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Q86VN1

- VPS36_HUMAN

UniProt

Q86VN1 - VPS36_HUMAN

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Protein

Vacuolar protein-sorting-associated protein 36

Gene
VPS36, C13orf9, EAP45, CGI-145
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 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)P3.1 Publication

GO - Molecular functioni

  1. phosphatidylinositol-3-phosphate binding Source: InterPro
  2. protein binding 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

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: Chromosome 13

Organism-specific databases

HGNCiHGNC:20312. VPS36.

Subcellular locationi

Cytoplasm. Endosome. Late endosome. Membrane. Nucleus Inferred
Note: Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation.5 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endosome Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. late endosome Source: UniProtKB-SubCell
  5. lysosome Source: Ensembl
  6. membrane Source: UniProtKB-SubCell
  7. 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.

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.
GenevestigatoriQ86VN1.

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. 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 ECM29.6 Publications

Protein-protein interaction databases

BioGridi119234. 32 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 – 2812
Beta strandi38 – 5114
Beta strandi59 – 624
Helixi63 – 653
Beta strandi66 – 727
Beta strandi81 – 866
Beta strandi93 – 953
Beta strandi105 – 1106
Helixi115 – 12814
Helixi175 – 19319
Helixi197 – 1993
Helixi215 – 22410
Helixi229 – 2324
Helixi233 – 2353
Helixi240 – 25920
Beta strandi262 – 2654
Helixi266 – 27510
Beta strandi278 – 2803
Helixi284 – 2929
Turni293 – 2986
Beta strandi300 – 3056
Beta strandi309 – 3157
Helixi320 – 3234
Helixi324 – 33310
Helixi339 – 3468
Helixi350 – 36213
Beta strandi365 – 3739
Beta strandi375 – 3795
Helixi381 – 3833

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ86VN1.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili160 – 18526 Reviewed predictionAdd
BLAST

Domaini

The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates the binding to ubiquitin and phosphoinosides.1 Publication

Sequence similaritiesi

Belongs to the VPS36 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG262969.
HOVERGENiHBG083632.
InParanoidiQ86VN1.
KOiK12190.
OMAiCCIAIPL.
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. Align

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

MDRFVWTSGL LEINETLVIQ QRGVRIYDGE EKIKFDAGTL LLSTHRLIWR    50
DQKNHECCMA ILLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS 100
SKNSYIKLSF KEHGQIEFYR RLSEEMTQRR WENMPVSQSL QTNRGPQPGR 150
IRAVGIVGIE RKLEEKRKET DKNISEAFED LSKLMIKAKE MVELSKSIAN 200
KIKDKQGDIT EDETIRFKSY LLSMGIANPV TRETYGSGTQ YHMQLAKQLA 250
GILQVPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP 300
LRLRVFDSGV MVIELQSHKE EEMVASALET VSEKGSLTSE EFAKLVGMSV 350
LLAKERLLLA EKMGHLCRDD SVEGLRFYPN LFMTQS 386
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 2. VSP_015342Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851M → V in CAI45953. 1 Publication
Sequence conflicti223 – 2231S → R in AAD34140. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS9434.1. [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]
GeneIDi51028.
KEGGihsa:51028.
UCSCiuc001vgq.3. human. [Q86VN1-1]

Polymorphism databases

DMDMi73920464.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9434.1. [Q86VN1-1 ]
RefSeqi NP_001269098.1. NM_001282169.1. [Q86VN1-2 ]
NP_057159.2. NM_016075.3. [Q86VN1-1 ]
UniGenei Hs.109520.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HTH X-ray 2.70 B 1-138 [» ]
2ZME X-ray 2.90 B 149-386 [» ]
3CUQ X-ray 2.61 B 169-386 [» ]
ProteinModelPortali Q86VN1.
SMRi Q86VN1. Positions 3-131, 172-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119234. 32 interactions.
DIPi DIP-29249N.
IntActi Q86VN1. 2 interactions.
MINTi MINT-3085996.
STRINGi 9606.ENSP00000367299.

PTM databases

PhosphoSitei Q86VN1.

Polymorphism databases

DMDMi 73920464.

Proteomic databases

MaxQBi Q86VN1.
PaxDbi Q86VN1.
PRIDEi Q86VN1.

Protocols and materials databases

DNASUi 51028.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378060 ; ENSP00000367299 ; ENSG00000136100 . [Q86VN1-1 ]
GeneIDi 51028.
KEGGi hsa:51028.
UCSCi uc001vgq.3. human. [Q86VN1-1 ]

Organism-specific databases

CTDi 51028.
GeneCardsi GC13M052986.
HGNCi HGNC:20312. VPS36.
HPAi HPA039734.
HPA043947.
MIMi 610903. gene.
neXtProti NX_Q86VN1.
PharmGKBi PA134990943.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262969.
HOVERGENi HBG083632.
InParanoidi Q86VN1.
KOi K12190.
OMAi CCIAIPL.
OrthoDBi EOG7VB2FM.
PhylomeDBi Q86VN1.
TreeFami TF314770.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi VPS36. human.
EvolutionaryTracei Q86VN1.
GeneWikii VPS36.
GenomeRNAii 51028.
NextBioi 53573.
PROi Q86VN1.
SOURCEi Search...

Gene expression databases

Bgeei Q86VN1.
CleanExi HS_VPS36.
Genevestigatori Q86VN1.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR007286. EAP30.
IPR021648. VPS36_GLUE.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF04157. EAP30. 1 hit.
PF11605. Vps36_ESCRT-II. 1 hit.
[Graphical view ]
PROSITEi PS51495. GLUE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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. 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.

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: September 3, 2014
This is version 114 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