| Tag | Content |
|---|
| 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 |
|---|
| 417 | QYIRTIGKLEPSYVI | ubiquitination | [1] | | 469 | TKLKDSSKLEEFIKT | ubiquitination | [1] | | 475 | SKLEEFIKTKSESEV | ubiquitination | [1] | | 535 | EALRYIGKLPFEQAE | ubiquitination | [1] | | 781 | YLVQKLQKQSQQIAQ | ubiquitination | [1] |
|
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 | |