WDR81_MOUSE - dbPTM
WDR81_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR81_MOUSE
UniProt AC Q5ND34
Protein Name WD repeat-containing protein 81 {ECO:0000312|MGI:MGI:2681828}
Gene Name Wdr81 {ECO:0000312|MGI:MGI:2681828}
Organism Mus musculus (Mouse).
Sequence Length 1934
Subcellular Localization Early endosome membrane
Peripheral membrane protein . Late endosome membrane . Lysosome membrane . Cytoplasmic vesicle, autophagosome membrane . Mitochondrion . Cytoplasm, cytosol .
Protein Description Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome. May also play a role in aggrephagy, the macroautophagic degradation of ubiquitinated protein aggregates. In this process, may regulate the interaction of SQSTM1 with ubiquitinated proteins and also recruit MAP1LC3C (By similarity). May also be involved in maintenance of normal mitochondrial structure and organization. [PubMed: 23595742]
Protein Sequence MAQGSRRRKVVLTAGSEGWSPSSGPDMEELLRSVERDLNIDARQLALAPGGTHVVALVSTRWLASLRERRLGPCPRAEGLGEAEVRTLLQRSVQRLPPGWTRVEVHGLRKRRLSYPLGGGVPFEEGSCSPETLTRFMQEVAAQNYRNLWRHAYHTYGQPYSHSTAPSALPALDSIRQALQRVYGCTFLPVGESIPCLSNVRDGPCPSRGSPACPSLLRAEALLESPEMLYVVHPYVQFSLHDVVTFSPAKLTNSQAKVLFLLFRVLRAMDACHRQGLACGALSLHHIAVDEKLCSELRLDLSAYEMPSEDENQEGSEEKNGTGIKSEKEGEGRTECPTCQKELRGLVLDWVHGRISNFHYLMQLNRLAGRRQGDPNYHPVLPWVVDFTTPYGRFRDLRKSKFRLNKGDKQLDFTYEMTRQAFVAGGAGSGEPPHVPHHISDVLSDITYYVYKARRTPRSVLCGHVRAQWEPHEYPATMERMQTWTPDECIPEFYTDPSIFCSIHPDMPDLDVPAWCSSNQEFVAAHRALLESWEVSQDLHHWIDLTFGYKLQGKEAVKEKNVCLHLVDAHTHLTSYGVVQLFDQPHPQRLAGSPALAPEPPLIPRLLVQPIREATGQEDISGQLINGAGRLVVEATPCETGWTRDRPGTGEDDLEQATEALDSISLPGKAGDQPGSSSSQASPGLLSFSAPSGSRPGRRSKAAGLDPGEGEEGKIVLPEGFSPIQALEELEKVGNFLAKGLGSQLEEPEKPHAQPPVHLQSLFHRDMQVLGVLLAEMVFATRVRILQPDAPLWVRFEAVRGLCIRHSKDIPVSLQPVLDTLLQLSGPKSPMVSKKGKLDPLFEYRPVSQGLPPPSPAQLLSPFSSVVPFPPYFPALHKFILLYQARRVEDEVQGRELAFALWQQLGAVLNDITPEGLEILLPFVLSLMSEEHTAVYTAWYLFEPVAKALGPKNANKYLLKPLIGAYESPCRLHGRFYLYTDCFVAQLVVRLGLQAFLTHLLPHVLQVLAGVEASQEEGKGLVGTTEDEESELPVSGPGSCAFGEEIQMDGQPAASSGLGLPDYRSGVSFHDQADLPDTEDFQAGLYVAESPQPQEAEAVSLGQLSDKSSTSEASQGEERGGDDGGAPADKNSVKSGDSSQDLKQSEGSEEEEEEEGCVVLEEDQEDEVTGTSELTLSDTMLSMETVVAPGDGRDREEEEEPLTEQTEGKEQKILLDTACKMVRWLSAKLGPTVASRHVARNLLRLLTSCYVGPTRQQFTVSSDDTPPLNAGNIYQKRPVLGDIVSGPVLSCLLHIAYLYGEPVLTYQYLPYISYLVAPGSNSNPSRLNSRKEAGLLAAVTLTQKIIVYLSDTTLMDILPRISHEVLLPVLGFLTSFVTGFPSGAQARTVLCVKTISLIALICLRIGQEMVQQHLSEPVATFFQVFSHLHELRQQDLPLDPKGCTEGQLPEATFSDGQRRPVDPTLLEELQKVFTLEMAYTIYVPFSCLLGDIIRKIIPNHELVGELAGLYLESMSPSSRNPASMEPTMASAGPEWDPQSGSCLQDDGHSGTFGSVLVGNRIQIPDSQPQSPGPLGSLSGVGSSGGLSNRNEDNALKRELPRSAHGLSGNWLAYWQYEIGVSQQDAHFHFHQIRLQSFPGHTGAVKCVAALSSEDFFLSGSKDRTVRLWPLYNYGDGTNETASRLIYAQHRKSVFYVGQLEAPQYVVSCDGAVHVWDPFTGKTLRTVDPSDSRVPLTAVAVMPAPHTSITMASSDSTLRFVDCRKPGLQHEFRLGGGLNPGLVRSLAVSPSGRSVVAGFSSGFMVLLDTRTGLVLRGWPAHEGDILQIKAVEGSVLISSSSDHSLTVWKELEQKPTHHYKSASDPIHTFDLYGSEVVTGTVANKIGVCSLLEPPSQATTKLSSENFRGTLTSLALLPTKRHLLLGSDNGIIRLLA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
13PhosphorylationRRRKVVLTAGSEGWS
CCCEEEEEECCCCCC
3.3329899451
52PhosphorylationLALAPGGTHVVALVS
HHCCCCCCEEEEEEE
3.5030165576
59PhosphorylationTHVVALVSTRWLASL
CEEEEEEEHHHHHHH
64.5530165576
60PhosphorylationHVVALVSTRWLASLR
EEEEEEEHHHHHHHH
42.8230165576
183PhosphorylationRQALQRVYGCTFLPV
HHHHHHHHCCEEECC
18.35-
302PhosphorylationSELRLDLSAYEMPSE
HHHCCCCHHCCCCCC
2.3029472430
304PhosphorylationLRLDLSAYEMPSEDE
HCCCCHHCCCCCCCC
40.9129472430
308PhosphorylationLSAYEMPSEDENQEG
CHHCCCCCCCCCCCC
2.5729472430
341UbiquitinationTECPTCQKELRGLVL
CCCCCHHHHHHHHHH
22.3522790023
341UbiquitinationTECPTCQKELRGLVL
CCCCCHHHHHHHHHH
22.3522790023
409UbiquitinationFRLNKGDKQLDFTYE
CCCCCCCCCCCEEEE
22.9922790023
409UbiquitinationFRLNKGDKQLDFTYE
CCCCCCCCCCCEEEE
22.9922790023
593PhosphorylationHPQRLAGSPALAPEP
CHHHCCCCCCCCCCC
22.7425338131
658PhosphorylationEDDLEQATEALDSIS
CCHHHHHHHHHHHCC
1.8429472430
663PhosphorylationQATEALDSISLPGKA
HHHHHHHHCCCCCCC
33.5521743459
665PhosphorylationTEALDSISLPGKAGD
HHHHHHCCCCCCCCC
4.5930352176
682PhosphorylationGSSSSQASPGLLSFS
CCCCCCCCCCEEEEC
43.7029514104
722PhosphorylationIVLPEGFSPIQALEE
EECCCCCCHHHHHHH
41.0026824392
743PhosphorylationFLAKGLGSQLEEPEK
HHHHCCCCCCCCCCC
39.0526643407
813PhosphorylationHSKDIPVSLQPVLDT
CCCCCCCCHHHHHHH
26.3220531401
820PhosphorylationSLQPVLDTLLQLSGP
CHHHHHHHHHHHHCC
21.4020531401
825PhosphorylationLDTLLQLSGPKSPMV
HHHHHHHHCCCCCCC
25.3226745281
829PhosphorylationLQLSGPKSPMVSKKG
HHHHCCCCCCCCCCC
3.4226745281
833PhosphorylationGPKSPMVSKKGKLDP
CCCCCCCCCCCCCCC
6.1326745281
960UbiquitinationNANKYLLKPLIGAYE
CHHHHCHHHHHCCCC
22790023
960UbiquitinationNANKYLLKPLIGAYE
CHHHHCHHHHHCCCC
22790023
1114PhosphorylationKSSTSEASQGEERGG
CCCCCCHHCCCCCCC
23684622
1132PhosphorylationGAPADKNSVKSGDSS
CCCCCCCCCCCCCCC
25521595
1135PhosphorylationADKNSVKSGDSSQDL
CCCCCCCCCCCCHHH
25195567
1138PhosphorylationNSVKSGDSSQDLKQS
CCCCCCCCCHHHHHC
25195567
1209UbiquitinationLTEQTEGKEQKILLD
CCCCCCCHHHHHHHH
22790023
1209UbiquitinationLTEQTEGKEQKILLD
CCCCCCCHHHHHHHH
22790023
1226PhosphorylationCKMVRWLSAKLGPTV
HHHHHHHHHHHCHHH
21454597
1228UbiquitinationMVRWLSAKLGPTVAS
HHHHHHHHHCHHHHH
22790023
1228UbiquitinationMVRWLSAKLGPTVAS
HHHHHHHHHCHHHHH
22790023
1232PhosphorylationLSAKLGPTVASRHVA
HHHHHCHHHHHHHHH
21454597
1235PhosphorylationKLGPTVASRHVARNL
HHCHHHHHHHHHHHH
28059163
1259PhosphorylationGPTRQQFTVSSDDTP
CCCCCEEEECCCCCC
29472430
1261PhosphorylationTRQQFTVSSDDTPPL
CCCEEEECCCCCCCC
29472430
1262PhosphorylationRQQFTVSSDDTPPLN
CCEEEECCCCCCCCC
29472430
1265PhosphorylationFTVSSDDTPPLNAGN
EEECCCCCCCCCCCC
29472430
1566PhosphorylationNRIQIPDSQPQSPGP
CEEECCCCCCCCCCC
27087446
1570PhosphorylationIPDSQPQSPGPLGSL
CCCCCCCCCCCCCCC
27087446
1576PhosphorylationQSPGPLGSLSGVGSS
CCCCCCCCCCCCCCC
25619855
1578PhosphorylationPGPLGSLSGVGSSGG
CCCCCCCCCCCCCCC
25619855
1582PhosphorylationGSLSGVGSSGGLSNR
CCCCCCCCCCCCCCC
25619855
1583PhosphorylationSLSGVGSSGGLSNRN
CCCCCCCCCCCCCCC
25619855
1587PhosphorylationVGSSGGLSNRNEDNA
CCCCCCCCCCCCCCH
25619855
1808PhosphorylationGFMVLLDTRTGLVLR
CEEEEEECCCCEEEC
23882026
1855PhosphorylationKELEQKPTHHYKSAS
HHHHCCCCCCCCCCC
25367039
1858PhosphorylationEQKPTHHYKSASDPI
HCCCCCCCCCCCCCC
25367039

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of WDR81_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR81_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of WDR81_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WDR81_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR81_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.

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