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Q91XD6

- VPS36_MOUSE

UniProt

Q91XD6 - VPS36_MOUSE

Protein

Vacuolar protein-sorting-associated protein 36

Gene

Vps36

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. phosphatidylinositol-3-phosphate binding Source: InterPro
    2. ubiquitin binding Source: MGI

    GO - Biological processi

    1. endosomal transport Source: MGI
    2. protein transport Source: UniProtKB-KW
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vacuolar protein-sorting-associated protein 36
    Alternative name(s):
    ESCRT-II complex subunit VPS36
    Gene namesi
    Name:Vps36
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1917410. Vps36.

    Subcellular locationi

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

    GO - Cellular componenti

    1. late endosome Source: MGI
    2. lysosome Source: MGI
    3. membrane Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386Vacuolar protein-sorting-associated protein 36PRO_0000215223Add
    BLAST

    Proteomic databases

    MaxQBiQ91XD6.
    PaxDbiQ91XD6.
    PRIDEiQ91XD6.

    PTM databases

    PhosphoSiteiQ91XD6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ91XD6.
    BgeeiQ91XD6.
    CleanExiMM_VPS36.
    GenevestigatoriQ91XD6.

    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 By similarity. Interacts (via GLUE domain) with ubiquitin. Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes By similarity. Interacts with ECM29 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi213894. 2 interactions.
    DIPiDIP-29247N.
    IntActiQ91XD6. 1 interaction.
    MINTiMINT-4121697.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 3014
    Beta strandi37 – 459
    Beta strandi47 – 537
    Helixi54 – 563
    Beta strandi63 – 653
    Beta strandi68 – 714
    Beta strandi82 – 854
    Beta strandi106 – 1138
    Turni115 – 1173
    Helixi118 – 12710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DX5X-ray3.35A1-139[»]
    ProteinModelPortaliQ91XD6.
    SMRiQ91XD6. Positions 3-131, 172-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91XD6.

    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.By similarity

    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.
    GeneTreeiENSGT00390000017209.
    HOGENOMiHOG000006822.
    HOVERGENiHBG083632.
    InParanoidiQ91XD6.
    KOiK12190.
    OMAiCCIAIPL.
    OrthoDBiEOG7VB2FM.
    PhylomeDBiQ91XD6.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q91XD6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRFVWTSGL LEINETLVIQ QRGVRVYDGE EKIKFDAGTL LLSTHRLIWR    50
    DQKNNECCMA IPLSQIVFIE EQAAGIGKSA KIVVHLHPAP SNKEPGPFQS 100
    SKNSYIRLSF KEHGQIEFYR RLSEEMTQRR WETVPVSQSL QTNKGPQPGR 150
    VRAVGIVGIE RKLEEKRKET DKNISEAFED LSKLMIKAKE MVELSKSIAN 200
    KIKEKQGDVT EDETIRFKSY LLSMGIANPV TRETYGSGTQ YHMQLAKQLA 250
    GILQAPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP 300
    IRLRVFDSGV MVIELQTHKE EEMVASALET VSERGSLTSE EFAKLVGMSV 350
    LLAKERLLLA EKMGHLCRDD SVEGLRFYPN LFMTQN 386
    Length:386
    Mass (Da):43,736
    Last modified:December 1, 2001 - v1
    Checksum:i0036479499DD89C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC010811 mRNA. Translation: AAH10811.1.
    AK008946 mRNA. Translation: BAB25984.1.
    CCDSiCCDS22171.1.
    RefSeqiNP_081614.1. NM_027338.1.
    UniGeneiMm.41453.

    Genome annotation databases

    EnsembliENSMUST00000033866; ENSMUSP00000033866; ENSMUSG00000031479.
    GeneIDi70160.
    KEGGimmu:70160.
    UCSCiuc009lct.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC010811 mRNA. Translation: AAH10811.1 .
    AK008946 mRNA. Translation: BAB25984.1 .
    CCDSi CCDS22171.1.
    RefSeqi NP_081614.1. NM_027338.1.
    UniGenei Mm.41453.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DX5 X-ray 3.35 A 1-139 [» ]
    ProteinModelPortali Q91XD6.
    SMRi Q91XD6. Positions 3-131, 172-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213894. 2 interactions.
    DIPi DIP-29247N.
    IntActi Q91XD6. 1 interaction.
    MINTi MINT-4121697.

    PTM databases

    PhosphoSitei Q91XD6.

    Proteomic databases

    MaxQBi Q91XD6.
    PaxDbi Q91XD6.
    PRIDEi Q91XD6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033866 ; ENSMUSP00000033866 ; ENSMUSG00000031479 .
    GeneIDi 70160.
    KEGGi mmu:70160.
    UCSCi uc009lct.1. mouse.

    Organism-specific databases

    CTDi 51028.
    MGIi MGI:1917410. Vps36.

    Phylogenomic databases

    eggNOGi NOG262969.
    GeneTreei ENSGT00390000017209.
    HOGENOMi HOG000006822.
    HOVERGENi HBG083632.
    InParanoidi Q91XD6.
    KOi K12190.
    OMAi CCIAIPL.
    OrthoDBi EOG7VB2FM.
    PhylomeDBi Q91XD6.
    TreeFami TF314770.

    Enzyme and pathway databases

    Reactomei REACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).

    Miscellaneous databases

    EvolutionaryTracei Q91XD6.
    NextBioi 331106.
    PROi Q91XD6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91XD6.
    Bgeei Q91XD6.
    CleanExi MM_VPS36.
    Genevestigatori Q91XD6.

    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. "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].
      Strain: FVB/N.
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-161.
      Strain: C57BL/6J.
      Tissue: Stomach.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 1-139 IN COMPLEX WITH RPS27A.

    Entry informationi

    Entry nameiVPS36_MOUSE
    AccessioniPrimary (citable) accession number: Q91XD6
    Secondary accession number(s): Q9CVA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3