q8WUM4; Q96CF2: CHMP4C; NbExp=3; IntAct=EBI-310624, EBI-1221015; CC Q8WUM4; P00533: EGFR; NbExp=4; IntAct=EBI-310624, EBI-297353; CC Q8WUM4; P06241: FYN; NbExp=6; IntAct=EBI-310624, EBI-515315; CC Q8WUM4; P08631: HCK; NbExp=4; IntAct=EBI-310624, EBI-346340; CC Q8WUM4; P17931: LGALS3; NbExp=2; IntAct=EBI-310624, EBI-1170392; CC Q8WUM4; O75340: PDCD6; NbExp=13; IntAct=EBI-310624, EBI-352915; CC Q8WUM4; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-310624, EBI-346595; CC Q8WUM4; P12931: SRC; NbExp=7; IntAct=EBI-310624, EBI-621482; CC Q8WUM4; Q99816: TSG101; NbExp=2; IntAct=EBI-310624, EBI-346882; CC Q8WUM4; Q9D8B3: Chmp4b; Xeno; NbExp=2; IntAct=EBI-310624, EBI-8322817; CC Q8WUM4; O91079: gag; Xeno; NbExp=7; IntAct=EBI-310624, EBI-40204927; CC Q8WUM4; P03347: gag; Xeno; NbExp=2; IntAct=EBI-310624, EBI-1220741; CC Q8WUM4; P69730: gag; Xeno; NbExp=2; IntAct=EBI-310624, EBI-1220941; CC Q8WUM4; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-310624, EBI-3957603; CC Q8WUM4; Q90VU7: nef; Xeno; NbExp=4; IntAct=EBI-310624, EBI-7460704; CC Q8WUM4; PRO_0000308465 [P29991]; Xeno; NbExp=3; IntAct=EBI-310624, EBI-8826747; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9QZA2}. Melanosome CC {ECO:0000269|PubMed:17081065}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:17556548, CC ECO:0000269|PubMed:17853893}. Secreted, extracellular exosome CC {ECO:0000269|PubMed:22660413}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:Q9WU78}. Midbody, Midbody ring CC {ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV. Colocalized with CEP55 at centrosomes of non-dividing CC cells. Component of the actomyosin-tight junction complex (By CC similarity). PDCD6IP targeting to the midbody requires the interaction CC with CEP55 (PubMed:18641129). {ECO:0000250|UniProtKB:Q9QZA2, CC ECO:0000250|UniProtKB:Q9WU78, ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, CC ECO:0000269|PubMed:18641129}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8WUM4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WUM4-2; Sequence=VSP_044860; CC Name=3; CC IsoId=Q8WUM4-3; Sequence=VSP_057190, VSP_057191; CC -!- PTM: May be phosphorylated on tyrosine residues by activated PDGFRB. CC {ECO:0000269|PubMed:20494825}. CC -!- DISEASE: Microcephaly 29, primary, autosomal recessive (MCPH29) CC [MIM:620047]: A form of microcephaly, a disease defined as a head CC circumference more than 3 standard deviations below the age, sex and CC ethnically matched mean. Brain weight is markedly reduced and the CC cerebral cortex is disproportionately small. MCPH29 is characterized by CC small head circumference apparent at birth and associated with global CC developmental delay, impaired intellectual development, speech delay, CC and behavioral abnormalities. Affected individuals also have poor CC overall growth with short stature, mild dysmorphic facial features, and CC seizures. {ECO:0000269|PubMed:32286682}. Note=The disease may be caused CC by variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA92092.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF349951; AAK20398.1; -; mRNA. DR EMBL; GQ131806; ACS12984.1; -; mRNA. DR EMBL; AF151793; AAF08220.1; -; mRNA. DR EMBL; BT007367; AAP36031.1; -; mRNA. DR EMBL; AC112220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC123901; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020066; AAH20066.1; -; mRNA. DR EMBL; BC068454; AAH68454.1; -; mRNA. DR EMBL; AK002122; BAA92092.1; ALT_INIT; mRNA. DR EMBL; AB037796; BAA92613.1; -; mRNA. DR CCDS; CCDS2660.1; -. [Q8WUM4-1] DR CCDS; CCDS54561.1; -. [Q8WUM4-2] DR RefSeq; NP_001155901.1; NM_001162429.3. [Q8WUM4-2] DR RefSeq; NP_001243121.1; NM_001256192.2. [Q8WUM4-3] DR RefSeq; NP_037506.2; NM_013374.5. [Q8WUM4-1] DR PDB; 2OEV; X-ray; 3.30 A; A=1-698. DR PDB; 2OEW; X-ray; 2.55 A; A=1-359. DR PDB; 2OEX; X-ray; 2.58 A; A/B=360-702. DR PDB; 2OJQ; X-ray; 2.87 A; A=360-702. DR PDB; 2R02; X-ray; 2.60 A; A=2-698. DR PDB; 2R03; X-ray; 2.59 A; A=2-698. DR PDB; 2R05; X-ray; 2.55 A; A=2-698. DR PDB; 2XS1; X-ray; 2.30 A; A=1-698. DR PDB; 2XS8; X-ray; 2.50 A; A=1-698. DR PDB; 2ZNE; X-ray; 2.20 A; C/D=799-812. DR PDB; 3C3O; X-ray; 2.15 A; A=1-359. DR PDB; 3C3Q; X-ray; 2.10 A; A=1-359. DR PDB; 3C3R; X-ray; 2.02 A; A=1-359. DR PDB; 3E1R; X-ray; 2.00 A; C=797-809. DR PDB; 3WUV; X-ray; 2.79 A; C/F/I/L/O/R=796-810. DR PDB; 4JJY; X-ray; 6.50 A; A/B=355-708. DR PDB; 5V3R; X-ray; 1.91 A; A=1-359. DR PDB; 5WA1; X-ray; 1.87 A; A=1-358. DR PDB; 6KP3; X-ray; 2.20 A; A=1-359. DR PDBsum; 2OEV; -. DR PDBsum; 2OEW; -. DR PDBsum; 2OEX; -. DR PDBsum; 2OJQ; -. DR PDBsum; 2R02; -. DR PDBsum; 2R03; -. DR PDBsum; 2R05; -. DR PDBsum; 2XS1; -. DR PDBsum; 2XS8; -. DR PDBsum; 2ZNE; -. DR PDBsum; 3C3O; -. DR PDBsum; 3C3Q; -. DR PDBsum; 3C3R; -. DR PDBsum; 3E1R; -. DR PDBsum; 3WUV; -. DR PDBsum; 4JJY; -. DR PDBsum; 5V3R; -. DR PDBsum; 5WA1; -. DR PDBsum; 6KP3; -. DR AlphaFoldDB; Q8WUM4; -. DR SMR; Q8WUM4; -. DR BioGRID; 115332; 266. DR ComplexPortal; CPX-3282; Syndecan-1-syntenin-1-ALIX complex. DR CORUM; Q8WUM4; -. DR DIP; DIP-29327N; -. DR FunCoup; Q8WUM4; 3071. DR IntAct; Q8WUM4; 150. DR MINT; Q8WUM4; -. DR STRING; 9606.ENSP00000411825; -. DR MoonDB; Q8WUM4; Predicted. DR GlyGen; Q8WUM4; 13 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (10 sites). DR iPTMnet; Q8WUM4; -. DR MetOSite; Q8WUM4; -. DR PhosphoSitePlus; Q8WUM4; -. DR SwissPalm; Q8WUM4; -. DR BioMuta; PDCD6IP; -. DR DMDM; 31076831; -. DR CPTAC; CPTAC-419; -. DR CPTAC; CPTAC-420; -. DR jPOST; Q8WUM4; -. DR MassIVE; Q8WUM4; -. DR PaxDb; 9606-ENSP00000411825; -. DR PeptideAtlas; Q8WUM4; -. DR PRIDE; Q8WUM4; -. DR ProteomicsDB; 20178; -. DR ProteomicsDB; 74695; -. [Q8WUM4-1] DR Pumba; Q8WUM4; -. DR Antibodypedia; 2777; 402 antibodies from 39 providers. DR DNASU; 10015; -. DR Ensembl; ENST00000307296.8; ENSP00000307387.3; ENSG00000170248.16. [Q8WUM4-1] DR Ensembl; ENST00000457054.6; ENSP00000411825.2; ENSG00000170248.16. [Q8WUM4-2] DR GeneID; 10015; -. DR KEGG; hsa:10015; -. DR MANE-Select; ENST00000307296.8; ENSP00000307387.3; NM_013374.6; NP_037506.2. DR UCSC; uc003cfx.5; human. [Q8WUM4-1] DR AGR; HGNC:8766; -. DR ClinPGx; PA33116; -. DR CTD; 10015; -. DR DisGeNET; 10015; -. DR GeneCards; PDCD6IP; -. DR HGNC; HGNC:8766; PDCD6IP. DR HPA; ENSG00000170248; Low tissue specificity. DR MalaCards; PDCD6IP; -. DR MIM; 608074; gene. DR MIM; 620047; phenotype. DR OpenTargets; ENSG00000170248; -. DR Orphanet; 2512; Autosomal recessive primary microcephaly. DR VEuPathDB; HostDB:ENSG00000170248; -. DR eggNOG; KOG2220; Eukaryota. DR GeneTree; ENSGT01130000278400; -. DR HOGENOM; CLU_007181_2_0_1; -. DR InParanoid; Q8WUM4; -. DR OMA; VSHAEEM; -. DR OrthoDB; 2141925at2759; -. DR PAN-GO; Q8WUM4; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q8WUM4; -. DR PathwayCommons; Q8WUM4; -. DR Reactome; R-HSA-162588; Budding and maturation of HIV virion. DR Reactome; R-HSA-5210891; Uptake and function of anthrax toxins. DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis. DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death. DR SignaLink; Q8WUM4; -. DR SIGNOR; Q8WUM4; -. DR Agora; ENSG00000170248; -. DR BioGRID-ORCS; 10015; 237 hits in 1158 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 8C2F96ED; Centrosome. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; PDCD6IP; human. DR EvolutionaryTrace; Q8WUM4; -. DR GeneWiki; PDCD6IP; -. DR GenomeRNAi; 10015; -. DR Pharos; Q8WUM4; Tbio. DR PRO; PR:Q8WUM4; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8WUM4; protein. DR Bgee; ENSG00000170248; Expressed in calcaneal tendon and 211 other cell types or tissues. DR ExpressionAtlas; Q8WUM4; baseline and differential. DR GO; GO:0042641; C:actomyosin; ISS:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IMP:UniProtKB. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0031871; F:proteinase activated receptor binding; IPI:UniProtKB. DR GO; GO:0000915; P:actomyosin contractile ring assembly; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB. DR GO; GO:0097734; P:extracellular exosome biogenesis; ISS:UniProtKB. DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB. DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB. DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB. DR GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL. DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB. DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IMP:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB. DR GO; GO:1903551; P:regulation of extracellular exosome assembly; IMP:UniProtKB. DR GO; GO:0090559; P:regulation of membrane permeability; ISS:UniProtKB. DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB. DR GO; GO:0046755; P:viral budding; IDA:UniProtKB. DR GO; GO:0039702; P:viral budding via host ESCRT complex; IGI:UniProtKB. DR CDD; cd09240; BRO1_Alix; 1. DR CDD; cd09235; V_Alix; 1. DR FunFam; 1.25.40.280:FF:000001; programmed cell death 6-interacting protein-like isoform X1; 1. DR FunFam; 1.20.140.50:FF:000001; programmed cell death 6-interacting protein-like isoform X2; 1. DR Gene3D; 1.20.120.560; alix/aip1 in complex with the ypdl late domain; 1. DR Gene3D; 1.20.140.50; alix/aip1 like domains; 1. DR Gene3D; 1.25.40.280; alix/aip1 like domains; 1. DR InterPro; IPR025304; ALIX_V_dom. DR InterPro; IPR004328; BRO1_dom. DR InterPro; IPR038499; BRO1_sf. DR PANTHER; PTHR23030; PCD6 INTERACTING PROTEIN-RELATED; 1. DR PANTHER; PTHR23030:SF39; PROGRAMMED CELL DEATH 6-INTERACTING PROTEIN; 1. DR Pfam; PF13949; ALIX_LYPXL_bnd; 1. DR Pfam; PF03097; BRO1; 1. DR SMART; SM01041; BRO1; 1. DR PROSITE; PS51180; BRO1; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle; KW Cell division; Cell junction; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Host-virus interaction; Intellectual disability; KW Methylation; Phosphoprotein; Primary microcephaly; Protein transport; KW Proteomics identification; Reference proteome; Secreted; Tight junction; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT CHAIN 2..868 FT /note="Programmed cell death 6-interacting protein" FT /id="PRO_0000218891" FT DOMAIN 3..392 FT /note="BRO1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526" FT REGION 176..868 FT /note="Interaction with EIAV p9" FT REGION 176..503 FT /note="Interaction with CHMP4A, CHMP4B and CHMP4C" FT REGION 418..868 FT /note="Interaction with SDCBP" FT /evidence="ECO:0000269|PubMed:22660413" FT REGION 503..868 FT /note="Self-association" FT REGION 713..809 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 717..720 FT /note="Interaction with TSG101" FT REGION 801..806 FT /note="Interaction with CEP55" FT /evidence="ECO:0000269|PubMed:18641129" FT REGION 832..868 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 864..868 FT /note="Essential to promote virus budding" FT COMPBIAS 737..763 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..791 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 792..807 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..860 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT MOD_RES 215 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 479 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 481 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 730 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 738 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 741 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 745 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 239 FT /note="K -> KYFYFQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044860" FT VAR_SEQ 240..271 FT /note="EVFPVLAAKHCIMQANAEYHQSILAKQQKKFG -> VSYCFYKHLLTLHVKY FT LDFFVYKKQVETYKEI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:19906316" FT /id="VSP_057190" FT VAR_SEQ 272..868 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:19906316" FT /id="VSP_057191" FT VARIANT 7 FT /note="V -> M (in dbSNP:rs11554560)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068975" FT VARIANT 309 FT /note="A -> T (in dbSNP:rs3792594)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_053017" FT VARIANT 378 FT /note="V -> I (in dbSNP:rs3203777)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_053018" FT VARIANT 429 FT /note="G -> S (in dbSNP:rs76608858)" FT /evidence="ECO:0000269|PubMed:22073189" FT /id="VAR_069765" FT VARIANT 550 FT /note="N -> S (in dbSNP:rs9813017)" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:11683497" FT /id="VAR_053019" FT VARIANT 638 FT /note="K -> E (in dbSNP:rs3183982)" FT /id="VAR_053020" FT VARIANT 730 FT /note="S -> L (in dbSNP:rs1127732)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_024381" FT MUTAGEN 199 FT /note="F->D: Does not support cytokinesis; loss of normal FT midbody formation; loss of CHMP4A-, CHMP4B- and FT CHMP4C-binding in a yeast two-hybrid assay; no effect on FT localization to the midbody; abolishes rescue of PTAP-type FT L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17428861, FT ECO:0000269|PubMed:18641129" FT MUTAGEN 212 FT /note="I->D: Does not support cytokinesis; loss of normal FT midbody formation; loss of CHMP4A-, CHMP4B- and FT CHMP4C-binding in a yeast two-hybrid assay; impairs rescue FT of PTAP-type L domain-deficient HIV-1 p6; no effect on FT localization to the midbody." FT /evidence="ECO:0000269|PubMed:17350572, FT ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129" FT MUTAGEN 216 FT /note="L->D: Abolishes interaction with CHMP4B and FT abolishes rescue of PTAP-type L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17428861" FT MUTAGEN 317 FT /note="F->A: Diminishes rescue of PTAP-type L FT domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17428861" FT MUTAGEN 318 FT /note="I->A: Greatly diminishes rescue of PTAP-type L FT domain--deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17428861" FT MUTAGEN 319 FT /note="Y->A: Greatly diminishes rescue of PTAP-type L FT domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17350572, FT ECO:0000269|PubMed:17428861" FT MUTAGEN 319 FT /note="Y->F: No effect on rescue of PTAP-type L FT domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17350572, FT ECO:0000269|PubMed:17428861" FT MUTAGEN 495 FT /note="F->D: Impairs rescue of PTAP-type L domain-deficient FT HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17350572" FT MUTAGEN 498 FT /note="V->D: Reduces interaction with HIV-1 p6 and EIAV p9; FT abolishes rescue of PTAP-type L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17277784, FT ECO:0000269|PubMed:17350572" FT MUTAGEN 509 FT /note="V->D: Abolishes interaction with HIV-1 p6; impairs FT rescue of PTAP-type L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17277784, FT ECO:0000269|PubMed:17350572" FT MUTAGEN 512 FT /note="C->A: No effect on interaction with HIV-1 p6; FT impairs rescue of PTAP-type L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17277784" FT MUTAGEN 676 FT /note="F->A: Loss of interaction with SDCBP." FT /evidence="ECO:0000269|PubMed:22660413" FT MUTAGEN 676 FT /note="F->D: Abolishes interaction with HIV-1 p6 and EIAV FT p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 FT p6; no effect on cytokinesis, nor on midbody formation." FT /evidence="ECO:0000269|PubMed:17277784, FT ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:17853893, FT ECO:0000269|PubMed:18641129" FT MUTAGEN 680 FT /note="L->D: Impairs rescue of PTAP-type L domain-deficient FT HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17350572" FT MUTAGEN 683 FT /note="I->A: No effect on interaction with HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17277784, FT ECO:0000269|PubMed:17350572" FT MUTAGEN 683 FT /note="I->D: Reduces interaction with HIV-1 p6 and EIAV p9; FT abolishes rescue of PTAP-type L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17277784, FT ECO:0000269|PubMed:17350572" FT MUTAGEN 717..720 FT /note="PSAP->AAAA: No effect on midbody formation, nor on FT cytokinesis; reduced TSG101-binding; no effect on HIV-1 FT release. Almost complete loss of TSG101-binding and FT impaired cytokinesis; when associated with 852-A--A-855." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 720 FT /note="P->L: Abolishes interaction with TSG101; no effect FT on rescue of PTAP-type L domain-deficient HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17350572" FT MUTAGEN 744..745 FT /note="PR->VD: No effect on midbody formation; loss of FT CD2AP- and SH3KBP1-binding in a yeast two-hybrid assay; no FT effect on HIV-1 release." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 757..759 FT /note="RPP->GAA: No effect on midbody formation; loss of FT SH3GL2-binding in a yeast two-hybrid assay." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 757..758 FT /note="RP->AA: Abolishes interaction with SH3GL1 and FT SH3GL2; no effect on rescue of PTAP-type L domain-deficient FT HIV-1 p6." FT /evidence="ECO:0000269|PubMed:17350572" FT MUTAGEN 794..813 FT /note="Missing: Does not support the formation of normal FT midbodies; loss of localization to the midbody; loss of FT CD2AP-, CEP55-, SH3GL2-, SH3KBP1-, TSG101-binding in a FT yeast two-hybrid assay." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 800..802 FT /note="GPP->AAA: Abolishes interaction with CEP55; inhibits FT support of cytokinesis." FT /evidence="ECO:0000269|PubMed:17853893" FT MUTAGEN 801..802 FT /note="PP->VD: Loss of midbody localization; does not FT support cytokinesis; loss of CEP55-binding in a yeast FT two-hybrid assay; no effect on HIV-1 release." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 801 FT /note="P->A: Decreased interaction with CEP55." FT /evidence="ECO:0000269|PubMed:18948538" FT MUTAGEN 802 FT /note="P->A: Decreased interaction with CEP55." FT /evidence="ECO:0000269|PubMed:18948538" FT MUTAGEN 803..804 FT /note="YP->VD: No effect on CEP55-binding in a yeast FT two-hybrid assay." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 805..806 FT /note="TY->VD: Loss of CEP55-binding in a yeast two-hybrid FT assay." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 806 FT /note="Y->A: Abolishes interaction with CEP55." FT /evidence="ECO:0000269|PubMed:18948538" FT MUTAGEN 852..855 FT /note="PSYP->ASAA: Loss of homoologimerization and reduced FT TSG101-binding; decreased HIV-1 release; no effect on FT cytokinesis. Almost complete loss of TSG101-binding and FT impaired cytokinesis; when associated with 717-A--A-720." FT /evidence="ECO:0000269|PubMed:18641129" FT MUTAGEN 864..865 FT /note="YY->AA: Loss of homooligomerization; reduced FT TSG101-binding; impaired HIV-1 release." FT /evidence="ECO:0000269|PubMed:18641129" FT CONFLICT 580 FT /note="M -> T (in Ref. 8; BAA92092)" FT /evidence="ECO:0000305" FT HELIX 18..28 FT /evidence="ECO:0007829|PDB:5WA1" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:6KP3" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:2OEV" FT HELIX 35..54 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 62..76 FT /evidence="ECO:0007829|PDB:5WA1" FT TURN 77..88 FT /evidence="ECO:0007829|PDB:5WA1" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:5WA1" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2R05" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:5V3R" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 116..136 FT /evidence="ECO:0007829|PDB:5WA1" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:2OEV" FT HELIX 143..170 FT /evidence="ECO:0007829|PDB:5WA1" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:2OEV" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 181..205 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 210..231 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 241..266 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 270..290 FT /evidence="ECO:0007829|PDB:5WA1" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 298..317 FT /evidence="ECO:0007829|PDB:5WA1" FT HELIX 326..328 FT /evidence="ECO:0007829|PDB:5WA1" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:3C3R" FT TURN 354..357 FT /evidence="ECO:0007829|PDB:5V3R" FT HELIX 361..398 FT /evidence="ECO:0007829|PDB:2XS1" FT TURN 399..402 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 403..406 FT /evidence="ECO:0007829|PDB:2XS1" FT STRAND 408..412 FT /evidence="ECO:0007829|PDB:2R05" FT HELIX 415..426 FT /evidence="ECO:0007829|PDB:2XS1" FT TURN 427..429 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 430..471 FT /evidence="ECO:0007829|PDB:2XS1" FT TURN 473..475 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 481..514 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 517..523 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 527..532 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 547..575 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 581..590 FT /evidence="ECO:0007829|PDB:2XS1" FT STRAND 591..593 FT /evidence="ECO:0007829|PDB:2R05" FT HELIX 596..639 FT /evidence="ECO:0007829|PDB:2XS1" FT HELIX 644..697 FT /evidence="ECO:0007829|PDB:2XS1" FT STRAND 802..805 FT /evidence="ECO:0007829|PDB:3E1R" FT TURN 810..813 FT /evidence="ECO:0007829|PDB:2ZNE" SQ SEQUENCE 868 AA; 96023 MW; 573588D1F612EC93 CRC64; MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LANGVLASLN LPAAIEDVSG DTVPQSILTK SRSVIEQGGI QTVDQLIKEL PELLQRNREI LDESLRLLDE EEATDNDLRA KFKERWQRTP SNELYKPLRA EGTNFRTVLD KAVQADGQVK ECYQSHRDTI VLLCKPEPEL NAAIPSANPA KTMQGSEVVN VLKSLLSNLD EVKKEREGLE NDLKSVNFDM TSKFLTALAQ DGVINEEALS VTELDRVYGG LTTKVQESLK KQEGLLKNIQ VSHQEFSKMK QSNNEANLRE EVLKNLATAY DNFVELVANL KEGTKFYNEL TEILVRFQNK CSDIVFARKT ERDELLKDLQ QSIAREPSAP SIPTPAYQSS PAGGHAPTPP TPAPRTMPPT KPQPPARPPP PVLPANRAPS ATAPSPVGAG TAAPAPSQTP GSAPPPQAQG PPYPTYPGYP GYCQMPMPMG YNPYAYGQYN MPYPPVYHQS PGQAPYPGPQ QPSYPFPQPP QQSYYPQQ //