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Q7LBR1

- CHM1B_HUMAN

UniProt

Q7LBR1 - CHM1B_HUMAN

Protein

Charged multivesicular body protein 1b

Gene

CHMP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. establishment of protein localization Source: UniProt
    3. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CHMP1B
    Synonyms:C18orf2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:24287. CHMP1B.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. late endosome membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi158 – 1592DE → AA: Diminishes interaction with VPS4B. 1 Publication
    Mutagenesisi178 – 1781T → R: Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-181 and R-184. 2 Publications
    Mutagenesisi181 – 1811A → R: Abolishes interaction with SPAScT and no effect on interaction with VPS4A; when associated with R-178 and R-184. 2 Publications
    Mutagenesisi184 – 1841E → A: Decreases interaction with SPAST. 2 Publications
    Mutagenesisi184 – 1841E → R: Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-178 and R-181. 2 Publications
    Mutagenesisi188 – 1881L → A: Abolishes interaction with SPAST and VPS4A; when associated with A-192. 2 Publications
    Mutagenesisi192 – 1921L → A: Abolishes interaction with SPAST and VPS4A; when associated with A-188. 3 Publications
    Mutagenesisi192 – 1921L → A: Abolishes interaction with VPS4B. 3 Publications
    Mutagenesisi195 – 1951L → A: Abolishes interaction with VPS4B. 2 Publications

    Organism-specific databases

    PharmGKBiPA142672110.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Charged multivesicular body protein 1bPRO_0000211454Add
    BLAST

    Proteomic databases

    MaxQBiQ7LBR1.
    PeptideAtlasiQ7LBR1.
    PRIDEiQ7LBR1.

    PTM databases

    PhosphoSiteiQ7LBR1.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ7LBR1.
    BgeeiQ7LBR1.
    CleanExiHS_C18orf2.
    HS_CHMP1B.
    GenevestigatoriQ7LBR1.

    Interactioni

    Subunit structurei

    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.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAMBPO956305EBI-2118090,EBI-396676
    USP8P408185EBI-2118090,EBI-1050865

    Protein-protein interaction databases

    BioGridi121394. 20 interactions.
    DIPiDIP-48534N.
    IntActiQ7LBR1. 9 interactions.
    MINTiMINT-6946813.

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi151 – 1599
    Helixi174 – 19320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EABX-ray2.50G/H/I/J/K/L148-197[»]
    ProteinModelPortaliQ7LBR1.
    SMRiQ7LBR1. Positions 148-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7LBR1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni132 – 15625Interaction with IST1Add
    BLAST
    Regioni174 – 19926Interaction with SPASTAdd
    BLAST
    Regioni180 – 19920Interaction with VTA1Add
    BLAST
    Regioni180 – 19617Interaction with VPS4A, MITD1 and STAMBPAdd
    BLAST
    Regioni183 – 19917Interaction with VPS4BAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili26 – 4823Sequence AnalysisAdd
    BLAST
    Coiled coili178 – 19922Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi186 – 19611MIT-interacting motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNF7 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    HOVERGENiHBG080200.
    KOiK12197.
    OMAiLWRNIEN.
    OrthoDBiEOG7BP843.
    PhylomeDBiQ7LBR1.
    TreeFamiTF300076.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q7LBR1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI    50
    HAENAIRQKN QAVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD 100
    ATLKTMNLEK ISALMDKFEH QFETLDVQTQ QMEDTMSSTT TLTTPQNQVD 150
    MLLQEMADEA GLDLNMELPQ GQTGSVGTSV ASAEQDELSQ RLARLRDQV 199
    Length:199
    Mass (Da):22,109
    Last modified:July 5, 2004 - v1
    Checksum:i8071E94D20D85AB5
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF306520 Genomic DNA. Translation: AAL48200.1.
    AF281064 mRNA. Translation: AAG01449.1. Different initiation.
    BC065933 mRNA. Translation: AAH65933.1.
    BC012733 mRNA. Translation: AAH12733.3.
    CCDSiCCDS54180.1.
    RefSeqiNP_065145.2. NM_020412.4.
    UniGeneiHs.656244.

    Genome annotation databases

    EnsembliENST00000526991; ENSP00000432279; ENSG00000255112.
    GeneIDi57132.
    KEGGihsa:57132.
    UCSCiuc002kqe.3. human.

    Polymorphism databases

    DMDMi73917735.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF306520 Genomic DNA. Translation: AAL48200.1 .
    AF281064 mRNA. Translation: AAG01449.1 . Different initiation.
    BC065933 mRNA. Translation: AAH65933.1 .
    BC012733 mRNA. Translation: AAH12733.3 .
    CCDSi CCDS54180.1.
    RefSeqi NP_065145.2. NM_020412.4.
    UniGenei Hs.656244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EAB X-ray 2.50 G/H/I/J/K/L 148-197 [» ]
    ProteinModelPortali Q7LBR1.
    SMRi Q7LBR1. Positions 148-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121394. 20 interactions.
    DIPi DIP-48534N.
    IntActi Q7LBR1. 9 interactions.
    MINTi MINT-6946813.

    PTM databases

    PhosphoSitei Q7LBR1.

    Polymorphism databases

    DMDMi 73917735.

    Proteomic databases

    MaxQBi Q7LBR1.
    PeptideAtlasi Q7LBR1.
    PRIDEi Q7LBR1.

    Protocols and materials databases

    DNASUi 57132.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000526991 ; ENSP00000432279 ; ENSG00000255112 .
    GeneIDi 57132.
    KEGGi hsa:57132.
    UCSCi uc002kqe.3. human.

    Organism-specific databases

    CTDi 57132.
    GeneCardsi GC18P011851.
    HGNCi HGNC:24287. CHMP1B.
    MIMi 606486. gene.
    neXtProti NX_Q7LBR1.
    PharmGKBi PA142672110.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG080200.
    KOi K12197.
    OMAi LWRNIEN.
    OrthoDBi EOG7BP843.
    PhylomeDBi Q7LBR1.
    TreeFami TF300076.

    Miscellaneous databases

    EvolutionaryTracei Q7LBR1.
    GeneWikii CHMP1B.
    GenomeRNAii 57132.
    NextBioi 63047.
    PROi Q7LBR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7LBR1.
    Bgeei Q7LBR1.
    CleanExi HS_C18orf2.
    HS_CHMP1B.
    Genevestigatori Q7LBR1.

    Family and domain databases

    InterProi IPR005024. Snf7.
    [Graphical view ]
    Pfami PF03357. Snf7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiCHM1B_HUMAN
    AccessioniPrimary (citable) accession number: Q7LBR1
    Secondary accession number(s): Q96E89, Q9HD41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 86 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3