Q9Y3E7 (CHMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Charged multivesicular body protein 3

Alternative name(s):
Chromatin-modifying protein 3
Neuroendocrine differentiation factor
Vacuolar protein sorting-associated protein 24
Short name=hVps24

Gene names

Name:	CHMP3
Synonyms:	CGI149, NEDF, VPS24
ORF Names:	CGI-149

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	222 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable core 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. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells. Ref.2 Ref.4 Ref.10 Ref.21 Ref.27
Subunit structure	Probable core 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. Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. May interact with IGFBP7; the relevance of such interaction however remains unclear. Interacts with CHMP2A. Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3. Ref.1 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.22 Ref.27 Ref.28
Subcellular location	Cytoplasm › cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane Probable. Note: Localizes to the midbody of dividing cells. Ref.2 Ref.14 Ref.21
Tissue specificity	Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.13
Domain	The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.
Miscellaneous	Its overexpression strongly inhibits HIV-1 release.
Sequence similarities	Belongs to the SNF7 family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Isopeptide bond Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular membrane organization Traceable author statement. Source: Reactome endosomal transport Traceable author statement. Source: Reactome protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAMBP	O95630	5	EBI-2118119,EBI-396676

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y3E7-1)

Also known as: Vps24alpha;

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: Q9Y3E7-2)

Also known as: Vps24beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Isoform 3 (identifier: Q9Y3E7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGLFGKTQEKPPKEL → MEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQ

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9Y3E7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-113: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Charged multivesicular body protein 3

PRO_0000211479

Regions

Region

1 – 113

113

Intramolecular interaction with C-terminus

Region

59 – 64

6

Important for autoinhibitory function

Region

151 – 222

72

Interaction with VPS4A

Region

151 – 220

70

Intramolecular interaction with N-terminus

Region

168 – 169

2

Important for autoinhibitory function

Region

203 – 207

5

Interaction with STAMBP

Region

221 – 222

2

Interaction with STAMBP

Coiled coil

22 – 54

33

Potential

Coiled coil

141 – 222

82

Potential

Motif

201 – 211

11

MIT-interacting motif

Sites

Binding site

216

1

STAMBP

Site

48

1

Important for autoinhibitory function

Amino acid modifications

Modified residue

116

1

Phosphoserine By similarity

Modified residue

126

1

Phosphothreonine By similarity

Modified residue

200

1

Phosphoserine Ref.19 Ref.23 Ref.24 Ref.26

Lipidation

2

1

N-myristoyl glycine Potential

Cross-link

179

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18

Natural variations

Alternative sequence

1 – 66

66

Missing in isoform 2.

VSP_041076

Alternative sequence

1 – 15

15

MGLFG…PPKEL → MEGELYSALKEEEASESVSS TNFSGEMHFYELVEDTKDGI WLVQ in isoform 3.

VSP_042124

Alternative sequence

74 – 113

40

Missing in isoform 4.

VSP_042125

Experimental info

Mutagenesis

24 – 25

2

RK → SA: Impairs HIV-1 release; when associated with S-28.

Mutagenesis

28

1

R → S: Impairs HIV-1 release; when associated with 24-S-A-25. Ref.27

Mutagenesis

48

1

V → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-64. Enhances inhibition of HIV-1 budding in vivo; when associated with D-168 and D-169. Ref.28

Mutagenesis

54

1

K → S: Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63. Ref.27

Mutagenesis

56

1

Q → N: Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63. Ref.27

Mutagenesis

59

1

V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169. Ref.27 Ref.28

Mutagenesis

59

1

V → E: Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63. Ref.27 Ref.28

Mutagenesis

62 – 63

2

VL → DE: Abolishes dimerization; when associated with S-54; N-56 and E-59. Ref.28

Mutagenesis

62

1

V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169. Ref.28

Mutagenesis

64

1

A → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48. Ref.28

Mutagenesis

78 – 79

2

YA → AE: Abolishes dimerization.

Mutagenesis

168 – 169

2

IL → DD: Induces assembly with CHMP2A into helical tubes in vitro and slightly enhances inhibition of HIV-1 budding in vivo. Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59 and D-62.

Mutagenesis

179 – 222

44

Missing: Membrane association; releases autoinhibition. Ref.15 Ref.17

Mutagenesis

216 – 217

2

RL → AA: Abolishes interaction with VPS4A and STAMBP.

Mutagenesis

221 – 222

2

Missing: Abolishes interaction with VPS4A and STAMBP. Ref.15

Mutagenesis

222

1

Missing: Impairs interaction with VPS4A and STAMBP. Ref.15

Sequence conflict

208

1

E → D in AAF26737. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

222

Helix Strand Turn

Details...

Helix

15 – 53

39

Helix

57 – 100

44

Helix

109 – 112

4

Turn

113 – 115

3

Beta strand

120 – 122

3

Helix

125 – 137

13

Helix

164 – 167

4

Helix

201 – 220

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Vps24alpha) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7B1ACE5EA453E8C0	FASTA	222	25,073
	10 20 30 40 50 60 MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC 70 80 90 100 110 120 IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI 130 140 150 160 170 180 PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA 190 200 210 220 PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS
	Isoform 2 (Vps24beta) [UniParc]. Checksum: 7B10B4D1FB7E1B62	FASTA	156	17,326
	10 20 30 40 50 60 MIRSRKAVSK LYASKAHMNS VLMGMKNQLA VLRVAGSLQK STEVMKAMQS LVKIPEIQAT 70 80 90 100 110 120 MRELSKEMMK AGIIEEMLED TFESMDDQEE MEEEAEMEID RILFEITAGA LGKAPSKVTD 130 140 150 ALPEPEPPGA MAASEDEEEE EEALEAMQSR LATLRS
	Isoform 3 [UniParc]. Checksum: 0BA3A646BBC05B51	FASTA	251	28,386
	10 20 30 40 50 60 MEGELYSALK EEEASESVSS TNFSGEMHFY ELVEDTKDGI WLVQVNEWSL KIRKEMRVVD 70 80 90 100 110 120 RQIRDIQREE EKVKRSVKDA AKKGQKDVCI VLAKEMIRSR KAVSKLYASK AHMNSVLMGM 130 140 150 160 170 180 KNQLAVLRVA GSLQKSTEVM KAMQSLVKIP EIQATMRELS KEMMKAGIIE EMLEDTFESM 190 200 210 220 230 240 DDQEEMEEEA EMEIDRILFE ITAGALGKAP SKVTDALPEP EPPGAMAASE DEEEEEEALE 250 AMQSRLATLR S
	Isoform 4 [UniParc]. Checksum: E2951422F9E1A226	FASTA	182	20,770
	10 20 30 40 50 60 MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC 70 80 90 100 110 120 IVLAKEMIRS RKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE 130 140 150 160 170 180 AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interaction of IGF-binding protein-related protein 1 with a novel protein, neuroendocrine differentiation factor, results in neuroendocrine differentiation of prostate cancer cells." Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G. J. Clin. Endocrinol. Metab. 86:4504-4511(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE INTERACTION WITH IGFBP7.
[2]	"mVps24p functions in EGF receptor sorting/trafficking from the early endosome." Yan Q., Hunt P.R., Frelin L., Vida T.A., Pevsner J., Bean A.J. Exp. Cell Res. 304:265-273(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION. Tissue: Heart.
[3]	"NovelFam3000 -- uncharacterized human protein domains conserved across model organisms." Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W. BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Characterization of a novel alternatively spliced human transcript encoding an N-terminally truncated Vps24 protein that suppresses the effects of Bax in an ESCRT independent manner in yeast." Khoury C.M., Yang Z., Ismail S., Greenwood M.T. Gene 391:233-241(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION. Tissue: Heart.
[5]	"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).
[6]	"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; 2 AND 3). Tissue: Amygdala, Pericardium and Synovial cell.
[7]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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].
[9]	"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: Uterus.
[10]	"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: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP4A.
[11]	"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: INTERACTION WITH CHMP2A AND VPS4A.
[12]	Erratum Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D. Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[13]	"Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1." Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I. J. Biol. Chem. 280:12799-12809(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[14]	"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.
[15]	"Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding." Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G., Goettlinger H. Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOINHIBITORY MECHANISM, INTRAMOLECULAR INTERACTION, INTERACTION WITH STAMBP AND VPS4A, MUTAGENESIS OF 216-ARG-LEU-217; 221-ARG-SER-222 AND SER-222.
[16]	"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 STAMBP, MASS SPECTROMETRY.
[17]	"Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain." Shim S., Kimpler L.A., Hanson P.I. Traffic 8:1068-1079(2007) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP4A, MUTAGENESIS OF 179-LYS--SER-222.
[18]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-179, MASS SPECTROMETRY.
[19]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Helical structures of ESCRT-III are disassembled by VPS4." Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G., Weissenhorn W. Science 321:1354-1357(2008) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMERIZATION WITH CHMP2A, ELECTRON MICROSCOPY.
[21]	"A dominant-negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes." Dukes J.D., Richardson J.D., Simmons R., Whitley P. Biochem. J. 411:233-239(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION.
[22]	"Structural basis for autoinhibition of ESCRT-III CHMP3." Lata S., Roessle M., Solomons J., Jamin M., Goettlinger H.G., Svergun D.I., Weissenhorn W. J. Mol. Biol. 378:818-827(2008) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOINHIBITORY MECHANISM, INTERACTION WITH STAMBP.
[23]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"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-200, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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].
[26]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY.
[27]	"Structural basis for budding by the ESCRT-III factor CHMP3." Muziol T., Pineda-Molina E., Ravelli R.B., Zamborlini A., Usami Y., Goettlinger H., Weissenhorn W. Dev. Cell 10:821-830(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-183, SUBUNIT, FUNCTION IN HIV-1 BUDDING, MUTAGENESIS OF 24-ARG-LYS-25; ARG-28; LYS-54; GLN-56; VAL-59; 62-VAL-LEU-63 AND 78-TYR-ALA-79.
[28]	"Structural basis for ESCRT-III protein autoinhibition." Bajorek M., Schubert H.L., McCullough J., Langelier C., Eckert D.M., Stubblefield W.M., Uter N.T., Myszka D.G., Hill C.P., Sundquist W.I. Nat. Struct. Mol. Biol. 16:754-762(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-222, INTERACTION WITH CHMP2A, MUTAGENESIS OF VAL-48; VAL-59; VAL-62; ALA-64 AND 168-ILE-LEU-169.
[29]	"Structural basis for Escrt-III Chmp3 recruitment of Amsh." Solomons J., Sabin C., Poudevigne E., Usami Y., Hulsik D.L., Macheboeuf P., Hartlieb B., Gottlinger H., Weissenhorn W. Structure 19:1149-1159(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 183-222 IN COMPLEX WITH STAMBP FRAGMENT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF219226 mRNA. Translation: AAF26737.1.
AY364249 mRNA. Translation: AAQ76808.1.
AF151907 mRNA. Translation: AAD34144.1.
AK290725 mRNA. Translation: BAF83414.1.
AK294389 mRNA. Translation: BAG57645.1.
AK312353 mRNA. Translation: BAG35273.1.
AK315835 mRNA. Translation: BAF98726.1.
AC015971 Genomic DNA. Translation: AAX93078.1.
AC064848 Genomic DNA. No translation available.
AC068288 Genomic DNA. Translation: AAY24211.1.
CH471053 Genomic DNA. Translation: EAW99448.1.
CH471053 Genomic DNA. Translation: EAW99449.1.
CH471053 Genomic DNA. Translation: EAW99450.1.
CH471053 Genomic DNA. Translation: EAW99451.1.
BC004419 mRNA. Translation: AAH04419.1.

IPI

IPI00100673.
IPI00478935.
IPI00979305.
IPI00981241.

RefSeq

NP_001005753.1. NM_001005753.2.
NP_001180446.1. NM_001193517.1.
NP_001185883.1. NM_001198954.1.
NP_057163.1. NM_016079.3.

UniGene

Hs.591582.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GD5	X-ray	2.80	A/B/C/D	9-183	[»]
2XZE	X-ray	1.75	Q/R	183-222	[»]
3FRT	X-ray	4.00	A/B	8-222	[»]
3FRV	X-ray	3.70	A	1-150	[»]

ProteinModelPortal

Q9Y3E7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48532N.

IntAct

Q9Y3E7. 5 interactions.

MINT

MINT-1185988.

STRING

9606.ENSP00000263856.

PTM databases

PhosphoSite

Q9Y3E7.

Polymorphism databases

DMDM

73917763.

Proteomic databases

PaxDb

Q9Y3E7.

PRIDE

Q9Y3E7.

Protocols and materials databases

DNASU

51652.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263856; ENSP00000263856; ENSG00000115561.
ENST00000409225; ENSP00000386590; ENSG00000115561.
ENST00000409727; ENSP00000387045; ENSG00000115561.
ENST00000439940; ENSP00000405575; ENSG00000115561.

GeneID

100526767.
51652.

KEGG

hsa:100526767.
hsa:51652.

UCSC

uc002srj.3. human.

Organism-specific databases

CTD

100526767.
51652.

GeneCards

GC02M086730.

HGNC

HGNC:29865. CHMP3.

HPA

HPA015673.

MIM

610052. gene.

neXtProt

NX_Q9Y3E7.

PharmGKB

PA134920495.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5491.

HOGENOM

HOG000177219.

HOVERGEN

HBG107031.

KO

K12193.

OMA

MSKEMMK.

OrthoDB

EOG4VT5ZB.

PhylomeDB

Q9Y3E7.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

Bgee

Q9Y3E7.

CleanEx

HS_VPS24.

Genevestigator

Q9Y3E7.

GermOnline

ENSG00000115561. Homo sapiens.

Family and domain databases

InterPro

IPR005024. Snf7.
[Graphical view]

Pfam

PF03357. Snf7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CHMP3. human.

EvolutionaryTrace

Q9Y3E7.

NextBio

55614.

SOURCE

Search...

Entry information

Entry name

CHMP3_HUMAN

Accession

Primary (citable) accession number: Q9Y3E7
Secondary accession number(s): A8K3W0 , B4DG34, B8ZZM0, B8ZZX5, Q3ZTS9, Q53S71, Q53SU5, Q9NZ51

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 101 of the entry and version 3 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.