Full text data of VPS25
VPS25
(DERP9, EAP20)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Vacuolar protein-sorting-associated protein 25; hVps25 (Dermal papilla-derived protein 9; ELL-associated protein of 20 kDa; ESCRT-II complex subunit VPS25)
Vacuolar protein-sorting-associated protein 25; hVps25 (Dermal papilla-derived protein 9; ELL-associated protein of 20 kDa; ESCRT-II complex subunit VPS25)
UniProt
Q9BRG1
ID VPS25_HUMAN Reviewed; 176 AA.
AC Q9BRG1; B2R581;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Vacuolar protein-sorting-associated protein 25;
DE Short=hVps25;
DE AltName: Full=Dermal papilla-derived protein 9;
DE AltName: Full=ELL-associated protein of 20 kDa;
DE AltName: Full=ESCRT-II complex subunit VPS25;
GN Name=VPS25; Synonyms=DERP9, EAP20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Ukai Y., Yamashita M., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SNF8; VPS36 AND CHMP6.
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 [6]
RP IDENTIFICATION IN THE ESCRT-II COMPLEX, AND INTERACTION WITH VPS36;
RP SNF8 AND CHMP6.
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
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [7]
RP ERRATUM.
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 [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP6.
RX PubMed=15511219; DOI=10.1042/BJ20041227;
RA Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K.,
RA Kobayashi T., Uchiyama Y., Maki M.;
RT "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly
RT with an ESCRT-II component EAP20 and regulates endosomal cargo
RT sorting.";
RL Biochem. J. 387:17-26(2005).
RN [9]
RP INTERACTION WITH MISFOLDED CFTR.
RX PubMed=15007060; DOI=10.1083/jcb.200312018;
RA Sharma M., Pampinella F., Nemes C., Benharouga M., So J., Du K.,
RA Bache K.G., Papsin B., Zerangue N., Stenmark H., Lukacs G.L.;
RT "Misfolding diverts CFTR from recycling to degradation: quality
RT control at early endosomes.";
RL J. Cell Biol. 164:923-933(2004).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=16889659; DOI=10.1186/1471-2148-6-59;
RA Slater R., Bishop N.E.;
RT "Genetic structure and evolution of the Vps25 family, a yeast ESCRT-II
RT component.";
RL BMC Evol. Biol. 6:59-59(2006).
RN [11]
RP INTERACTION WITH SNF8; VPS36 AND CHMP6, AND SUBCELLULAR LOCATION.
RX PubMed=16973552; DOI=10.1128/JVI.01049-06;
RA Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I.,
RA White P.L., Hill C.P., Kaplan J., Ward D., Sundquist W.I.;
RT "Human ESCRT-II complex and its role in human immunodeficiency virus
RT type 1 release.";
RL J. Virol. 80:9465-9480(2006).
RN [12]
RP FUNCTION.
RX PubMed=18723511; DOI=10.1074/jbc.M804157200;
RA Pincetic A., Medina G., Carter C., Leis J.;
RT "Avian sarcoma virus and human immunodeficiency virus, type 1 use
RT different subsets of ESCRT proteins to facilitate the budding
RT process.";
RL J. Biol. Chem. 283:29822-29830(2008).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN COMPLEX WITH SNF8 AND VPS36.
RX PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004;
RA Im Y.J., Hurley J.H.;
RT "Integrated structural model and membrane targeting mechanism of the
RT human ESCRT-II complex.";
RL Dev. Cell 14:902-913(2008).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 102-176 IN COMPLEX WITH
RP CHMP6, AND MUTAGENESIS OF VAL-124 AND THR-126.
RX PubMed=19686684; DOI=10.1016/j.devcel.2009.07.008;
RA Im Y.J., Wollert T., Boura E., Hurley J.H.;
RT "Structure and function of the ESCRT-II-III interface in
RT multivesicular body biogenesis.";
RL Dev. Cell 17:234-243(2009).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting
CC complex required for transport II), which is required for
CC multivesicular body (MVB) formation and sorting of endosomal cargo
CC proteins into MVBs. The MVB pathway mediates delivery of
CC transmembrane proteins into the lumen of the lysosome for
CC degradation. The ESCRT-II complex is probably involved in the
CC recruitment of the ESCRT-III complex. The ESCRT-II complex may
CC also play a role in transcription regulation, possibly via its
CC interaction with ELL. The ESCRT-II complex may be involved in
CC facilitating the budding of certain RNA viruses.
CC -!- SUBUNIT: Component of a complex at least composed of ELL,
CC SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 (By similarity). Component
CC of the endosomal sorting complex required for transport II (ESCRT-
CC II), composed of SNF8, VPS36 and 2 copies of VPS25. Interacts with
CC CFTR; the interaction requires misfolded CFTR. Interacts (via C-
CC terminal half) with the ESCRT-III subunit CHMP6 (via N-terminal
CC half).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Nucleus,
CC nucleoplasm. Note=Distributes diffusely throughout the cytoplasm
CC and nucleoplasm, but exhibits a punctate distribution on
CC coexpression with CHMP6.
CC -!- TISSUE SPECIFICITY: Expressed at the mRNA level in kidney, liver,
CC pancreas, and placenta. Lower levels of expression are found in
CC heart, skeletal muscle, brain and lung.
CC -!- SIMILARITY: Belongs to the VPS25 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB014763; BAB87804.1; -; mRNA.
DR EMBL; AK312092; BAG35028.1; -; mRNA.
DR EMBL; CH471152; EAW60879.1; -; Genomic_DNA.
DR EMBL; BC006282; AAH06282.1; -; mRNA.
DR RefSeq; NP_115729.1; NM_032353.3.
DR UniGene; Hs.500165; -.
DR PDB; 2ZME; X-ray; 2.90 A; C/D=1-102.
DR PDB; 3CUQ; X-ray; 2.61 A; C/D=1-176.
DR PDB; 3HTU; X-ray; 2.00 A; A/C/E/G=102-176.
DR PDBsum; 2ZME; -.
DR PDBsum; 3CUQ; -.
DR PDBsum; 3HTU; -.
DR ProteinModelPortal; Q9BRG1; -.
DR SMR; Q9BRG1; 4-176.
DR IntAct; Q9BRG1; 4.
DR MINT; MINT-5003482; -.
DR STRING; 9606.ENSP00000253794; -.
DR PhosphoSite; Q9BRG1; -.
DR DMDM; 73920459; -.
DR PaxDb; Q9BRG1; -.
DR PeptideAtlas; Q9BRG1; -.
DR PRIDE; Q9BRG1; -.
DR DNASU; 84313; -.
DR Ensembl; ENST00000253794; ENSP00000253794; ENSG00000131475.
DR GeneID; 84313; -.
DR KEGG; hsa:84313; -.
DR UCSC; uc002ibi.3; human.
DR CTD; 84313; -.
DR GeneCards; GC17P040925; -.
DR HGNC; HGNC:28122; VPS25.
DR MIM; 610907; gene.
DR neXtProt; NX_Q9BRG1; -.
DR PharmGKB; PA142670614; -.
DR eggNOG; NOG270942; -.
DR HOGENOM; HOG000191978; -.
DR HOVERGEN; HBG080015; -.
DR InParanoid; Q9BRG1; -.
DR KO; K12189; -.
DR OMA; PPFFTIQ; -.
DR OrthoDB; EOG7BGHN9; -.
DR PhylomeDB; Q9BRG1; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR EvolutionaryTrace; Q9BRG1; -.
DR GeneWiki; VPS25; -.
DR GenomeRNAi; 84313; -.
DR NextBio; 74014; -.
DR PRO; PR:Q9BRG1; -.
DR ArrayExpress; Q9BRG1; -.
DR Bgee; Q9BRG1; -.
DR CleanEx; HS_VPS25; -.
DR Genevestigator; Q9BRG1; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.570; -; 1.
DR InterPro; IPR008570; ESCRT-II_cplx_vps25-sub.
DR InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR13149; PTHR13149; 1.
DR Pfam; PF05871; ESCRT-II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Endosome; Membrane;
KW Nucleus; Polymorphism; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1 176 Vacuolar protein-sorting-associated
FT protein 25.
FT /FTId=PRO_0000215216.
FT VARIANT 76 76 I -> V (in dbSNP:rs34494804).
FT /FTId=VAR_048940.
FT MUTAGEN 124 124 V->E: Abolishes binding to CHMP6.
FT MUTAGEN 126 126 T->K: Abolishes binding to CHMP6.
FT HELIX 9 12
FT HELIX 14 17
FT HELIX 23 44
FT STRAND 48 50
FT HELIX 51 55
FT STRAND 60 62
FT TURN 63 66
FT HELIX 71 84
FT STRAND 86 89
FT STRAND 91 99
FT HELIX 104 116
FT TURN 117 119
FT STRAND 123 125
FT HELIX 127 132
FT TURN 135 138
FT TURN 140 143
FT HELIX 146 158
FT STRAND 161 165
FT TURN 167 169
FT STRAND 172 175
SQ SEQUENCE 176 AA; 20748 MW; 34963A53C3DA4DD5 CRC64;
MAMSFEWPWQ YRFPPFFTLQ PNVDTRQKQL AAWCSLVLSF CRLHKQSSMT VMEAQESPLF
NNVKLQRKLP VESIQIVLEE LRKKGNLEWL DKSKSSFLIM WRRPEEWGKL IYQWVSRSGQ
NNSVFTLYEL TNGEDTEDEE FHGLDEATLL RALQALQQEH KAEIITVSDG RGVKFF
//
ID VPS25_HUMAN Reviewed; 176 AA.
AC Q9BRG1; B2R581;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Vacuolar protein-sorting-associated protein 25;
DE Short=hVps25;
DE AltName: Full=Dermal papilla-derived protein 9;
DE AltName: Full=ELL-associated protein of 20 kDa;
DE AltName: Full=ESCRT-II complex subunit VPS25;
GN Name=VPS25; Synonyms=DERP9, EAP20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Ukai Y., Yamashita M., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SNF8; VPS36 AND CHMP6.
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 [6]
RP IDENTIFICATION IN THE ESCRT-II COMPLEX, AND INTERACTION WITH VPS36;
RP SNF8 AND CHMP6.
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
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [7]
RP ERRATUM.
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 [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP6.
RX PubMed=15511219; DOI=10.1042/BJ20041227;
RA Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K.,
RA Kobayashi T., Uchiyama Y., Maki M.;
RT "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly
RT with an ESCRT-II component EAP20 and regulates endosomal cargo
RT sorting.";
RL Biochem. J. 387:17-26(2005).
RN [9]
RP INTERACTION WITH MISFOLDED CFTR.
RX PubMed=15007060; DOI=10.1083/jcb.200312018;
RA Sharma M., Pampinella F., Nemes C., Benharouga M., So J., Du K.,
RA Bache K.G., Papsin B., Zerangue N., Stenmark H., Lukacs G.L.;
RT "Misfolding diverts CFTR from recycling to degradation: quality
RT control at early endosomes.";
RL J. Cell Biol. 164:923-933(2004).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=16889659; DOI=10.1186/1471-2148-6-59;
RA Slater R., Bishop N.E.;
RT "Genetic structure and evolution of the Vps25 family, a yeast ESCRT-II
RT component.";
RL BMC Evol. Biol. 6:59-59(2006).
RN [11]
RP INTERACTION WITH SNF8; VPS36 AND CHMP6, AND SUBCELLULAR LOCATION.
RX PubMed=16973552; DOI=10.1128/JVI.01049-06;
RA Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I.,
RA White P.L., Hill C.P., Kaplan J., Ward D., Sundquist W.I.;
RT "Human ESCRT-II complex and its role in human immunodeficiency virus
RT type 1 release.";
RL J. Virol. 80:9465-9480(2006).
RN [12]
RP FUNCTION.
RX PubMed=18723511; DOI=10.1074/jbc.M804157200;
RA Pincetic A., Medina G., Carter C., Leis J.;
RT "Avian sarcoma virus and human immunodeficiency virus, type 1 use
RT different subsets of ESCRT proteins to facilitate the budding
RT process.";
RL J. Biol. Chem. 283:29822-29830(2008).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN COMPLEX WITH SNF8 AND VPS36.
RX PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004;
RA Im Y.J., Hurley J.H.;
RT "Integrated structural model and membrane targeting mechanism of the
RT human ESCRT-II complex.";
RL Dev. Cell 14:902-913(2008).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 102-176 IN COMPLEX WITH
RP CHMP6, AND MUTAGENESIS OF VAL-124 AND THR-126.
RX PubMed=19686684; DOI=10.1016/j.devcel.2009.07.008;
RA Im Y.J., Wollert T., Boura E., Hurley J.H.;
RT "Structure and function of the ESCRT-II-III interface in
RT multivesicular body biogenesis.";
RL Dev. Cell 17:234-243(2009).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting
CC complex required for transport II), which is required for
CC multivesicular body (MVB) formation and sorting of endosomal cargo
CC proteins into MVBs. The MVB pathway mediates delivery of
CC transmembrane proteins into the lumen of the lysosome for
CC degradation. The ESCRT-II complex is probably involved in the
CC recruitment of the ESCRT-III complex. The ESCRT-II complex may
CC also play a role in transcription regulation, possibly via its
CC interaction with ELL. The ESCRT-II complex may be involved in
CC facilitating the budding of certain RNA viruses.
CC -!- SUBUNIT: Component of a complex at least composed of ELL,
CC SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 (By similarity). Component
CC of the endosomal sorting complex required for transport II (ESCRT-
CC II), composed of SNF8, VPS36 and 2 copies of VPS25. Interacts with
CC CFTR; the interaction requires misfolded CFTR. Interacts (via C-
CC terminal half) with the ESCRT-III subunit CHMP6 (via N-terminal
CC half).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Nucleus,
CC nucleoplasm. Note=Distributes diffusely throughout the cytoplasm
CC and nucleoplasm, but exhibits a punctate distribution on
CC coexpression with CHMP6.
CC -!- TISSUE SPECIFICITY: Expressed at the mRNA level in kidney, liver,
CC pancreas, and placenta. Lower levels of expression are found in
CC heart, skeletal muscle, brain and lung.
CC -!- SIMILARITY: Belongs to the VPS25 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB014763; BAB87804.1; -; mRNA.
DR EMBL; AK312092; BAG35028.1; -; mRNA.
DR EMBL; CH471152; EAW60879.1; -; Genomic_DNA.
DR EMBL; BC006282; AAH06282.1; -; mRNA.
DR RefSeq; NP_115729.1; NM_032353.3.
DR UniGene; Hs.500165; -.
DR PDB; 2ZME; X-ray; 2.90 A; C/D=1-102.
DR PDB; 3CUQ; X-ray; 2.61 A; C/D=1-176.
DR PDB; 3HTU; X-ray; 2.00 A; A/C/E/G=102-176.
DR PDBsum; 2ZME; -.
DR PDBsum; 3CUQ; -.
DR PDBsum; 3HTU; -.
DR ProteinModelPortal; Q9BRG1; -.
DR SMR; Q9BRG1; 4-176.
DR IntAct; Q9BRG1; 4.
DR MINT; MINT-5003482; -.
DR STRING; 9606.ENSP00000253794; -.
DR PhosphoSite; Q9BRG1; -.
DR DMDM; 73920459; -.
DR PaxDb; Q9BRG1; -.
DR PeptideAtlas; Q9BRG1; -.
DR PRIDE; Q9BRG1; -.
DR DNASU; 84313; -.
DR Ensembl; ENST00000253794; ENSP00000253794; ENSG00000131475.
DR GeneID; 84313; -.
DR KEGG; hsa:84313; -.
DR UCSC; uc002ibi.3; human.
DR CTD; 84313; -.
DR GeneCards; GC17P040925; -.
DR HGNC; HGNC:28122; VPS25.
DR MIM; 610907; gene.
DR neXtProt; NX_Q9BRG1; -.
DR PharmGKB; PA142670614; -.
DR eggNOG; NOG270942; -.
DR HOGENOM; HOG000191978; -.
DR HOVERGEN; HBG080015; -.
DR InParanoid; Q9BRG1; -.
DR KO; K12189; -.
DR OMA; PPFFTIQ; -.
DR OrthoDB; EOG7BGHN9; -.
DR PhylomeDB; Q9BRG1; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR EvolutionaryTrace; Q9BRG1; -.
DR GeneWiki; VPS25; -.
DR GenomeRNAi; 84313; -.
DR NextBio; 74014; -.
DR PRO; PR:Q9BRG1; -.
DR ArrayExpress; Q9BRG1; -.
DR Bgee; Q9BRG1; -.
DR CleanEx; HS_VPS25; -.
DR Genevestigator; Q9BRG1; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.570; -; 1.
DR InterPro; IPR008570; ESCRT-II_cplx_vps25-sub.
DR InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR13149; PTHR13149; 1.
DR Pfam; PF05871; ESCRT-II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Endosome; Membrane;
KW Nucleus; Polymorphism; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1 176 Vacuolar protein-sorting-associated
FT protein 25.
FT /FTId=PRO_0000215216.
FT VARIANT 76 76 I -> V (in dbSNP:rs34494804).
FT /FTId=VAR_048940.
FT MUTAGEN 124 124 V->E: Abolishes binding to CHMP6.
FT MUTAGEN 126 126 T->K: Abolishes binding to CHMP6.
FT HELIX 9 12
FT HELIX 14 17
FT HELIX 23 44
FT STRAND 48 50
FT HELIX 51 55
FT STRAND 60 62
FT TURN 63 66
FT HELIX 71 84
FT STRAND 86 89
FT STRAND 91 99
FT HELIX 104 116
FT TURN 117 119
FT STRAND 123 125
FT HELIX 127 132
FT TURN 135 138
FT TURN 140 143
FT HELIX 146 158
FT STRAND 161 165
FT TURN 167 169
FT STRAND 172 175
SQ SEQUENCE 176 AA; 20748 MW; 34963A53C3DA4DD5 CRC64;
MAMSFEWPWQ YRFPPFFTLQ PNVDTRQKQL AAWCSLVLSF CRLHKQSSMT VMEAQESPLF
NNVKLQRKLP VESIQIVLEE LRKKGNLEWL DKSKSSFLIM WRRPEEWGKL IYQWVSRSGQ
NNSVFTLYEL TNGEDTEDEE FHGLDEATLL RALQALQQEH KAEIITVSDG RGVKFF
//
MIM
610907
*RECORD*
*FIELD* NO
610907
*FIELD* TI
*610907 VACUOLAR PROTEIN SORTING 25, S. CEREVISIAE, HOMOLOG OF; VPS25
;;ELL-ASSOCIATED PROTEIN, 20-KD; EAP20
read more*FIELD* TX
DESCRIPTION
VPS25, VPS36 (610903), and SNF8 (610904) form ESCRT-II (endosomal
sorting complex required for transport II), a complex involved in
endocytosis of ubiquitinated membrane proteins. VPS25, VPS36, and SNF8
are also associated in a multiprotein complex with RNA polymerase II
elongation factor (ELL; 600284) (Slagsvold et al., 2005; Kamura et al.,
2001).
CLONING
Kamura et al. (2001) purified the Ell-containing complex from rat liver
extracts, and by peptide sequencing and database analysis, they
identified mouse and human VPS25, which they called EAP20. The deduced
mouse and human proteins contain 176 amino acids, have calculated
molecular masses of 21 kD, and are identical.
GENE FUNCTION
Using mouse proteins expressed in mammalian and insect cells, Kamura et
al. (2001) found that Eap30 (SNF8) and Eap20 could be
coimmunoprecipitated in the absence of Eap45 (VPS36), and that Eap20 and
Eap45 could be coimmunoprecipitated in the absence of Eap30. However,
little Eap30 was coimmunoprecipitated with Eap45 in the absence of
Eap20. Kamura et al. (2001) concluded that EAP20 bridges EAP30 and EAP45
and thereby nucleates assembly of the EAP complex.
By coimmunoprecipitation of epitope-tagged proteins expressed in HEK293
cells, Yorikawa et al. (2005) showed that CHMP6 (610901) interacted with
CHMP4B (610897) and EAP20. In vitro pull-down assays using recombinant
proteins demonstrated direct physical interaction that was mediated by
the N-terminal basic half of CHMP6. Epitope-tagged EAP20 localized
diffusely in transfected HeLa cells, but it exhibited a punctate
distribution when coexpressed with CHMP6.
MAPPING
Hartz (2007) mapped the VPS25 gene to chromosome 17q21.3 based on an
alignment of the VPS25 sequence (GenBank GENBANK AB014763) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/2/2007.
2. Kamura, T.; Burian, D.; Khalili, H.; Schmidt, S. L.; Sato, S.;
Liu, W.-J.; Conrad, M. N.; Conaway, R. C.; Conaway, J. W.; Shilatifard,
A.: Cloning and characterization of ELL-associated proteins EAP45
and EAP20: a role for yeast EAP-like proteins in regulation of gene
expression by glucose. J. Biol. Chem. 276: 16528-16533, 2001.
3. Slagsvold, T.; Aasland, R.; Hirano, S.; Bache, K. G.; Raiborg,
C.; Trambaiolo, D.; Wakatsuki, S.; Stenmark, H.: Eap45 in mammalian
ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain. J.
Biol. Chem. 280: 19600-19606, 2005.
4. Yorikawa, C.; Shibata, H.; Waguri, S.; Hatta, K.; Horii, M.; Katoh,
K.; Kobayashi, T.; Uchiyama, Y.; Maki, M.: Human CHMP6, a myristoylated
ESCRT-III protein, interacts directly with an ESCRT-II component EAP20
and regulates endosomal cargo sorting. Biochem. J. 387: 17-26, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2007
*FIELD* ED
mgross: 04/02/2007
*RECORD*
*FIELD* NO
610907
*FIELD* TI
*610907 VACUOLAR PROTEIN SORTING 25, S. CEREVISIAE, HOMOLOG OF; VPS25
;;ELL-ASSOCIATED PROTEIN, 20-KD; EAP20
read more*FIELD* TX
DESCRIPTION
VPS25, VPS36 (610903), and SNF8 (610904) form ESCRT-II (endosomal
sorting complex required for transport II), a complex involved in
endocytosis of ubiquitinated membrane proteins. VPS25, VPS36, and SNF8
are also associated in a multiprotein complex with RNA polymerase II
elongation factor (ELL; 600284) (Slagsvold et al., 2005; Kamura et al.,
2001).
CLONING
Kamura et al. (2001) purified the Ell-containing complex from rat liver
extracts, and by peptide sequencing and database analysis, they
identified mouse and human VPS25, which they called EAP20. The deduced
mouse and human proteins contain 176 amino acids, have calculated
molecular masses of 21 kD, and are identical.
GENE FUNCTION
Using mouse proteins expressed in mammalian and insect cells, Kamura et
al. (2001) found that Eap30 (SNF8) and Eap20 could be
coimmunoprecipitated in the absence of Eap45 (VPS36), and that Eap20 and
Eap45 could be coimmunoprecipitated in the absence of Eap30. However,
little Eap30 was coimmunoprecipitated with Eap45 in the absence of
Eap20. Kamura et al. (2001) concluded that EAP20 bridges EAP30 and EAP45
and thereby nucleates assembly of the EAP complex.
By coimmunoprecipitation of epitope-tagged proteins expressed in HEK293
cells, Yorikawa et al. (2005) showed that CHMP6 (610901) interacted with
CHMP4B (610897) and EAP20. In vitro pull-down assays using recombinant
proteins demonstrated direct physical interaction that was mediated by
the N-terminal basic half of CHMP6. Epitope-tagged EAP20 localized
diffusely in transfected HeLa cells, but it exhibited a punctate
distribution when coexpressed with CHMP6.
MAPPING
Hartz (2007) mapped the VPS25 gene to chromosome 17q21.3 based on an
alignment of the VPS25 sequence (GenBank GENBANK AB014763) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/2/2007.
2. Kamura, T.; Burian, D.; Khalili, H.; Schmidt, S. L.; Sato, S.;
Liu, W.-J.; Conrad, M. N.; Conaway, R. C.; Conaway, J. W.; Shilatifard,
A.: Cloning and characterization of ELL-associated proteins EAP45
and EAP20: a role for yeast EAP-like proteins in regulation of gene
expression by glucose. J. Biol. Chem. 276: 16528-16533, 2001.
3. Slagsvold, T.; Aasland, R.; Hirano, S.; Bache, K. G.; Raiborg,
C.; Trambaiolo, D.; Wakatsuki, S.; Stenmark, H.: Eap45 in mammalian
ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain. J.
Biol. Chem. 280: 19600-19606, 2005.
4. Yorikawa, C.; Shibata, H.; Waguri, S.; Hatta, K.; Horii, M.; Katoh,
K.; Kobayashi, T.; Uchiyama, Y.; Maki, M.: Human CHMP6, a myristoylated
ESCRT-III protein, interacts directly with an ESCRT-II component EAP20
and regulates endosomal cargo sorting. Biochem. J. 387: 17-26, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2007
*FIELD* ED
mgross: 04/02/2007