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Protein

Charged multivesicular body protein 5

Gene

Chmp5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity).By similarity

GO - Biological processi

  • cell separation after cytokinesis Source: MGI
  • endosome to lysosome transport Source: MGI
  • lysosome organization Source: MGI
  • mitotic metaphase plate congression Source: MGI
  • multivesicular body sorting pathway Source: ParkinsonsUK-UCL
  • nucleus organization Source: MGI
  • protein transport Source: UniProtKB-KW
  • regulation of centrosome duplication Source: MGI
  • regulation of mitotic spindle assembly Source: MGI
  • regulation of receptor recycling Source: MGI
  • viral budding Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 5
Alternative name(s):
Chromatin-modifying protein 5
SNF7 domain-containing protein 2
Gene namesi
Name:Chmp5
Synonyms:Snf7dc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1924209. Chmp5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Charged multivesicular body protein 5PRO_0000211501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861PhosphoserineBy similarity

Post-translational modificationi

ISGylated. Isgylation inhibits its interaction with VTA1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D7S9.
MaxQBiQ9D7S9.
PaxDbiQ9D7S9.
PRIDEiQ9D7S9.

PTM databases

iPTMnetiQ9D7S9.
PhosphoSiteiQ9D7S9.

Expressioni

Gene expression databases

BgeeiQ9D7S9.
CleanExiMM_CHMP5.
GenevisibleiQ9D7S9. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi218428. 2 interactions.
MINTiMINT-4085099.
STRINGi10090.ENSMUSP00000030128.

Structurei

3D structure databases

ProteinModelPortaliQ9D7S9.
SMRiQ9D7S9. Positions 151-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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

eggNOGiKOG1655. Eukaryota.
ENOG410XPDA. LUCA.
GeneTreeiENSGT00550000074817.
HOGENOMiHOG000191086.
HOVERGENiHBG055759.
InParanoidiQ9D7S9.
KOiK12198.
OMAiANEIQES.
OrthoDBiEOG7JMGFX.
PhylomeDBiQ9D7S9.
TreeFamiTF300122.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D7S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRFFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK
60 70 80 90 100
KMREGPAKNM VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK
110 120 130 140 150
DTKTTVDAMK LGVKEMKKAY KEVKIDQIED LQDQLEDMME DANEIQEALG
160 170 180 190 200
RSYGTPELDE DDLEAELDAL GDELLADEDS SYLDEAASAP AIPEGVPTDT
210
KNKDGVLVDE FGLPQIPAS
Length:219
Mass (Da):24,576
Last modified:June 1, 2001 - v1
Checksum:i38D13A6AD601A040
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008911 mRNA. Translation: BAB25962.1.
AK147058 mRNA. Translation: BAE27642.1.
BC006947 mRNA. Translation: AAH06947.1.
CCDSiCCDS18053.1.
RefSeqiNP_084090.1. NM_029814.1.
UniGeneiMm.212763.

Genome annotation databases

EnsembliENSMUST00000030128; ENSMUSP00000030128; ENSMUSG00000028419.
GeneIDi76959.
KEGGimmu:76959.
UCSCiuc008sia.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008911 mRNA. Translation: BAB25962.1.
AK147058 mRNA. Translation: BAE27642.1.
BC006947 mRNA. Translation: AAH06947.1.
CCDSiCCDS18053.1.
RefSeqiNP_084090.1. NM_029814.1.
UniGeneiMm.212763.

3D structure databases

ProteinModelPortaliQ9D7S9.
SMRiQ9D7S9. Positions 151-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218428. 2 interactions.
MINTiMINT-4085099.
STRINGi10090.ENSMUSP00000030128.

PTM databases

iPTMnetiQ9D7S9.
PhosphoSiteiQ9D7S9.

Proteomic databases

EPDiQ9D7S9.
MaxQBiQ9D7S9.
PaxDbiQ9D7S9.
PRIDEiQ9D7S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030128; ENSMUSP00000030128; ENSMUSG00000028419.
GeneIDi76959.
KEGGimmu:76959.
UCSCiuc008sia.1. mouse.

Organism-specific databases

CTDi51510.
MGIiMGI:1924209. Chmp5.

Phylogenomic databases

eggNOGiKOG1655. Eukaryota.
ENOG410XPDA. LUCA.
GeneTreeiENSGT00550000074817.
HOGENOMiHOG000191086.
HOVERGENiHBG055759.
InParanoidiQ9D7S9.
KOiK12198.
OMAiANEIQES.
OrthoDBiEOG7JMGFX.
PhylomeDBiQ9D7S9.
TreeFamiTF300122.

Enzyme and pathway databases

ReactomeiR-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

ChiTaRSiChmp5. mouse.
PROiQ9D7S9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D7S9.
CleanExiMM_CHMP5.
GenevisibleiQ9D7S9. MM.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Strain: C57BL/6J.
    Tissue: Amnion and Stomach.
  2. "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: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCHMP5_MOUSE
AccessioniPrimary (citable) accession number: Q9D7S9
Secondary accession number(s): Q3UI64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 107 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

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.