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 24-JAN-2024, entry version 177. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 57. 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; 9606-ENSP00000367299; -. DR PeptideAtlas; Q86VN1; -. DR ProteomicsDB; 70043; -. [Q86VN1-1] DR ProteomicsDB; 70044; -. [Q86VN1-2] DR Pumba; Q86VN1; -. DR Antibodypedia; 24193; 108 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 AGR; HGNC:20312; -. 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; 1423843at2759; -. 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; 86 hits in 1172 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 186 other cell types or tissues. DR ExpressionAtlas; Q86VN1; baseline and differential. 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:0043130; F:ubiquitin binding; IMP:UniProtKB. DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL. DR GO; GO:0090148; P:membrane fission; NAS: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 CDD; cd13226; PH-GRAM-like_Eap45; 1. DR DisProt; DP02599; -. DR Gene3D; 6.10.140.260; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. 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; VACUOLAR PROTEIN-SORTING-ASSOCIATED PROTEIN 36; 1. DR PANTHER; PTHR13128:SF12; VACUOLAR PROTEIN-SORTING-ASSOCIATED PROTEIN 36; 1. DR Pfam; PF04157; EAP30; 1. DR Pfam; PF11605; Vps36_ESCRT-II; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. DR PROSITE; PS51495; GLUE; 1. DR Genevisible; Q86VN1; HS. 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 //