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Protein

Vacuolar-sorting protein SNF8

Gene

SNF8

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

Functioni

Component of the endosomal sorting complex required for transport II (ESCRT-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 by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).4 Publications

GO - Molecular functioni

  • channel regulator activity Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: MGI

GO - Biological processi

  • autophagy Source: ParkinsonsUK-UCL
  • early endosome to late endosome transport Source: UniProtKB
  • endocytic recycling Source: UniProtKB
  • endosomal transport Source: Reactome
  • membrane organization Source: Reactome
  • multivesicular body assembly Source: ParkinsonsUK-UCL
  • multivesicular body sorting pathway Source: ParkinsonsUK-UCL
  • positive regulation of exosomal secretion Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of protein catabolic process Source: UniProtKB
  • protein targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: GO_Central
  • regulation of multivesicular body size involved in endosome transport Source: UniProtKB
  • regulation of protein catabolic process Source: UniProtKB
  • regulation of protein complex stability Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of viral budding via host ESCRT complex Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar-sorting protein SNF8
Alternative name(s):
ELL-associated protein of 30 kDa
ESCRT-II complex subunit VPS22
Short name:
hVps22
Gene namesi
Name:SNF8
Synonyms:EAP30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17028. SNF8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endosome membrane Source: UniProtKB
  • ESCRT II complex Source: ParkinsonsUK-UCL
  • extracellular exosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • recycling endosome Source: UniProtKB
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670892.

Polymorphism and mutation databases

BioMutaiSNF8.
DMDMi73919323.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Vacuolar-sorting protein SNF8PRO_0000215209Add
BLAST

Proteomic databases

EPDiQ96H20.
MaxQBiQ96H20.
PaxDbiQ96H20.
PRIDEiQ96H20.

PTM databases

iPTMnetiQ96H20.
PhosphoSiteiQ96H20.

Expressioni

Gene expression databases

BgeeiQ96H20.
CleanExiHS_SNF8.
ExpressionAtlasiQ96H20. baseline and differential.
GenevisibleiQ96H20. HS.

Organism-specific databases

HPAiHPA059320.

Interactioni

Subunit structurei

Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS25 and VPS36. SNF8 is essential for the stability of the ESCRT-II complex. ESCRT-II interacts with ELL. Interacts with TSG101 (via the C-terminal domain). Interacts with RILPL1 (via the N-terminal domain); which recruits ESCRT-II to the endosome membranes. Interacts with 14-3-3 proteins.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ELLP551993EBI-747719,EBI-1245868
GOLGA2Q083793EBI-747719,EBI-618309
KDM1AO603412EBI-747719,EBI-710124
MCM2P497368EBI-747719,EBI-374819
POLR2AP249282EBI-747719,EBI-295301
PRMT6Q96LA82EBI-747719,EBI-912440
STAU1O95793-23EBI-747719,EBI-358189
TRIM54Q9BYV23EBI-747719,EBI-2130429
VAC14Q08AM63EBI-747719,EBI-2107455
VPS25Q9BRG17EBI-747719,EBI-741945

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi116425. 41 interactions.
IntActiQ96H20. 16 interactions.
MINTiMINT-5001874.
STRINGi9606.ENSP00000421380.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 6024Combined sources
Helixi62 – 7514Combined sources
Helixi86 – 916Combined sources
Helixi93 – 11523Combined sources
Beta strandi116 – 1205Combined sources
Helixi121 – 13010Combined sources
Turni131 – 1344Combined sources
Helixi141 – 15111Combined sources
Helixi152 – 1543Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi159 – 1635Combined sources
Beta strandi166 – 1705Combined sources
Helixi178 – 18710Combined sources
Turni188 – 1903Combined sources
Beta strandi191 – 1933Combined sources
Helixi195 – 2028Combined sources
Helixi206 – 21813Combined sources
Beta strandi223 – 2319Combined sources
Beta strandi233 – 2353Combined sources
Helixi249 – 2513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZMEX-ray2.90A1-258[»]
3CUQX-ray2.61A25-258[»]
ProteinModelPortaliQ96H20.
SMRiQ96H20. Positions 34-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96H20.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili27 – 5327Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SNF8 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3341. Eukaryota.
ENOG410XPVM. LUCA.
GeneTreeiENSGT00390000007843.
HOGENOMiHOG000170930.
HOVERGENiHBG079872.
InParanoidiQ96H20.
KOiK12188.
OMAiWFPSLFP.
OrthoDBiEOG73FQNG.
PhylomeDBiQ96H20.
TreeFamiTF105950.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR007286. EAP30.
IPR016689. ESCRT-2_cplx_Snf8.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12806. PTHR12806. 1 hit.
PfamiPF04157. EAP30. 1 hit.
[Graphical view]
PIRSFiPIRSF017215. ESCRT2_Vps22. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96H20-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF
60 70 80 90 100
ASKHKQEIRK NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL
110 120 130 140 150
GVQIIEVCLA LKHRNGGLIT LEELHQQVLK GRGKFAQDVS QDDLIRAIKK
160 170 180 190 200
LKALGTGFGI IPVGGTYLIQ SVPAELNMDH TVVLQLAEKN GYVTVSEIKA
210 220 230 240 250
SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF TDLYSQEITA

EEAREALP
Length:258
Mass (Da):28,864
Last modified:December 1, 2001 - v1
Checksum:iFD6CBA6BC0A4485E
GO
Isoform 2 (identifier: Q96H20-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-189: Missing.

Note: No experimental confirmation available.
Show »
Length:257
Mass (Da):28,736
Checksum:i14D47FA5682C9197
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501A → P in AAD46560 (PubMed:10419521).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei189 – 1891Missing in isoform 2. 1 PublicationVSP_015340

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156102 mRNA. Translation: AAD46560.1.
BC008976 mRNA. Translation: AAH08976.1.
BC038830 mRNA. Translation: AAH38830.1.
CCDSiCCDS11541.1. [Q96H20-1]
RefSeqiNP_001304121.1. NM_001317192.1. [Q96H20-2]
NP_001304122.1. NM_001317193.1.
NP_001304123.1. NM_001317194.1.
NP_009172.2. NM_007241.3. [Q96H20-1]
UniGeneiHs.127249.

Genome annotation databases

EnsembliENST00000290330; ENSP00000290330; ENSG00000159210. [Q96H20-2]
ENST00000502492; ENSP00000421380; ENSG00000159210. [Q96H20-1]
GeneIDi11267.
KEGGihsa:11267.
UCSCiuc002ioj.5. human. [Q96H20-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156102 mRNA. Translation: AAD46560.1.
BC008976 mRNA. Translation: AAH08976.1.
BC038830 mRNA. Translation: AAH38830.1.
CCDSiCCDS11541.1. [Q96H20-1]
RefSeqiNP_001304121.1. NM_001317192.1. [Q96H20-2]
NP_001304122.1. NM_001317193.1.
NP_001304123.1. NM_001317194.1.
NP_009172.2. NM_007241.3. [Q96H20-1]
UniGeneiHs.127249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZMEX-ray2.90A1-258[»]
3CUQX-ray2.61A25-258[»]
ProteinModelPortaliQ96H20.
SMRiQ96H20. Positions 34-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116425. 41 interactions.
IntActiQ96H20. 16 interactions.
MINTiMINT-5001874.
STRINGi9606.ENSP00000421380.

PTM databases

iPTMnetiQ96H20.
PhosphoSiteiQ96H20.

Polymorphism and mutation databases

BioMutaiSNF8.
DMDMi73919323.

Proteomic databases

EPDiQ96H20.
MaxQBiQ96H20.
PaxDbiQ96H20.
PRIDEiQ96H20.

Protocols and materials databases

DNASUi11267.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290330; ENSP00000290330; ENSG00000159210. [Q96H20-2]
ENST00000502492; ENSP00000421380; ENSG00000159210. [Q96H20-1]
GeneIDi11267.
KEGGihsa:11267.
UCSCiuc002ioj.5. human. [Q96H20-1]

Organism-specific databases

CTDi11267.
GeneCardsiSNF8.
H-InvDBHIX0135631.
HGNCiHGNC:17028. SNF8.
HPAiHPA059320.
MIMi610904. gene.
neXtProtiNX_Q96H20.
PharmGKBiPA142670892.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3341. Eukaryota.
ENOG410XPVM. LUCA.
GeneTreeiENSGT00390000007843.
HOGENOMiHOG000170930.
HOVERGENiHBG079872.
InParanoidiQ96H20.
KOiK12188.
OMAiWFPSLFP.
OrthoDBiEOG73FQNG.
PhylomeDBiQ96H20.
TreeFamiTF105950.

Enzyme and pathway databases

ReactomeiR-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

ChiTaRSiSNF8. human.
EvolutionaryTraceiQ96H20.
GeneWikiiSNF8.
GenomeRNAii11267.
NextBioi42875.
PROiQ96H20.
SOURCEiSearch...

Gene expression databases

BgeeiQ96H20.
CleanExiHS_SNF8.
ExpressionAtlasiQ96H20. baseline and differential.
GenevisibleiQ96H20. HS.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR007286. EAP30.
IPR016689. ESCRT-2_cplx_Snf8.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12806. PTHR12806. 1 hit.
PfamiPF04157. EAP30. 1 hit.
[Graphical view]
PIRSFiPIRSF017215. ESCRT2_Vps22. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II."
    Schmidt A.E., Miller T., Schmidt S.L., Shiekhattar R., Shilatifard A.
    J. Biol. Chem. 274:21981-21985(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Pancreas and Placenta.
  3. Cited for: SELF-ASSOCIATION, INTERACTION WITH VPS25; VPS36 AND TSG101.
  4. "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 AND VPS25.
  5. Erratum
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
  6. "RILP interacts with the VPS22 component of the ESCRT-II complex."
    Progida C., Spinosa M.R., De Luca A., Bucci C.
    Biochem. Biophys. Res. Commun. 347:1074-1079(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RILPL1, SUBCELLULAR LOCATION.
  7. "RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment."
    Wang T., Hong W.
    Biochem. Biophys. Res. Commun. 350:413-423(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPS25; VPS36 AND RILPL1, SUBCELLULAR LOCATION.
  8. "Rapid identification of 14-3-3-binding proteins by protein microarray analysis."
    Satoh J., Nanri Y., Yamamura T.
    J. Neurosci. Methods 152:278-288(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3 PROTEINS.
  9. "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 VPS25; VPS36 AND TSG101, SUBCELLULAR LOCATION.
  10. "RILP is required for the proper morphology and function of late endosomes."
    Progida C., Malerod L., Stuffers S., Brech A., Bucci C., Stenmark H.
    J. Cell Sci. 120:3729-3737(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation."
    Maleroed L., Stuffers S., Brech A., Stenmark H.
    Traffic 8:1617-1629(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  12. "Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking."
    Raiborg C., Malerod L., Pedersen N.M., Stenmark H.
    Exp. Cell Res. 314:801-813(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: FUNCTION.
  15. "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) OF 25-258 IN COMPLEX WITH VPS25 AND VPS36.

Entry informationi

Entry nameiSNF8_HUMAN
AccessioniPrimary (citable) accession number: Q96H20
Secondary accession number(s): Q8IXY3, Q9UN50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 130 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.