WDR81_HUMAN - dbPTM
WDR81_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR81_HUMAN
UniProt AC Q562E7
Protein Name WD repeat-containing protein 81 {ECO:0000312|HGNC:HGNC:26600}
Gene Name WDR81 {ECO:0000312|HGNC:HGNC:26600}
Organism Homo sapiens (Human).
Sequence Length 1941
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. [PubMed: 26783301 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]
Protein Sequence MAQGSGGREGALRTPAGGWHSPPSPDMQELLRSVERDLSIDPRQLAPAPGGTHVVALVPARWLASLRDRRLPLGPCPRAEGLGEAEVRTLLQRSVQRLPAGWTRVEVHGLRKRRLSYPLGGGLPFEDGSCGPETLTRFMQEVAAQNYRNLWRHAYHTYGQPYSHSPAPSAVPALDSVRQALQRVYGCSFLPVGETTQCPSYAREGPCPPRGSPACPSLLRAEALLESPEMLYVVHPYVQFSLHDVVTFSPAKLTNSQAKVLFILFRVLRAMDACHRQGLACGALSLYHIAVDEKLCSELRLDLSAYERPEEDENEEAPVARDEAGIVSQEEQGGQPGQPTGQEELRSLVLDWVHGRISNFHYLMQLNRLAGRRQGDPNYHPVLPWVVDFTTPHGRFRDLRKSKFRLNKGDKQLDFTYEMTRQAFVAGGAGGGEPPHVPHHISDVLSDITYYVYKARRTPRSVLCGHVRAQWEPHEYPASMERMQNWTPDECIPEFYTDPSIFRSIHPDMPDLDVPAWCSSSQEFVAAHRALLESREVSRDLHHWIDLTFGYKLQGKEAVKEKNVCLHLVDAHTHLASYGVVQLFDQPHPQRLAGAPALAPEPPLIPKLLVQTIQETTGREDFTENPGQLPNGVGRPVLEATPCEASWTRDRPVAGEDDLEQATEALDSISLAGKAGDQLGSSSQASPGLLSFSVASASRPGRRNKAAGADPGEGEEGRILLPEGFNPMQALEELEKTGNFLAKGLGGLLEVPEQPRVQPAVPLQCLLHRDMQALGVLLAEMVFATRVRTLQPDAPLWVRFQAVRGLCTRHPKEVPVSLQPVLDTLLQMSGPEVPMGAERGKLDQLFEYRPVSQGLPPPCPSQLLSPFSSVVPFPPYFPALHRFILLYQARRVEDEAQGRELVFALWQQLGAVLKDITPEGLEILLPFVLSLMSEEHTAVYTAWYLFEPVAKALGPKNANKYLLKPLIGAYESPCQLHGRFYLYTDCFVAQLMVRLGLQAFLTHLLPHVLQVLAGAEASQEESKDLAGAAEEEESGLPGAGPGSCAFGEEIPMDGEPPASSGLGLPDYTSGVSFHDQADLPETEDFQAGLYVTESPQPQEAEAVSLGRLSDKSSTSETSLGEERAPDEGGAPVDKSSLRSGDSSQDLKQSEGSEEEEEEEDSCVVLEEEEGEQEEVTGASELTLSDTVLSMETVVAGGSGGDGEEEEEALPEQSEGKEQKILLDTACKMVRWLSAKLGPTVASRHVARNLLRLLTSCYVGPTRQQFTVSSGESPPLSAGNIYQKRPVLGDIVSGPVLSCLLHIARLYGEPVLTYQYLPYISYLVAPGSASGPSRLNSRKEAGLLAAVTLTQKIIVYLSDTTLMDILPRISHEVLLPVLSFLTSLVTGFPSGAQARTILCVKTISLIALICLRIGQEMVQQHLSEPVATFFQVFSQLHELRQQDLKLDPAGRGEGQLPQVVFSDGQQRPVDPALLDELQKVFTLEMAYTIYVPFSCLLGDIIRKIIPNHELVGELAALYLESISPSSRNPASVEPTMPGTGPEWDPHGGGCPQDDGHSGTFGSVLVGNRIQIPNDSRPENPGPLGPISGVGGGGLGSGSDDNALKQELPRSVHGLSGNWLAYWQYEIGVSQQDAHFHFHQIRLQSFPGHSGAVKCVAPLSSEDFFLSGSKDRTVRLWPLYNYGDGTSETAPRLVYTQHRKSVFFVGQLEAPQHVVSCDGAVHVWDPFTGKTLRTVEPLDSRVPLTAVAVMPAPHTSITMASSDSTLRFVDCRKPGLQHEFRLGGGLNPGLVRALAISPSGRSVVAGFSSGFMVLLDTRTGLVLRGWPAHEGDILQIKAVEGSVLVSSSSDHSLTVWKELEQKPTHHYKSASDPIHTFDLYGSEVVTGTVSNKIGVCSLLEPPSQATTKLSSENFRGTLTSLALLPTKRHLLLGSDNGVIRLLA
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
21PhosphorylationTPAGGWHSPPSPDMQ
CCCCCCCCCCCCCHH
22.0127251275
52PhosphorylationLAPAPGGTHVVALVP
CCCCCCCCEEEEEEE
3.50-
65PhosphorylationVPARWLASLRDRRLP
EEHHHHHHHCCCCCC
42.3724719451
116PhosphorylationGLRKRRLSYPLGGGL
CCCCCCCCCCCCCCC
58.1328348404
217PhosphorylationRGSPACPSLLRAEAL
CCCCCCHHHHHHHHH
29.5729449344
294UbiquitinationYHIAVDEKLCSELRL
HHHHHCHHHHHHHCC
8.52-
347PhosphorylationTGQEELRSLVLDWVH
CCHHHHHHHHHHHHH
2.3224719451
354 (in isoform 2)Ubiquitination-2.0421906983
362PhosphorylationGRISNFHYLMQLNRL
HCHHHHHHHHHHHHH
15.8024719451
417PhosphorylationDKQLDFTYEMTRQAF
CCCCCEEEEECCHHH
17.5227642862
454UbiquitinationDITYYVYKARRTPRS
HHHHHHHHCCCCCCC
39.33-
496PhosphorylationDECIPEFYTDPSIFR
CCCCHHHCCCHHHHH
31.3427642862
552 (in isoform 1)Ubiquitination-39.0421906983
552UbiquitinationIDLTFGYKLQGKEAV
HHCCCCEEECCHHHH
39.04-
668PhosphorylationQATEALDSISLAGKA
HHHHHHHHHCCCCCC
4.5930108239
670PhosphorylationTEALDSISLAGKAGD
HHHHHHHCCCCCCCC
5.0830108239
681PhosphorylationKAGDQLGSSSQASPG
CCCCCCCCCCCCCCC
32.1325627689
682PhosphorylationAGDQLGSSSQASPGL
CCCCCCCCCCCCCCC
6.0327251275
683PhosphorylationGDQLGSSSQASPGLL
CCCCCCCCCCCCCCE
39.2627251275
686PhosphorylationLGSSSQASPGLLSFS
CCCCCCCCCCCEEEE
45.1525159151
691PhosphorylationQASPGLLSFSVASAS
CCCCCCEEEEECCCC
4.3728857561
696PhosphorylationLLSFSVASASRPGRR
CEEEEECCCCCCCCC
3.6725627689
698PhosphorylationSFSVASASRPGRRNK
EEEECCCCCCCCCCC
35.7225627689
705UbiquitinationSRPGRRNKAAGADPG
CCCCCCCCCCCCCCC
13.37-
736UbiquitinationQALEELEKTGNFLAK
HHHHHHHHHCCHHHH
35.41-
743UbiquitinationKTGNFLAKGLGGLLE
HHCCHHHHCCCCCCC
6.91-
956UbiquitinationVAKALGPKNANKYLL
HHHHHCCCCHHHHCH
-
964UbiquitinationNANKYLLKPLIGAYE
CHHHHCHHHHHCCCC
-
1109PhosphorylationAVSLGRLSDKSSTSE
EEECCCCCCCCCCCC
26329039
1112PhosphorylationLGRLSDKSSTSETSL
CCCCCCCCCCCCCCC
29255136
1113PhosphorylationGRLSDKSSTSETSLG
CCCCCCCCCCCCCCC
29255136
1114PhosphorylationRLSDKSSTSETSLGE
CCCCCCCCCCCCCCC
29255136
1115PhosphorylationLSDKSSTSETSLGEE
CCCCCCCCCCCCCCC
27732954
1117PhosphorylationDKSSTSETSLGEERA
CCCCCCCCCCCCCCC
29255136
1118PhosphorylationKSSTSETSLGEERAP
CCCCCCCCCCCCCCC
28192239
1134UbiquitinationEGGAPVDKSSLRSGD
CCCCCCCHHHHCCCC
-
1135PhosphorylationGGAPVDKSSLRSGDS
CCCCCCHHHHCCCCC
30266825
1136PhosphorylationGAPVDKSSLRSGDSS
CCCCCHHHHCCCCCC
25849741
1139PhosphorylationVDKSSLRSGDSSQDL
CCHHHHCCCCCCHHH
23403867
1142PhosphorylationSSLRSGDSSQDLKQS
HHHCCCCCCHHHHHC
26657352
1219UbiquitinationQSEGKEQKILLDTAC
CCCCHHHHHHHHHHH
-
1235UbiquitinationMVRWLSAKLGPTVAS
HHHHHHHHHCHHHHH
-
1239PhosphorylationLSAKLGPTVASRHVA
HHHHHCHHHHHHHHH
-
1242PhosphorylationKLGPTVASRHVARNL
HHCHHHHHHHHHHHH
23532336
1254PhosphorylationRNLLRLLTSCYVGPT
HHHHHHHHHCCCCCC
24719451
1266PhosphorylationGPTRQQFTVSSGESP
CCCCCEEEECCCCCC
28450419
1268PhosphorylationTRQQFTVSSGESPPL
CCCEEEECCCCCCCC
28450419
1269PhosphorylationRQQFTVSSGESPPLS
CCEEEECCCCCCCCC
28450419
1272PhosphorylationFTVSSGESPPLSAGN
EEECCCCCCCCCCCC
29507054
1276PhosphorylationSGESPPLSAGNIYQK
CCCCCCCCCCCCCCC
28450419
1313PhosphorylationYGEPVLTYQYLPYIS
HCCCEEEEEECCCEE
-
1318PhosphorylationLTYQYLPYISYLVAP
EEEEECCCEEEEECC
-
1603UbiquitinationGSDDNALKQELPRSV
CCCCHHHHHHCCCCC
-
1667PhosphorylationEDFFLSGSKDRTVRL
CCCCCCCCCCCEEEE
24260401
1668UbiquitinationDFFLSGSKDRTVRLW
CCCCCCCCCCEEEEE
-
1699PhosphorylationVYTQHRKSVFFVGQL
EEECCCCEEEEEECC
27251275
1738PhosphorylationRTVEPLDSRVPLTAV
CEECCCCCCCCEEEE
29759185
1844PhosphorylationVEGSVLVSSSSDHSL
EECEEEEECCCCCCE
-
1860UbiquitinationVWKELEQKPTHHYKS
HHHHHHCCCCCCCCC
-
1906UbiquitinationPPSQATTKLSSENFR
CCCCCCCCCCCCCCC
-
1915PhosphorylationSSENFRGTLTSLALL
CCCCCCCHHHHHHHC
-
1917PhosphorylationENFRGTLTSLALLPT
CCCCCHHHHHHHCCC
-
1918PhosphorylationNFRGTLTSLALLPTK
CCCCHHHHHHHCCCC
-
1924PhosphorylationTSLALLPTKRHLLLG
HHHHHCCCCCCEECC
-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR81_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SQSTM_HUMANSQSTM1physical
28404643
MLP3C_HUMANMAP1LC3Cphysical
28404643
UBC_HUMANUBCphysical
28404643
WDR91_HUMANWDR91physical
28404643

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR81_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP