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Q9BRG1 (VPS25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein-sorting-associated protein 25

Short name=hVps25
Alternative name(s):
Dermal papilla-derived protein 9
ELL-associated protein of 20 kDa
ESCRT-II complex subunit VPS25
Gene names
Name:VPS25
Synonyms:DERP9, EAP20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. The ESCRT-II complex may be involved in facilitating the budding of certain RNA viruses. Ref.12

Subunit structure

Component of a complex at least composed of ELL, SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 By similarity. Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS36 and 2 copies of VPS25. Interacts with CFTR; the interaction requires misfolded CFTR. Interacts (via C-terminal half) with the ESCRT-III subunit CHMP6 (via N-terminal half). Ref.5 Ref.6 Ref.8 Ref.9 Ref.11

Subcellular location

Cytoplasm. Endosome membrane. Nucleusnucleoplasm. Note: Distributes diffusely throughout the cytoplasm and nucleoplasm, but exhibits a punctate distribution on coexpression with CHMP6. Ref.8 Ref.11

Tissue specificity

Expressed at the mRNA level in kidney, liver, pancreas, and placenta. Lower levels of expression are found in heart, skeletal muscle, brain and lung. Ref.10

Sequence similarities

Belongs to the VPS25 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 176176Vacuolar protein-sorting-associated protein 25
PRO_0000215216

Natural variations

Natural variant761I → V.
Corresponds to variant rs34494804 [ dbSNP | Ensembl ].
VAR_048940

Experimental info

Mutagenesis1241V → E: Abolishes binding to CHMP6. Ref.15
Mutagenesis1261T → K: Abolishes binding to CHMP6. Ref.15

Secondary structure

...................................... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BRG1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 34963A53C3DA4DD5

FASTA17620,748
        10         20         30         40         50         60 
MAMSFEWPWQ YRFPPFFTLQ PNVDTRQKQL AAWCSLVLSF CRLHKQSSMT VMEAQESPLF 

        70         80         90        100        110        120 
NNVKLQRKLP VESIQIVLEE LRKKGNLEWL DKSKSSFLIM WRRPEEWGKL IYQWVSRSGQ 

       130        140        150        160        170 
NNSVFTLYEL TNGEDTEDEE FHGLDEATLL RALQALQQEH KAEIITVSDG RGVKFF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a dermal papilla derived gene."
Ikeda A., Ukai Y., Yamashita M., Yoshimoto M.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hair follicle dermal papilla.
[2]"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. expand/collapse author list , 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].
Tissue: Cerebellum.
[3]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Skin.
[5]"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 SNF8; VPS36 AND CHMP6.
[6]"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: IDENTIFICATION IN THE ESCRT-II COMPLEX, INTERACTION WITH VPS36; SNF8 AND CHMP6.
[7]Erratum
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[8]"Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting."
Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K., Kobayashi T., Uchiyama Y., Maki M.
Biochem. J. 387:17-26(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHMP6.
[9]"Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes."
Sharma M., Pampinella F., Nemes C., Benharouga M., So J., Du K., Bache K.G., Papsin B., Zerangue N., Stenmark H., Lukacs G.L.
J. Cell Biol. 164:923-933(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MISFOLDED CFTR.
[10]"Genetic structure and evolution of the Vps25 family, a yeast ESCRT-II component."
Slater R., Bishop N.E.
BMC Evol. Biol. 6:59-59(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release."
Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I., White P.L., Hill C.P., Kaplan J., Ward D., Sundquist W.I.
J. Virol. 80:9465-9480(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNF8; VPS36 AND CHMP6, SUBCELLULAR LOCATION.
[12]"Avian sarcoma virus and human immunodeficiency virus, type 1 use different subsets of ESCRT proteins to facilitate the budding process."
Pincetic A., Medina G., Carter C., Leis J.
J. Biol. Chem. 283:29822-29830(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex."
Im Y.J., Hurley J.H.
Dev. Cell 14:902-913(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN COMPLEX WITH SNF8 AND VPS36.
[15]"Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis."
Im Y.J., Wollert T., Boura E., Hurley J.H.
Dev. Cell 17:234-243(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 102-176 IN COMPLEX WITH CHMP6, MUTAGENESIS OF VAL-124 AND THR-126.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014763 mRNA. Translation: BAB87804.1.
AK312092 mRNA. Translation: BAG35028.1.
CH471152 Genomic DNA. Translation: EAW60879.1.
BC006282 mRNA. Translation: AAH06282.1.
CCDSCCDS11438.1.
RefSeqNP_115729.1. NM_032353.3.
UniGeneHs.500165.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZMEX-ray2.90C/D1-102[»]
3CUQX-ray2.61C/D1-176[»]
3HTUX-ray2.00A/C/E/G102-176[»]
ProteinModelPortalQ9BRG1.
SMRQ9BRG1. Positions 4-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124039. 28 interactions.
IntActQ9BRG1. 4 interactions.
MINTMINT-5003482.
STRING9606.ENSP00000253794.

PTM databases

PhosphoSiteQ9BRG1.

Polymorphism databases

DMDM73920459.

Proteomic databases

MaxQBQ9BRG1.
PaxDbQ9BRG1.
PeptideAtlasQ9BRG1.
PRIDEQ9BRG1.

Protocols and materials databases

DNASU84313.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253794; ENSP00000253794; ENSG00000131475.
GeneID84313.
KEGGhsa:84313.
UCSCuc002ibi.3. human.

Organism-specific databases

CTD84313.
GeneCardsGC17P040925.
HGNCHGNC:28122. VPS25.
HPACAB004978.
HPA052217.
HPA057284.
MIM610907. gene.
neXtProtNX_Q9BRG1.
PharmGKBPA142670614.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270942.
HOGENOMHOG000191978.
HOVERGENHBG080015.
InParanoidQ9BRG1.
KOK12189.
OMAPPFFTIQ.
OrthoDBEOG7BGHN9.
PhylomeDBQ9BRG1.
TreeFamTF317731.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ9BRG1.
BgeeQ9BRG1.
CleanExHS_VPS25.
GenevestigatorQ9BRG1.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.10.570. 1 hit.
InterProIPR008570. ESCRT-II_cplx_vps25-sub.
IPR014041. ESCRT-II_cplx_Vps25-sub_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR13149. PTHR13149. 1 hit.
PfamPF05871. ESCRT-II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BRG1.
GeneWikiVPS25.
GenomeRNAi84313.
NextBio74014.
PROQ9BRG1.
SOURCESearch...

Entry information

Entry nameVPS25_HUMAN
AccessionPrimary (citable) accession number: Q9BRG1
Secondary accession number(s): B2R581
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM