WDR91_HUMAN - dbPTM
WDR91_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR91_HUMAN
UniProt AC A4D1P6
Protein Name WD repeat-containing protein 91 {ECO:0000312|HGNC:HGNC:24997}
Gene Name WDR91 {ECO:0000312|HGNC:HGNC:24997}
Organism Homo sapiens (Human).
Sequence Length 747
Subcellular Localization Early endosome membrane
Peripheral membrane protein . Late endosome membrane .
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 MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQPQSSAKKESFGGQGTKGKDPTSGAKDGKSLLSGLATGESGWSQHRQRRLQDHGKERKELFSTTTSQCAEKKPEASGPEAEPCPELHTEPVEPLTRASSAGPEGGGVRPEQPFIVLGQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVIKVWSFNPIMQTKASSISKSPLLSLEWATKRDRLLLLGSGVGTVRLYDTEAKKNLCEININDNMPRILSLACSPNGASFVCSAAAPSLTSQVDFSAPDIGSKGMNQVPGRLLLWDTKTMKQQLQFSLDPEPIAINCTAFNHNGNLLVTGAADGVIRLFDMQQHECAMSWRAHYGEVYSVEFSYDENTVYSIGEDGKFIQWNIHKSGLKVSEYSLPSDATGPFVLSGYSGYKQVQVPRGRLFAFDSEGNYMLTCSATGGVIYKLGGDEKVLESCLSLGGHRAPVVTVDWSTAMDCGTCLTASMDGKIKLTTLLAHKA
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
80PhosphorylationFSRLEDIYRPTIHKL
HHHHHHHHHHHHHHH		23.90-
90PhosphorylationTIHKLKTSLFRFYLV
HHHHHHHHHHHEEEE		24.7524719451
95PhosphorylationKTSLFRFYLVYTIQT
HHHHHHEEEEEEEEC		7.3325404012
98PhosphorylationLFRFYLVYTIQTNRN
HHHEEEEEEEECCCC		8.7725404012
99PhosphorylationFRFYLVYTIQTNRND
HHEEEEEEEECCCCH		10.1025404012
102PhosphorylationYLVYTIQTNRNDKAQ
EEEEEEECCCCHHHH		32.0925404012
114UbiquitinationKAQEFFAKQATELQN
HHHHHHHHHHHHHHH		35.0029967540
139PhosphorylationPFLPSPDTNPTFATY
ECCCCCCCCCCHHHH		46.6232645325
198UbiquitinationENEVLRQKLFALQAE
HHHHHHHHHHHHHHH		38.86-
247PhosphorylationSELAMVCSQRNASLS
HHHHHHHHHCCCCCC		22.2928857561
252PhosphorylationVCSQRNASLSQSPRV
HHHHCCCCCCCCCCH		31.9125159151
254PhosphorylationSQRNASLSQSPRVGF
HHCCCCCCCCCCHHH		26.5623663014
256PhosphorylationRNASLSQSPRVGFLS
CCCCCCCCCCHHHHH		15.9929255136
263PhosphorylationSPRVGFLSSLLPQSK
CCCHHHHHHHCCCCC		19.3728857561
264PhosphorylationPRVGFLSSLLPQSKK
CCHHHHHHHCCCCCC		35.7528857561
269PhosphorylationLSSLLPQSKKSPSRL
HHHHCCCCCCCCCCC		39.8628857561
270UbiquitinationSSLLPQSKKSPSRLS
HHHCCCCCCCCCCCC		52.61-
272PhosphorylationLLPQSKKSPSRLSPA
HCCCCCCCCCCCCCC		31.6625159151
274PhosphorylationPQSKKSPSRLSPAQG
CCCCCCCCCCCCCCC		53.6030108239
277PhosphorylationKKSPSRLSPAQGPPQ
CCCCCCCCCCCCCCC		19.6525159151
287PhosphorylationQGPPQPQSSAKKESF
CCCCCCCCCCCCHHC		38.6628985074
288PhosphorylationGPPQPQSSAKKESFG
CCCCCCCCCCCHHCC		38.5725159151
293PhosphorylationQSSAKKESFGGQGTK
CCCCCCHHCCCCCCC		37.7626657352
305PhosphorylationGTKGKDPTSGAKDGK
CCCCCCCCCCCCCCH		50.34-
320PhosphorylationSLLSGLATGESGWSQ
HHHHHHHCCCCCHHH		46.6630108239
323PhosphorylationSGLATGESGWSQHRQ
HHHHCCCCCHHHHHH		47.0828857561
326PhosphorylationATGESGWSQHRQRRL
HCCCCCHHHHHHHHH		21.4530108239
345PhosphorylationKERKELFSTTTSQCA
HHHHHHHHCCHHHHH		37.1528857561
346PhosphorylationERKELFSTTTSQCAE
HHHHHHHCCHHHHHH		27.1028857561
348PhosphorylationKELFSTTTSQCAEKK
HHHHHCCHHHHHHCC		19.52-
349PhosphorylationELFSTTTSQCAEKKP
HHHHCCHHHHHHCCC		22.5928857561
381PhosphorylationVEPLTRASSAGPEGG
CCCCCCCCCCCCCCC		19.8928857561
382PhosphorylationEPLTRASSAGPEGGG
CCCCCCCCCCCCCCC		35.9430108239
425PhosphorylationCSGRRVASLDVDGVI
CCCCEEEEEECCCEE		23.42-
436PhosphorylationDGVIKVWSFNPIMQT
CCEEEEEEECCCCCC		20.38-
443PhosphorylationSFNPIMQTKASSISK
EECCCCCCCCHHCCC		15.9329978859
444UbiquitinationFNPIMQTKASSISKS
ECCCCCCCCHHCCCC		29.40-
446PhosphorylationPIMQTKASSISKSPL
CCCCCCCHHCCCCCC		29.7529978859
447PhosphorylationIMQTKASSISKSPLL
CCCCCCHHCCCCCCC		35.4229978859
449PhosphorylationQTKASSISKSPLLSL
CCCCHHCCCCCCCCC		29.0929759185
451PhosphorylationKASSISKSPLLSLEW
CCHHCCCCCCCCCHH		17.6229759185
455PhosphorylationISKSPLLSLEWATKR
CCCCCCCCCHHCCCC		31.7429759185
461AcetylationLSLEWATKRDRLLLL
CCCHHCCCCCEEEEE		44.5525953088
470PhosphorylationDRLLLLGSGVGTVRL
CEEEEECCCCCEEEE		30.21-
474PhosphorylationLLGSGVGTVRLYDTE
EECCCCCEEEEEEHH		10.47-
484UbiquitinationLYDTEAKKNLCEINI
EEEHHHHHCEEEEEC		63.30-
547PhosphorylationGRLLLWDTKTMKQQL
CEEEEEECCHHHHHH		19.4830206219
549PhosphorylationLLLWDTKTMKQQLQF
EEEEECCHHHHHHCC		31.5230206219
599PhosphorylationQQHECAMSWRAHYGE
CCHHHHHEHHHCCCE		8.55-
703PhosphorylationGDEKVLESCLSLGGH
CCHHHHHHHHHCCCC		19.0522210691
706PhosphorylationKVLESCLSLGGHRAP
HHHHHHHHCCCCCCC		29.3322210691
740PhosphorylationMDGKIKLTTLLAHKA
CCCEEEEEEECCCCC		15.47-
741PhosphorylationDGKIKLTTLLAHKA-
CCEEEEEEECCCCC-		30.15-
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 WDR91_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR91_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 WDR91_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WDR91_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR91_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.

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