Tag | Content |
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CPLM ID | CPLM-018489 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Vacuolar protein sorting-associated protein 11 homolog |
Protein Synonyms/Alias | |
Gene Name | Vps11 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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417 | QYIRTIGKLEPSYVI | ubiquitination | [1] | 469 | TKLKDSSKLEEFIKT | ubiquitination | [1] | 475 | SKLEEFIKTKSESEV | ubiquitination | [1] | 535 | EALRYIGKLPFEQAE | ubiquitination | [1] | 781 | YLVQKLQKQSQQIAQ | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes (By similarity). |
Sequence Annotation | REPEAT 411 561 CHCR 1. REPEAT 572 736 CHCR 2. ZN_FING 822 861 RING-type. |
Keyword | Coiled coil; Complete proteome; Cytoplasmic vesicle; Endosome; Lysosome; Membrane; Metal-binding; Nucleotide-binding; Protein transport; Reference proteome; Repeat; Transport; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 941 AA |
Protein Sequence | MAAYLQWRRF VFFEKELVKE PLGNDGAAPG AAPVSGSAAS KFLCLPPGIT VCDSGRGSLV 60 FGDMEGQIWF LPRSLQLTGF QAYKLRVTHL YQLKQHNILA SVGEDEEGIN PLVKIWNLEK 120 RDGGNPLCTR IFPAIPGTEP TVVSCLTVHE NLNFMAIGFT DGSVTLNKGD ITRDRHSKTQ 180 ILHKGNYPVT GLAFRQAGKT THLFVVTTEN VQSYIVSGKD YPRVELDTHG CGLRCSALSD 240 PSQDLQFIVA GDECVYLYQP DERGPCFAFE GHKLIVHWFR GYLVIVSRDR KVSPKSEFTS 300 RDSQNSDKQI LNIYDLCNKF IAYSAGFEDI VDVLAEWGSL YVLTRDGRVH ALQEKDTQTK 360 LEMLFKKNLF EMAINLAKSQ HLDSDGLAQI FMQYGDHLYS KGNHDGAVQQ YIRTIGKLEP 420 SYVIRKFLDA QRIHNLTAYL QTLHRQSLAN ADHTTLLLNC YTKLKDSSKL EEFIKTKSES 480 EVHFDVETAI KVLRQAGYYS HALYLAENHA HHEWYLKIQL EDIKNYQEAL RYIGKLPFEQ 540 AESNMKRYGK TLMHHIPEQT TQLLKGLCTD YRPSLEGRGD REALSCRASS EEFIPIFANN 600 PRELKAFLEH MSEVQPDSPQ GIYDTLLELR LQNWAHEKDP QAKEKLHAEA ISLLKSGRFC 660 DVFDKALVLC QMHDFQDGVL YLYEQGKLFQ QIMHYHMQHE QYRQVIAVCE RHGEQEPSLW 720 EQALSYFARK EEDCKEYVAA VLRHIENKSL MPPLLVVQTL AHNSTATLSI IRDYLVQKLQ 780 KQSQQIAQDE LRVRRYREET TRIRQEIQEL KASPKIFQKT KCSICNSALE LPSVHFLCGH 840 SFHQHCFESY SESDADCPTC LPENRKVMDM IRAQEQKRDL HDQFQHQLKC SNDSFSVIAD 900 YFGRGVFNKL TLLTDPPTAR LTPSLEAGLQ RDLLMHSRRG T 941 |
Gene Ontology | GO:0005884; C:actin filament; IDA:MGI. GO:0005769; C:early endosome; IDA:MGI. GO:0030139; C:endocytic vesicle; ISS:UniProtKB. GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006886; P:intracellular protein transport; IEA:InterPro. GO:0016192; P:vesicle-mediated transport; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |