Full text data of SNF8
SNF8
(EAP30)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Vacuolar-sorting protein SNF8 (ELL-associated protein of 30 kDa; ESCRT-II complex subunit VPS22; hVps22)
Vacuolar-sorting protein SNF8 (ELL-associated protein of 30 kDa; ESCRT-II complex subunit VPS22; hVps22)
UniProt
Q96H20
ID SNF8_HUMAN Reviewed; 258 AA.
AC Q96H20; Q8IXY3; Q9UN50;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Vacuolar-sorting protein SNF8;
DE AltName: Full=ELL-associated protein of 30 kDa;
DE AltName: Full=ESCRT-II complex subunit VPS22;
DE Short=hVps22;
GN Name=SNF8; Synonyms=EAP30;
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].
RX PubMed=10419521; DOI=10.1074/jbc.274.31.21981;
RA Schmidt A.E., Miller T., Schmidt S.L., Shiekhattar R., Shilatifard A.;
RT "Cloning and characterization of the EAP30 subunit of the ELL complex
RT that confers derepression of transcription by RNA polymerase II.";
RL J. Biol. Chem. 274:21981-21985(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pancreas, and Placenta;
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 [3]
RP SELF-ASSOCIATION, AND INTERACTION WITH VPS25; VPS36 AND TSG101.
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 [4]
RP IDENTIFICATION IN THE ESCRT-II COMPLEX, AND INTERACTION WITH VPS36 AND
RP VPS25.
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 [5]
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 [6]
RP INTERACTION WITH RILPL1, AND SUBCELLULAR LOCATION.
RX PubMed=16857164; DOI=10.1016/j.bbrc.2006.07.007;
RA Progida C., Spinosa M.R., De Luca A., Bucci C.;
RT "RILP interacts with the VPS22 component of the ESCRT-II complex.";
RL Biochem. Biophys. Res. Commun. 347:1074-1079(2006).
RN [7]
RP INTERACTION WITH VPS25; VPS36 AND RILPL1, AND SUBCELLULAR LOCATION.
RX PubMed=17010938; DOI=10.1016/j.bbrc.2006.09.064;
RA Wang T., Hong W.;
RT "RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their
RT membrane recruitment.";
RL Biochem. Biophys. Res. Commun. 350:413-423(2006).
RN [8]
RP INTERACTION WITH 14-3-3 PROTEINS.
RX PubMed=16260042; DOI=10.1016/j.jneumeth.2005.09.015;
RA Satoh J., Nanri Y., Yamamura T.;
RT "Rapid identification of 14-3-3-binding proteins by protein microarray
RT analysis.";
RL J. Neurosci. Methods 152:278-288(2006).
RN [9]
RP INTERACTION WITH VPS25; VPS36 AND TSG101, 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 [10]
RP FUNCTION.
RX PubMed=17959629; DOI=10.1242/jcs.017301;
RA Progida C., Malerod L., Stuffers S., Brech A., Bucci C., Stenmark H.;
RT "RILP is required for the proper morphology and function of late
RT endosomes.";
RL J. Cell Sci. 120:3729-3737(2007).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17714434; DOI=10.1111/j.1600-0854.2007.00630.x;
RA Maleroed L., Stuffers S., Brech A., Stenmark H.;
RT "Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor
RT and chemokine receptors destined for lysosomal degradation.";
RL Traffic 8:1617-1629(2007).
RN [12]
RP FUNCTION.
RX PubMed=18031739; DOI=10.1016/j.yexcr.2007.10.014;
RA Raiborg C., Malerod L., Pedersen N.M., Stenmark H.;
RT "Differential functions of Hrs and ESCRT proteins in endocytic
RT membrane trafficking.";
RL Exp. Cell Res. 314:801-813(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) OF 25-258 IN COMPLEX WITH VPS25
RP 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).
CC -!- FUNCTION: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs.
CC The MVB pathway mediates delivery of transmembrane proteins into
CC the lumen of the lysosome for degradation. The ESCRT-II complex is
CC probably involved in the recruitment of the ESCRT-III complex. The
CC ESCRT-II complex may also play a role in transcription regulation
CC by participating in derepression of transcription by RNA
CC polymerase II, possibly via its interaction with ELL. Required for
CC degradation of both endocytosed EGF and EGFR, but not for the EGFR
CC ligand-mediated internalization. It is also required for the
CC degradation of CXCR4.
CC -!- SUBUNIT: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II), composed of SNF8, VPS25 and VPS36. SNF8
CC is essential for the stability of the ESCRT-II complex. ESCRT-II
CC interacts with ELL. Interacts with TSG101 (via the C-terminal
CC domain). Interacts with RILPL1 (via the N-terminal domain); which
CC recruits ESCRT-II to the endosome membranes. Interacts with 14-3-3
CC proteins.
CC -!- INTERACTION:
CC P55199:ELL; NbExp=3; IntAct=EBI-747719, EBI-1245868;
CC O60341:KDM1A; NbExp=2; IntAct=EBI-747719, EBI-710124;
CC P49736:MCM2; NbExp=8; IntAct=EBI-747719, EBI-374819;
CC P24928:POLR2A; NbExp=2; IntAct=EBI-747719, EBI-295301;
CC Q96LA8:PRMT6; NbExp=2; IntAct=EBI-747719, EBI-912440;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Nucleus
CC (Probable). Late endosome membrane. Note=Recruited to the endosome
CC membrane to participate in vesicle formation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96H20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96H20-2; Sequence=VSP_015340;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the SNF8 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; AF156102; AAD46560.1; -; mRNA.
DR EMBL; BC008976; AAH08976.1; -; mRNA.
DR EMBL; BC038830; AAH38830.1; -; mRNA.
DR RefSeq; NP_009172.2; NM_007241.2.
DR UniGene; Hs.127249; -.
DR PDB; 2ZME; X-ray; 2.90 A; A=1-258.
DR PDB; 3CUQ; X-ray; 2.61 A; A=25-258.
DR PDBsum; 2ZME; -.
DR PDBsum; 3CUQ; -.
DR ProteinModelPortal; Q96H20; -.
DR SMR; Q96H20; 34-252.
DR IntAct; Q96H20; 10.
DR MINT; MINT-5001874; -.
DR STRING; 9606.ENSP00000290330; -.
DR PhosphoSite; Q96H20; -.
DR DMDM; 73919323; -.
DR PaxDb; Q96H20; -.
DR PRIDE; Q96H20; -.
DR DNASU; 11267; -.
DR Ensembl; ENST00000290330; ENSP00000290330; ENSG00000159210.
DR Ensembl; ENST00000502492; ENSP00000421380; ENSG00000159210.
DR GeneID; 11267; -.
DR KEGG; hsa:11267; -.
DR UCSC; uc002ioj.3; human.
DR CTD; 11267; -.
DR GeneCards; GC17M047007; -.
DR H-InvDB; HIX0135631; -.
DR HGNC; HGNC:17028; SNF8.
DR MIM; 610904; gene.
DR neXtProt; NX_Q96H20; -.
DR PharmGKB; PA142670892; -.
DR eggNOG; NOG318316; -.
DR HOGENOM; HOG000170930; -.
DR HOVERGEN; HBG079872; -.
DR InParanoid; Q96H20; -.
DR KO; K12188; -.
DR OMA; QFQEMCA; -.
DR OrthoDB; EOG73FQNG; -.
DR PhylomeDB; Q96H20; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR EvolutionaryTrace; Q96H20; -.
DR GeneWiki; SNF8; -.
DR GenomeRNAi; 11267; -.
DR NextBio; 42875; -.
DR PRO; PR:Q96H20; -.
DR ArrayExpress; Q96H20; -.
DR Bgee; Q96H20; -.
DR CleanEx; HS_SNF8; -.
DR Genevestigator; Q96H20; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR GO; GO:0008134; F:transcription factor binding; IDA:MGI.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR007286; EAP30.
DR InterPro; IPR016689; ESCRT-2_cplx_Snf8.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR12806; PTHR12806; 1.
DR Pfam; PF04157; EAP30; 1.
DR PIRSF; PIRSF017215; ESCRT2_Vps22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Endosome; Membrane; Nucleus; Protein transport;
KW Reference proteome; Transcription; Transcription regulation;
KW Transport.
FT CHAIN 1 258 Vacuolar-sorting protein SNF8.
FT /FTId=PRO_0000215209.
FT COILED 27 53 Potential.
FT VAR_SEQ 189 189 Missing (in isoform 2).
FT /FTId=VSP_015340.
FT CONFLICT 250 250 A -> P (in Ref. 1; AAD46560).
FT HELIX 37 60
FT HELIX 62 75
FT HELIX 86 91
FT HELIX 93 115
FT STRAND 116 120
FT HELIX 121 130
FT TURN 131 134
FT HELIX 141 151
FT HELIX 152 154
FT STRAND 155 157
FT STRAND 159 163
FT STRAND 166 170
FT HELIX 178 187
FT TURN 188 190
FT STRAND 191 193
FT HELIX 195 202
FT HELIX 206 218
FT STRAND 223 231
FT STRAND 233 235
FT HELIX 249 251
SQ SEQUENCE 258 AA; 28864 MW; FD6CBA6BC0A4485E CRC64;
MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK
NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT
LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH
TVVLQLAEKN GYVTVSEIKA SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF
TDLYSQEITA EEAREALP
//
ID SNF8_HUMAN Reviewed; 258 AA.
AC Q96H20; Q8IXY3; Q9UN50;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Vacuolar-sorting protein SNF8;
DE AltName: Full=ELL-associated protein of 30 kDa;
DE AltName: Full=ESCRT-II complex subunit VPS22;
DE Short=hVps22;
GN Name=SNF8; Synonyms=EAP30;
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].
RX PubMed=10419521; DOI=10.1074/jbc.274.31.21981;
RA Schmidt A.E., Miller T., Schmidt S.L., Shiekhattar R., Shilatifard A.;
RT "Cloning and characterization of the EAP30 subunit of the ELL complex
RT that confers derepression of transcription by RNA polymerase II.";
RL J. Biol. Chem. 274:21981-21985(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pancreas, and Placenta;
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 [3]
RP SELF-ASSOCIATION, AND INTERACTION WITH VPS25; VPS36 AND TSG101.
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 [4]
RP IDENTIFICATION IN THE ESCRT-II COMPLEX, AND INTERACTION WITH VPS36 AND
RP VPS25.
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 [5]
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 [6]
RP INTERACTION WITH RILPL1, AND SUBCELLULAR LOCATION.
RX PubMed=16857164; DOI=10.1016/j.bbrc.2006.07.007;
RA Progida C., Spinosa M.R., De Luca A., Bucci C.;
RT "RILP interacts with the VPS22 component of the ESCRT-II complex.";
RL Biochem. Biophys. Res. Commun. 347:1074-1079(2006).
RN [7]
RP INTERACTION WITH VPS25; VPS36 AND RILPL1, AND SUBCELLULAR LOCATION.
RX PubMed=17010938; DOI=10.1016/j.bbrc.2006.09.064;
RA Wang T., Hong W.;
RT "RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their
RT membrane recruitment.";
RL Biochem. Biophys. Res. Commun. 350:413-423(2006).
RN [8]
RP INTERACTION WITH 14-3-3 PROTEINS.
RX PubMed=16260042; DOI=10.1016/j.jneumeth.2005.09.015;
RA Satoh J., Nanri Y., Yamamura T.;
RT "Rapid identification of 14-3-3-binding proteins by protein microarray
RT analysis.";
RL J. Neurosci. Methods 152:278-288(2006).
RN [9]
RP INTERACTION WITH VPS25; VPS36 AND TSG101, 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 [10]
RP FUNCTION.
RX PubMed=17959629; DOI=10.1242/jcs.017301;
RA Progida C., Malerod L., Stuffers S., Brech A., Bucci C., Stenmark H.;
RT "RILP is required for the proper morphology and function of late
RT endosomes.";
RL J. Cell Sci. 120:3729-3737(2007).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17714434; DOI=10.1111/j.1600-0854.2007.00630.x;
RA Maleroed L., Stuffers S., Brech A., Stenmark H.;
RT "Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor
RT and chemokine receptors destined for lysosomal degradation.";
RL Traffic 8:1617-1629(2007).
RN [12]
RP FUNCTION.
RX PubMed=18031739; DOI=10.1016/j.yexcr.2007.10.014;
RA Raiborg C., Malerod L., Pedersen N.M., Stenmark H.;
RT "Differential functions of Hrs and ESCRT proteins in endocytic
RT membrane trafficking.";
RL Exp. Cell Res. 314:801-813(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) OF 25-258 IN COMPLEX WITH VPS25
RP 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).
CC -!- FUNCTION: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs.
CC The MVB pathway mediates delivery of transmembrane proteins into
CC the lumen of the lysosome for degradation. The ESCRT-II complex is
CC probably involved in the recruitment of the ESCRT-III complex. The
CC ESCRT-II complex may also play a role in transcription regulation
CC by participating in derepression of transcription by RNA
CC polymerase II, possibly via its interaction with ELL. Required for
CC degradation of both endocytosed EGF and EGFR, but not for the EGFR
CC ligand-mediated internalization. It is also required for the
CC degradation of CXCR4.
CC -!- SUBUNIT: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II), composed of SNF8, VPS25 and VPS36. SNF8
CC is essential for the stability of the ESCRT-II complex. ESCRT-II
CC interacts with ELL. Interacts with TSG101 (via the C-terminal
CC domain). Interacts with RILPL1 (via the N-terminal domain); which
CC recruits ESCRT-II to the endosome membranes. Interacts with 14-3-3
CC proteins.
CC -!- INTERACTION:
CC P55199:ELL; NbExp=3; IntAct=EBI-747719, EBI-1245868;
CC O60341:KDM1A; NbExp=2; IntAct=EBI-747719, EBI-710124;
CC P49736:MCM2; NbExp=8; IntAct=EBI-747719, EBI-374819;
CC P24928:POLR2A; NbExp=2; IntAct=EBI-747719, EBI-295301;
CC Q96LA8:PRMT6; NbExp=2; IntAct=EBI-747719, EBI-912440;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Nucleus
CC (Probable). Late endosome membrane. Note=Recruited to the endosome
CC membrane to participate in vesicle formation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96H20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96H20-2; Sequence=VSP_015340;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the SNF8 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; AF156102; AAD46560.1; -; mRNA.
DR EMBL; BC008976; AAH08976.1; -; mRNA.
DR EMBL; BC038830; AAH38830.1; -; mRNA.
DR RefSeq; NP_009172.2; NM_007241.2.
DR UniGene; Hs.127249; -.
DR PDB; 2ZME; X-ray; 2.90 A; A=1-258.
DR PDB; 3CUQ; X-ray; 2.61 A; A=25-258.
DR PDBsum; 2ZME; -.
DR PDBsum; 3CUQ; -.
DR ProteinModelPortal; Q96H20; -.
DR SMR; Q96H20; 34-252.
DR IntAct; Q96H20; 10.
DR MINT; MINT-5001874; -.
DR STRING; 9606.ENSP00000290330; -.
DR PhosphoSite; Q96H20; -.
DR DMDM; 73919323; -.
DR PaxDb; Q96H20; -.
DR PRIDE; Q96H20; -.
DR DNASU; 11267; -.
DR Ensembl; ENST00000290330; ENSP00000290330; ENSG00000159210.
DR Ensembl; ENST00000502492; ENSP00000421380; ENSG00000159210.
DR GeneID; 11267; -.
DR KEGG; hsa:11267; -.
DR UCSC; uc002ioj.3; human.
DR CTD; 11267; -.
DR GeneCards; GC17M047007; -.
DR H-InvDB; HIX0135631; -.
DR HGNC; HGNC:17028; SNF8.
DR MIM; 610904; gene.
DR neXtProt; NX_Q96H20; -.
DR PharmGKB; PA142670892; -.
DR eggNOG; NOG318316; -.
DR HOGENOM; HOG000170930; -.
DR HOVERGEN; HBG079872; -.
DR InParanoid; Q96H20; -.
DR KO; K12188; -.
DR OMA; QFQEMCA; -.
DR OrthoDB; EOG73FQNG; -.
DR PhylomeDB; Q96H20; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR EvolutionaryTrace; Q96H20; -.
DR GeneWiki; SNF8; -.
DR GenomeRNAi; 11267; -.
DR NextBio; 42875; -.
DR PRO; PR:Q96H20; -.
DR ArrayExpress; Q96H20; -.
DR Bgee; Q96H20; -.
DR CleanEx; HS_SNF8; -.
DR Genevestigator; Q96H20; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR GO; GO:0008134; F:transcription factor binding; IDA:MGI.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR007286; EAP30.
DR InterPro; IPR016689; ESCRT-2_cplx_Snf8.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR12806; PTHR12806; 1.
DR Pfam; PF04157; EAP30; 1.
DR PIRSF; PIRSF017215; ESCRT2_Vps22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Endosome; Membrane; Nucleus; Protein transport;
KW Reference proteome; Transcription; Transcription regulation;
KW Transport.
FT CHAIN 1 258 Vacuolar-sorting protein SNF8.
FT /FTId=PRO_0000215209.
FT COILED 27 53 Potential.
FT VAR_SEQ 189 189 Missing (in isoform 2).
FT /FTId=VSP_015340.
FT CONFLICT 250 250 A -> P (in Ref. 1; AAD46560).
FT HELIX 37 60
FT HELIX 62 75
FT HELIX 86 91
FT HELIX 93 115
FT STRAND 116 120
FT HELIX 121 130
FT TURN 131 134
FT HELIX 141 151
FT HELIX 152 154
FT STRAND 155 157
FT STRAND 159 163
FT STRAND 166 170
FT HELIX 178 187
FT TURN 188 190
FT STRAND 191 193
FT HELIX 195 202
FT HELIX 206 218
FT STRAND 223 231
FT STRAND 233 235
FT HELIX 249 251
SQ SEQUENCE 258 AA; 28864 MW; FD6CBA6BC0A4485E CRC64;
MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK
NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT
LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH
TVVLQLAEKN GYVTVSEIKA SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF
TDLYSQEITA EEAREALP
//
MIM
610904
*RECORD*
*FIELD* NO
610904
*FIELD* TI
*610904 SNF8, S. CEREVISIAE, HOMOLOG OF; SNF8
;;VACUOLAR PROTEIN SORTING 22, S. CEREVISIAE, HOMOLOG OF; VPS22;;
read moreELL-ASSOCIATED PROTEIN, 30-KD; EAP30
*FIELD* TX
DESCRIPTION
SNF8, VPS25 (610907), and VPS36 (610903) form ESCRT-II (endosomal
sorting complex required for transport II), a complex involved in
endocytosis of ubiquitinated membrane proteins. SNF8, VPS25, and VPS36
are also associated in a multiprotein complex with RNA polymerase II
elongation factor (ELL; 600284) (Slagsvold et al., 2005; Kamura et al.,
2001).
CLONING
Schmidt et al. (1999) purified the Ell-containing complex from rat liver
extracts, and by peptide sequencing and EST database analysis, they
obtained a full-length cDNA encoding SNF8, which they called EAP30. The
deduced protein contains 258 amino acids.
GENE FUNCTION
Schmidt et al. (1999) found that recombinant EAP30 could interact with
recombinant ELL in vitro and derepress the inhibitory activity of ELL
against RNA polymerase II (see 180660).
Using mouse proteins expressed in mammalian and insect cells, Kamura et
al. (2001) found that Eap30 and Eap20 (VPS25) 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.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNF8
gene to chromosome 17 (TMAP D17S1827).
*FIELD* RF
1. 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.
2. Schmidt, A. E.; Miller, T.; Schmidt, S. L.; Shiekhattar, R.; Shilatifard,
A.: Cloning and characterization of the EAP30 subunit of the ELL
complex that confers derepression of transcription by RNA polymerase
II. J. Biol. Chem. 274: 21981-21985, 1999.
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.
*FIELD* CD
Patricia A. Hartz: 4/2/2007
*FIELD* ED
mgross: 02/20/2013
terry: 2/20/2013
mgross: 4/2/2007
*RECORD*
*FIELD* NO
610904
*FIELD* TI
*610904 SNF8, S. CEREVISIAE, HOMOLOG OF; SNF8
;;VACUOLAR PROTEIN SORTING 22, S. CEREVISIAE, HOMOLOG OF; VPS22;;
read moreELL-ASSOCIATED PROTEIN, 30-KD; EAP30
*FIELD* TX
DESCRIPTION
SNF8, VPS25 (610907), and VPS36 (610903) form ESCRT-II (endosomal
sorting complex required for transport II), a complex involved in
endocytosis of ubiquitinated membrane proteins. SNF8, VPS25, and VPS36
are also associated in a multiprotein complex with RNA polymerase II
elongation factor (ELL; 600284) (Slagsvold et al., 2005; Kamura et al.,
2001).
CLONING
Schmidt et al. (1999) purified the Ell-containing complex from rat liver
extracts, and by peptide sequencing and EST database analysis, they
obtained a full-length cDNA encoding SNF8, which they called EAP30. The
deduced protein contains 258 amino acids.
GENE FUNCTION
Schmidt et al. (1999) found that recombinant EAP30 could interact with
recombinant ELL in vitro and derepress the inhibitory activity of ELL
against RNA polymerase II (see 180660).
Using mouse proteins expressed in mammalian and insect cells, Kamura et
al. (2001) found that Eap30 and Eap20 (VPS25) 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.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNF8
gene to chromosome 17 (TMAP D17S1827).
*FIELD* RF
1. 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.
2. Schmidt, A. E.; Miller, T.; Schmidt, S. L.; Shiekhattar, R.; Shilatifard,
A.: Cloning and characterization of the EAP30 subunit of the ELL
complex that confers derepression of transcription by RNA polymerase
II. J. Biol. Chem. 274: 21981-21985, 1999.
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.
*FIELD* CD
Patricia A. Hartz: 4/2/2007
*FIELD* ED
mgross: 02/20/2013
terry: 2/20/2013
mgross: 4/2/2007