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Q9NZZ3

- CHMP5_HUMAN

UniProt

Q9NZZ3 - CHMP5_HUMAN

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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

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 - 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
Complete GO annotation...

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 Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB-KW
  5. nucleus Source: Ensembl
Complete GO annotation...

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 – 17617Combined sources
Helixi181 – 1888Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074817.
HOGENOMiHOG000191086.
HOVERGENiHBG055759.
InParanoidiQ9NZZ3.
KOiK12198.
OMAiVWNMEQA.
OrthoDBiEOG7JMGFX.
PhylomeDBiQ9NZZ3.
TreeFamiTF300122.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[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

        10         20         30         40         50
MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK
60 70 80 90 100
KMREGPAKNM VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK
110 120 130 140 150
DTKTTVDAMK LGVKEMKKAY KQVKIDQIED LQDQLEDMME DANEIQEALS
160 170 180 190 200
RSYGTPELDE DDLEAELDAL GDELLADEDS SYLDEAASAP AIPEGVPTDT
210
KNKDGVLVDE FGLPQIPAS
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00550000074817.
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_fam.
[Graphical view ]
Pfami PF03357. Snf7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 117 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

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