VPS36_HUMAN
ID VPS36_HUMAN Reviewed; 386 AA.
AC Q86VN1; A8K125; Q3ZCV7; Q5H9S1; Q5VXB6; Q9H8Z5; Q9Y3E3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Vacuolar protein-sorting-associated protein 36;
DE AltName: Full=ELL-associated protein of 45 kDa;
DE AltName: Full=ESCRT-II complex subunit VPS36;
GN Name=VPS36; Synonyms=C13orf9, EAP45; ORFNames=CGI-145;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 68-386.
RC TISSUE=Brain, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH VPS25; SNF8 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 [8]
RP IDENTIFICATION IN THE ESCRT-II COMPLEX, AND INTERACTION WITH VPS25; SNF8
RP 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 sorting
RT factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [9]
RP ERRATUM OF PUBMED:14519844.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [10]
RP INTERACTION WITH VPS25 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 [11]
RP INTERACTION WITH VPS25; SNF8 AND TSG101, UBIQUITIN-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16973552; DOI=10.1128/jvi.01049-06;
RA Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I., White P.L.,
RA Hill C.P., Kaplan J., Ward D., Sundquist W.I.;
RT "Human ESCRT-II complex and its role in human immunodeficiency virus type 1
RT release.";
RL J. Virol. 80:9465-9480(2006).
RN [12]
RP SUBCELLULAR LOCATION.
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 and
RT chemokine receptors destined for lysosomal degradation.";
RL Traffic 8:1617-1629(2007).
RN [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-138 IN COMPLEX WITH UBIQUITIN,
RP AND MUTAGENESIS OF LEU-10; VAL-67; PHE-68 AND GLU-70.
RX PubMed=17057716; DOI=10.1038/nsmb1160;
RA Alam S.L., Langelier C., Whitby F.G., Koirala S., Robinson H., Hill C.P.,
RA Sundquist W.I.;
RT "Structural basis for ubiquitin recognition by the human ESCRT-II EAP45
RT GLUE domain.";
RL Nat. Struct. Mol. Biol. 13:1029-1030(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 169-386 IN COMPLEX WITH VPS25 AND
RP SNF8.
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 human
RT ESCRT-II complex.";
RL Dev. Cell 14:902-913(2008).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC MVB pathway mediates delivery of transmembrane proteins into the lumen
CC of the lysosome for degradation. The ESCRT-II complex is probably
CC involved in the recruitment of the ESCRT-III complex. Its ability to
CC bind ubiquitin probably plays a role in endosomal sorting of
CC ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex
CC may also play a role in transcription regulation, possibly via its
CC interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.
CC -!- SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30,
CC VPS25/EAP20 and VPS36/EAP45 (By similarity). Component of the endosomal
CC sorting complex required for transport II (ESCRT-II), composed of SNF8,
CC VPS36 and two copies of VPS25 (PubMed:14519844). Interacts with VPS25,
CC SNF8, TSG101 and CHMP6 (PubMed:14505570, PubMed:14519844,
CC PubMed:16973552, PubMed:18539118). Interacts (via GLUE domain) with
CC ubiquitin (PubMed:17057716). Interacts with RILPL1 (via the C-terminal
CC domain); which recruits ESCRT-II to the endosome membranes
CC (PubMed:17010938). Interacts with ECPAS (PubMed:20682791).
CC {ECO:0000250|UniProtKB:P0C0A2, ECO:0000250|UniProtKB:Q91XD6,
CC ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
CC ECO:0000269|PubMed:16973552, ECO:0000269|PubMed:17010938,
CC ECO:0000269|PubMed:17057716, ECO:0000269|PubMed:18539118,
CC ECO:0000269|PubMed:20682791}.
CC -!- INTERACTION:
CC Q86VN1; Q96H20: SNF8; NbExp=6; IntAct=EBI-4401822, EBI-747719;
CC Q86VN1; Q9BRG1: VPS25; NbExp=6; IntAct=EBI-4401822, EBI-741945;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome. Late endosome
CC {ECO:0000250|UniProtKB:Q91XD6}. Membrane. Nucleus {ECO:0000305}.
CC Note=Colocalizes with ubiquitinated proteins on late endosomes.
CC Recruited to the endosome membrane to participate in vesicle formation.
CC {ECO:0000250|UniProtKB:Q91XD6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86VN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VN1-2; Sequence=VSP_015342;
CC -!- DOMAIN: The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates
CC binding to ubiquitin and phosphoinosides.
CC {ECO:0000250|UniProtKB:Q91XD6}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14451.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF151903; AAD34140.1; -; mRNA.
DR EMBL; AK023182; BAB14451.1; ALT_INIT; mRNA.
DR EMBL; AK289740; BAF82429.1; -; mRNA.
DR EMBL; CR933653; CAI45953.1; -; mRNA.
DR EMBL; AL359513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471274; EAW55895.1; -; Genomic_DNA.
DR EMBL; BC037279; AAH37279.1; -; mRNA.
DR EMBL; BC050439; AAH50439.1; -; mRNA.
DR CCDS; CCDS73577.1; -. [Q86VN1-2]
DR CCDS; CCDS9434.1; -. [Q86VN1-1]
DR RefSeq; NP_001269098.1; NM_001282169.1. [Q86VN1-2]
DR RefSeq; NP_057159.2; NM_016075.3. [Q86VN1-1]
DR PDB; 2HTH; X-ray; 2.70 A; B=1-138.
DR PDB; 2ZME; X-ray; 2.90 A; B=149-386.
DR PDB; 3CUQ; X-ray; 2.61 A; B=169-386.
DR PDBsum; 2HTH; -.
DR PDBsum; 2ZME; -.
DR PDBsum; 3CUQ; -.
DR AlphaFoldDB; Q86VN1; -.
DR SMR; Q86VN1; -.
DR BioGRID; 119234; 54.
DR ComplexPortal; CPX-2506; ESCRT-II complex.
DR CORUM; Q86VN1; -.
DR DIP; DIP-29249N; -.
DR IntAct; Q86VN1; 12.
DR MINT; Q86VN1; -.
DR STRING; 9606.ENSP00000367299; -.
DR iPTMnet; Q86VN1; -.
DR MetOSite; Q86VN1; -.
DR PhosphoSitePlus; Q86VN1; -.
DR BioMuta; VPS36; -.
DR DMDM; 73920464; -.
DR EPD; Q86VN1; -.
DR jPOST; Q86VN1; -.
DR MassIVE; Q86VN1; -.
DR MaxQB; Q86VN1; -.
DR PaxDb; Q86VN1; -.
DR PeptideAtlas; Q86VN1; -.
DR PRIDE; Q86VN1; -.
DR ProteomicsDB; 70043; -. [Q86VN1-1]
DR ProteomicsDB; 70044; -. [Q86VN1-2]
DR Antibodypedia; 24193; 73 antibodies from 20 providers.
DR DNASU; 51028; -.
DR Ensembl; ENST00000378060.9; ENSP00000367299.3; ENSG00000136100.14. [Q86VN1-1]
DR Ensembl; ENST00000611132.4; ENSP00000484968.1; ENSG00000136100.14. [Q86VN1-2]
DR GeneID; 51028; -.
DR KEGG; hsa:51028; -.
DR MANE-Select; ENST00000378060.9; ENSP00000367299.3; NM_016075.4; NP_057159.2.
DR UCSC; uc001vgq.4; human. [Q86VN1-1]
DR CTD; 51028; -.
DR DisGeNET; 51028; -.
DR GeneCards; VPS36; -.
DR HGNC; HGNC:20312; VPS36.
DR HPA; ENSG00000136100; Low tissue specificity.
DR MIM; 610903; gene.
DR neXtProt; NX_Q86VN1; -.
DR OpenTargets; ENSG00000136100; -.
DR PharmGKB; PA134990943; -.
DR VEuPathDB; HostDB:ENSG00000136100; -.
DR eggNOG; KOG2760; Eukaryota.
DR GeneTree; ENSGT00390000017209; -.
DR HOGENOM; CLU_015433_0_0_1; -.
DR InParanoid; Q86VN1; -.
DR OMA; TLNARVW; -.
DR OrthoDB; 981902at2759; -.
DR PhylomeDB; Q86VN1; -.
DR TreeFam; TF314770; -.
DR PathwayCommons; Q86VN1; -.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR SignaLink; Q86VN1; -.
DR BioGRID-ORCS; 51028; 84 hits in 1093 CRISPR screens.
DR ChiTaRS; VPS36; human.
DR EvolutionaryTrace; Q86VN1; -.
DR GeneWiki; VPS36; -.
DR GenomeRNAi; 51028; -.
DR Pharos; Q86VN1; Tbio.
DR PRO; PR:Q86VN1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q86VN1; protein.
DR Bgee; ENSG00000136100; Expressed in upper arm skin and 184 other tissues.
DR ExpressionAtlas; Q86VN1; baseline and differential.
DR Genevisible; Q86VN1; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0000814; C:ESCRT II complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR DisProt; DP02599; -.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID00218; -.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS51495; GLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endosome;
KW Lipid-binding; Membrane; Nucleus; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1..386
FT /note="Vacuolar protein-sorting-associated protein 36"
FT /id="PRO_0000215222"
FT DOMAIN 1..88
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 105..138
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT COILED 160..185
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015342"
FT MUTAGEN 10
FT /note="L->D: No effect on interaction with ubiquitin."
FT /evidence="ECO:0000269|PubMed:17057716"
FT MUTAGEN 67
FT /note="V->A: Reduces affinity for ubiquitin up to 10-fold."
FT /evidence="ECO:0000269|PubMed:17057716"
FT MUTAGEN 68
FT /note="F->A: Reduces affinity for ubiquitin up to 10-fold."
FT /evidence="ECO:0000269|PubMed:17057716"
FT MUTAGEN 70
FT /note="E->A: Reduces affinity for ubiquitin up to 10-fold."
FT /evidence="ECO:0000269|PubMed:17057716"
FT CONFLICT 185
FT /note="M -> V (in Ref. 3; CAI45953)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> R (in Ref. 1; AAD34140)"
FT /evidence="ECO:0000305"
FT STRAND 17..28
FT /evidence="ECO:0007829|PDB:2HTH"
FT STRAND 38..51
FT /evidence="ECO:0007829|PDB:2HTH"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2HTH"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2HTH"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2HTH"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2HTH"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2HTH"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2HTH"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:2HTH"
FT HELIX 175..193
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2ZME"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:3CUQ"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:3CUQ"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:3CUQ"
FT TURN 293..298
FT /evidence="ECO:0007829|PDB:3CUQ"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:3CUQ"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:3CUQ"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:3CUQ"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:3CUQ"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:3CUQ"
SQ SEQUENCE 386 AA; 43817 MW; 21E1E66F71BA7764 CRC64;
MDRFVWTSGL LEINETLVIQ QRGVRIYDGE EKIKFDAGTL LLSTHRLIWR DQKNHECCMA
ILLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS SKNSYIKLSF KEHGQIEFYR
RLSEEMTQRR WENMPVSQSL QTNRGPQPGR IRAVGIVGIE RKLEEKRKET DKNISEAFED
LSKLMIKAKE MVELSKSIAN KIKDKQGDIT EDETIRFKSY LLSMGIANPV TRETYGSGTQ
YHMQLAKQLA GILQVPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP
LRLRVFDSGV MVIELQSHKE EEMVASALET VSEKGSLTSE EFAKLVGMSV LLAKERLLLA
EKMGHLCRDD SVEGLRFYPN LFMTQS
