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Q86VN1 (VPS36_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein-sorting-associated protein 36
Alternative name(s):
ELL-associated protein of 45 kDa
ESCRT-II complex subunit VPS36
Gene names
Name:VPS36
Synonyms:C13orf9, EAP45
ORF Names:CGI-145
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 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 bodies (MVBs) 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. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3. Ref.10

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 two copies of VPS25. Interacts with VPS25, SNF8, TSG101 and VPS36. Interacts (via GLUE domain) with ubiquitin. Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes. Interacts with ECM29. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14

Subcellular location

Cytoplasm. Endosome. Late endosome. Membrane. Nucleus Probable. Note: Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Domain

The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates the binding to ubiquitin and phosphoinosides. Ref.10

Sequence similarities

Belongs to the VPS36 family.

Contains 1 GLUE C-terminal domain.

Contains 1 GLUE N-terminal domain.

Sequence caution

The sequence BAB14451.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86VN1-1)

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: Q86VN1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Vacuolar protein-sorting-associated protein 36
PRO_0000215222

Regions

Domain1 – 8888GLUE N-terminal
Domain105 – 13834GLUE C-terminal
Coiled coil160 – 18526 Potential

Natural variations

Alternative sequence1 – 5858Missing in isoform 2.
VSP_015342

Experimental info

Mutagenesis101L → D: No effect on interaction with ubiquitin. Ref.16
Mutagenesis671V → A: Reduces affinity for ubiquitin up to 10-fold. Ref.16
Mutagenesis681F → A: Reduces affinity for ubiquitin up to 10-fold. Ref.16
Mutagenesis701E → A: Reduces affinity for ubiquitin up to 10-fold. Ref.16
Sequence conflict1851M → V in CAI45953. Ref.3
Sequence conflict2231S → R in AAD34140. Ref.1

Secondary structure

..................................................... 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 21E1E66F71BA7764

FASTA38643,817
        10         20         30         40         50         60 
MDRFVWTSGL LEINETLVIQ QRGVRIYDGE EKIKFDAGTL LLSTHRLIWR DQKNHECCMA 

        70         80         90        100        110        120 
ILLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS SKNSYIKLSF KEHGQIEFYR 

       130        140        150        160        170        180 
RLSEEMTQRR WENMPVSQSL QTNRGPQPGR IRAVGIVGIE RKLEEKRKET DKNISEAFED 

       190        200        210        220        230        240 
LSKLMIKAKE MVELSKSIAN KIKDKQGDIT EDETIRFKSY LLSMGIANPV TRETYGSGTQ 

       250        260        270        280        290        300 
YHMQLAKQLA GILQVPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP 

       310        320        330        340        350        360 
LRLRVFDSGV MVIELQSHKE EEMVASALET VSEKGSLTSE EFAKLVGMSV LLAKERLLLA 

       370        380 
EKMGHLCRDD SVEGLRFYPN LFMTQS 

« Hide

Isoform 2 [UniParc].

Checksum: F6078BBD25CC0032
Show »

FASTA32836,958

References

« Hide 'large scale' references
[1]"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).
[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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-386.
Tissue: Brain and Teratocarcinoma.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Retina.
[4]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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: Brain.
[7]"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 VPS25; SNF8 AND TSG101.
[8]"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.
[9]Erratum
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[10]"Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain."
Slagsvold T., Aasland R., Hirano S., Bache K.G., Raiborg C., Trambaiolo D., Wakatsuki S., Stenmark H.
J. Biol. Chem. 280:19600-19606(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, INTERACTION WITH UBIQUITIN.
[11]"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 AND RILPL1, SUBCELLULAR LOCATION.
[12]"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; SNF8 AND TSG101, UBIQUITIN-BINDING, SUBCELLULAR LOCATION.
[13]"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: SUBCELLULAR LOCATION.
[14]"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
[15]"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].
[16]"Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain."
Alam S.L., Langelier C., Whitby F.G., Koirala S., Robinson H., Hill C.P., Sundquist W.I.
Nat. Struct. Mol. Biol. 13:1029-1030(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-138 IN COMPLEX WITH UBIQUITIN, MUTAGENESIS OF LEU-10; VAL-67; PHE-68 AND GLU-70.
[17]"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 169-386 IN COMPLEX WITH VPS25 AND SNF8.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF151903 mRNA. Translation: AAD34140.1.
AK023182 mRNA. Translation: BAB14451.1. Different initiation.
AK289740 mRNA. Translation: BAF82429.1.
CR933653 mRNA. Translation: CAI45953.1.
AL359513 Genomic DNA. Translation: CAH71658.1.
CH471274 Genomic DNA. Translation: EAW55895.1.
BC037279 mRNA. Translation: AAH37279.1.
BC050439 mRNA. Translation: AAH50439.1.
CCDSCCDS9434.1. [Q86VN1-1]
RefSeqNP_001269098.1. NM_001282169.1. [Q86VN1-2]
NP_057159.2. NM_016075.3. [Q86VN1-1]
UniGeneHs.109520.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HTHX-ray2.70B1-138[»]
2ZMEX-ray2.90B149-386[»]
3CUQX-ray2.61B169-386[»]
ProteinModelPortalQ86VN1.
SMRQ86VN1. Positions 3-131, 172-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119234. 32 interactions.
DIPDIP-29249N.
IntActQ86VN1. 2 interactions.
MINTMINT-3085996.
STRING9606.ENSP00000367299.

PTM databases

PhosphoSiteQ86VN1.

Polymorphism databases

DMDM73920464.

Proteomic databases

MaxQBQ86VN1.
PaxDbQ86VN1.
PRIDEQ86VN1.

Protocols and materials databases

DNASU51028.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378060; ENSP00000367299; ENSG00000136100. [Q86VN1-1]
GeneID51028.
KEGGhsa:51028.
UCSCuc001vgq.3. human. [Q86VN1-1]

Organism-specific databases

CTD51028.
GeneCardsGC13M052986.
HGNCHGNC:20312. VPS36.
HPAHPA039734.
HPA043947.
MIM610903. gene.
neXtProtNX_Q86VN1.
PharmGKBPA134990943.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262969.
HOVERGENHBG083632.
InParanoidQ86VN1.
KOK12190.
OMACCIAIPL.
OrthoDBEOG7VB2FM.
PhylomeDBQ86VN1.
TreeFamTF314770.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

BgeeQ86VN1.
CleanExHS_VPS36.
GenevestigatorQ86VN1.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR007286. EAP30.
IPR021648. VPS36_GLUE.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF04157. EAP30. 1 hit.
PF11605. Vps36_ESCRT-II. 1 hit.
[Graphical view]
PROSITEPS51495. GLUE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVPS36. human.
EvolutionaryTraceQ86VN1.
GeneWikiVPS36.
GenomeRNAi51028.
NextBio53573.
PROQ86VN1.
SOURCESearch...

Entry information

Entry nameVPS36_HUMAN
AccessionPrimary (citable) accession number: Q86VN1
Secondary accession number(s): A8K125 expand/collapse secondary AC list , Q3ZCV7, Q5H9S1, Q5VXB6, Q9H8Z5, Q9Y3E3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 113 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 chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM