WIPI2_HUMAN - dbPTM
WIPI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WIPI2_HUMAN
UniProt AC Q9Y4P8
Protein Name WD repeat domain phosphoinositide-interacting protein 2
Gene Name WIPI2
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization Preautophagosomal structure membrane
Peripheral membrane protein
Cytoplasmic side . Localizes to omegasomes membranes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Enriched at preautophagosomal
Protein Description Early component of the autophagy machinery being involved in formation of preautophagosomal structures and their maturation into mature phagosomes in response to phosphatidylinositol 3-phosphate (PtdIns3P). May bind PtdIns3P.; Isoform 4: Recruits the ATG12-ATG5-ATG16L1 complex to omegasomes and preautophagosomal structures, resulting in ATG8 family proteins lipidation and starvation-induced autophagy. Isoform 4 is also required for autophagic clearance of pathogenic bacteria. Isoform 4 binds the membrane surrounding Salmonella and recruits the ATG12-5-16L1 complex, initiating LC3 conjugation, autophagosomal membrane formation, and engulfment of Salmonella..
Protein Sequence MNLASQSGEAGAGQLLFANFNQDNTEVKGASRAAGLGRRAVVWSLAVGSKSGYKFFSLSSVDKLEQIYECTDTEDVCIVERLFSSSLVAIVSLKAPRKLKVCHFKKGTEICNYSYSNTILAVKLNRQRLIVCLEESLYIHNIRDMKVLHTIRETPPNPAGLCALSINNDNCYLAYPGSATIGEVQVFDTINLRAANMIPAHDSPLAALAFDASGTKLATASEKGTVIRVFSIPEGQKLFEFRRGVKRCVSICSLAFSMDGMFLSASSNTETVHIFKLETVKEKPPEEPTTWTGYFGKVLMASTSYLPSQVTEMFNQGRAFATVRLPFCGHKNICSLATIQKIPRLLVGAADGYLYMYNLDPQEGGECALMKQHRLDGSLETTNEILDSASHDCPLVTQTYGAAAGKGTYVPSSPTRLAYTDDLGAVGGACLEDEASALRLDEDSEHPPMILRTD
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
21 (in isoform 5)Phosphorylation-48.3724275569
24 (in isoform 5)Phosphorylation-28.5124275569
27 (in isoform 5)Phosphorylation-6.9724275569
28UbiquitinationNQDNTEVKGASRAAG
CCCCCCCCCHHHHCC		42.39-
29 (in isoform 5)Phosphorylation-33.6824275569
35 (in isoform 5)Phosphorylation-27.9024275569
115PhosphorylationTEICNYSYSNTILAV
CEECCCCCCCEEEEE		8.7925332170
118PhosphorylationCNYSYSNTILAVKLN
CCCCCCCEEEEEEEC		16.0725332170
146UbiquitinationIHNIRDMKVLHTIRE
EEECCCCEEEEEECC		46.03-
157 (in isoform 3)Ubiquitination-40.0121906983
164 (in isoform 3)Ubiquitination-5.2921906983
178 (in isoform 3)Ubiquitination-20.1021906983
198 (in isoform 4)Ubiquitination-2.4621906983
198 (in isoform 2)Ubiquitination-2.4621906983
205 (in isoform 2)Ubiquitination-5.1521906983
205 (in isoform 4)Ubiquitination-5.1521906983
211 (in isoform 5)Ubiquitination-33.9321906983
216UbiquitinationAFDASGTKLATASEK
EECCCCCEEEEECCC		39.3821906983
216 (in isoform 1)Ubiquitination-39.3821906983
218 (in isoform 5)Ubiquitination-11.5921906983
219 (in isoform 2)Ubiquitination-40.9521906983
219 (in isoform 4)Ubiquitination-40.9521906983
223 (in isoform 1)Ubiquitination-58.3421906983
223MalonylationKLATASEKGTVIRVF
EEEEECCCCCEEEEE		58.3426320211
223UbiquitinationKLATASEKGTVIRVF
EEEEECCCCCEEEEE		58.34-
223AcetylationKLATASEKGTVIRVF
EEEEECCCCCEEEEE		58.3423749302
232 (in isoform 5)Ubiquitination-2.1521906983
237UbiquitinationFSIPEGQKLFEFRRG
EECCCCHHHHHHHHH		67.032190698
237 (in isoform 1)Ubiquitination-67.0321906983
283UbiquitinationKLETVKEKPPEEPTT
EEEECCCCCCCCCCC		61.22-
292PhosphorylationPEEPTTWTGYFGKVL
CCCCCCCCCCCCCHH		21.6625690035
294PhosphorylationEPTTWTGYFGKVLMA
CCCCCCCCCCCHHHH		11.2025690035
302PhosphorylationFGKVLMASTSYLPSQ
CCCHHHHCCCCCCHH		12.1527251275
303PhosphorylationGKVLMASTSYLPSQV
CCHHHHCCCCCCHHH		16.3227251275
304PhosphorylationKVLMASTSYLPSQVT
CHHHHCCCCCCHHHH		23.3727251275
305PhosphorylationVLMASTSYLPSQVTE
HHHHCCCCCCHHHHH		23.7928555341
308PhosphorylationASTSYLPSQVTEMFN
HCCCCCCHHHHHHHH		34.39-
322 (in isoform 3)Phosphorylation-10.3322210691
329 (in isoform 3)Phosphorylation-34.8722210691
331UbiquitinationRLPFCGHKNICSLAT
ECCCCCCCCCCCHHH		33.04-
331AcetylationRLPFCGHKNICSLAT
ECCCCCCCCCCCHHH		33.0426051181
331 (in isoform 3)Phosphorylation-33.0422210691
341UbiquitinationCSLATIQKIPRLLVG
CCHHHHHHCCHHHHC		51.32-
363 (in isoform 2)Phosphorylation-74.6522210691
370 (in isoform 2)Phosphorylation-1.7722210691
371UbiquitinationGGECALMKQHRLDGS
CCEEEEEEEEECCCC		43.75-
372 (in isoform 2)Phosphorylation-16.9922210691
376 (in isoform 5)Phosphorylation-44.5922210691
378PhosphorylationKQHRLDGSLETTNEI
EEEECCCCCCCHHHH		23.7727966365
381 (in isoform 6)Phosphorylation-39.9722210691
381PhosphorylationRLDGSLETTNEILDS
ECCCCCCCHHHHHHH		39.9727251275
382PhosphorylationLDGSLETTNEILDSA
CCCCCCCHHHHHHHH		22.8327251275
383 (in isoform 5)Phosphorylation-41.5522210691
385 (in isoform 5)Phosphorylation-5.8522210691
388 (in isoform 6)Phosphorylation-28.3822210691
388PhosphorylationTTNEILDSASHDCPL
CHHHHHHHHCCCCCE		28.3825849741
390 (in isoform 6)Phosphorylation-24.6622210691
390PhosphorylationNEILDSASHDCPLVT
HHHHHHHCCCCCEEE		24.6629978859
397PhosphorylationSHDCPLVTQTYGAAA
CCCCCEEEEECCCCC		23.9119664994
397O-linked_GlycosylationSHDCPLVTQTYGAAA
CCCCCEEEEECCCCC		23.91OGP
399PhosphorylationDCPLVTQTYGAAAGK
CCCEEEEECCCCCCC		17.9826074081
400PhosphorylationCPLVTQTYGAAAGKG
CCEEEEECCCCCCCC		8.5829978859
408PhosphorylationGAAAGKGTYVPSSPT
CCCCCCCEECCCCCC		25.4923927012
409PhosphorylationAAAGKGTYVPSSPTR
CCCCCCEECCCCCCE		21.0223927012
412PhosphorylationGKGTYVPSSPTRLAY
CCCEECCCCCCEEEE		38.6223927012
413PhosphorylationKGTYVPSSPTRLAYT
CCEECCCCCCEEEEE		24.9919664994
415PhosphorylationTYVPSSPTRLAYTDD
EECCCCCCEEEEECC		40.0219664994
419PhosphorylationSSPTRLAYTDDLGAV
CCCCEEEEECCCCCC		18.4626074081
420PhosphorylationSPTRLAYTDDLGAVG
CCCEEEEECCCCCCC		19.8926074081
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
-KUbiquitinationE3 ubiquitin ligaseHUWE1Q7Z6Z7
PMID:30646805
-KUbiquitinationE3 ubiquitin ligaseCRL4A-
PMID:30898011
-KUbiquitinationE3 ubiquitin ligaseCRLB-
PMID:30898011
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WIPI2_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 WIPI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN6_HUMANCOPS6physical
16169070
BTBD8_HUMANBTBD8physical
20562859
NUDC_HUMANNUDCphysical
20562859
FLNC_HUMANFLNCphysical
20562859
GCN1_HUMANGCN1L1physical
20562859
PFKAP_HUMANPFKPphysical
20562859
DNJB1_HUMANDNAJB1physical
20562859
DYN2_HUMANDNM2physical
20562859
ZFAN6_HUMANZFAND6physical
22939629
A16L1_HUMANATG16L1physical
24954904
ATG5_HUMANATG5physical
24954904
ATG12_HUMANATG12physical
24954904
CP070_HUMANC16orf70physical
26186194
BCAS3_HUMANBCAS3physical
26186194
NAGK_HUMANNAGKphysical
26186194
RBGP1_HUMANRABGAP1physical
26186194
A16L1_HUMANATG16L1physical
26186194
DPH1_HUMANDPH1physical
26186194
BNI3L_HUMANBNIP3Lphysical
26186194
ATG5_HUMANATG5physical
26186194
DPH2_HUMANDPH2physical
26186194
CP070_HUMANC16orf70physical
28514442
A16L1_HUMANATG16L1physical
28514442
BCAS3_HUMANBCAS3physical
28514442
ATG5_HUMANATG5physical
28514442
BNI3L_HUMANBNIP3Lphysical
28514442
DPH2_HUMANDPH2physical
28514442
DPH1_HUMANDPH1physical
28514442
RBGP1_HUMANRABGAP1physical
28514442
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 WIPI2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASSSPECTROMETRY.

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