Q96H20 (SNF8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar-sorting protein SNF8

Alternative name(s):
ELL-associated protein of 30 kDa
ESCRT-II complex subunit VPS22
Short name=hVps22

Gene names

Name:	SNF8
Synonyms:	EAP30

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.11 Ref.12
Subunit structure	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. Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Subcellular location	Cytoplasm. Endosome membrane. Nucleus Probable. Late endosome membrane. Note: Recruited to the endosome membrane to participate in vesicle formation. Ref.6 Ref.7 Ref.9 Ref.11
Sequence similarities	Belongs to the SNF8 family.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular membrane organization Traceable author statement. Source: Reactome endosome transport Traceable author statement. Source: Reactome protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: MGI transcription, DNA-dependent 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 transcription factor complex Inferred from direct assay Ref.1. Source: MGI
Molecular function	transcription factor binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q96H20-1)

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: Q96H20-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 258

258

Vacuolar-sorting protein SNF8

PRO_0000215209

Regions

Coiled coil

27 – 53

27

Potential

Natural variations

Alternative sequence

189

1

Missing in isoform 2.

VSP_015340

Experimental info

Sequence conflict

250

1

A → P in AAD46560. Ref.1

Secondary structure

1

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258

Helix Strand Turn

Details...

Helix

37 – 60

24

Helix

62 – 72

11

Helix

87 – 90

4

Turn

97 – 99

3

Helix

103 – 112

10

Helix

121 – 129

9

Helix

141 – 151

11

Beta strand

167 – 169

3

Helix

178 – 187

10

Helix

195 – 202

8

Helix

206 – 218

13

Beta strand

223 – 227

5

Beta strand

233 – 235

3

Helix

249 – 251

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: FD6CBA6BC0A4485E	FASTA	258	28,864
	10 20 30 40 50 60 MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK 70 80 90 100 110 120 NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT 130 140 150 160 170 180 LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH 190 200 210 220 230 240 TVVLQLAEKN GYVTVSEIKA SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF 250 TDLYSQEITA EEAREALP
	Isoform 2 [UniParc]. Checksum: 14D47FA5682C9197	FASTA	257	28,736
	10 20 30 40 50 60 MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK 70 80 90 100 110 120 NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT 130 140 150 160 170 180 LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH 190 200 210 220 230 240 TVVLQLAENG YVTVSEIKAS LKWETERARQ VLEHLLKEGL AWLDLQAPGE AHYWLPALFT 250 DLYSQEITAE EAREALP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10419521] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Pancreas and Placenta.
[3]	"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: 14505570] [Abstract] 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: 14519844] [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: 16857164] [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: 17010938] [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: 16260042] [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: 16973552] [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: 17959629] [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: 17714434] [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: 18031739] [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: 21269460] [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: 18539118] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 25-258 IN COMPLEX WITH VPS25 AND VPS36.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF156102 mRNA. Translation: AAD46560.1.
BC008976 mRNA. Translation: AAH08976.1.
BC038830 mRNA. Translation: AAH38830.1.

IPI

IPI00101524.
IPI00640699.

RefSeq

NP_009172.2. NM_007241.2.

UniGene

Hs.127249.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZME	X-ray	2.90	A	1-258	[»]
3CUQ	X-ray	2.61	A	25-258	[»]

ProteinModelPortal

Q96H20.

SMR

Q96H20. Positions 34-252.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96H20. 4 interactions.

MINT

MINT-5001874.

STRING

Q96H20.

PTM databases

PhosphoSite

Q96H20.

Polymorphism databases

DMDM

73919323.

Proteomic databases

PRIDE

Q96H20.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290330; ENSP00000290330; ENSG00000159210.

GeneID

11267.

KEGG

hsa:11267.

UCSC

uc002ioj.1. human.
uc002iok.1. human.

Organism-specific databases

CTD

11267.

GeneCards

GC17M047007.

H-InvDB

HIX0135631.
HIX0202482.

HGNC

HGNC:17028. SNF8.

MIM

610904. gene.

neXtProt

NX_Q96H20.

PharmGKB

PA142670892.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11395.

GeneTree

ENSGT00390000007843.

HOGENOM

HBG397278.

HOVERGEN

HBG079872.

InParanoid

Q96H20.

OMA

QFQEMCA.

OrthoDB

EOG4V6ZHD.

PhylomeDB

Q96H20.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpress

Q96H20.

Bgee

Q96H20.

CleanEx

HS_SNF8.

Genevestigator

Q96H20.

GermOnline

ENSG00000159210. Homo sapiens.

Family and domain databases

InterPro

IPR007286. EAP30.
IPR016689. ESCRT-2_cplx_Snf8.
[Graphical view]

KO

K12188.

PANTHER

PTHR12806. EAP30. 1 hit.

Pfam

PF04157. EAP30. 1 hit.
[Graphical view]

PIRSF

PIRSF017215. ESCRT2_Vps22. 1 hit.

ProtoNet

Search...

Other

NextBio

42875.

SOURCE

Search...

Entry information

Entry name

SNF8_HUMAN

Accession

Primary (citable) accession number: Q96H20
Secondary accession number(s): Q8IXY3, Q9UN50

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 86 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.