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Q7LBR1 (CHM1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 1b
Alternative name(s):
CHMP1.5
Chromatin-modifying protein 1b
Short name=CHMP1b
Vacuolar protein sorting-associated protein 46-2
Short name=Vps46-2
Short name=hVps46-2
Gene names
Name:CHMP1B
Synonyms:C18orf2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 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. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release. Ref.5 Ref.13

Subunit structure

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 CHMP1A. Interacts with VTA1; the interaction probably involves the open conformation of CHMP1B. Interacts with CHMP2A. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with SPAST (via MIT domain); the interaction is direct. Interacts with IST1. Interacts with MITD1. Interacts with STAMBP. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16

Subcellular location

Cytoplasmcytosol. Endosome. Late endosome membrane; Peripheral membrane protein Probable. Note: Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body. Ref.7 Ref.9 Ref.16

Tissue specificity

Widely expressed. Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta and brain. Ref.1

Sequence similarities

Belongs to the SNF7 family.

Sequence caution

The sequence AAG01449.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 199199Charged multivesicular body protein 1b
PRO_0000211454

Regions

Region132 – 15625Interaction with IST1
Region174 – 19926Interaction with SPAST
Region180 – 19920Interaction with VTA1
Region180 – 19617Interaction with VPS4A, MITD1 and STAMBP
Region183 – 19917Interaction with VPS4B
Coiled coil26 – 4823 Potential
Coiled coil178 – 19922 Potential
Motif186 – 19611MIT-interacting motif

Experimental info

Mutagenesis158 – 1592DE → AA: Diminishes interaction with VPS4B. Ref.11
Mutagenesis1781T → R: Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-181 and R-184. Ref.11 Ref.16
Mutagenesis1811A → R: Abolishes interaction with SPAScT and no effect on interaction with VPS4A; when associated with R-178 and R-184. Ref.11 Ref.16
Mutagenesis1841E → A: Decreases interaction with SPAST. Ref.11 Ref.16
Mutagenesis1841E → R: Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-178 and R-181. Ref.11 Ref.16
Mutagenesis1881L → A: Abolishes interaction with SPAST and VPS4A; when associated with A-192. Ref.11 Ref.16
Mutagenesis1921L → A: Abolishes interaction with SPAST and VPS4A; when associated with A-188. Ref.10 Ref.11 Ref.16
Mutagenesis1921L → A: Abolishes interaction with VPS4B. Ref.10 Ref.11 Ref.16
Mutagenesis1951L → A: Abolishes interaction with VPS4B. Ref.10 Ref.11

Secondary structure

..... 199
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7LBR1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8071E94D20D85AB5

FASTA19922,109
        10         20         30         40         50         60 
MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN 

        70         80         90        100        110        120 
QAVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD ATLKTMNLEK ISALMDKFEH 

       130        140        150        160        170        180 
QFETLDVQTQ QMEDTMSSTT TLTTPQNQVD MLLQEMADEA GLDLNMELPQ GQTGSVGTSV 

       190 
ASAEQDELSQ RLARLRDQV 

« Hide

References

« Hide 'large scale' references
[1]"C18orf2, a novel, highly conserved intronless gene within intron 5 of the GNAL gene on chromosome 18p11."
Vuoristo J.T., Berrettini W.H., Ala-Kokko L.
Cytogenet. Cell Genet. 93:19-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]"CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Melanoma and Ovary.
[4]"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: INTERACTION WITH CHMP1A; VPS4A AND VPS4B.
[5]"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, INTERACTION WITH CHMP1A; CHMP2A AND VPS4A.
[6]Erratum
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[7]"The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B."
Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.
Hum. Mol. Genet. 14:19-38(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SPAST.
[8]"Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A."
Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J., Sundquist W.I.
Proc. Natl. Acad. Sci. U.S.A. 102:13813-13818(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS4A.
[9]"A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH STAMBP.
[10]"ESCRT-III recognition by VPS4 ATPases."
Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A., Ghaffarian S., Sundquist W.I.
Nature 449:740-744(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS4A AND VPS4B, MUTAGENESIS OF LEU-192 AND LEU-195.
[11]"Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly."
Shim S., Merrill S.A., Hanson P.I.
Mol. Biol. Cell 19:2661-2672(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VTA1 AND VPS4B, MUTAGENESIS OF 158-ASP-GLU-159.
[12]"Essential role of hIST1 in cytokinesis."
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M., Ameer-Beg S., Bowers K., Martin-Serrano J.
Mol. Biol. Cell 20:1374-1387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IST1; VTA1; VPS4A; MITD1 AND STAMBP.
[13]"Biochemical analyses of human IST1 and its function in cytokinesis."
Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IST1.
[14]"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].
[15]"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: INTERACTION WITH VPS4A.
[16]"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 145-194 IN COMPLEX WITH SPAST, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A, MUTAGENESIS OF THR-178; ALA-181; GLU-184; LEU-188 AND LEU-192.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF306520 Genomic DNA. Translation: AAL48200.1.
AF281064 mRNA. Translation: AAG01449.1. Different initiation.
BC065933 mRNA. Translation: AAH65933.1.
BC012733 mRNA. Translation: AAH12733.3.
RefSeqNP_065145.2. NM_020412.4.
UniGeneHs.656244.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EABX-ray2.50G/H/I/J/K/L148-197[»]
ProteinModelPortalQ7LBR1.
SMRQ7LBR1. Positions 148-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121394. 20 interactions.
DIPDIP-48534N.
IntActQ7LBR1. 9 interactions.
MINTMINT-6946813.

PTM databases

PhosphoSiteQ7LBR1.

Polymorphism databases

DMDM73917735.

Proteomic databases

PeptideAtlasQ7LBR1.
PRIDEQ7LBR1.

Protocols and materials databases

DNASU57132.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000526991; ENSP00000432279; ENSG00000255112.
GeneID57132.
KEGGhsa:57132.
UCSCuc002kqe.3. human.

Organism-specific databases

CTD57132.
GeneCardsGC18P011851.
HGNCHGNC:24287. CHMP1B.
MIM606486. gene.
neXtProtNX_Q7LBR1.
PharmGKBPA142672110.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG080200.
KOK12197.
OMARSAKKCD.
OrthoDBEOG7BP843.
PhylomeDBQ7LBR1.
TreeFamTF300076.

Gene expression databases

ArrayExpressQ7LBR1.
BgeeQ7LBR1.
CleanExHS_C18orf2.
HS_CHMP1B.
GenevestigatorQ7LBR1.

Family and domain databases

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

Other

EvolutionaryTraceQ7LBR1.
GeneWikiCHMP1B.
GenomeRNAi57132.
NextBio63047.
PROQ7LBR1.
SOURCESearch...

Entry information

Entry nameCHM1B_HUMAN
AccessionPrimary (citable) accession number: Q7LBR1
Secondary accession number(s): Q96E89, Q9HD41
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 82 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 chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM