Q9HD42 (CHM1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Charged multivesicular body protein 1a

Alternative name(s):
Chromatin-modifying protein 1a
Short name=CHMP1a
Vacuolar protein sorting-associated protein 46-1
Short name=Vps46-1
Short name=hVps46-1

Gene names

Name:	CHMP1A
Synonyms:	CHMP1, KIAA0047, PCOLN3, PRSM1

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	196 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 to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing. Ref.1 Ref.2 Ref.7 Ref.12 Ref.15
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. Self-associates. Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B. Interacts with PHF1. Interacts with IST1. Interacts with MITD1. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.15
Subcellular location	Cytoplasm. Endosome membrane; Peripheral membrane protein. Nucleus matrix. Note: The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On overexpression, it localizes to nuclear bodies characterized by nuclease-resistant condensed chromatin. Ref.2 Ref.7
Tissue specificity	Expressed in placenta, cultured skin fibroblasts and in osteoblast cell line MG-63. Ref.1
Induction	By muristerone. Ref.2
Sequence similarities	Belongs to the SNF7 family.
Caution	Was originally (Ref.1) thought to be a metalloprotease (PRSM1). This was based on a wrong translation of the ORF which gave rise to a putative protein of 318 AA containing a pattern reminiscent of zinc metalloproteases.
Sequence caution	The sequence AAC50775.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame. The sequence BAA07557.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Biological process	Cell cycle Cell division Protein transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis Inferred from mutant phenotype Ref.12. Source: UniProtKB gene silencing Inferred from direct assay Ref.2. Source: UniProtKB mitotic chromosome condensation Inferred from direct assay Ref.2. Source: UniProtKB negative regulation of S phase of mitotic cell cycle Inferred from mutant phenotype Ref.2. Source: UniProtKB negative regulation of transcription by glucose Inferred from direct assay PubMed 9837962. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW vesicle-mediated transport Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	condensed nuclear chromosome Inferred from direct assay Ref.2. Source: UniProtKB early endosome Inferred from direct assay Ref.7. Source: UniProtKB endomembrane system Inferred from direct assay Ref.7. Source: UniProtKB endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center Inferred from direct assay Ref.7. Source: UniProtKB nuclear matrix Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	metallopeptidase activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAMBP	O95630	3	EBI-1057156,EBI-396676
USP8	P40818	2	EBI-1057156,EBI-1050865

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.2 (identifier: Q9HD42-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9HD42-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

Charged multivesicular body protein 1a

PRO_0000211448

Regions

Coiled coil

5 – 47

43

Potential

Coiled coil

102 – 124

23

Potential

Motif

185 – 195

11

MIT-interacting motif

Natural variations

Alternative sequence

1 – 128

128

Missing in isoform 2.

VSP_051716

Experimental info

Mutagenesis

191

1

L → A: No effect on interaction with IST1; when associated with L-194. Ref.12

Mutagenesis

194

1

L → A: No effect on interaction with IST1; when associated with L-194. Ref.12

Sequence conflict

77

1

Q → D in AAC50775. Ref.1

Secondary structure

1

.

.

.

196

Helix Strand Turn

Details...

Helix

184 – 195

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 85D0ED7D10828D60	FASTA	196	21,703
	10 20 30 40 50 60 MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALLQK NVECARVYAE NAIRKKNEGV 70 80 90 100 110 120 NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL STMDLQKVSS VMDRFEQQVQ 130 140 150 160 170 180 NLDVHTSVME DSMSSATTLT TPQEQVDSLI MQIAEENGLE VLDQLSQLPE GASAVGESSV 190 RSQEDQLSRR LAALRN
	Isoform 2 [UniParc]. Checksum: F58834B1C0E254DB	FASTA	68	7,363
	10 20 30 40 50 60 MEDSMSSATT LTTPQEQVDS LIMQIAEENG LEVLDQLSQL PEGASAVGES SVRSQEDQLS RRLAALRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)." Scott I.C., Halila R., Jenkins J.M., Mehan S., Apostolou S., Winqvist R., Callen D.F., Prockop D.J., Peltonen L., Kadler K.E. Gene 174:135-143(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, TISSUE SPECIFICITY. Tissue: Fibroblast and Placenta.
[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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION. Tissue: Placenta.
[3]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1 AND 2). Tissue: Brain and Kidney.
[7]	"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins." Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M. J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A.
[8]	"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 CHMP1B; VPS4A AND VPS4B.
[9]	"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: SELF-ASSOCIATION, INTERACTION WITH CHMP1B AND VPS4A.
[10]	Erratum Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D. Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[11]	"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.
[12]	"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, MUTAGENESIS OF LEU-191 AND LEU-194.
[13]	"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].
[14]	"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: STRUCTURE BY NMR OF 180-196 IN COMPLEX WITH VPS4A.
[15]	"ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes." Hadders M.A., Agromayor M., Obita T., Perisic O., Caballe A., Kloc M., Lamers M.H., Williams R.L., Martin-Serrano J. Proc. Natl. Acad. Sci. U.S.A. 109:17424-17429(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 184-196 IN COMPLEX WITH MITD1, FUNCTION, INTERACTION WITH MITD1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U58048 mRNA. Translation: AAC50775.1. Sequence problems.
AF281063 mRNA. Translation: AAG01448.1.
D38554 mRNA. Translation: BAA07557.1. Sequence problems.
BT006841 mRNA. Translation: AAP35487.1.
AC010538 Genomic DNA. No translation available.
BC007527 mRNA. No translation available.
BC010000 mRNA. Translation: AAH10000.2.
BC132711 mRNA. Translation: AAI32712.1.
BC132713 mRNA. Translation: AAI32714.1.

IPI

IPI00382452.
IPI01015759.

PIR

JC4963.

RefSeq

NP_002759.2. NM_002768.4.

UniGene

Hs.589427.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JQ9	NMR	-	B	180-196	[»]
2YMB	X-ray	3.40	F/H	184-196	[»]
4A5X	X-ray	1.91	C/D	184-196	[»]

ProteinModelPortal

Q9HD42.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-50647N.

IntAct

Q9HD42. 3 interactions.

MINT

MINT-6946738.

STRING

9606.ENSP00000253475.

PTM databases

PhosphoSite

Q9HD42.

Polymorphism databases

DMDM

62510514.

Proteomic databases

PaxDb

Q9HD42.

PRIDE

Q9HD42.

Protocols and materials databases

DNASU

5119.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000397901; ENSP00000380998; ENSG00000131165.

GeneID

5119.

KEGG

hsa:5119.

UCSC

uc002fnu.3. human.

Organism-specific databases

CTD

5119.

GeneCards

GC16M089710.

H-InvDB

HIX0013363.

HGNC

HGNC:8740. CHMP1A.

MIM

164010. gene.

neXtProt

NX_Q9HD42.

PharmGKB

PA33085.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG331649.

HOGENOM

HOG000241980.

HOVERGEN

HBG080200.

OrthoDB

EOG4PVP0T.

Gene expression databases

ArrayExpress

Q9HD42.

Bgee

Q9HD42.

CleanEx

HS_CHMP1A.

Genevestigator

Q9HD42.

Family and domain databases

InterPro

IPR005024. Snf7.
[Graphical view]

Pfam

PF03357. Snf7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CHMP1A. human.

EvolutionaryTrace

Q9HD42.

GenomeRNAi

5119.

NextBio

19738.

SOURCE

Search...

Entry information

Entry name

CHM1A_HUMAN

Accession

Primary (citable) accession number: Q9HD42
Secondary accession number(s): A2RU09 , Q14468, Q15779, Q96G31

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 96 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.