Q7LBR1 (CHM1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CHMP1B
Synonyms:	C18orf2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Subcellular location	Cytoplasm › cytosol. 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.15
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
Domain	Coiled coil
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from mutant phenotype Ref.13. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAMBP	O95630	5	EBI-2118090,EBI-396676
USP8	P40818	4	EBI-2118090,EBI-1050865

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 199

199

Charged multivesicular body protein 1b

PRO_0000211454

Regions

Region

132 – 156

25

Interaction with IST1

Region

174 – 199

26

Interaction with SPAST

Region

180 – 199

20

Interaction with VTA1

Region

180 – 196

17

Interaction with VPS4A, MITD1 and STAMBP

Region

183 – 199

17

Interaction with VPS4B

Coiled coil

26 – 48

23

Potential

Coiled coil

178 – 199

22

Potential

Motif

186 – 196

11

MIT-interacting motif

Experimental info

Mutagenesis

158 – 159

2

DE → AA: Diminishes interaction with VPS4B. Ref.11

Mutagenesis

178

1

T → R: Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-181 and R-184. Ref.11 Ref.15

Mutagenesis

181

1

A → R: Abolishes interaction with SPAScT and no effect on interaction with VPS4A; when associated with R-178 and R-184. Ref.11 Ref.15

Mutagenesis

184

1

E → A: Decreases interaction with SPAST. Ref.11 Ref.15

Mutagenesis

184

1

E → R: Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-178 and R-181. Ref.11 Ref.15

Mutagenesis

188

1

L → A: Abolishes interaction with SPAST and VPS4A; when associated with A-192. Ref.11 Ref.15

Mutagenesis

192

1

L → A: Abolishes interaction with SPAST and VPS4A; when associated with A-188. Ref.10 Ref.11 Ref.15

Mutagenesis

192

1

L → A: Abolishes interaction with VPS4B. Ref.10 Ref.11 Ref.15

Mutagenesis

195

1

L → A: Abolishes interaction with VPS4B. Ref.10 Ref.11

Secondary structure

1

.

.

.

.

.

199

Helix Strand Turn

Details...

Helix

151 – 159

9

Helix

174 – 193

20

Sequences

	Sequence		Length	Mass (Da)
	Q7LBR1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 8071E94D20D85AB5	FASTA	199	22,109
	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

References

	« Hide 'large scale' referencesShow '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]	"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.

IPI

IPI00156984.

RefSeq

NP_065145.2. NM_020412.4.

UniGene

Hs.656244.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EAB	X-ray	2.50	G/H/I/J/K/L	148-197	[»]

ProteinModelPortal

Q7LBR1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48534N.

IntAct

Q7LBR1. 8 interactions.

MINT

MINT-6946813.

PTM databases

PhosphoSite

Q7LBR1.

Polymorphism databases

DMDM

73917735.

Proteomic databases

PeptideAtlas

Q7LBR1.

PRIDE

Q7LBR1.

Protocols and materials databases

DNASU

57132.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000526991; ENSP00000432279; ENSG00000255112.

GeneID

57132.

KEGG

hsa:57132.

UCSC

uc002kqe.3. human.

Organism-specific databases

CTD

57132.

GeneCards

GC18P011851.

HGNC

HGNC:24287. CHMP1B.

MIM

606486. gene.

neXtProt

NX_Q7LBR1.

PharmGKB

PA142672110.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG080200.

KO

K12197.

OMA

EHLFNLK.

Gene expression databases

ArrayExpress

Q7LBR1.

Bgee

Q7LBR1.

CleanEx

HS_C18orf2.
HS_CHMP1B.

Genevestigator

Q7LBR1.

Family and domain databases

InterPro

IPR005024. Snf7.
[Graphical view]

Pfam

PF03357. Snf7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q7LBR1.

GenomeRNAi

57132.

NextBio

63047.

SOURCE

Search...

Entry information

Entry name

CHM1B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.