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Protein

Charged multivesicular body protein 4b

Gene

Chmp4b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Biological processProtein 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1922858 Chmp4b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002114902 – 224Charged multivesicular body protein 4bAdd BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei6N6-acetyllysineCombined sources1
Modified residuei114N6-acetyllysineBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei223PhosphoserineBy similarity1

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
PhosphoSitePlusiQ9D8B3

Expressioni

Gene expression databases

BgeeiENSMUSG00000038467
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 sequentially. 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

Binary interactionsi

WithEntry#Exp.IntActNotes
PDCD6IPQ8WUM42EBI-8322817,EBI-310624From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi217613, 85 interactors
DIPiDIP-61322N
IntActiQ9D8B3, 88 interactors
MINTiQ9D8B3
STRINGi10090.ENSMUSP00000036206

Structurei

3D structure databases

ProteinModelPortaliQ9D8B3
SMRiQ9D8B3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 153Intramolecular interaction with C-terminusBy similarityAdd BLAST152
Regioni154 – 224Intramolecular interaction with N-terminusBy similarityAdd BLAST71

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili23 – 183Sequence analysisAdd BLAST161

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
OMAiMQVNTLE
OrthoDBiEOG091G0V7X
PhylomeDBiQ9D8B3
TreeFamiTF314269

Family and domain databases

InterProiView protein in InterPro
IPR005024 Snf7_fam
PfamiView protein in Pfam
PF03357 Snf7, 1 hit

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 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)DescriptionActionsGraphical viewLength
Sequence conflicti167E → K in AK008205 (PubMed:16141072).Curated1

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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiCHM4B_MOUSE
AccessioniPrimary (citable) accession number: Q9D8B3
Secondary accession number(s): A2AVM1
, Q3TXM7, Q91VM7, Q922P1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: March 28, 2018
This is version 138 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health