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Protein

Charged multivesicular body protein 4b

Gene

Chmp4b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable core 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. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 4b
Alternative name(s):
Chromatin-modifying protein 4b
Short name:
CHMP4b
Gene namesi
Name:Chmp4b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1922858. Chmp4b.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Late endosome membrane By similarity; Peripheral membrane protein By similarity
  • Midbody By similarity
  • Nucleus envelope By similarity

  • Note: Recruited to the nuclear envelope by CHMP7 during late anaphase.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytoplasmic side of plasma membrane Source: MGI
  • cytosol Source: ParkinsonsUK-UCL
  • endosome Source: MGI
  • ESCRT III complex Source: UniProtKB
  • extracellular exosome Source: MGI
  • late endosome membrane Source: UniProtKB-SubCell
  • membrane Source: ParkinsonsUK-UCL
  • membrane coat Source: MGI
  • midbody Source: MGI
  • nuclear envelope Source: UniProtKB
  • nucleus Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 224223Charged multivesicular body protein 4bPRO_0000211490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei6 – 61N6-acetyllysineCombined sources
Modified residuei114 – 1141N6-acetyllysineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei223 – 2231PhosphoserineBy similarity

Post-translational modificationi

ISGylated. Isgylation weakens its interaction with VPS4A (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D8B3.
MaxQBiQ9D8B3.
PaxDbiQ9D8B3.
PeptideAtlasiQ9D8B3.
PRIDEiQ9D8B3.

PTM databases

iPTMnetiQ9D8B3.
PhosphoSiteiQ9D8B3.

Expressioni

Gene expression databases

BgeeiQ9D8B3.
CleanExiMM_CHMP4B.
GenevisibleiQ9D8B3. MM.

Interactioni

Subunit structurei

Probable core 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 CHMP6 and CHMP4C. Interacts with PDCD6IP; the interaction is direct. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP7. Interacts with CFTR; the interaction requires misfolded CFTR. Interacts with PTPN23 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi217613. 85 interactions.
DIPiDIP-61322N.
IntActiQ9D8B3. 88 interactions.
MINTiMINT-4092439.
STRINGi10090.ENSMUSP00000036206.

Structurei

3D structure databases

ProteinModelPortaliQ9D8B3.
SMRiQ9D8B3. Positions 23-97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 153152Intramolecular interaction with C-terminusBy similarityAdd
BLAST
Regioni154 – 22471Intramolecular interaction with N-terminusBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili23 – 183161Sequence analysisAdd
BLAST

Domaini

The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).By similarity

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1656. Eukaryota.
ENOG410YE9I. LUCA.
GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
HOVERGENiHBG050928.
InParanoidiQ9D8B3.
KOiK12194.
OMAiMKELETW.
OrthoDBiEOG7PGDSH.
PhylomeDBiQ9D8B3.
TreeFamiTF314269.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D8B3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE
60 70 80 90 100
LTAAKKHGTK NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN
110 120 130 140 150
TNTEVLKNMG YAAKAMKAAH DNMDIDKVDE LMQDIADQQE LAEEISTAIS
160 170 180 190 200
KPVGFGEEFD EDELMAELEE LEQEELDKNL LEISGPETVP LPNVPSVALP
210 220
SKPAKKKEEE DDDMKELENW AGSM
Length:224
Mass (Da):24,936
Last modified:November 1, 2002 - v2
Checksum:iDB1D79C3C9ECCB2F
GO

Sequence cautioni

The sequence AAH06905.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AK008205 differs from that shown. Reason: Erroneous termination at position 56. Translated as Lys.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671E → K in AK008205 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008205 mRNA. No translation available.
AK156473 mRNA. Translation: BAE33724.1.
AK159193 mRNA. Translation: BAE34888.1.
AL929557 Genomic DNA. Translation: CAM20092.1.
BC006905 mRNA. Translation: AAH06905.1. Different initiation.
BC011429 mRNA. Translation: AAH11429.1.
BC059279 mRNA. Translation: AAH59279.1.
CCDSiCCDS16938.1.
RefSeqiNP_083638.1. NM_029362.3.
UniGeneiMm.262480.

Genome annotation databases

EnsembliENSMUST00000044277; ENSMUSP00000036206; ENSMUSG00000038467.
GeneIDi75608.
KEGGimmu:75608.
UCSCiuc008njp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008205 mRNA. No translation available.
AK156473 mRNA. Translation: BAE33724.1.
AK159193 mRNA. Translation: BAE34888.1.
AL929557 Genomic DNA. Translation: CAM20092.1.
BC006905 mRNA. Translation: AAH06905.1. Different initiation.
BC011429 mRNA. Translation: AAH11429.1.
BC059279 mRNA. Translation: AAH59279.1.
CCDSiCCDS16938.1.
RefSeqiNP_083638.1. NM_029362.3.
UniGeneiMm.262480.

3D structure databases

ProteinModelPortaliQ9D8B3.
SMRiQ9D8B3. Positions 23-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217613. 85 interactions.
DIPiDIP-61322N.
IntActiQ9D8B3. 88 interactions.
MINTiMINT-4092439.
STRINGi10090.ENSMUSP00000036206.

PTM databases

iPTMnetiQ9D8B3.
PhosphoSiteiQ9D8B3.

Proteomic databases

EPDiQ9D8B3.
MaxQBiQ9D8B3.
PaxDbiQ9D8B3.
PeptideAtlasiQ9D8B3.
PRIDEiQ9D8B3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044277; ENSMUSP00000036206; ENSMUSG00000038467.
GeneIDi75608.
KEGGimmu:75608.
UCSCiuc008njp.1. mouse.

Organism-specific databases

CTDi128866.
MGIiMGI:1922858. Chmp4b.

Phylogenomic databases

eggNOGiKOG1656. Eukaryota.
ENOG410YE9I. LUCA.
GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
HOVERGENiHBG050928.
InParanoidiQ9D8B3.
KOiK12194.
OMAiMKELETW.
OrthoDBiEOG7PGDSH.
PhylomeDBiQ9D8B3.
TreeFamiTF314269.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

ChiTaRSiChmp4b. mouse.
PROiQ9D8B3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8B3.
CleanExiMM_CHMP4B.
GenevisibleiQ9D8B3. 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 and NOD.
    Tissue: Small intestine and Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCHM4B_MOUSE
AccessioniPrimary (citable) accession number: Q9D8B3
Secondary accession number(s): A2AVM1
, Q3TXM7, Q91VM7, Q922P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: July 6, 2016
This is version 126 of the entry and version 2 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.