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Protein

Vacuolar protein sorting-associated protein 11 homolog

Gene

VPS11

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

Functioni

Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (PubMed:21148287). Involved in the retrograde Shiga toxin transport (PubMed:23593995).5 Publications3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri822 – 86140RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • nucleotide binding Source: UniProtKB-KW
  • protein binding, bridging Source: GO_Central
  • protein domain specific binding Source: UniProtKB
  • syntaxin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • endosomal vesicle fusion Source: UniProtKB
  • endosome organization Source: GO_Central
  • endosome to lysosome transport Source: UniProtKB
  • intracellular protein transport Source: InterPro
  • lysosome organization Source: GO_Central
  • positive regulation of cellular protein catabolic process Source: UniProtKB
  • positive regulation of early endosome to late endosome transport Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • regulation of organelle assembly Source: UniProtKB
  • regulation of protein stability Source: ParkinsonsUK-UCL
  • regulation of SNARE complex assembly Source: GO_Central
  • vesicle docking involved in exocytosis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 11 homolog
Short name:
hVPS11
Alternative name(s):
RING finger protein 108
Gene namesi
Name:VPS11
Synonyms:RNF108
ORF Names:PP3476
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14583. VPS11.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB-SubCell
  • clathrin-coated vesicle Source: UniProtKB-SubCell
  • early endosome Source: UniProtKB-SubCell
  • endocytic vesicle Source: UniProtKB
  • endosome Source: UniProtKB
  • HOPS complex Source: UniProtKB
  • late endosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37902.

Polymorphism and mutation databases

BioMutaiVPS11.
DMDMi23396928.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 941940Vacuolar protein sorting-associated protein 11 homologPRO_0000055902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei813 – 8131PhosphoserineCombined sources
Modified residuei924 – 9241PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H270.
MaxQBiQ9H270.
PeptideAtlasiQ9H270.
PRIDEiQ9H270.

PTM databases

iPTMnetiQ9H270.
PhosphoSiteiQ9H270.

Expressioni

Tissue specificityi

Ubiquitous. Expression was highest in heart and low in lung.

Gene expression databases

CleanExiHS_VPS11.
ExpressionAtlasiQ9H270. baseline and differential.
GenevisibleiQ9H270. HS.

Organism-specific databases

HPAiHPA039020.

Interactioni

Subunit structurei

Core component of at least two putative endosomal tethering complexes, the homotypic fusion and vacuole protein sorting (HOPS) complex and the class C core vacuaole/endosome tethering (CORVET) complex. Their common core is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:11382755, PubMed:20434987, PubMed:23351085, PubMed:23901104, PubMed:25266290, PubMed:25783203). Interacts with TGFBRAP1, MON1B, STX7, STX17, EZR, RDX, MSN, ECM29 (PubMed:11382755, PubMed:20682791, PubMed:21148287, PubMed:24554770, PubMed:25266290). Interacts with RAB5C (By similarity). Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (By similarity).By similarity3 Publications7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P352262EBI-373380,EBI-2341576
KRTAP10-8P604103EBI-373380,EBI-10171774
STX7O154002EBI-373380,EBI-3221827
TGFBRAP1Q8WUH22EBI-373380,EBI-2954829
VPS16Q9H2696EBI-373380,EBI-2655929
VPS18Q9P2538EBI-373380,EBI-1053363
Vps33aQ636154EBI-373380,EBI-918669From a different organism.

GO - Molecular functioni

  • protein binding, bridging Source: GO_Central
  • protein domain specific binding Source: UniProtKB
  • syntaxin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120930. 48 interactions.
IntActiQ9H270. 32 interactions.
MINTiMINT-1402371.

Structurei

3D structure databases

ProteinModelPortaliQ9H270.
SMRiQ9H270. Positions 140-218, 821-864.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati411 – 561151CHCR 1Add
BLAST
Repeati572 – 736165CHCR 2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili772 – 81342Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the VPS11 family.Curated
Contains 2 CHCR (clathrin heavy-chain) repeats.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri822 – 86140RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000216424.
HOVERGENiHBG055822.
InParanoidiQ9H270.
KOiK20179.
PhylomeDBiQ9H270.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000547. Clathrin_H-chain/VPS_repeat.
IPR016528. VPS11.
IPR024763. VPS11_C.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23323:SF24. PTHR23323:SF24. 1 hit.
PfamiPF00637. Clathrin. 1 hit.
PF12451. VPS11_C. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEiPS50236. CHCR. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYLQWRRF VFFDKELVKE PLSNDGAAPG ATPASGSAAS KFLCLPPGIT
60 70 80 90 100
VCDSGRGSLV FGDMEGQIWF LPRSLQLTGF QAYKLRVTHL YQLKQHNILA
110 120 130 140 150
SVGEDEEGIN PLVKIWNLEK RDGGNPLCTR IFPAIPGTEP TVVSCLTVHE
160 170 180 190 200
NLNFMAIGFT DGSVTLNKGD ITRDRHSKTQ ILHKGNYPVT GLAFRQAGKT
210 220 230 240 250
THLFVVTTEN VQSYIVSGKD YPRVELDTHG CGLRCSALSD PSQDLQFIVA
260 270 280 290 300
GDECVYLYQP DERGPCFAFE GHKLIAHWFR GYLIIVSRDR KVSPKSEFTS
310 320 330 340 350
RDSQSSDKQI LNIYDLCNKF IAYSTVFEDV VDVLAEWGSL YVLTRDGRVH
360 370 380 390 400
ALQEKDTQTK LEMLFKKNLF EMAINLAKSQ HLDSDGLAQI FMQYGDHLYS
410 420 430 440 450
KGNHDGAVQQ YIRTIGKLEP SYVIRKFLDA QRIHNLTAYL QTLHRQSLAN
460 470 480 490 500
ADHTTLLLNC YTKLKDSSKL EEFIKKKSES EVHFDVETAI KVLRQAGYYS
510 520 530 540 550
HALYLAENHA HHEWYLKIQL EDIKNYQEAL RYIGKLPFEQ AESNMKRYGK
560 570 580 590 600
ILMHHIPEQT TQLLKGLCTD YRPSLEGRSD REAPGCRANS EEFIPIFANN
610 620 630 640 650
PRELKAFLEH MSEVQPDSPQ GIYDTLLELR LQNWAHEKDP QVKEKLHAEA
660 670 680 690 700
ISLLKSGRFC DVFDKALVLC QMHDFQDGVL YLYEQGKLFQ QIMHYHMQHE
710 720 730 740 750
QYRQVISVCE RHGEQDPSLW EQALSYFARK EEDCKEYVAA VLKHIENKNL
760 770 780 790 800
MPPLLVVQTL AHNSTATLSV IRDYLVQKLQ KQSQQIAQDE LRVRRYREET
810 820 830 840 850
TRIRQEIQEL KASPKIFQKT KCSICNSALE LPSVHFLCGH SFHQHCFESY
860 870 880 890 900
SESDADCPTC LPENRKVMDM IRAQEQKRDL HDQFQHQLRC SNDSFSVIAD
910 920 930 940
YFGRGVFNKL TLLTDPPTAR LTSSLEAGLQ RDLLMHSRRG T
Length:941
Mass (Da):107,837
Last modified:March 1, 2001 - v1
Checksum:iC1F8E538ED1B56DB
GO

Sequence cautioni

The sequence AAG23761.1 differs from that shown. Reason: Frameshift at positions 439 and 924. Curated
The sequence BAB15320.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti635 – 6362AH → VI in BAA95163 (PubMed:11382755).Curated
Sequence conflicti871 – 8711I → T in BAB15320 (PubMed:14702039).Curated
Sequence conflicti889 – 8891R → K in BAA95163 (PubMed:11382755).Curated
Sequence conflicti889 – 8891R → K in AAG23761 (PubMed:15498874).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti770 – 7701V → I.
Corresponds to variant rs11558589 [ dbSNP | Ensembl ].
VAR_059813

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308800 mRNA. Translation: AAG34677.1.
AB027508 mRNA. Translation: BAA95163.2.
BC012051 mRNA. Translation: AAH12051.2.
BC065563 mRNA. Translation: AAH65563.1.
AF258558 mRNA. Translation: AAG23761.1. Frameshift.
AK026012 mRNA. Translation: BAB15320.1. Different initiation.
CCDSiCCDS73404.1.
RefSeqiNP_001277114.1. NM_001290185.1.
NP_068375.3. NM_021729.5.
UniGeneiHs.234282.

Genome annotation databases

EnsembliENST00000620429; ENSP00000479680; ENSG00000160695.
GeneIDi55823.
KEGGihsa:55823.
UCSCiuc058ier.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308800 mRNA. Translation: AAG34677.1.
AB027508 mRNA. Translation: BAA95163.2.
BC012051 mRNA. Translation: AAH12051.2.
BC065563 mRNA. Translation: AAH65563.1.
AF258558 mRNA. Translation: AAG23761.1. Frameshift.
AK026012 mRNA. Translation: BAB15320.1. Different initiation.
CCDSiCCDS73404.1.
RefSeqiNP_001277114.1. NM_001290185.1.
NP_068375.3. NM_021729.5.
UniGeneiHs.234282.

3D structure databases

ProteinModelPortaliQ9H270.
SMRiQ9H270. Positions 140-218, 821-864.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120930. 48 interactions.
IntActiQ9H270. 32 interactions.
MINTiMINT-1402371.

PTM databases

iPTMnetiQ9H270.
PhosphoSiteiQ9H270.

Polymorphism and mutation databases

BioMutaiVPS11.
DMDMi23396928.

Proteomic databases

EPDiQ9H270.
MaxQBiQ9H270.
PeptideAtlasiQ9H270.
PRIDEiQ9H270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000620429; ENSP00000479680; ENSG00000160695.
GeneIDi55823.
KEGGihsa:55823.
UCSCiuc058ier.1. human.

Organism-specific databases

CTDi55823.
GeneCardsiVPS11.
H-InvDBHIX0010281.
HGNCiHGNC:14583. VPS11.
HPAiHPA039020.
MIMi608549. gene.
neXtProtiNX_Q9H270.
PharmGKBiPA37902.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000216424.
HOVERGENiHBG055822.
InParanoidiQ9H270.
KOiK20179.
PhylomeDBiQ9H270.

Miscellaneous databases

GeneWikiiVPS11.
GenomeRNAii55823.
PROiQ9H270.
SOURCEiSearch...

Gene expression databases

CleanExiHS_VPS11.
ExpressionAtlasiQ9H270. baseline and differential.
GenevisibleiQ9H270. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000547. Clathrin_H-chain/VPS_repeat.
IPR016528. VPS11.
IPR024763. VPS11_C.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23323:SF24. PTHR23323:SF24. 1 hit.
PfamiPF00637. Clathrin. 1 hit.
PF12451. VPS11_C. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEiPS50236. CHCR. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of human VPS18, VPS11, VPS16, and VPS33."
    Huizing M., Didier A., Walenta J., Anikster Y., Gahl W.A., Kraemer H.
    Gene 264:241-247(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7."
    Kim B.Y., Kraemer H., Yamamoto A., Kominami E., Kohsaka S., Akazawa C.
    J. Biol. Chem. 276:29393-29402(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS16; VPS18; VPS33A AND STX7.
    Tissue: Brain.
  3. "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].
    Tissue: Eye and Skin.
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-941.
  5. "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] OF 575-941.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Placenta.
  7. "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.
  8. "Identification of the switch in early-to-late endosome transition."
    Poteryaev D., Datta S., Ackema K., Zerial M., Spang A.
    Cell 141:497-508(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MON1B.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes."
    Chirivino D., Del Maestro L., Formstecher E., Hupe P., Raposo G., Louvard D., Arpin M.
    Mol. Biol. Cell 22:375-385(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EZR; RDX AND MSN, SUBCELLULAR LOCATION.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Tethering complexes in the endocytic pathway: CORVET and HOPS."
    Solinger J.A., Spang A.
    FEBS J. 280:2743-2757(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON THE HOPS AND CORVET COMPLEXES.
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813 AND SER-924, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. Cited for: INTERACTION WITH VPS16; VPS18 AND VPS39.
  15. "The ERM proteins ezrin and moesin regulate retrograde Shiga toxin transport."
    Kvalvaag A.S., Pust S., Sundet K.I., Engedal N., Simm R., Sandvig K.
    Traffic 14:839-852(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17."
    Jiang P., Nishimura T., Sakamaki Y., Itakura E., Hatta T., Natsume T., Mizushima N.
    Mol. Biol. Cell 25:1327-1337(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE HOPS COMPLEX, INTERACTION WITH STX17.
  17. "Mammalian CORVET is required for fusion and conversion of distinct early endosome subpopulations."
    Perini E.D., Schaefer R., Stoeter M., Kalaidzidis Y., Zerial M.
    Traffic 15:1366-1389(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CORVET COMPLEX, SUBUNIT, INTERACTION WITH TGFBRAP1.
  18. "Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes."
    Wartosch L., Guenesdogan U., Graham S.C., Luzio J.P.
    Traffic 16:727-742(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FUNCTION OF THE HOPS COMPLEX, SUBUNIT.

Entry informationi

Entry nameiVPS11_HUMAN
AccessioniPrimary (citable) accession number: Q9H270
Secondary accession number(s): Q8WY89
, Q96EP8, Q9H6D9, Q9HCS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 152 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.