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Protein

Charged multivesicular body protein 4b

Gene

CHMP4B

Organism
Homo sapiens (Human)
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 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. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release.5 Publications

GO - Molecular functioni

  1. identical protein binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. cell separation after cytokinesis Source: UniProtKB
  2. endosomal transport Source: Reactome
  3. maintenance of lens transparency Source: UniProtKB
  4. membrane organization Source: Reactome
  5. mitotic metaphase plate congression Source: UniProtKB
  6. negative regulation of autophagic vacuole assembly Source: UniProtKB
  7. negative regulation of cell death Source: UniProtKB
  8. negative regulation of neuron death Source: UniProtKB
  9. nucleus organization Source: UniProtKB
  10. positive regulation of viral release from host cell Source: UniProtKB
  11. posttranslational protein targeting to membrane Source: UniProtKB
  12. protein homooligomerization Source: UniProtKB
  13. regulation of centrosome duplication Source: UniProtKB
  14. regulation of mitotic spindle assembly Source: UniProtKB
  15. regulation of viral process Source: UniProtKB
  16. ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
  17. vacuolar transport Source: InterPro
  18. viral budding Source: UniProtKB
  19. viral budding via host ESCRT complex Source: UniProtKB
  20. viral life cycle Source: Reactome
  21. 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 4b
Alternative name(s):
Chromatin-modifying protein 4b
Short name:
CHMP4b
SNF7 homolog associated with Alix 1
SNF7-2
Short name:
hSnf7-2
Vacuolar protein sorting-associated protein 32-2
Short name:
Vps32-2
Short name:
hVps32-2
Gene namesi
Name:CHMP4B
Synonyms:C20orf178, SHAX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16171. CHMP4B.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic side of plasma membrane Source: UniProtKB
  3. cytosol Source: Reactome
  4. endosome Source: UniProtKB
  5. ESCRT III complex Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. late endosome membrane Source: UniProtKB-SubCell
  8. membrane coat Source: UniProtKB
  9. midbody Source: FlyBase
  10. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Cataract 31, multiple types (CTRCT31)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT31 includes posterior polar, progressive posterior subcapsular, nuclear, and anterior subcapsular cataracts.

See also OMIM:605387
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291D → V in CTRCT31. 1 Publication
VAR_037579
Natural varianti161 – 1611E → K in CTRCT31. 1 Publication
VAR_037580

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MIMi605387. phenotype.
Orphaneti98993. Posterior polar cataract.
PharmGKBiPA25721.

Polymorphism and mutation databases

BioMutaiCHMP4B.
DMDMi24636296.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 224223Charged multivesicular body protein 4bPRO_0000211489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei114 – 1141N6-acetyllysine1 Publication
Modified residuei184 – 1841Phosphoserine1 Publication
Modified residuei223 – 2231Phosphoserine2 Publications

Post-translational modificationi

ISGylated. Isgylation weakens its interaction with VPS4A.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9H444.
PeptideAtlasiQ9H444.
PRIDEiQ9H444.

PTM databases

PhosphoSiteiQ9H444.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in heart and skeletal muscle. Also expressed in brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes.1 Publication

Gene expression databases

BgeeiQ9H444.
CleanExiHS_CHMP4B.
GenevestigatoriQ9H444.

Organism-specific databases

HPAiHPA041401.

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 PTPN23.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN23Q9H3S72EBI-749627,EBI-724478

Protein-protein interaction databases

BioGridi126170. 26 interactions.
DIPiDIP-29924N.
IntActiQ9H444. 10 interactions.
MINTiMINT-5000054.
STRINGi9606.ENSP00000217402.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 5735Combined sources
Helixi62 – 9635Combined sources
Helixi209 – 2124Combined sources
Helixi215 – 2228Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3QX-ray2.10B207-224[»]
3UM3X-ray3.80B121-224[»]
4ABMX-ray1.80A/B/C/D23-97[»]
ProteinModelPortaliQ9H444.
SMRiQ9H444. Positions 23-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H444.

Family & Domainsi

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.

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
HOVERGENiHBG050928.
InParanoidiQ9H444.
KOiK12194.
OMAiMKELETW.
OrthoDBiEOG7PGDSH.
PhylomeDBiQ9H444.
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.

Q9H444-1 [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 LPNVPSIALP
210 220
SKPAKKKEEE DDDMKELENW AGSM
Length:224
Mass (Da):24,950
Last modified:March 1, 2001 - v1
Checksum:iDB1D79DD3803CB2F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291D → V in CTRCT31. 1 Publication
VAR_037579
Natural varianti161 – 1611E → K in CTRCT31. 1 Publication
VAR_037580

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB100261 mRNA. Translation: BAC79375.1.
AY329085 mRNA. Translation: AAQ91194.1.
AL050349 Genomic DNA. Translation: CAC14088.1.
CH471077 Genomic DNA. Translation: EAW76293.1.
CH471077 Genomic DNA. Translation: EAW76294.1.
BC033859 mRNA. Translation: AAH33859.1.
CCDSiCCDS13228.1.
RefSeqiNP_789782.1. NM_176812.4.
UniGeneiHs.472471.

Genome annotation databases

EnsembliENST00000217402; ENSP00000217402; ENSG00000101421.
GeneIDi128866.
KEGGihsa:128866.
UCSCiuc002xaa.3. human.

Polymorphism and mutation databases

BioMutaiCHMP4B.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB100261 mRNA. Translation: BAC79375.1.
AY329085 mRNA. Translation: AAQ91194.1.
AL050349 Genomic DNA. Translation: CAC14088.1.
CH471077 Genomic DNA. Translation: EAW76293.1.
CH471077 Genomic DNA. Translation: EAW76294.1.
BC033859 mRNA. Translation: AAH33859.1.
CCDSiCCDS13228.1.
RefSeqiNP_789782.1. NM_176812.4.
UniGeneiHs.472471.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3QX-ray2.10B207-224[»]
3UM3X-ray3.80B121-224[»]
4ABMX-ray1.80A/B/C/D23-97[»]
ProteinModelPortaliQ9H444.
SMRiQ9H444. Positions 23-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126170. 26 interactions.
DIPiDIP-29924N.
IntActiQ9H444. 10 interactions.
MINTiMINT-5000054.
STRINGi9606.ENSP00000217402.

PTM databases

PhosphoSiteiQ9H444.

Polymorphism and mutation databases

BioMutaiCHMP4B.
DMDMi24636296.

Proteomic databases

MaxQBiQ9H444.
PeptideAtlasiQ9H444.
PRIDEiQ9H444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217402; ENSP00000217402; ENSG00000101421.
GeneIDi128866.
KEGGihsa:128866.
UCSCiuc002xaa.3. human.

Organism-specific databases

CTDi128866.
GeneCardsiGC20P032399.
HGNCiHGNC:16171. CHMP4B.
HPAiHPA041401.
MIMi605387. phenotype.
610897. gene.
neXtProtiNX_Q9H444.
Orphaneti98993. Posterior polar cataract.
PharmGKBiPA25721.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
HOVERGENiHBG050928.
InParanoidiQ9H444.
KOiK12194.
OMAiMKELETW.
OrthoDBiEOG7PGDSH.
PhylomeDBiQ9H444.
TreeFamiTF314269.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiCHMP4B. human.
EvolutionaryTraceiQ9H444.
GeneWikiiCHMP4B.
GenomeRNAii128866.
NextBioi82502.
PROiQ9H444.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H444.
CleanExiHS_CHMP4B.
GenevestigatoriQ9H444.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting."
    Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E., Yoshimori T., Maki M.
    J. Biol. Chem. 278:39104-39113(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDCD6IP.
  2. "Structure and function of human Vps20 and Snf7 proteins."
    Peck J.W., Bowden E.T., Burbelo P.D.
    Biochem. J. 377:693-700(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PDCD6IP.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Brain, Lung and Testis.
  6. Bienvenut W.V., Lempens A., Norman J.C.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 18-28 AND 78-107, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding."
    Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.
    Cell 114:689-699(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH PDCD6IP.
  9. Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP6; CHMP4C; PDCD6IP; VPS4A AND VPS4B.
  10. "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, SELF-ASSOCIATION, INTERACTION WITH CHMP2A; CHMP4A; CHMP4C; CHMP6; PDCD6IP AND VPS4A.
  11. Erratum
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
  12. "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms."
    Katoh K., Shibata H., Hatta K., Maki M.
    Arch. Biochem. Biophys. 421:159-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH PDCD6IP.
  13. "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting."
    Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K., Kobayashi T., Uchiyama Y., Maki M.
    Biochem. J. 387:17-26(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHMP6.
  14. "Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes."
    Sharma M., Pampinella F., Nemes C., Benharouga M., So J., Du K., Bache K.G., Papsin B., Zerangue N., Stenmark H., Lukacs G.L.
    J. Cell Biol. 164:923-933(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MISFOLDED CFTR.
  15. "CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway."
    Horii M., Shibata H., Kobayashi R., Katoh K., Yorikawa C., Yasuda J., Maki M.
    Biochem. J. 400:23-32(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHMP7.
  16. "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding."
    Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G., Goettlinger H.
    Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOINHIBITORY MECHANISM, INTRAMOLECULAR INTERACTION.
  17. "Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site."
    Usami Y., Popov S., Goettlinger H.G.
    J. Virol. 81:6614-6622(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD6IP.
  18. "Brox, a novel farnesylated Bro1 domain-containing protein that associates with charged multivesicular body protein 4 (CHMP4)."
    Ichioka F., Kobayashi R., Katoh K., Shibata H., Maki M.
    FEBS J. 275:682-692(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BROX.
  19. "Plasma membrane deformation by circular arrays of ESCRT-III protein filaments."
    Hanson P.I., Roth R., Lin Y., Heuser J.E.
    J. Cell Biol. 180:389-402(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SELF-ASSOCIATION, STRUCTURE BY ELECTRON CRYOMICROSCOPY.
  20. "The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis."
    Doyotte A., Mironov A., McKenzie E., Woodman P.
    Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN23.
  21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-6 AND LYS-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "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-184 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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 VPS4A.
  25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  27. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  28. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 207-224 IN COMPLEX WITH PDCD6IP.
  29. "CHMP4B, a novel gene for autosomal dominant cataracts linked to chromosome 20q."
    Shiels A., Bennett T.M., Knopf H.L.S., Yamada K., Yoshiura K., Niikawa N., Shim S., Hanson P.I.
    Am. J. Hum. Genet. 81:596-606(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CTRCT31 VAL-129 AND LYS-161.

Entry informationi

Entry nameiCHM4B_HUMAN
AccessioniPrimary (citable) accession number: Q9H444
Secondary accession number(s): E1P5N4, Q53ZD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 122 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

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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 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.