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Q86VN1

- VPS36_HUMAN

UniProt

Q86VN1 - VPS36_HUMAN

Protein

Vacuolar protein-sorting-associated protein 36

Gene

VPS36

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.1 Publication

    GO - Molecular functioni

    1. phosphatidylinositol-3-phosphate binding Source: InterPro
    2. protein binding Source: UniProt

    GO - Biological processi

    1. endosomal transport Source: Reactome
    2. membrane organization Source: Reactome
    3. protein transport Source: UniProtKB-KW
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vacuolar protein-sorting-associated protein 36
    Alternative name(s):
    ELL-associated protein of 45 kDa
    ESCRT-II complex subunit VPS36
    Gene namesi
    Name:VPS36
    Synonyms:C13orf9, EAP45
    ORF Names:CGI-145
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:20312. VPS36.

    Subcellular locationi

    Cytoplasm. Endosome. Late endosome. Membrane. Nucleus Curated
    Note: Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. late endosome Source: UniProtKB-SubCell
    5. lysosome Source: Ensembl
    6. membrane Source: UniProtKB-SubCell
    7. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101L → D: No effect on interaction with ubiquitin. 1 Publication
    Mutagenesisi67 – 671V → A: Reduces affinity for ubiquitin up to 10-fold. 1 Publication
    Mutagenesisi68 – 681F → A: Reduces affinity for ubiquitin up to 10-fold. 1 Publication
    Mutagenesisi70 – 701E → A: Reduces affinity for ubiquitin up to 10-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA134990943.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386Vacuolar protein-sorting-associated protein 36PRO_0000215222Add
    BLAST

    Proteomic databases

    MaxQBiQ86VN1.
    PaxDbiQ86VN1.
    PRIDEiQ86VN1.

    PTM databases

    PhosphoSiteiQ86VN1.

    Expressioni

    Gene expression databases

    BgeeiQ86VN1.
    CleanExiHS_VPS36.
    GenevestigatoriQ86VN1.

    Organism-specific databases

    HPAiHPA039734.
    HPA043947.

    Interactioni

    Subunit structurei

    Component of a complex at least composed of ELL, SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 By similarity. Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS36 and two copies of VPS25. Interacts with VPS25, SNF8, TSG101 and VPS36. Interacts (via GLUE domain) with ubiquitin. Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes. Interacts with ECM29.By similarity8 Publications

    Protein-protein interaction databases

    BioGridi119234. 32 interactions.
    DIPiDIP-29249N.
    IntActiQ86VN1. 2 interactions.
    MINTiMINT-3085996.
    STRINGi9606.ENSP00000367299.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 2812
    Beta strandi38 – 5114
    Beta strandi59 – 624
    Helixi63 – 653
    Beta strandi66 – 727
    Beta strandi81 – 866
    Beta strandi93 – 953
    Beta strandi105 – 1106
    Helixi115 – 12814
    Helixi175 – 19319
    Helixi197 – 1993
    Helixi215 – 22410
    Helixi229 – 2324
    Helixi233 – 2353
    Helixi240 – 25920
    Beta strandi262 – 2654
    Helixi266 – 27510
    Beta strandi278 – 2803
    Helixi284 – 2929
    Turni293 – 2986
    Beta strandi300 – 3056
    Beta strandi309 – 3157
    Helixi320 – 3234
    Helixi324 – 33310
    Helixi339 – 3468
    Helixi350 – 36213
    Beta strandi365 – 3739
    Beta strandi375 – 3795
    Helixi381 – 3833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HTHX-ray2.70B1-138[»]
    2ZMEX-ray2.90B149-386[»]
    3CUQX-ray2.61B169-386[»]
    ProteinModelPortaliQ86VN1.
    SMRiQ86VN1. Positions 3-131, 172-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86VN1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8888GLUE N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 13834GLUE C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili160 – 18526Sequence AnalysisAdd
    BLAST

    Domaini

    The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates the binding to ubiquitin and phosphoinosides.1 Publication

    Sequence similaritiesi

    Belongs to the VPS36 family.Curated
    Contains 1 GLUE C-terminal domain.PROSITE-ProRule annotation
    Contains 1 GLUE N-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG262969.
    HOVERGENiHBG083632.
    InParanoidiQ86VN1.
    KOiK12190.
    OMAiCCIAIPL.
    OrthoDBiEOG7VB2FM.
    PhylomeDBiQ86VN1.
    TreeFamiTF314770.

    Family and domain databases

    Gene3Di1.10.10.10. 2 hits.
    InterProiIPR007286. EAP30.
    IPR021648. VPS36_GLUE.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF04157. EAP30. 1 hit.
    PF11605. Vps36_ESCRT-II. 1 hit.
    [Graphical view]
    PROSITEiPS51495. GLUE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86VN1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDRFVWTSGL LEINETLVIQ QRGVRIYDGE EKIKFDAGTL LLSTHRLIWR    50
    DQKNHECCMA ILLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS 100
    SKNSYIKLSF KEHGQIEFYR RLSEEMTQRR WENMPVSQSL QTNRGPQPGR 150
    IRAVGIVGIE RKLEEKRKET DKNISEAFED LSKLMIKAKE MVELSKSIAN 200
    KIKDKQGDIT EDETIRFKSY LLSMGIANPV TRETYGSGTQ YHMQLAKQLA 250
    GILQVPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP 300
    LRLRVFDSGV MVIELQSHKE EEMVASALET VSEKGSLTSE EFAKLVGMSV 350
    LLAKERLLLA EKMGHLCRDD SVEGLRFYPN LFMTQS 386
    Length:386
    Mass (Da):43,817
    Last modified:June 1, 2003 - v1
    Checksum:i21E1E66F71BA7764
    GO
    Isoform 2 (identifier: Q86VN1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-58: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):36,958
    Checksum:iF6078BBD25CC0032
    GO

    Sequence cautioni

    The sequence BAB14451.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851M → V in CAI45953. (PubMed:17974005)Curated
    Sequence conflicti223 – 2231S → R in AAD34140. (PubMed:10810093)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5858Missing in isoform 2. 1 PublicationVSP_015342Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151903 mRNA. Translation: AAD34140.1.
    AK023182 mRNA. Translation: BAB14451.1. Different initiation.
    AK289740 mRNA. Translation: BAF82429.1.
    CR933653 mRNA. Translation: CAI45953.1.
    AL359513 Genomic DNA. Translation: CAH71658.1.
    CH471274 Genomic DNA. Translation: EAW55895.1.
    BC037279 mRNA. Translation: AAH37279.1.
    BC050439 mRNA. Translation: AAH50439.1.
    CCDSiCCDS9434.1. [Q86VN1-1]
    RefSeqiNP_001269098.1. NM_001282169.1. [Q86VN1-2]
    NP_057159.2. NM_016075.3. [Q86VN1-1]
    UniGeneiHs.109520.

    Genome annotation databases

    EnsembliENST00000378060; ENSP00000367299; ENSG00000136100. [Q86VN1-1]
    GeneIDi51028.
    KEGGihsa:51028.
    UCSCiuc001vgq.3. human. [Q86VN1-1]

    Polymorphism databases

    DMDMi73920464.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151903 mRNA. Translation: AAD34140.1 .
    AK023182 mRNA. Translation: BAB14451.1 . Different initiation.
    AK289740 mRNA. Translation: BAF82429.1 .
    CR933653 mRNA. Translation: CAI45953.1 .
    AL359513 Genomic DNA. Translation: CAH71658.1 .
    CH471274 Genomic DNA. Translation: EAW55895.1 .
    BC037279 mRNA. Translation: AAH37279.1 .
    BC050439 mRNA. Translation: AAH50439.1 .
    CCDSi CCDS9434.1. [Q86VN1-1 ]
    RefSeqi NP_001269098.1. NM_001282169.1. [Q86VN1-2 ]
    NP_057159.2. NM_016075.3. [Q86VN1-1 ]
    UniGenei Hs.109520.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HTH X-ray 2.70 B 1-138 [» ]
    2ZME X-ray 2.90 B 149-386 [» ]
    3CUQ X-ray 2.61 B 169-386 [» ]
    ProteinModelPortali Q86VN1.
    SMRi Q86VN1. Positions 3-131, 172-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119234. 32 interactions.
    DIPi DIP-29249N.
    IntActi Q86VN1. 2 interactions.
    MINTi MINT-3085996.
    STRINGi 9606.ENSP00000367299.

    PTM databases

    PhosphoSitei Q86VN1.

    Polymorphism databases

    DMDMi 73920464.

    Proteomic databases

    MaxQBi Q86VN1.
    PaxDbi Q86VN1.
    PRIDEi Q86VN1.

    Protocols and materials databases

    DNASUi 51028.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378060 ; ENSP00000367299 ; ENSG00000136100 . [Q86VN1-1 ]
    GeneIDi 51028.
    KEGGi hsa:51028.
    UCSCi uc001vgq.3. human. [Q86VN1-1 ]

    Organism-specific databases

    CTDi 51028.
    GeneCardsi GC13M052986.
    HGNCi HGNC:20312. VPS36.
    HPAi HPA039734.
    HPA043947.
    MIMi 610903. gene.
    neXtProti NX_Q86VN1.
    PharmGKBi PA134990943.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262969.
    HOVERGENi HBG083632.
    InParanoidi Q86VN1.
    KOi K12190.
    OMAi CCIAIPL.
    OrthoDBi EOG7VB2FM.
    PhylomeDBi Q86VN1.
    TreeFami TF314770.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).

    Miscellaneous databases

    ChiTaRSi VPS36. human.
    EvolutionaryTracei Q86VN1.
    GeneWikii VPS36.
    GenomeRNAii 51028.
    NextBioi 53573.
    PROi Q86VN1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q86VN1.
    CleanExi HS_VPS36.
    Genevestigatori Q86VN1.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    InterProi IPR007286. EAP30.
    IPR021648. VPS36_GLUE.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF04157. EAP30. 1 hit.
    PF11605. Vps36_ESCRT-II. 1 hit.
    [Graphical view ]
    PROSITEi PS51495. GLUE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-386.
      Tissue: Brain and Teratocarcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Retina.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. Cited for: INTERACTION WITH VPS25; SNF8 AND TSG101.
    8. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ESCRT-II COMPLEX, INTERACTION WITH VPS36; SNF8 AND CHMP6.
    9. Erratum
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
    10. "Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain."
      Slagsvold T., Aasland R., Hirano S., Bache K.G., Raiborg C., Trambaiolo D., Wakatsuki S., Stenmark H.
      J. Biol. Chem. 280:19600-19606(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, INTERACTION WITH UBIQUITIN.
    11. "RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment."
      Wang T., Hong W.
      Biochem. Biophys. Res. Commun. 350:413-423(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS25 AND RILPL1, SUBCELLULAR LOCATION.
    12. "Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release."
      Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I., White P.L., Hill C.P., Kaplan J., Ward D., Sundquist W.I.
      J. Virol. 80:9465-9480(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS25; SNF8 AND TSG101, UBIQUITIN-BINDING, SUBCELLULAR LOCATION.
    13. "Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation."
      Maleroed L., Stuffers S., Brech A., Stenmark H.
      Traffic 8:1617-1629(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
      Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
      J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain."
      Alam S.L., Langelier C., Whitby F.G., Koirala S., Robinson H., Hill C.P., Sundquist W.I.
      Nat. Struct. Mol. Biol. 13:1029-1030(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-138 IN COMPLEX WITH UBIQUITIN, MUTAGENESIS OF LEU-10; VAL-67; PHE-68 AND GLU-70.
    17. "Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex."
      Im Y.J., Hurley J.H.
      Dev. Cell 14:902-913(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 169-386 IN COMPLEX WITH VPS25 AND SNF8.

    Entry informationi

    Entry nameiVPS36_HUMAN
    AccessioniPrimary (citable) accession number: Q86VN1
    Secondary accession number(s): A8K125
    , Q3ZCV7, Q5H9S1, Q5VXB6, Q9H8Z5, Q9Y3E3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3