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Protein

Vacuolar protein-sorting-associated protein 36

Gene

VPS36

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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.

GO - Molecular functioni

  • phosphatidylinositol-3-phosphate binding Source: InterPro
  • protein C-terminus binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein-sorting-associated protein 36
Alternative name(s):
ELL-associated protein of 45 kDa
ESCRT-II complex subunit VPS36
Gene namesi
Name:VPS36
Synonyms:C13orf9, EAP45
ORF Names:CGI-145
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20312. VPS36.

Subcellular locationi

  • Cytoplasm
  • Endosome
  • Late endosome By similarity
  • Membrane
  • Nucleus Curated

  • Note: Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation.By similarity

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB
  • lysosome Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101L → D: No effect on interaction with ubiquitin. 1 Publication
Mutagenesisi67 – 671V → A: Reduces affinity for ubiquitin up to 10-fold. 1 Publication
Mutagenesisi68 – 681F → A: Reduces affinity for ubiquitin up to 10-fold. 1 Publication
Mutagenesisi70 – 701E → A: Reduces affinity for ubiquitin up to 10-fold. 1 Publication

Organism-specific databases

PharmGKBiPA134990943.

Polymorphism and mutation databases

DMDMi73920464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Vacuolar protein-sorting-associated protein 36PRO_0000215222Add
BLAST

Proteomic databases

MaxQBiQ86VN1.
PaxDbiQ86VN1.
PRIDEiQ86VN1.

PTM databases

PhosphoSiteiQ86VN1.

Expressioni

Gene expression databases

BgeeiQ86VN1.
CleanExiHS_VPS36.
GenevisibleiQ86VN1. HS.

Organism-specific databases

HPAiHPA039734.
HPA043947.

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 two copies of VPS25 (PubMed:14519844). Interacts with VPS25, SNF8, TSG101 and CHMP6 (PubMed:14505570, PubMed:14519844, PubMed:16973552, PubMed:18539118). Interacts (via GLUE domain) with ubiquitin (PubMed:17057716). Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes (PubMed:17010938). Interacts with ECM29 (PubMed:20682791).By similarity7 Publications

Protein-protein interaction databases

BioGridi119234. 35 interactions.
DIPiDIP-29249N.
IntActiQ86VN1. 2 interactions.
MINTiMINT-3085996.
STRINGi9606.ENSP00000367299.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 2812Combined sources
Beta strandi38 – 5114Combined sources
Beta strandi59 – 624Combined sources
Helixi63 – 653Combined sources
Beta strandi66 – 727Combined sources
Beta strandi81 – 866Combined sources
Beta strandi93 – 953Combined sources
Beta strandi105 – 1106Combined sources
Helixi115 – 12814Combined sources
Helixi175 – 19319Combined sources
Helixi197 – 1993Combined sources
Helixi215 – 22410Combined sources
Helixi229 – 2324Combined sources
Helixi233 – 2353Combined sources
Helixi240 – 25920Combined sources
Beta strandi262 – 2654Combined sources
Helixi266 – 27510Combined sources
Beta strandi278 – 2803Combined sources
Helixi284 – 2929Combined sources
Turni293 – 2986Combined sources
Beta strandi300 – 3056Combined sources
Beta strandi309 – 3157Combined sources
Helixi320 – 3234Combined sources
Helixi324 – 33310Combined sources
Helixi339 – 3468Combined sources
Helixi350 – 36213Combined sources
Beta strandi365 – 3739Combined sources
Beta strandi375 – 3795Combined sources
Helixi381 – 3833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HTHX-ray2.70B1-138[»]
2ZMEX-ray2.90B149-386[»]
3CUQX-ray2.61B169-386[»]
ProteinModelPortaliQ86VN1.
SMRiQ86VN1. Positions 3-131, 172-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86VN1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8888GLUE N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini105 – 13834GLUE C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili160 – 18526Sequence AnalysisAdd
BLAST

Domaini

The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates binding to ubiquitin and phosphoinosides.By similarity

Sequence similaritiesi

Belongs to the VPS36 family.Curated
Contains 1 GLUE C-terminal domain.PROSITE-ProRule annotation
Contains 1 GLUE N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG262969.
GeneTreeiENSGT00390000017209.
HOVERGENiHBG083632.
InParanoidiQ86VN1.
KOiK12190.
OMAiFQSSKYS.
OrthoDBiEOG7VB2FM.
PhylomeDBiQ86VN1.
TreeFamiTF314770.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR007286. EAP30.
IPR021648. VPS36_GLUE.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04157. EAP30. 1 hit.
PF11605. Vps36_ESCRT-II. 1 hit.
[Graphical view]
PROSITEiPS51495. GLUE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q86VN1-1) [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
MDRFVWTSGL LEINETLVIQ QRGVRIYDGE EKIKFDAGTL LLSTHRLIWR
60 70 80 90 100
DQKNHECCMA ILLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS
110 120 130 140 150
SKNSYIKLSF KEHGQIEFYR RLSEEMTQRR WENMPVSQSL QTNRGPQPGR
160 170 180 190 200
IRAVGIVGIE RKLEEKRKET DKNISEAFED LSKLMIKAKE MVELSKSIAN
210 220 230 240 250
KIKDKQGDIT EDETIRFKSY LLSMGIANPV TRETYGSGTQ YHMQLAKQLA
260 270 280 290 300
GILQVPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP
310 320 330 340 350
LRLRVFDSGV MVIELQSHKE EEMVASALET VSEKGSLTSE EFAKLVGMSV
360 370 380
LLAKERLLLA EKMGHLCRDD SVEGLRFYPN LFMTQS
Length:386
Mass (Da):43,817
Last modified:June 1, 2003 - v1
Checksum:i21E1E66F71BA7764
GO
Isoform 2 (identifier: Q86VN1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Note: No experimental confirmation available.
Show »
Length:328
Mass (Da):36,958
Checksum:iF6078BBD25CC0032
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851M → V in CAI45953 (PubMed:17974005).Curated
Sequence conflicti223 – 2231S → R in AAD34140 (PubMed:10810093).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 2. 1 PublicationVSP_015342Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS73577.1. [Q86VN1-2]
CCDS9434.1. [Q86VN1-1]
RefSeqiNP_001269098.1. NM_001282169.1. [Q86VN1-2]
NP_057159.2. NM_016075.3. [Q86VN1-1]
UniGeneiHs.109520.

Genome annotation databases

EnsembliENST00000378060; ENSP00000367299; ENSG00000136100. [Q86VN1-1]
ENST00000611132; ENSP00000484968; ENSG00000136100. [Q86VN1-2]
GeneIDi51028.
KEGGihsa:51028.
UCSCiuc001vgq.3. human. [Q86VN1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS73577.1. [Q86VN1-2]
CCDS9434.1. [Q86VN1-1]
RefSeqiNP_001269098.1. NM_001282169.1. [Q86VN1-2]
NP_057159.2. NM_016075.3. [Q86VN1-1]
UniGeneiHs.109520.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HTHX-ray2.70B1-138[»]
2ZMEX-ray2.90B149-386[»]
3CUQX-ray2.61B169-386[»]
ProteinModelPortaliQ86VN1.
SMRiQ86VN1. Positions 3-131, 172-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119234. 35 interactions.
DIPiDIP-29249N.
IntActiQ86VN1. 2 interactions.
MINTiMINT-3085996.
STRINGi9606.ENSP00000367299.

PTM databases

PhosphoSiteiQ86VN1.

Polymorphism and mutation databases

DMDMi73920464.

Proteomic databases

MaxQBiQ86VN1.
PaxDbiQ86VN1.
PRIDEiQ86VN1.

Protocols and materials databases

DNASUi51028.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378060; ENSP00000367299; ENSG00000136100. [Q86VN1-1]
ENST00000611132; ENSP00000484968; ENSG00000136100. [Q86VN1-2]
GeneIDi51028.
KEGGihsa:51028.
UCSCiuc001vgq.3. human. [Q86VN1-1]

Organism-specific databases

CTDi51028.
GeneCardsiGC13M052986.
HGNCiHGNC:20312. VPS36.
HPAiHPA039734.
HPA043947.
MIMi610903. gene.
neXtProtiNX_Q86VN1.
PharmGKBiPA134990943.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262969.
GeneTreeiENSGT00390000017209.
HOVERGENiHBG083632.
InParanoidiQ86VN1.
KOiK12190.
OMAiFQSSKYS.
OrthoDBiEOG7VB2FM.
PhylomeDBiQ86VN1.
TreeFamiTF314770.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiVPS36. human.
EvolutionaryTraceiQ86VN1.
GeneWikiiVPS36.
GenomeRNAii51028.
NextBioi53573.
PROiQ86VN1.
SOURCEiSearch...

Gene expression databases

BgeeiQ86VN1.
CleanExiHS_VPS36.
GenevisibleiQ86VN1. HS.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR007286. EAP30.
IPR021648. VPS36_GLUE.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04157. EAP30. 1 hit.
PF11605. Vps36_ESCRT-II. 1 hit.
[Graphical view]
PROSITEiPS51495. GLUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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 VPS25; 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. "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.
  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 VPS25; SNF8 AND TSG101, UBIQUITIN-BINDING, SUBCELLULAR LOCATION.
  12. "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.
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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.
  16. "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.

Entry informationi

Entry nameiVPS36_HUMAN
AccessioniPrimary (citable) accession number: Q86VN1
Secondary accession number(s): A8K125
, Q3ZCV7, Q5H9S1, Q5VXB6, Q9H8Z5, Q9Y3E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 122 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 13
    Human chromosome 13: 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

External Data

Dasty 3

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 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.