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Programmed cell death 6-interacting protein (PDCD6-interacting protein) (ALG-2-interacting protein 1) (ALG-2-interacting protein X) (Hp95)

 PDC6I_HUMAN             Reviewed;         868 AA.
Q8WUM4; C5MQH7; E9PFU1; Q6NUS1; Q9BX86; Q9NUN0; Q9P2H2; Q9UKL5;
23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-DEC-2017, entry version 169.
RecName: Full=Programmed cell death 6-interacting protein;
Short=PDCD6-interacting protein;
AltName: Full=ALG-2-interacting protein 1;
AltName: Full=ALG-2-interacting protein X;
AltName: Full=Hp95;
Name=PDCD6IP; Synonyms=AIP1, ALIX, KIAA1375;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-550.
PubMed=11683497; DOI=10.1046/j.1432-0436.2001.670406.x;
Wu Y., Pan S., Che S., He G., Nelman-Gonzalez M., Weil M.M., Kuang J.;
"Overexpression of Hp95 induces G1 phase arrest in confluent HeLa
cells.";
Differentiation 67:139-153(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=19906316; DOI=10.1186/1471-2164-10-518;
Wang P., Yu P., Gao P., Shi T., Ma D.;
"Discovery of novel human transcript variants by analysis of intronic
single-block EST with polyadenylation site.";
BMC Genomics 10:518-518(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-309 AND
LEU-730.
Li H., Shioda T., Isselbacher K.J.;
"Molecular cloning of human ALG-2 interacting protein 1 (AIP1).";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS MET-7 AND ILE-378.
TISSUE=Lymph, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-23; 111-120; 216-229; 439-446; 457-469 AND
542-553, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Glen H., Frame M.C.;
Submitted (MAR-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-868 (ISOFORM 1), AND
VARIANT ILE-378.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-868 (ISOFORM 1), AND
VARIANT SER-550.
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[10]
INTERACTION WITH CHMP4A AND CHMP4B.
PubMed=12860994; DOI=10.1074/jbc.M301604200;
Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E.,
Yoshimori T., Maki M.;
"The ALG-2-interacting protein Alix associates with CHMP4b, a human
homologue of yeast Snf7 that is involved in multivesicular body
sorting.";
J. Biol. Chem. 278:39104-39113(2003).
[11]
FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), INTERACTION WITH
CHMP4A; CHMP4B AND CHMP4C, AND INTERACTION WITH HIV-1 P6 AND EIAV P9
(MICROBIAL INFECTION).
PubMed=14505569; DOI=10.1016/S0092-8674(03)00653-6;
Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
"AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning
in virus budding.";
Cell 114:689-699(2003).
[12]
FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), SELF-ASSOCIATION,
INTERACTION WITH TSG101; CHMP4A; CHMP4B CHMP4C, AND SUBCELLULAR
LOCATION.
PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
"The protein network of HIV budding.";
Cell 114:701-713(2003).
[13]
SELF-ASSOCIATION, INTERACTION WITH TSG101; CHMP4A; CHMP4B AND CHMP4C,
AND INTERACTION WITH EIAV P9 (MICROBIAL INFECTION).
PubMed=14519844; DOI=10.1073/pnas.2133846100;
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
"Divergent retroviral late-budding domains recruit vacuolar protein
sorting factors by using alternative adaptor proteins.";
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
[14]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[15]
INTERACTION WITH CHMP4A; CHMP4B AND CHMP4C.
PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
Katoh K., Shibata H., Hatta K., Maki M.;
"CHMP4b is a major binding partner of the ALG-2-interacting protein
Alix among the three CHMP4 isoforms.";
Arch. Biochem. Biophys. 421:159-165(2004).
[16]
INTERACTION WITH CHMP4A; CHMP4B AND CHMP4C.
PubMed=14583093; DOI=10.1042/BJ20031347;
Peck J.W., Bowden E.T., Burbelo P.D.;
"Structure and function of human Vps20 and Snf7 proteins.";
Biochem. J. 377:693-700(2004).
[17]
FUNCTION IN ENDOSOME ORGANIZATION.
PubMed=14739459; DOI=10.1126/science.1092425;
Matsuo H., Chevallier J., Mayran N., Le Blanc I., Ferguson C.,
Faure J., Blanc N.S., Matile S., Dubochet J., Sadoul R., Parton R.G.,
Vilbois F., Gruenberg J.;
"Role of LBPA and Alix in multivesicular liposome formation and
endosome organization.";
Science 303:531-534(2004).
[18]
INTERACTION WITH SGSM3, AND SUBCELLULAR LOCATION.
PubMed=15849434; DOI=10.1271/bbb.69.861;
Ichioka F., Horii M., Katoh K., Terasawa Y., Shibata H., Maki M.;
"Identification of Rab GTPase-activating protein-like protein
(RabGAPLP) as a novel Alix/AIP1-interacting protein.";
Biosci. Biotechnol. Biochem. 69:861-865(2005).
[19]
INTERACTION WITH MURINE LEUKEMIA VIRUS GAG POLYPROTEIN.
PubMed=15908698; DOI=10.1074/jbc.M413735200;
Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R.,
Bertrand E., Basyuk E.;
"Tsg101 and Alix interact with murine leukemia virus Gag and cooperate
with Nedd4 ubiquitin ligases during budding.";
J. Biol. Chem. 280:27004-27012(2005).
[20]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[21]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PDCD6.
PubMed=16957052; DOI=10.1091/mbc.E06-05-0444;
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.;
"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum
exit sites by Sec31A and stabilizes the localization of Sec31A.";
Mol. Biol. Cell 17:4876-4887(2006).
[22]
FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55
AND CD2AP, AND MUTAGENESIS OF ILE-212; PHE-676 AND 800-GLY--PRO-802.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[23]
FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), INTERACTION WITH
CHMP4B, AND MUTAGENESIS OF PHE-199; LEU-216; PHE-317; ILE-318 AND
TYR-319.
PubMed=17428861; DOI=10.1128/JVI.00314-07;
Usami Y., Popov S., Goettlinger H.G.;
"Potent rescue of human immunodeficiency virus type 1 late domain
mutants by ALIX/AIP1 depends on its CHMP4 binding site.";
J. Virol. 81:6614-6622(2007).
[24]
FUNCTION IN CYTOKINESIS AND HIV1 RELEASE, SUBCELLULAR LOCATION, AND
INTERACTION WITH CEP55.
PubMed=17556548; DOI=10.1126/science.1143422;
Carlton J.G., Martin-Serrano J.;
"Parallels between cytokinesis and retroviral budding: a role for the
ESCRT machinery.";
Science 316:1908-1912(2007).
[25]
INTERACTION WITH PDCD6.
PubMed=18256029; DOI=10.1074/jbc.M800717200;
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
Maki M.;
"Identification of Alix-type and non-Alix-type ALG-2-binding sites in
human phospholipid scramblase 3: differential binding to an
alternatively spliced isoform and amino acid-substituted mutants.";
J. Biol. Chem. 283:9623-9632(2008).
[26]
FUNCTION IN CYTOKINESIS AND HIV1 RELEASE, INTERACTION WITH CEP55 AND
TSG101, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-199; ILE-212;
PHE-676; 717-PRO--PRO-720; 744-PRO-ARG-745; 757-ARG--PRO-759;
794-PRO--CYS-813; 801-PRO-PRO-802; 803-TYR-PRO-804; 805-THR-TYR-806;
852-PRO--PRO-855 AND 864-TYR-TYR-865.
PubMed=18641129; DOI=10.1073/pnas.0802008105;
Carlton J.G., Agromayor M., Martin-Serrano J.;
"Differential requirements for Alix and ESCRT-III in cytokinesis and
HIV-1 release.";
Proc. Natl. Acad. Sci. U.S.A. 105:10541-10546(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730; THR-738 AND
THR-741, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
INTERACTION WITH TSG101.
PubMed=19520058; DOI=10.1016/j.bbrc.2009.06.015;
Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H.,
Shibata H., Maki M.;
"Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor
that bridges Alix and TSG101.";
Biochem. Biophys. Res. Commun. 386:237-241(2009).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[31]
PHOSPHORYLATION, AND INTERACTION WITH PDGFRB.
PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004;
Wardega P., Heldin C.H., Lennartsson J.;
"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects
cell proliferation but not migration.";
Cell. Signal. 22:1363-1368(2010).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-738 AND THR-741, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
INTERACTION WITH ARRDC1.
PubMed=21191027; DOI=10.1128/JVI.02045-10;
Rauch S., Martin-Serrano J.;
"Multiple interactions between the ESCRT machinery and arrestin-
related proteins: implications for PPXY-dependent budding.";
J. Virol. 85:3546-3556(2011).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[36]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SDCBP AND SDC2, AND
MUTAGENESIS OF PHE-676.
PubMed=22660413; DOI=10.1038/ncb2502;
Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G.,
Geeraerts A., Ivarsson Y., Depoortere F., Coomans C., Vermeiren E.,
Zimmermann P., David G.;
"Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
Nat. Cell Biol. 14:677-685(2012).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479 AND SER-481, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-745, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[40]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[41]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 1-698, INTERACTION WITH
CHMP4A; HIV-1 P6; EIAV P9; TSG101; SH3GL1 AND SH3GL2, AND MUTAGENESIS
OF ILE-212; TYR-319; PHE-495; VAL-498; VAL-509; PHE-676; LEU-680;
ILE-683; PRO-720 AND 757-ARG-PRO-758.
PubMed=17350572; DOI=10.1016/j.cell.2007.01.035;
Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I.,
Hill C.P.;
"Structural and biochemical studies of ALIX/AIP1 and its role in
retrovirus budding.";
Cell 128:841-852(2007).
[42]
X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 360-702, INTERACTION WITH
HIV-1 P6, AND MUTAGENESIS OF VAL-498; VAL-509; CYS-512; PHE-676 AND
ILE-683.
PubMed=17277784; DOI=10.1038/nsmb1203;
Lee S., Joshi A., Nagashima K., Freed E.O., Hurley J.H.;
"Structural basis for viral late-domain binding to Alix.";
Nat. Struct. Mol. Biol. 14:194-199(2007).
[43]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 2-698 IN COMPLEX WITH HIV-1
P6, X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 2-698 IN COMPLEX WITH
HIV-1 P9, AND INTERACTION WITH EIAV P9.
PubMed=18066081; DOI=10.1038/nsmb1319;
Zhai Q., Fisher R.D., Chung H.Y., Myszka D.G., Sundquist W.I.,
Hill C.P.;
"Structural and functional studies of ALIX interactions with YPX(n)L
late domains of HIV-1 and EIAV.";
Nat. Struct. Mol. Biol. 15:43-49(2008).
[44]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-359 IN COMPLEX WITH
CHMP4A, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-359 IN COMPLEX WITH
CHMP4B, AND X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 1-359 IN COMPLEX
WITH CHMP4C.
PubMed=18511562; DOI=10.1073/pnas.0801567105;
McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
"ALIX-CHMP4 interactions in the human ESCRT pathway.";
Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
[45]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 797-809 IN COMPLEX WITH
CEP55, AND MUTAGENESIS OF PRO-801; PRO-802 AND TYR-806.
PubMed=18948538; DOI=10.1126/science.1162042;
Lee H.H., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J.H.;
"Midbody targeting of the ESCRT machinery by a noncanonical coiled
coil in CEP55.";
Science 322:576-580(2008).
[46]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 799-812 IN COMPLEX WITH
PDCD6.
PubMed=18940611; DOI=10.1016/j.str.2008.07.012;
Suzuki H., Kawasaki M., Inuzuka T., Okumura M., Kakiuchi T.,
Shibata H., Wakatsuki S., Maki M.;
"Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide
complex: Ca2+/EF3-driven arginine switch mechanism.";
Structure 16:1562-1573(2008).
[47]
VARIANT SER-429.
PubMed=22073189; DOI=10.1371/journal.pone.0026741;
Benitez B.A., Alvarado D., Cai Y., Mayo K., Chakraverty S., Norton J.,
Morris J.C., Sands M.S., Goate A., Cruchaga C.;
"Exome-sequencing confirms DNAJC5 mutations as cause of adult neuronal
ceroid-lipofuscinosis.";
PLoS ONE 6:E26741-E26741(2011).
-!- FUNCTION: Multifunctional protein involved in endocytosis,
multivesicular body biogenesis, membrane repair, cytokinesis,
apoptosis and maintenance of tight junction integrity. Class E VPS
protein involved in concentration and sorting of cargo proteins of
the multivesicular body (MVB) for incorporation into intralumenal
vesicles (ILVs) that are generated by invagination and scission
from the limiting membrane of the endosome. Binds to the
phospholipid lysobisphosphatidic acid (LBPA) which is abundant in
MVBs internal membranes. The MVB pathway requires the sequential
function of ESCRT-O, -I,-II and -III complexes (PubMed:14739459).
The ESCRT machinery also functions in topologically equivalent
membrane fission events, such as the terminal stages of
cytokinesis (PubMed:17853893, PubMed:17556548). Adapter for a
subset of ESCRT-III proteins, such as CHMP4, to function at
distinct membranes. Required for completion of cytokinesis
(PubMed:17853893, PubMed:17556548, PubMed:18641129). May play a
role in the regulation of both apoptosis and cell proliferation.
Regulates exosome biogenesis in concert with SDC1/4 and SDCBP
(PubMed:22660413). By interacting with F-actin, PARD3 and TJP1
secures the proper assembly and positioning of actomyosin-tight
junction complex at the apical sides of adjacent epithelial cells
that defines a spatial membrane domain essential for the
maintenance of epithelial cell polarity and barrier (By
similarity). {ECO:0000250|UniProtKB:Q9WU78,
ECO:0000269|PubMed:14739459, ECO:0000269|PubMed:17556548,
ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129,
ECO:0000269|PubMed:22660413}.
-!- FUNCTION: (Microbial infection) Involved in HIV-1 virus budding.
Can replace TSG101 it its role of supporting HIV-1 release; this
function requires the interaction with CHMP4B. The ESCRT machinery
also functions in topologically equivalent membrane fission
events, such as enveloped virus budding (HIV-1 and other
lentiviruses). {ECO:0000269|PubMed:14505569,
ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:18641129}.
-!- SUBUNIT: Self-associates (PubMed:14505570, PubMed:14519844).
Interacts with SH3KBP1/CIN85 (By similarity). Interacts with PDCD6
in a calcium -dependent manner (PubMed:16957052, PubMed:18256029,
PubMed:18940611). Interacts with TSG101 in a calcium-dependent
manner; PDCD6IP homooligomerization may be required for TSG101-
binding (PubMed:14505570, PubMed:14519844, PubMed:18641129,
PubMed:19520058, PubMed:17350572). Interacts with SGSM3
(PubMed:15849434). Directly interacts with CHMP4A, CHMP4B and
CHMP4C (PubMed:12860994, PubMed:14505569, PubMed:14505570,
PubMed:14519844, PubMed:14678797, PubMed:14583093,
PubMed:17428861, PubMed:17350572, PubMed:18511562). Directly
interacts with CEP55 in a 1:2 stoechiometry (PubMed:17853893,
PubMed:17556548, PubMed:18641129, PubMed:18948538). The
interaction with CEP55 is required for PDCD6IP targeting to the
midbody (PubMed:18641129). May interact with PDGFRB
(PubMed:20494825). Interacts with SH3GL1 and SH3GL2/endophilin-1
(PubMed:17350572). Forms a complex with SDCBP and SDC2
(PubMed:22660413). Found in a complex with F-actin, TJP1/ZO-1 and
PARD3 (By similarity). Interacts with CD2AP (PubMed:17853893).
Interacts with ARRDC1 (PubMed:21191027).
{ECO:0000250|UniProtKB:Q9QZA2, ECO:0000250|UniProtKB:Q9WU78,
ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569,
ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797,
ECO:0000269|PubMed:15849434, ECO:0000269|PubMed:16957052,
ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:17428861,
ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18256029, ECO:0000269|PubMed:18511562,
ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18948538, ECO:0000269|PubMed:19520058,
ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:21191027,
ECO:0000269|PubMed:22660413}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 p6
(PubMed:14505569, PubMed:17350572, PubMed:17277784,
PubMed:18066081). Interacts with HIV-1 p9 (PubMed:18066081).
Interacts with EIAV p9 (PubMed:14505569, PubMed:14519844,
PubMed:17350572, PubMed:18066081). Interacts with murine leukemia
virus Gag polyprotein (via LYPX(n)L motif) (PubMed:15908698).
{ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14519844,
ECO:0000269|PubMed:15908698, ECO:0000269|PubMed:17277784,
ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:18066081}.
-!- INTERACTION:
P29991:- (xeno); NbExp=3; IntAct=EBI-310624, EBI-8826747;
Q9Y5K6:CD2AP; NbExp=2; IntAct=EBI-310624, EBI-298152;
Q53EZ4:CEP55; NbExp=14; IntAct=EBI-310624, EBI-747776;
Q9BY43:CHMP4A; NbExp=3; IntAct=EBI-310624, EBI-747981;
Q9H444:CHMP4B; NbExp=6; IntAct=EBI-310624, EBI-749627;
Q9D8B3:Chmp4b (xeno); NbExp=2; IntAct=EBI-310624, EBI-8322817;
Q96CF2:CHMP4C; NbExp=3; IntAct=EBI-310624, EBI-1221015;
P06241:FYN; NbExp=6; IntAct=EBI-310624, EBI-515315;
P03347:gag (xeno); NbExp=2; IntAct=EBI-310624, EBI-1220741;
P69730:gag (xeno); NbExp=2; IntAct=EBI-310624, EBI-1220941;
P08631:HCK; NbExp=4; IntAct=EBI-310624, EBI-346340;
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-310624, EBI-3957603;
P17931:LGALS3; NbExp=2; IntAct=EBI-310624, EBI-1170392;
Q90VU7:nef (xeno); NbExp=4; IntAct=EBI-310624, EBI-7460704;
O75340:PDCD6; NbExp=11; IntAct=EBI-310624, EBI-352915;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9QZA2}. Melanosome
{ECO:0000269|PubMed:17081065}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}.
Secreted, exosome {ECO:0000269|PubMed:22660413}. Cell junction,
tight junction {ECO:0000250|UniProtKB:Q9WU78}. Midbody, Midbody
ring {ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129}.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV. Colocalized with CEP55 at centrosomes of non-
dividing cells. Component of the actomyosin-tight junction complex
(By similarity). PDCD6IP targeting to the midbody requires the
interaction with CEP55 (PubMed:18641129).
{ECO:0000250|UniProtKB:Q9QZA2, ECO:0000250|UniProtKB:Q9WU78,
ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:17556548,
ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8WUM4-1; Sequence=Displayed;
Name=2;
IsoId=Q8WUM4-2; Sequence=VSP_044860;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8WUM4-3; Sequence=VSP_057190, VSP_057191;
-!- PTM: May be phosphorylated on tyrosine residues by activated
PDGFRB. {ECO:0000269|PubMed:20494825}.
-!- SEQUENCE CAUTION:
Sequence=BAA92092.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF349951; AAK20398.1; -; mRNA.
EMBL; GQ131806; ACS12984.1; -; mRNA.
EMBL; AF151793; AAF08220.1; -; mRNA.
EMBL; BT007367; AAP36031.1; -; mRNA.
EMBL; AC112220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC123901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020066; AAH20066.1; -; mRNA.
EMBL; BC068454; AAH68454.1; -; mRNA.
EMBL; AK002122; BAA92092.1; ALT_INIT; mRNA.
EMBL; AB037796; BAA92613.1; -; mRNA.
CCDS; CCDS2660.1; -. [Q8WUM4-1]
CCDS; CCDS54561.1; -. [Q8WUM4-2]
RefSeq; NP_001155901.1; NM_001162429.2. [Q8WUM4-2]
RefSeq; NP_001243121.1; NM_001256192.1. [Q8WUM4-3]
RefSeq; NP_037506.2; NM_013374.5. [Q8WUM4-1]
UniGene; Hs.475896; -.
PDB; 2OEV; X-ray; 3.30 A; A=1-698.
PDB; 2OEW; X-ray; 2.55 A; A=1-359.
PDB; 2OEX; X-ray; 2.58 A; A/B=360-702.
PDB; 2OJQ; X-ray; 2.87 A; A=360-702.
PDB; 2R02; X-ray; 2.60 A; A=2-698.
PDB; 2R03; X-ray; 2.59 A; A=2-698.
PDB; 2R05; X-ray; 2.55 A; A=2-698.
PDB; 2XS1; X-ray; 2.30 A; A=1-698.
PDB; 2XS8; X-ray; 2.50 A; A=1-698.
PDB; 2ZNE; X-ray; 2.20 A; C/D=799-812.
PDB; 3C3O; X-ray; 2.15 A; A=1-359.
PDB; 3C3Q; X-ray; 2.10 A; A=1-359.
PDB; 3C3R; X-ray; 2.02 A; A=1-359.
PDB; 3E1R; X-ray; 2.00 A; C=797-809.
PDB; 3WUV; X-ray; 2.79 A; C/F/I/L/O/R=796-810.
PDB; 4JJY; X-ray; 6.50 A; A/B=355-708.
PDBsum; 2OEV; -.
PDBsum; 2OEW; -.
PDBsum; 2OEX; -.
PDBsum; 2OJQ; -.
PDBsum; 2R02; -.
PDBsum; 2R03; -.
PDBsum; 2R05; -.
PDBsum; 2XS1; -.
PDBsum; 2XS8; -.
PDBsum; 2ZNE; -.
PDBsum; 3C3O; -.
PDBsum; 3C3Q; -.
PDBsum; 3C3R; -.
PDBsum; 3E1R; -.
PDBsum; 3WUV; -.
PDBsum; 4JJY; -.
ProteinModelPortal; Q8WUM4; -.
SMR; Q8WUM4; -.
BioGrid; 115332; 112.
DIP; DIP-29327N; -.
IntAct; Q8WUM4; 62.
MINT; MINT-4999333; -.
STRING; 9606.ENSP00000411825; -.
iPTMnet; Q8WUM4; -.
PhosphoSitePlus; Q8WUM4; -.
SwissPalm; Q8WUM4; -.
BioMuta; PDCD6IP; -.
DMDM; 31076831; -.
UCD-2DPAGE; Q8WUM4; -.
EPD; Q8WUM4; -.
MaxQB; Q8WUM4; -.
PaxDb; Q8WUM4; -.
PeptideAtlas; Q8WUM4; -.
PRIDE; Q8WUM4; -.
DNASU; 10015; -.
Ensembl; ENST00000307296; ENSP00000307387; ENSG00000170248. [Q8WUM4-1]
Ensembl; ENST00000457054; ENSP00000411825; ENSG00000170248. [Q8WUM4-2]
GeneID; 10015; -.
KEGG; hsa:10015; -.
UCSC; uc003cfx.5; human. [Q8WUM4-1]
CTD; 10015; -.
DisGeNET; 10015; -.
EuPathDB; HostDB:ENSG00000170248.13; -.
GeneCards; PDCD6IP; -.
H-InvDB; HIX0163463; -.
HGNC; HGNC:8766; PDCD6IP.
HPA; CAB016212; -.
HPA; HPA011905; -.
MIM; 608074; gene.
neXtProt; NX_Q8WUM4; -.
OpenTargets; ENSG00000170248; -.
PharmGKB; PA33116; -.
eggNOG; KOG2220; Eukaryota.
eggNOG; ENOG410XQX6; LUCA.
GeneTree; ENSGT00780000121909; -.
HOGENOM; HOG000006938; -.
HOVERGEN; HBG053533; -.
InParanoid; Q8WUM4; -.
KO; K12200; -.
OMA; SDFCFAR; -.
OrthoDB; EOG091G04NC; -.
PhylomeDB; Q8WUM4; -.
TreeFam; TF323502; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
ChiTaRS; PDCD6IP; human.
EvolutionaryTrace; Q8WUM4; -.
GeneWiki; PDCD6IP; -.
GenomeRNAi; 10015; -.
PRO; PR:Q8WUM4; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000170248; -.
CleanEx; HS_PDCD6IP; -.
ExpressionAtlas; Q8WUM4; baseline and differential.
Genevisible; Q8WUM4; HS.
GO; GO:0042641; C:actomyosin; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070971; C:endoplasmic reticulum exit site; IMP:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0031871; F:proteinase activated receptor binding; IPI:UniProtKB.
GO; GO:0000915; P:actomyosin contractile ring assembly; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:1903551; P:regulation of extracellular exosome assembly; IMP:UniProtKB.
GO; GO:0090559; P:regulation of membrane permeability; ISS:UniProtKB.
GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0046755; P:viral budding; IDA:UniProtKB.
GO; GO:0039702; P:viral budding via host ESCRT complex; IGI:UniProtKB.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
InterPro; IPR025304; ALIX_V_dom.
InterPro; IPR004328; BRO1_dom.
Pfam; PF13949; ALIX_LYPXL_bnd; 1.
Pfam; PF03097; BRO1; 1.
SMART; SM01041; BRO1; 1.
PROSITE; PS51180; BRO1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Cell cycle; Cell division; Cell junction; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing;
Host-virus interaction; Methylation; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Secreted; Tight junction;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7}.
CHAIN 2 868 Programmed cell death 6-interacting
protein.
/FTId=PRO_0000218891.
DOMAIN 3 392 BRO1. {ECO:0000255|PROSITE-
ProRule:PRU00526}.
REGION 176 868 Interaction with EIAV p9.
REGION 176 503 Interaction with CHMP4A, CHMP4B and
CHMP4C.
REGION 418 868 Interaction with SDCBP.
{ECO:0000269|PubMed:22660413}.
REGION 503 868 Self-association.
REGION 717 720 Interaction with TSG101.
REGION 801 806 Interaction with CEP55.
{ECO:0000269|PubMed:18641129}.
REGION 864 868 Essential to promote virus budding.
COMPBIAS 717 860 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7}.
MOD_RES 215 215 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 479 479 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 738 738 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 741 741 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 745 745 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 239 239 K -> KYFYFQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044860.
VAR_SEQ 240 271 EVFPVLAAKHCIMQANAEYHQSILAKQQKKFG -> VSYCF
YKHLLTLHVKYLDFFVYKKQVETYKEI (in isoform
3). {ECO:0000303|PubMed:19906316}.
/FTId=VSP_057190.
VAR_SEQ 272 868 Missing (in isoform 3).
{ECO:0000303|PubMed:19906316}.
/FTId=VSP_057191.
VARIANT 7 7 V -> M (in dbSNP:rs11554560).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_068975.
VARIANT 309 309 A -> T (in dbSNP:rs3792594).
{ECO:0000269|Ref.3}.
/FTId=VAR_053017.
VARIANT 378 378 V -> I (in dbSNP:rs3203777).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_053018.
VARIANT 429 429 G -> S (in dbSNP:rs76608858).
{ECO:0000269|PubMed:22073189}.
/FTId=VAR_069765.
VARIANT 550 550 N -> S (in dbSNP:rs9813017).
{ECO:0000269|PubMed:10718198,
ECO:0000269|PubMed:11683497}.
/FTId=VAR_053019.
VARIANT 638 638 K -> E (in dbSNP:rs3183982).
/FTId=VAR_053020.
VARIANT 730 730 S -> L (in dbSNP:rs1127732).
{ECO:0000269|Ref.3}.
/FTId=VAR_024381.
MUTAGEN 199 199 F->D: Does not support cytokinesis; loss
of normal midbody formation; loss of
CHMP4A-, CHMP4B- and CHMP4C-binding in a
yeast two-hybrid assay; no effect on
localization to the midbody; abolishes
rescue of PTAP-type L domain-deficient
HIV-1 p6. {ECO:0000269|PubMed:17428861,
ECO:0000269|PubMed:18641129}.
MUTAGEN 212 212 I->D: Does not support cytokinesis; loss
of normal midbody formation; loss of
CHMP4A-, CHMP4B- and CHMP4C-binding in a
yeast two-hybrid assay; impairs rescue of
PTAP-type L domain-deficient HIV-1 p6; no
effect on localization to the midbody.
{ECO:0000269|PubMed:17350572,
ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18641129}.
MUTAGEN 216 216 L->D: Abolishes interaction with CHMP4B
and abolishes rescue of PTAP-type L
domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17428861}.
MUTAGEN 317 317 F->A: Diminishes rescue of PTAP-type L
domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17428861}.
MUTAGEN 318 318 I->A: Greatly diminishes rescue of PTAP-
type L domain--deficient HIV-1 p6.
{ECO:0000269|PubMed:17428861}.
MUTAGEN 319 319 Y->A: Greatly diminishes rescue of PTAP-
type L domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17350572,
ECO:0000269|PubMed:17428861}.
MUTAGEN 319 319 Y->F: No effect on rescue of PTAP-type L
domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17350572,
ECO:0000269|PubMed:17428861}.
MUTAGEN 495 495 F->D: Impairs rescue of PTAP-type L
domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17350572}.
MUTAGEN 498 498 V->D: Reduces interaction with HIV-1 p6
and EIAV p9; abolishes rescue of PTAP-
type L domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17277784,
ECO:0000269|PubMed:17350572}.
MUTAGEN 509 509 V->D: Abolishes interaction with HIV-1
p6; impairs rescue of PTAP-type L domain-
deficient HIV-1 p6.
{ECO:0000269|PubMed:17277784,
ECO:0000269|PubMed:17350572}.
MUTAGEN 512 512 C->A: No effect on interaction with HIV-1
p6; impairs rescue of PTAP-type L domain-
deficient HIV-1 p6.
{ECO:0000269|PubMed:17277784}.
MUTAGEN 676 676 F->A: Loss of interaction with SDCBP.
{ECO:0000269|PubMed:22660413}.
MUTAGEN 676 676 F->D: Abolishes interaction with HIV-1 p6
and EIAV p9; abolishes rescue of PTAP-
type L domain-deficient HIV-1 p6; no
effect on cytokinesis, nor on midbody
formation. {ECO:0000269|PubMed:17277784,
ECO:0000269|PubMed:17350572,
ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18641129}.
MUTAGEN 680 680 L->D: Impairs rescue of PTAP-type L
domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17350572}.
MUTAGEN 683 683 I->A: No effect on interaction with HIV-1
p6. {ECO:0000269|PubMed:17277784,
ECO:0000269|PubMed:17350572}.
MUTAGEN 683 683 I->D: Reduces interaction with HIV-1 p6
and EIAV p9; abolishes rescue of PTAP-
type L domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17277784,
ECO:0000269|PubMed:17350572}.
MUTAGEN 717 720 PSAP->AAAA: No effect on midbody
formation, nor on cytokinesis; reduced
TSG101-binding; no effect on HIV-1
release. Almost complete loss of TSG101-
binding and impaired cytokinesis; when
associated with 852-A--A-855.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 720 720 P->L: Abolishes interaction with TSG101;
no effect on rescue of PTAP-type L
domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17350572}.
MUTAGEN 744 745 PR->VD: No effect on midbody formation;
loss of CD2AP- and SH3KBP1-binding in a
yeast two-hybrid assay; no effect on HIV-
1 release. {ECO:0000269|PubMed:18641129}.
MUTAGEN 757 759 RPP->GAA: No effect on midbody formation;
loss of SH3GL2-binding in a yeast two-
hybrid assay.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 757 758 RP->AA: Abolishes interaction with SH3GL1
and SH3GL2; no effect on rescue of PTAP-
type L domain-deficient HIV-1 p6.
{ECO:0000269|PubMed:17350572}.
MUTAGEN 794 813 Missing: Does not support the formation
of normal midbodies; loss of localization
to the midbody; loss of CD2AP-, CEP55-,
SH3GL2-, SH3KBP1-, TSG101-binding in a
yeast two-hybrid assay.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 800 802 GPP->AAA: Abolishes interaction with
CEP55; inhibits support of cytokinesis.
{ECO:0000269|PubMed:17853893}.
MUTAGEN 801 802 PP->VD: Loss of midbody localization;
does not support cytokinesis; loss of
CEP55-binding in a yeast two-hybrid
assay; no effect on HIV-1 release.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 801 801 P->A: Decreased interaction with CEP55.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 802 802 P->A: Decreased interaction with CEP55.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 803 804 YP->VD: No effect on CEP55-binding in a
yeast two-hybrid assay.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 805 806 TY->VD: Loss of CEP55-binding in a yeast
two-hybrid assay.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 806 806 Y->A: Abolishes interaction with CEP55.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 852 855 PSYP->ASAA: Loss of homoologimerization
and reduced TSG101-binding; decreased
HIV-1 release; no effect on cytokinesis.
Almost complete loss of TSG101-binding
and impaired cytokinesis; when associated
with 717-A--A-720.
{ECO:0000269|PubMed:18641129}.
MUTAGEN 864 865 YY->AA: Loss of homooligomerization;
reduced TSG101-binding; impaired HIV-1
release. {ECO:0000269|PubMed:18641129}.
CONFLICT 580 580 M -> T (in Ref. 8; BAA92092).
{ECO:0000305}.
HELIX 18 28 {ECO:0000244|PDB:3C3R}.
STRAND 33 35 {ECO:0000244|PDB:3C3R}.
HELIX 39 55 {ECO:0000244|PDB:3C3R}.
HELIX 62 78 {ECO:0000244|PDB:3C3R}.
TURN 79 83 {ECO:0000244|PDB:3C3R}.
TURN 84 86 {ECO:0000244|PDB:2XS1}.
STRAND 93 96 {ECO:0000244|PDB:3C3R}.
STRAND 98 100 {ECO:0000244|PDB:2R05}.
STRAND 104 106 {ECO:0000244|PDB:3C3R}.
STRAND 110 114 {ECO:0000244|PDB:3C3R}.
HELIX 116 136 {ECO:0000244|PDB:3C3R}.
STRAND 140 142 {ECO:0000244|PDB:2OEV}.
HELIX 143 170 {ECO:0000244|PDB:3C3R}.
STRAND 171 173 {ECO:0000244|PDB:2OEV}.
TURN 177 179 {ECO:0000244|PDB:3C3R}.
HELIX 181 205 {ECO:0000244|PDB:3C3R}.
HELIX 210 231 {ECO:0000244|PDB:3C3R}.
HELIX 241 266 {ECO:0000244|PDB:3C3R}.
HELIX 270 290 {ECO:0000244|PDB:3C3R}.
TURN 292 294 {ECO:0000244|PDB:3C3R}.
HELIX 298 317 {ECO:0000244|PDB:3C3R}.
HELIX 326 328 {ECO:0000244|PDB:3C3R}.
STRAND 348 350 {ECO:0000244|PDB:3C3R}.
TURN 354 357 {ECO:0000244|PDB:3C3Q}.
HELIX 361 398 {ECO:0000244|PDB:2XS1}.
TURN 399 402 {ECO:0000244|PDB:2XS1}.
HELIX 403 406 {ECO:0000244|PDB:2XS1}.
STRAND 408 412 {ECO:0000244|PDB:2R05}.
HELIX 415 426 {ECO:0000244|PDB:2XS1}.
TURN 427 429 {ECO:0000244|PDB:2XS1}.
HELIX 430 471 {ECO:0000244|PDB:2XS1}.
TURN 473 475 {ECO:0000244|PDB:2XS1}.
HELIX 481 514 {ECO:0000244|PDB:2XS1}.
HELIX 517 523 {ECO:0000244|PDB:2XS1}.
HELIX 527 532 {ECO:0000244|PDB:2XS1}.
HELIX 541 543 {ECO:0000244|PDB:2XS1}.
HELIX 547 575 {ECO:0000244|PDB:2XS1}.
HELIX 581 590 {ECO:0000244|PDB:2XS1}.
STRAND 591 593 {ECO:0000244|PDB:2R05}.
HELIX 596 639 {ECO:0000244|PDB:2XS1}.
HELIX 644 697 {ECO:0000244|PDB:2XS1}.
STRAND 802 805 {ECO:0000244|PDB:3E1R}.
TURN 810 813 {ECO:0000244|PDB:2ZNE}.
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


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