Q9NZZ3 (CHMP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Charged multivesicular body protein 5

Alternative name(s):
Chromatin-modifying protein 5
SNF7 domain-containing protein 2
Vacuolar protein sorting-associated protein 60
Short name=Vps60
Short name=hVps60

Gene names

Name:	CHMP5
Synonyms:	C9orf83, SNF7DC2
ORF Names:	CGI-34, HSPC177, PNAS-114, PNAS-2

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	219 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 HIV-1 p6- and p9-dependent virus release. Ref.8
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 VTA1. Interacts with CHMP2A. Interacts with VTA1; the interaction involves soluble CHMP5. Ref.8 Ref.10 Ref.12
Subcellular location	Cytoplasm › cytosol. Endosome membrane; Peripheral membrane protein Probable. Note: Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Ref.10 Ref.11
Sequence similarities	Belongs to the SNF7 family.
Sequence caution	The sequence AAG23821.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular membrane organization Traceable author statement. Source: Reactome endosomal transport Traceable author statement. Source: Reactome endosome to lysosome transport Inferred from electronic annotation. Source: Compara lysosome organization Inferred from electronic annotation. Source: Compara protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of receptor recycling Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAMBP	O95630	2	EBI-751303,EBI-396676

Alternative products

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

Isoform 1 (identifier: Q9NZZ3-1)

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: Q9NZZ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     166-219: ELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIPAS → GWSSGG

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 219

219

Charged multivesicular body protein 5

PRO_0000211500

Regions

Region

121 – 158

38

Interaction with VTA1

Coiled coil

26 – 179

154

Potential

Amino acid modifications

Modified residue

86

1

Phosphoserine Ref.14

Natural variations

Alternative sequence

166 – 219

54

ELDAL…QIPAS → GWSSGG in isoform 2.

VSP_042556

Natural variant

86

1

S → P.
Corresponds to variant rs11540558 [ dbSNP | Ensembl ].

VAR_052029

Experimental info

Sequence conflict

14

1

P → R in AAD27743. Ref.1

Sequence conflict

19

1

D → G in AAH16698. Ref.6

Sequence conflict

84 – 93

10

QQSFNMEQAN → NSHSTWTGH in AAD27743. Ref.1

Sequence conflict

122

1

Q → P in AAD27743. Ref.1

Secondary structure

1

.

.

.

.

.

219

Helix Strand Turn

Details...

Helix

160 – 176

17

Helix

181 – 188

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C99695F66FD7E126	FASTA	219	24,571
	10 20 30 40 50 60 MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM 70 80 90 100 110 120 VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY 130 140 150 160 170 180 KQVKIDQIED LQDQLEDMME DANEIQEALS RSYGTPELDE DDLEAELDAL GDELLADEDS 190 200 210 SYLDEAASAP AIPEGVPTDT KNKDGVLVDE FGLPQIPAS
	Isoform 2 [UniParc]. Checksum: A4986DBBA8926742	FASTA	171	19,520
	10 20 30 40 50 60 MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM 70 80 90 100 110 120 VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY 130 140 150 160 170 KQVKIDQIED LQDQLEDMME DANEIQEALS RSYGTPELDE DDLEAGWSSG G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord blood.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Hippocampus.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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. , 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].
[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] (ISOFORM 1). Tissue: Bone marrow, Brain, Kidney and Urinary bladder.
[7]	"Human acute promyelocytic leukemia cell line NB4's apoptosis related genes." Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-219 (ISOFORM 1). Tissue: Promyelocytic leukemia.
[8]	"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 CHMP2A.
[9]	Erratum Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D. Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[10]	"The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells." Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L., Hill J., Schnegelberger R., Sundquist W.I., Kaplan J. J. Biol. Chem. 280:10548-10555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VTA1.
[11]	"Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis." Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I. EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation." Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T. J. Biol. Chem. 282:9805-9812(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VTA1, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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-86, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132968 mRNA. Translation: AAD27743.1.
AF161525 mRNA. Translation: AAF29140.1.
AK295744 mRNA. Translation: BAG58578.1.
AK315455 mRNA. Translation: BAG37842.1.
AL356472 Genomic DNA. Translation: CAH72744.1.
CH471071 Genomic DNA. Translation: EAW58512.1.
BC006974 mRNA. Translation: AAH06974.1.
BC007457 mRNA. Translation: AAH07457.1.
BC016698 mRNA. Translation: AAH16698.1.
BC020796 mRNA. Translation: AAH20796.1.
BC021168 mRNA. Translation: AAH21168.1.
AF275810 mRNA. Translation: AAG23821.1. Different initiation.
AF229832 mRNA. Translation: AAF42917.1.

IPI

IPI00100796.
IPI00981695.

RefSeq

NP_001182465.1. NM_001195536.1.
NP_057494.3. NM_016410.5.

UniGene

Hs.635313.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LXM	NMR	-	B	139-195	[»]
3ULY	X-ray	2.60	B	151-219	[»]
3UM0	X-ray	3.10	B	200-219	[»]
3UM1	X-ray	2.71	B/E	151-219	[»]
3UM2	X-ray	2.59	B/E	200-219	[»]

ProteinModelPortal

Q9NZZ3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-50420N.

IntAct

Q9NZZ3. 3 interactions.

MINT

MINT-1466639.

STRING

9606.ENSP00000223500.

PTM databases

PhosphoSite

Q9NZZ3.

Polymorphism databases

DMDM

51702157.

Proteomic databases

PaxDb

Q9NZZ3.

PeptideAtlas

Q9NZZ3.

PRIDE

Q9NZZ3.

Protocols and materials databases

DNASU

51510.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000223500; ENSP00000223500; ENSG00000086065.
ENST00000419016; ENSP00000442725; ENSG00000086065.

GeneID

51510.

KEGG

hsa:51510.

UCSC

uc003zsm.4. human.
uc011lnv.2. human.

Organism-specific databases

CTD

51510.

GeneCards

GC09P033257.

HGNC

HGNC:26942. CHMP5.

HPA

CAB033874.
HPA042883.
HPA056437.

MIM

610900. gene.

neXtProt

NX_Q9NZZ3.

PharmGKB

PA134903143.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG300000.

HOGENOM

HOG000191086.

HOVERGEN

HBG055759.

InParanoid

Q9NZZ3.

KO

K12198.

OMA

NQSFNME.

OrthoDB

EOG4PK290.

PhylomeDB

Q9NZZ3.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

Bgee

Q9NZZ3.

CleanEx

HS_CHMP5.

Genevestigator

Q9NZZ3.

GermOnline

ENSG00000086065. Homo sapiens.

Family and domain databases

InterPro

IPR005024. Snf7.
[Graphical view]

Pfam

PF03357. Snf7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CHMP5. human.

GenomeRNAi

51510.

NextBio

55198.

SOURCE

Search...

Entry information

Entry name

CHMP5_HUMAN

Accession

Primary (citable) accession number: Q9NZZ3
Secondary accession number(s): B2RD95 , B4DIR6, Q5VXW2, Q96AV2, Q9HB68, Q9NYS4, Q9Y323

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 102 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.