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Q9NZZ3

- CHMP5_HUMAN

UniProt

Q9NZZ3 - CHMP5_HUMAN

Protein

Charged multivesicular body protein 5

Gene

CHMP5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. endosomal transport Source: Reactome
    2. endosome to lysosome transport Source: Ensembl
    3. lysosome organization Source: Ensembl
    4. membrane organization Source: Reactome
    5. protein transport Source: UniProtKB-KW
    6. regulation of receptor recycling Source: Ensembl
    7. viral life cycle Source: Reactome
    8. viral process Source: Reactome

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Charged multivesicular body protein 5
    Alternative name(s):
    Chromatin-modifying protein 5
    SNF7 domain-containing protein 2
    Vacuolar protein sorting-associated protein 60
    Short name:
    Vps60
    Short name:
    hVps60
    Gene namesi
    Name:CHMP5
    Synonyms:C9orf83, SNF7DC2
    ORF Names:CGI-34, HSPC177, PNAS-114, PNAS-2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:26942. CHMP5.

    Subcellular locationi

    Cytoplasmcytosol. Endosome membrane Curated; Peripheral membrane protein Curated
    Note: Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134903143.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 219219Charged multivesicular body protein 5PRO_0000211500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861Phosphoserine1 Publication

    Post-translational modificationi

    ISGylated. Isgylation inhibits its interaction with VTA1.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NZZ3.
    PaxDbiQ9NZZ3.
    PeptideAtlasiQ9NZZ3.
    PRIDEiQ9NZZ3.

    PTM databases

    PhosphoSiteiQ9NZZ3.

    Expressioni

    Gene expression databases

    BgeeiQ9NZZ3.
    CleanExiHS_CHMP5.
    GenevestigatoriQ9NZZ3.

    Organism-specific databases

    HPAiCAB033874.
    HPA042883.
    HPA056437.

    Interactioni

    Subunit structurei

    Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Interacts with VTA1. Interacts with CHMP2A. Interacts with VTA1; the interaction involves soluble CHMP5.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAMBPO956302EBI-751303,EBI-396676

    Protein-protein interaction databases

    BioGridi119579. 23 interactions.
    DIPiDIP-50420N.
    IntActiQ9NZZ3. 5 interactions.
    MINTiMINT-1466639.
    STRINGi9606.ENSP00000223500.

    Structurei

    Secondary structure

    1
    219
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi160 – 17617
    Helixi181 – 1888

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LXMNMR-B139-195[»]
    3ULYX-ray2.60B151-219[»]
    3UM0X-ray3.10B200-219[»]
    3UM1X-ray2.71B/E151-219[»]
    3UM2X-ray2.59B/E200-219[»]
    ProteinModelPortaliQ9NZZ3.
    SMRiQ9NZZ3. Positions 154-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni121 – 15838Interaction with VTA1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili26 – 179154Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNF7 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG300000.
    HOGENOMiHOG000191086.
    HOVERGENiHBG055759.
    InParanoidiQ9NZZ3.
    KOiK12198.
    OMAiVWNMEQA.
    OrthoDBiEOG7JMGFX.
    PhylomeDBiQ9NZZ3.
    TreeFamiTF300122.

    Family and domain databases

    InterProiIPR005024. Snf7.
    [Graphical view]
    PfamiPF03357. Snf7. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZZ3-1) [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

    MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK    50
    KMREGPAKNM VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK 100
    DTKTTVDAMK LGVKEMKKAY KQVKIDQIED LQDQLEDMME DANEIQEALS 150
    RSYGTPELDE DDLEAELDAL GDELLADEDS SYLDEAASAP AIPEGVPTDT 200
    KNKDGVLVDE FGLPQIPAS 219
    Length:219
    Mass (Da):24,571
    Last modified:October 1, 2000 - v1
    Checksum:iC99695F66FD7E126
    GO
    Isoform 2 (identifier: Q9NZZ3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         166-219: ELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIPAS → GWSSGG

    Note: No experimental confirmation available.

    Show »
    Length:171
    Mass (Da):19,520
    Checksum:iA4986DBBA8926742
    GO

    Sequence cautioni

    The sequence AAG23821.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141P → R in AAD27743. (PubMed:10810093)Curated
    Sequence conflicti19 – 191D → G in AAH16698. (PubMed:15489334)Curated
    Sequence conflicti84 – 9310QQSFNMEQAN → NSHSTWTGH in AAD27743. (PubMed:10810093)Curated
    Sequence conflicti122 – 1221Q → P in AAD27743. (PubMed:10810093)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861S → P.
    Corresponds to variant rs11540558 [ dbSNP | Ensembl ].
    VAR_052029

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei166 – 21954ELDAL…QIPAS → GWSSGG in isoform 2. 1 PublicationVSP_042556Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132968 mRNA. Translation: AAD27743.1.
    AF161525 mRNA. Translation: AAF29140.1.
    AK295744 mRNA. Translation: BAG58578.1.
    AK315455 mRNA. Translation: BAG37842.1.
    AL356472 Genomic DNA. Translation: CAH72744.1.
    CH471071 Genomic DNA. Translation: EAW58512.1.
    BC006974 mRNA. Translation: AAH06974.1.
    BC007457 mRNA. Translation: AAH07457.1.
    BC016698 mRNA. Translation: AAH16698.1.
    BC020796 mRNA. Translation: AAH20796.1.
    BC021168 mRNA. Translation: AAH21168.1.
    AF275810 mRNA. Translation: AAG23821.1. Different initiation.
    AF229832 mRNA. Translation: AAF42917.1.
    CCDSiCCDS56569.1. [Q9NZZ3-2]
    CCDS6537.1. [Q9NZZ3-1]
    RefSeqiNP_001182465.1. NM_001195536.1. [Q9NZZ3-2]
    NP_057494.3. NM_016410.5. [Q9NZZ3-1]
    UniGeneiHs.635313.

    Genome annotation databases

    EnsembliENST00000223500; ENSP00000223500; ENSG00000086065. [Q9NZZ3-1]
    ENST00000419016; ENSP00000442725; ENSG00000086065. [Q9NZZ3-2]
    GeneIDi51510.
    KEGGihsa:51510.
    UCSCiuc003zsm.4. human. [Q9NZZ3-1]
    uc011lnv.2. human. [Q9NZZ3-2]

    Polymorphism databases

    DMDMi51702157.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132968 mRNA. Translation: AAD27743.1 .
    AF161525 mRNA. Translation: AAF29140.1 .
    AK295744 mRNA. Translation: BAG58578.1 .
    AK315455 mRNA. Translation: BAG37842.1 .
    AL356472 Genomic DNA. Translation: CAH72744.1 .
    CH471071 Genomic DNA. Translation: EAW58512.1 .
    BC006974 mRNA. Translation: AAH06974.1 .
    BC007457 mRNA. Translation: AAH07457.1 .
    BC016698 mRNA. Translation: AAH16698.1 .
    BC020796 mRNA. Translation: AAH20796.1 .
    BC021168 mRNA. Translation: AAH21168.1 .
    AF275810 mRNA. Translation: AAG23821.1 . Different initiation.
    AF229832 mRNA. Translation: AAF42917.1 .
    CCDSi CCDS56569.1. [Q9NZZ3-2 ]
    CCDS6537.1. [Q9NZZ3-1 ]
    RefSeqi NP_001182465.1. NM_001195536.1. [Q9NZZ3-2 ]
    NP_057494.3. NM_016410.5. [Q9NZZ3-1 ]
    UniGenei Hs.635313.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LXM NMR - B 139-195 [» ]
    3ULY X-ray 2.60 B 151-219 [» ]
    3UM0 X-ray 3.10 B 200-219 [» ]
    3UM1 X-ray 2.71 B/E 151-219 [» ]
    3UM2 X-ray 2.59 B/E 200-219 [» ]
    ProteinModelPortali Q9NZZ3.
    SMRi Q9NZZ3. Positions 154-189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119579. 23 interactions.
    DIPi DIP-50420N.
    IntActi Q9NZZ3. 5 interactions.
    MINTi MINT-1466639.
    STRINGi 9606.ENSP00000223500.

    PTM databases

    PhosphoSitei Q9NZZ3.

    Polymorphism databases

    DMDMi 51702157.

    Proteomic databases

    MaxQBi Q9NZZ3.
    PaxDbi Q9NZZ3.
    PeptideAtlasi Q9NZZ3.
    PRIDEi Q9NZZ3.

    Protocols and materials databases

    DNASUi 51510.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223500 ; ENSP00000223500 ; ENSG00000086065 . [Q9NZZ3-1 ]
    ENST00000419016 ; ENSP00000442725 ; ENSG00000086065 . [Q9NZZ3-2 ]
    GeneIDi 51510.
    KEGGi hsa:51510.
    UCSCi uc003zsm.4. human. [Q9NZZ3-1 ]
    uc011lnv.2. human. [Q9NZZ3-2 ]

    Organism-specific databases

    CTDi 51510.
    GeneCardsi GC09P033257.
    HGNCi HGNC:26942. CHMP5.
    HPAi CAB033874.
    HPA042883.
    HPA056437.
    MIMi 610900. gene.
    neXtProti NX_Q9NZZ3.
    PharmGKBi PA134903143.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300000.
    HOGENOMi HOG000191086.
    HOVERGENi HBG055759.
    InParanoidi Q9NZZ3.
    KOi K12198.
    OMAi VWNMEQA.
    OrthoDBi EOG7JMGFX.
    PhylomeDBi Q9NZZ3.
    TreeFami TF300122.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Miscellaneous databases

    ChiTaRSi CHMP5. human.
    GeneWikii CHMP5.
    GenomeRNAii 51510.
    NextBioi 55198.
    PROi Q9NZZ3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NZZ3.
    CleanExi HS_CHMP5.
    Genevestigatori Q9NZZ3.

    Family and domain databases

    InterProi IPR005024. Snf7.
    [Graphical view ]
    Pfami PF03357. Snf7. 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. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(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: Bone marrow, Brain, Kidney and Urinary bladder.
    7. "Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
      Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-219 (ISOFORM 1).
      Tissue: Promyelocytic leukemia.
    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: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP2A.
    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. "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells."
      Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L., Hill J., Schnegelberger R., Sundquist W.I., Kaplan J.
      J. Biol. Chem. 280:10548-10555(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VTA1.
    11. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
      Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
      EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation."
      Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T.
      J. Biol. Chem. 282:9805-9812(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VTA1, IDENTIFICATION BY MASS SPECTROMETRY.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
      Kuang Z., Seo E.J., Leis J.
      J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION, INTERACTION WITH VTA1.

    Entry informationi

    Entry nameiCHMP5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZZ3
    Secondary accession number(s): B2RD95
    , B4DIR6, Q5VXW2, Q96AV2, Q9HB68, Q9NYS4, Q9Y323
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 116 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3