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Showing Protein Programmed cell death 6-interacting protein (HMDBP07936)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP07936
Secondary Accession Numbers
  • 13647
Name Programmed cell death 6-interacting protein
Synonyms
  1. ALG-2-interacting protein 1
  2. Hp95
  3. PDCD6-interacting protein
Gene Name PDCD6IP
Protein Type Unknown
Biological Properties
General Function Cell cycle control, cell division, chromosome partitioning
Specific Function 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 appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. Melanosome
  4. cytoskeleton
  5. cytosol
  6. centrosome
Gene Properties
Chromosome Location Chromosome:3
Locus 3p22.3
SNPs PDCD6IP
Gene Sequence 
>2607 bp
ATGGCGACATTCATCTCGGTGCAGCTGAAAAAGACCTCAGAGGTGGACCTGGCCAAGCCG
CTGGTGAAGTTCATCCAGCAGACTTACCCAAGCGGCGGGGAAGAGCAGGCCCAGTACTGC
CGCGCGGCGGAGGAGCTCAGCAAGCTGCGCCGCGCCGCAGTCGGTCGTCCGCTGGACAAG
CACGAGGGCGCGCTCGAGACGCTCCTGAGATATTATGATCAGATTTGTTCTATTGAACCC
AAATTCCCATTTTCTGAAAATCAGATCTGCTTGACATTTACCTGGAAGGATGCTTTCGAT
AAAGGTTCACTTTTTGGAGGCTCTGTAAAACTGGCTCTTGCAAGCTTAGGATATGAAAAG
AGCTGTGTGTTGTTCAATTGTGCAGCCTTAGCTAGCCAAATTGCAGCAGAACAGAACCTG
GATAATGATGAAGGATTGAAAATCGCTGCTAAACATTACCAGTTTGCTAGTGGTGCCTTT
TTACATATTAAAGAGACGGTTTTATCTGCCTTAAGTCGAGAGCCGACCGTGGACATATCT
CCAGATACTGTTGGGACCCTCAGTCTTATTATGCTGGCACAGGCTCAAGAAGTATTTTTT
TTAAAAGCCACAAGAGATAAAATGAAAGATGCCATCATAGCTAAATTGGCTAATCAGGCT
GCAGATTATTTTGGTGATGCTTTCAAACAGTGTCAATACAAAGATACTCTCCCCAAGGAG
GTGTTCCCTGTCTTGGCTGCAAAGCACTGTATCATGCAGGCCAATGCTGAGTACCATCAG
TCTATCCTGGCAAAACAGCAGAAGAAATTTGGAGAAGAAATTGCAAGGTTACAGCATGCA
GCAGAACTGATTAAAACAGTGGCATCTCGCTATGATGAATATGTTAATGTGAAGGATTTT
TCTGACAAAATCAATCGTGCCCTTGCTGCAGCAAAGAAGGATAATGACTTCATTTATCAT
GATCGAGTTCCAGACCTTAAAGATCTAGATCCTATTGGCAAAGCCACACTTGTGAAATCT
ACCCCGGTCAATGTACCCATCAGTCAGAAATTTACTGATCTGTTTGAGAAGATGGTTCCC
GTGTCAGTACAGCAGTCTTTGGCTGCCTATAATCAGAGGAAAGCCGATTTGGTTAACAGA
TCAATTGCTCAGATGAGAGAAGCCACCACTTTGGCAAATGGGGTGCTAGCTTCCCTTAAT
CTTCCAGCAGCAATTGAAGATGTGTCTGGAGACACTGTACCTCAGTCTATATTGACTAAA
TCCAGATCTGTGATTGAACAGGGAGGCATCCAGACTGTTGATCAGTTGATTAAAGAACTG
CCTGAATTACTGCAACGAAATAGAGAAATCCTAGATGAGTCATTAAGGTTGTTGGATGAA
GAAGAAGCAACCGATAATGATTTAAGAGCAAAATTTAAGGAACGTTGGCAAAGGACACCA
TCCAATGAACTGTATAAGCCTTTAAGAGCAGAGGGAACCAACTTCAGAACAGTTTTAGAT
AAAGCTGTGCAGGCAGATGGACAAGTGAAAGAATGTTACCAGTCTCATCGTGACACCATC
GTGCTTTTGTGTAAGCCAGAGCCTGAGCTGAATGCTGCCATCCCTTCTGCTAATCCAGCA
AAGACCATGCAGGGCAGTGAGGTTGTAAATGTCTTAAAATCCTTATTGTCAAATCTTGAT
GAAGTAAAGAAGGAAAGAGAGGGTCTGGAGAATGACTTGAAATCTGTGAATTTTGACATG
ACAAGCAAGTTTTTGACAGCCCTGGCTCAAGATGGTGTGATAAATGAAGAAGCTCTTTCT
GTTACTGAACTAGATCGAGTCTATGGAGGTCTTACAACTAAAGTCCAAGAATCTCTAAAG
AAACAGGAGGGACTTCTTAAAAATATTCAGGTCTCACATCAGGAATTTTCAAAAATGAAA
CAATCTAATAATGAAGCTAACTTAAGAGAAGAAGTTTTGAAGAATTTAGCTACTGCATAT
GACAACTTTGTTGAACTTGTAGCTAATTTGAAGGAAGGCACAAAGTTTTACAATGAGTTG
ACTGAAATCCTGGTCAGGTTCCAGAACAAATGCAGTGATATAGTTTTTGCACGGAAGACA
GAAAGAGATGAACTCTTAAAGGACTTGCAACAAAGCATTGCCAGAGAACCTAGTGCTCCT
TCAATTCCTACACCTGCGTATCAGTCCTCACCAGCAGGAGGACATGCACCAACTCCTCCA
ACTCCAGCGCCAAGAACCATGCCGCCTACTAAGCCCCAGCCCCCAGCCAGGCCTCCACCA
CCTGTGCTTCCAGCAAATCGAGCTCCTTCTGCTACTGCTCCATCTCCAGTGGGGGCTGGG
ACTGCTGCGCCAGCTCCATCACAAACGCCTGGCTCAGCTCCTCCTCCACAGGCGCAGGGA
CCACCCTATCCCACCTATCCAGGATATCCTGGGTATTGCCAAATGCCCATGCCCATGGGC
TATAATCCTTATGCGTATGGCCAGTATAATATGCCATATCCACCAGTGTATCACCAGAGT
CCTGGACAGGCTCCATACCCGGGACCCCAGCAGCCTTCATACCCCTTCCCTCAGCCCCCA
CAGCAGTCTTACTATCCACAGCAGTAA
Protein Properties
Number of Residues 868
Molecular Weight 96022.3
Theoretical pI 6.46
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Programmed cell death 6-interacting protein
MATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAAVGRPLDK
HEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEK
SCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSREPTVDIS
PDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKE
VFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDF
SDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTDLFEKMVP
VSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTK
SRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTP
SNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPA
KTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEALS
VTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAY
DNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAP
SIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAG
TAAPAPSQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQS
PGQAPYPGPQQPSYPFPQPPQQSYYPQQ
GenBank ID Protein 22027538
UniProtKB/Swiss-Prot ID Q8WUM4
UniProtKB/Swiss-Prot Entry Name PDC6I_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_013374.4
GeneCard ID PDCD6IP
GenAtlas ID PDCD6IP
HGNC ID HGNC:8766
References
General References
  1. 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed:17081065 ]
  7. Nagase T, Kikuno R, Ishikawa KI, 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. 2000 Feb 28;7(1):65-73. [PubMed:10718198 ]
  8. Morita E, Sandrin V, Chung HY, Morham SG, Gygi SP, Rodesch CK, Sundquist WI: Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 2007 Oct 3;26(19):4215-27. Epub 2007 Sep 13. [PubMed:17853893 ]
  9. 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. 2008 Apr 11;283(15):9623-32. doi: 10.1074/jbc.M800717200. Epub 2008 Feb 6. [PubMed:18256029 ]
  10. Wu Y, Pan S, Che S, He G, Nelman-Gonzalez M, Weil MM, Kuang J: Overexpression of Hp95 induces G1 phase arrest in confluent HeLa cells. Differentiation. 2001 Jun;67(4-5):139-53. [PubMed:11683497 ]
  11. Katoh K, Shibata H, Suzuki H, Nara 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. 2003 Oct 3;278(40):39104-13. Epub 2003 Jul 14. [PubMed:12860994 ]
  12. Strack B, Calistri A, Craig S, Popova E, Gottlinger HG: AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell. 2003 Sep 19;114(6):689-99. [PubMed:14505569 ]
  13. von Schwedler UK, Stuchell M, Muller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Krausslich HG, Kaplan J, Morham SG, Sundquist WI: The protein network of HIV budding. Cell. 2003 Sep 19;114(6):701-13. [PubMed:14505570 ]
  14. Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD: Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12414-9. Epub 2003 Sep 30. [PubMed:14519844 ]
  15. 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. 2004 Jan 1;421(1):159-65. [PubMed:14678797 ]
  16. Peck JW, Bowden ET, Burbelo PD: Structure and function of human Vps20 and Snf7 proteins. Biochem J. 2004 Feb 1;377(Pt 3):693-700. [PubMed:14583093 ]
  17. Matsuo H, Chevallier J, Mayran N, Le Blanc I, Ferguson C, Faure J, Blanc NS, Matile S, Dubochet J, Sadoul R, Parton RG, Vilbois F, Gruenberg J: Role of LBPA and Alix in multivesicular liposome formation and endosome organization. Science. 2004 Jan 23;303(5657):531-4. [PubMed:14739459 ]
  18. 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. 2005 Apr;69(4):861-5. [PubMed:15849434 ]
  19. 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. 2005 Jul 22;280(29):27004-12. Epub 2005 May 21. [PubMed:15908698 ]
  20. 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. 2006 Nov;17(11):4876-87. Epub 2006 Sep 6. [PubMed:16957052 ]
  21. Usami Y, Popov S, Gottlinger HG: Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. J Virol. 2007 Jun;81(12):6614-22. Epub 2007 Apr 11. [PubMed:17428861 ]
  22. Carlton JG, Martin-Serrano J: Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science. 2007 Jun 29;316(5833):1908-12. Epub 2007 Jun 7. [PubMed:17556548 ]
  23. 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. 2009 Aug 14;386(1):237-41. doi: 10.1016/j.bbrc.2009.06.015. Epub 2009 Jun 9. [PubMed:19520058 ]
  24. Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP: Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell. 2007 Mar 9;128(5):841-52. [PubMed:17350572 ]
  25. Lee S, Joshi A, Nagashima K, Freed EO, Hurley JH: Structural basis for viral late-domain binding to Alix. Nat Struct Mol Biol. 2007 Mar;14(3):194-9. Epub 2007 Feb 4. [PubMed:17277784 ]
  26. Zhai Q, Fisher RD, Chung HY, Myszka DG, Sundquist WI, Hill CP: Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV. Nat Struct Mol Biol. 2008 Jan;15(1):43-9. Epub 2007 Dec 9. [PubMed:18066081 ]
  27. McCullough J, Fisher RD, Whitby FG, Sundquist WI, Hill CP: ALIX-CHMP4 interactions in the human ESCRT pathway. Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7687-91. doi: 10.1073/pnas.0801567105. Epub 2008 May 29. [PubMed:18511562 ]
  28. Lee HH, Elia N, Ghirlando R, Lippincott-Schwartz J, Hurley JH: Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55. Science. 2008 Oct 24;322(5901):576-80. doi: 10.1126/science.1162042. [PubMed:18948538 ]
  29. 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. 2008 Oct 8;16(10):1562-73. doi: 10.1016/j.str.2008.07.012. [PubMed:18940611 ]