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Q9BRG1

- VPS25_HUMAN

UniProt

Q9BRG1 - VPS25_HUMAN

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Protein

Vacuolar protein-sorting-associated protein 25

Gene

VPS25

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. protein homodimerization activity Source: UniProt

GO - Biological processi

  1. endosomal transport Source: Reactome
  2. membrane organization Source: Reactome
  3. protein transport Source: UniProtKB-KW
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:VPS25
Synonyms:DERP9, EAP20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:28122. VPS25.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endosome membrane Source: UniProt
  3. extracellular vesicular exosome Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. nucleolus Source: HPA
  6. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1241V → E: Abolishes binding to CHMP6. 1 Publication
Mutagenesisi126 – 1261T → K: Abolishes binding to CHMP6. 1 Publication

Organism-specific databases

PharmGKBiPA142670614.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 176176Vacuolar protein-sorting-associated protein 25PRO_0000215216Add
BLAST

Proteomic databases

MaxQBiQ9BRG1.
PaxDbiQ9BRG1.
PeptideAtlasiQ9BRG1.
PRIDEiQ9BRG1.

PTM databases

PhosphoSiteiQ9BRG1.

Expressioni

Tissue specificityi

Expressed at the mRNA level in kidney, liver, pancreas, and placenta. Lower levels of expression are found in heart, skeletal muscle, brain and lung.1 Publication

Gene expression databases

BgeeiQ9BRG1.
CleanExiHS_VPS25.
ExpressionAtlasiQ9BRG1. baseline and differential.
GenevestigatoriQ9BRG1.

Organism-specific databases

HPAiCAB004978.
HPA052217.
HPA057284.

Interactioni

Subunit structurei

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).By similarity7 Publications

Protein-protein interaction databases

BioGridi124039. 28 interactions.
IntActiQ9BRG1. 4 interactions.
MINTiMINT-5003482.
STRINGi9606.ENSP00000253794.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined sources
Helixi14 – 174Combined sources
Helixi23 – 4422Combined sources
Beta strandi48 – 503Combined sources
Helixi51 – 555Combined sources
Beta strandi60 – 623Combined sources
Turni63 – 664Combined sources
Helixi71 – 8414Combined sources
Beta strandi86 – 894Combined sources
Beta strandi91 – 999Combined sources
Helixi104 – 11613Combined sources
Turni117 – 1193Combined sources
Beta strandi123 – 1253Combined sources
Helixi127 – 1326Combined sources
Turni135 – 1384Combined sources
Turni140 – 1434Combined sources
Helixi146 – 15813Combined sources
Beta strandi161 – 1655Combined sources
Turni167 – 1693Combined sources
Beta strandi172 – 1754Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZMEX-ray2.90C/D1-102[»]
3CUQX-ray2.61C/D1-176[»]
3HTUX-ray2.00A/C/E/G102-176[»]
ProteinModelPortaliQ9BRG1.
SMRiQ9BRG1. Positions 4-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BRG1.

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS25 family.Curated

Phylogenomic databases

eggNOGiNOG270942.
GeneTreeiENSGT00390000014892.
HOGENOMiHOG000191978.
HOVERGENiHBG080015.
InParanoidiQ9BRG1.
KOiK12189.
OMAiPPFFTIQ.
OrthoDBiEOG7BGHN9.
PhylomeDBiQ9BRG1.
TreeFamiTF317731.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.570. 1 hit.
InterProiIPR008570. ESCRT-II_cplx_vps25-sub.
IPR014041. ESCRT-II_cplx_Vps25-sub_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13149. PTHR13149. 1 hit.
PfamiPF05871. ESCRT-II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BRG1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMSFEWPWQ YRFPPFFTLQ PNVDTRQKQL AAWCSLVLSF CRLHKQSSMT
60 70 80 90 100
VMEAQESPLF NNVKLQRKLP VESIQIVLEE LRKKGNLEWL DKSKSSFLIM
110 120 130 140 150
WRRPEEWGKL IYQWVSRSGQ NNSVFTLYEL TNGEDTEDEE FHGLDEATLL
160 170
RALQALQQEH KAEIITVSDG RGVKFF
Length:176
Mass (Da):20,748
Last modified:June 1, 2001 - v1
Checksum:i34963A53C3DA4DD5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761I → V.
Corresponds to variant rs34494804 [ dbSNP | Ensembl ].
VAR_048940

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014763 mRNA. Translation: BAB87804.1.
AK312092 mRNA. Translation: BAG35028.1.
CH471152 Genomic DNA. Translation: EAW60879.1.
BC006282 mRNA. Translation: AAH06282.1.
CCDSiCCDS11438.1.
RefSeqiNP_115729.1. NM_032353.3.
UniGeneiHs.500165.

Genome annotation databases

EnsembliENST00000253794; ENSP00000253794; ENSG00000131475.
GeneIDi84313.
KEGGihsa:84313.
UCSCiuc002ibi.3. human.

Polymorphism databases

DMDMi73920459.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014763 mRNA. Translation: BAB87804.1 .
AK312092 mRNA. Translation: BAG35028.1 .
CH471152 Genomic DNA. Translation: EAW60879.1 .
BC006282 mRNA. Translation: AAH06282.1 .
CCDSi CCDS11438.1.
RefSeqi NP_115729.1. NM_032353.3.
UniGenei Hs.500165.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZME X-ray 2.90 C/D 1-102 [» ]
3CUQ X-ray 2.61 C/D 1-176 [» ]
3HTU X-ray 2.00 A/C/E/G 102-176 [» ]
ProteinModelPortali Q9BRG1.
SMRi Q9BRG1. Positions 4-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124039. 28 interactions.
IntActi Q9BRG1. 4 interactions.
MINTi MINT-5003482.
STRINGi 9606.ENSP00000253794.

PTM databases

PhosphoSitei Q9BRG1.

Polymorphism databases

DMDMi 73920459.

Proteomic databases

MaxQBi Q9BRG1.
PaxDbi Q9BRG1.
PeptideAtlasi Q9BRG1.
PRIDEi Q9BRG1.

Protocols and materials databases

DNASUi 84313.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253794 ; ENSP00000253794 ; ENSG00000131475 .
GeneIDi 84313.
KEGGi hsa:84313.
UCSCi uc002ibi.3. human.

Organism-specific databases

CTDi 84313.
GeneCardsi GC17P040925.
HGNCi HGNC:28122. VPS25.
HPAi CAB004978.
HPA052217.
HPA057284.
MIMi 610907. gene.
neXtProti NX_Q9BRG1.
PharmGKBi PA142670614.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270942.
GeneTreei ENSGT00390000014892.
HOGENOMi HOG000191978.
HOVERGENi HBG080015.
InParanoidi Q9BRG1.
KOi K12189.
OMAi PPFFTIQ.
OrthoDBi EOG7BGHN9.
PhylomeDBi Q9BRG1.
TreeFami TF317731.

Enzyme and pathway databases

Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

ChiTaRSi VPS25. human.
EvolutionaryTracei Q9BRG1.
GeneWikii VPS25.
GenomeRNAii 84313.
NextBioi 74014.
PROi Q9BRG1.
SOURCEi Search...

Gene expression databases

Bgeei Q9BRG1.
CleanExi HS_VPS25.
ExpressionAtlasi Q9BRG1. baseline and differential.
Genevestigatori Q9BRG1.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.10.10.570. 1 hit.
InterProi IPR008570. ESCRT-II_cplx_vps25-sub.
IPR014041. ESCRT-II_cplx_Vps25-sub_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR13149. PTHR13149. 1 hit.
Pfami PF05871. ESCRT-II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiVPS25_HUMAN
AccessioniPrimary (citable) accession number: Q9BRG1
Secondary accession number(s): B2R581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3