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Q9H444 (CHM4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CHMP4B
Synonyms:C20orf178, SHAX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9 Ref.10 Ref.19

Subunit structure

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. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.24

Subcellular location

Cytoplasmcytosol. Late endosome membrane; Peripheral membrane protein Probable Ref.1 Ref.13.

Tissue specificity

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. Ref.12

Domain

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.

Post-translational modification

ISGylated. Isgylation weakens its interaction with VPS4A. Ref.24

Involvement in disease

Cataract 31, multiple types (CTRCT31) [MIM:605387]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Sequence similarities

Belongs to the SNF7 family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Endosome
Membrane
   DiseaseCataract
Disease mutation
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processendosomal transport

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

negative regulation of autophagic vacuole assembly

Inferred from mutant phenotype PubMed 21975012. Source: UniProt

negative regulation of neuron death

Inferred from mutant phenotype PubMed 21975012. Source: UniProt

posttranslational protein targeting to membrane

Inferred from mutant phenotype PubMed 21975012. Source: UniProt

protein homooligomerization

Inferred from direct assay Ref.19. Source: UniProt

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentESCRT III complex

Inferred from direct assay PubMed 21975012. Source: UniProt

cytoplasm

Inferred from direct assay PubMed 21975012. Source: UniProt

cytoplasmic side of plasma membrane

Inferred from direct assay Ref.19. Source: UniProt

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 22724069. Source: FlyBase

nucleus

Inferred from direct assay PubMed 21975012. Source: UniProt

   Molecular_functionidentical protein binding

Inferred from direct assay Ref.19. Source: UniProt

protein binding

Inferred from physical interaction PubMed 20208530Ref.24. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPN23Q9H3S72EBI-749627,EBI-724478

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 224223Charged multivesicular body protein 4b
PRO_0000211489

Regions

Coiled coil23 – 183161 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.21 Ref.26
Modified residue61N6-acetyllysine Ref.21
Modified residue1141N6-acetyllysine Ref.21
Modified residue1841Phosphoserine Ref.22
Modified residue2231Phosphoserine Ref.22 Ref.25

Natural variations

Natural variant1291D → V in CTRCT31. Ref.28
VAR_037579
Natural variant1611E → K in CTRCT31. Ref.28
VAR_037580

Secondary structure

......... 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H444 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: DB1D79DD3803CB2F

FASTA22424,950
        10         20         30         40         50         60 
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE LTAAKKHGTK 

        70         80         90        100        110        120 
NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN TNTEVLKNMG YAAKAMKAAH 

       130        140        150        160        170        180 
DNMDIDKVDE LMQDIADQQE LAEEISTAIS KPVGFGEEFD EDELMAELEE LEQEELDKNL 

       190        200        210        220 
LEISGPETVP LPNVPSIALP SKPAKKKEEE DDDMKELENW AGSM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The protein network of HIV budding."
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.
Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract]
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].
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"ALIX-CHMP4 interactions in the human ESCRT pathway."
McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.
Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 207-224 IN COMPLEX WITH PDCD6IP.
[28]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13228.1.
RefSeqNP_789782.1. NM_176812.4.
UniGeneHs.472471.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3QX-ray2.10B207-224[»]
3UM3X-ray3.80B121-224[»]
4ABMX-ray1.80A/B/C/D23-97[»]
ProteinModelPortalQ9H444.
SMRQ9H444. Positions 23-97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126170. 25 interactions.
DIPDIP-29924N.
IntActQ9H444. 10 interactions.
MINTMINT-5000054.
STRING9606.ENSP00000217402.

PTM databases

PhosphoSiteQ9H444.

Polymorphism databases

DMDM24636296.

Proteomic databases

MaxQBQ9H444.
PeptideAtlasQ9H444.
PRIDEQ9H444.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217402; ENSP00000217402; ENSG00000101421.
GeneID128866.
KEGGhsa:128866.
UCSCuc002xaa.3. human.

Organism-specific databases

CTD128866.
GeneCardsGC20P032399.
HGNCHGNC:16171. CHMP4B.
HPAHPA041401.
MIM605387. phenotype.
610897. gene.
neXtProtNX_Q9H444.
Orphanet98993. Posterior polar cataract.
PharmGKBPA25721.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000209960.
HOVERGENHBG050928.
InParanoidQ9H444.
KOK12194.
OMACAINLAC.
OrthoDBEOG7PGDSH.
PhylomeDBQ9H444.
TreeFamTF314269.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

BgeeQ9H444.
CleanExHS_CHMP4B.
GenevestigatorQ9H444.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHMP4B. human.
EvolutionaryTraceQ9H444.
GeneWikiCHMP4B.
GenomeRNAi128866.
NextBio82502.
PROQ9H444.
SOURCESearch...

Entry information

Entry nameCHM4B_HUMAN
AccessionPrimary (citable) accession number: Q9H444
Secondary accession number(s): E1P5N4, Q53ZD6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM