ID B7Z879_HUMAN Unreviewed; 931 AA.
AC B7Z879;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Vacuolar protein sorting-associated protein 11 homolog {ECO:0000256|PIRNR:PIRNR007860};
GN Name=VPS11 {ECO:0000313|Ensembl:ENSP00000481807.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAH13865.1};
RN [1] {ECO:0000313|Ensembl:ENSP00000481807.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2] {ECO:0000313|EMBL:BAH13865.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAH13865.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5] {ECO:0000313|Ensembl:ENSP00000486795}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport and
CC autophagic pathways. Believed to act as a core component of the
CC putative HOPS and CORVET endosomal tethering complexes.
CC {ECO:0000256|PIRNR:PIRNR007860}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000256|PIRNR:PIRNR007860}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR007860}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR007860}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004630, ECO:0000256|PIRNR:PIRNR007860};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630,
CC ECO:0000256|PIRNR:PIRNR007860}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004630, ECO:0000256|PIRNR:PIRNR007860}.
CC Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR007860}. Early endosome
CC {ECO:0000256|PIRNR:PIRNR007860}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000256|PIRNR:PIRNR007860}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000256|PIRNR:PIRNR007860}.
CC -!- SIMILARITY: Belongs to the VPS11 family.
CC {ECO:0000256|ARBA:ARBA00007070, ECO:0000256|PIRNR:PIRNR007860}.
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DR EMBL; AP003392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF511489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK302973; BAH13865.1; -; mRNA.
DR RefSeq; NP_001277114.1; NM_001290185.1.
DR RefSeq; NP_068375.3; NM_021729.5.
DR Antibodypedia; 32587; 256 antibodies from 33 providers.
DR DNASU; 55823; -.
DR Ensembl; ENST00000614944.4; ENSP00000481807.1; ENSG00000160695.16.
DR Ensembl; ENST00000629865; ENSP00000486795; ENSG00000280616.
DR GeneID; 55823; -.
DR KEGG; hsa:55823; -.
DR UCSC; uc031yhi.2; human.
DR CTD; 55823; -.
DR HGNC; HGNC:14583; VPS11.
DR VEuPathDB; HostDB:ENSG00000160695; -.
DR GeneTree; ENSGT00940000153635; -.
DR OrthoDB; 5491867at2759; -.
DR BioGRID-ORCS; 55823; 57 hits in 366 CRISPR screens.
DR ChiTaRS; VPS11; human.
DR GenomeRNAi; 55823; -.
DR Proteomes; UP000005640; Unplaced.
DR Bgee; ENSG00000160695; Expressed in prefrontal cortex and 98 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR016528; VPS11.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PIRSF; PIRSF007860; VPS11; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Autophagy {ECO:0000256|PIRNR:PIRNR007860};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR007860};
KW Endosome {ECO:0000256|PIRNR:PIRNR007860};
KW Lysosome {ECO:0000256|PIRNR:PIRNR007860};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR007860};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR007860};
KW Proteomics identification {ECO:0007829|EPD:B7Z879,
KW ECO:0007829|MaxQB:B7Z879};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transport {ECO:0000256|PIRNR:PIRNR007860};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 812..850
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 769..803
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 931 AA; 107375 MW; 932001ABEAD0EBC9 CRC64;
MKSVCRRGPC RAPLWFSWSS RVVLWSTGRK KEVHLLTCYQ LSNPGRLLDY PAHMEGQIWF
LPRSLQLTGF QAYKLRVTHL YQLKQHNILA SVGEDEEGIN PLVKIWNLEK RDGGNPLCTR
IFPAIPGTEP TVVSCLTVHE NLNFMAIGFT DGSVTLNKGD ITRDRHSKTQ ILHKGNYPVT
GLAFRQAGKT THLFVVTTEN VQSYIVSGKD YPRVELDTHG CGLRCSALSD PSQDLQFIVA
GDECVYLYQP DERGPCFAFE GHKLIAHWFR GYLIIVSRDR KVSPKSEFTS RDSQSSDKQI
LNIYDLCNKF IAYSTVFEDV VDVLAEWGSL YVLTRDGRVH ALQEKDTQTK LEMLFKKNLF
EMAINLAKSQ HLDSDGLAQI FMQYGDHLYS KGNHDGAVQQ YIRTIGKLEP SYVIRKFLDA
QRIHNLTAYL QTLHRQSLAN ADHTTLLLNC YTKLKDSSKL EEFIKKKSES EVHFDVETAI
KVLRQAGYYS HALYLAENHA HHEWYLKIQL EDIKNYQEAL RYIGKLPFEQ AESNMKRYGK
ILMHHIPEQT TQLLKGLCTD YRPSLEGRSD REAPGCRANS EEFIPIFANN PRELKAFLEH
MSEVQPDSPQ GIYDTLLELR LQNWAHEKDP QVKEKLHAEA ISLLKSGRFC DVFDKALVLC
QMHDFQDGVL YLYEQGKLFQ QIMHYHMQHE QYRQVISVCE RHGEQDPSLW EQALSYFARK
EEDCKEYVAA VLKHIENKNL MPPLLVVQTL AHNSTATLSV IRDYLVQKLQ KQSQQIAQDE
LRVRRYREET TRIRQEIQEL KASPKIFQKT KCSICNSALE LPSVHFLCGH SFHQHCFESY
SESDADCPTC LPENRKVMDM IRAQEQKRDL HDQFQHQLKC SNDSFSVIAD YFGRGVFNKL
TLLTDPPTAR LTSSLEAGLQ RDLLMHSRRG T
//
