PPIL2_HUMAN - dbPTM
PPIL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIL2_HUMAN
UniProt AC Q13356
Protein Name RING-type E3 ubiquitin-protein ligase PPIL2 {ECO:0000305}
Gene Name PPIL2 {ECO:0000312|HGNC:HGNC:9261}
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Nucleus . May also localize to the cytoplasm and the cell membrane.
Protein Description Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation. [PubMed: 11435423 May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance]
Protein Sequence MGKRQHQKDKMYITCAEYTHFYGGKKPDLPQTNFRRLPFDHCSLSLQPFVYPVCTPDGIVFDLLNIVPWLKKYGTNPSNGEKLDGRSLIKLNFSKNSEGKYHCPVLFTVFTNNTHIVAVRTTGNVYAYEAVEQLNIKAKNFRDLLTDEPFSRQDIITLQDPTNLDKFNVSNFYHVKNNMKIIDPDEEKAKQDPSYYLKNTNAETRETLQELYKEFKGDEILAATMKAPEKKKVDKLNAAHYSTGKVSASFTSTAMVPETTHEAAAIDEDVLRYQFVKKKGYVRLHTNKGDLNLELHCDLTPKTCENFIRLCKKHYYDGTIFHRSIRNFVIQGGDPTGTGTGGESYWGKPFKDEFRPNLSHTGRGILSMANSGPNSNRSQFFITFRSCAYLDKKHTIFGRVVGGFDVLTAMENVESDPKTDRPKEEIRIDATTVFVDPYEEADAQIAQERKTQLKVAPETKVKSSQPQAGSQGPQTFRQGVGKYINPAATKRAAEEEPSTSATVPMSKKKPSRGFGDFSSW
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
12PhosphorylationQHQKDKMYITCAEYT
CHHCCCEEEEEECCH		9.98-
18PhosphorylationMYITCAEYTHFYGGK
EEEEEECCHHHCCCC		6.2329052541
19PhosphorylationYITCAEYTHFYGGKK
EEEEECCHHHCCCCC		9.3029052541
22PhosphorylationCAEYTHFYGGKKPDL
EECCHHHCCCCCCCC		19.8429052541
72UbiquitinationNIVPWLKKYGTNPSN
HHHHHHHHHCCCCCC		46.90-
82UbiquitinationTNPSNGEKLDGRSLI
CCCCCCCCCCCCEEE		53.96-
82 (in isoform 2)Ubiquitination-53.96-
87PhosphorylationGEKLDGRSLIKLNFS
CCCCCCCEEEEECCC		39.7224719451
90 (in isoform 2)Ubiquitination-42.54-
90UbiquitinationLDGRSLIKLNFSKNS
CCCCEEEEECCCCCC		42.54-
95UbiquitinationLIKLNFSKNSEGKYH
EEEECCCCCCCCCEE		61.43-
95 (in isoform 2)Ubiquitination-61.43-
139UbiquitinationEQLNIKAKNFRDLLT
HHHCCCCCCHHHHHC		52.17-
166 (in isoform 1)Ubiquitination-41.8421890473
166 (in isoform 2)Ubiquitination-41.8421890473
166UbiquitinationQDPTNLDKFNVSNFY
CCCCCCCCCCCCCEE		41.842189047
170PhosphorylationNLDKFNVSNFYHVKN
CCCCCCCCCEEEEEC		23.4828555341
176UbiquitinationVSNFYHVKNNMKIID
CCCEEEEECCEEECC		29.32-
180 (in isoform 2)Ubiquitination-38.34-
180UbiquitinationYHVKNNMKIIDPDEE
EEEECCEEECCCCHH		38.34-
190UbiquitinationDPDEEKAKQDPSYYL
CCCHHHHHCCCCHHH		67.32-
194PhosphorylationEKAKQDPSYYLKNTN
HHHHCCCCHHHCCCC		34.4029083192
195PhosphorylationKAKQDPSYYLKNTNA
HHHCCCCHHHCCCCH		20.4322468782
196PhosphorylationAKQDPSYYLKNTNAE
HHCCCCHHHCCCCHH		18.6122468782
198 (in isoform 2)Ubiquitination-45.67-
198UbiquitinationQDPSYYLKNTNAETR
CCCCHHHCCCCHHHH		45.67-
200PhosphorylationPSYYLKNTNAETRET
CCHHHCCCCHHHHHH		33.9322468782
212PhosphorylationRETLQELYKEFKGDE
HHHHHHHHHHHCCCH		14.0227642862
213 (in isoform 2)Ubiquitination-70.11-
213UbiquitinationETLQELYKEFKGDEI
HHHHHHHHHHCCCHH		70.11-
216SumoylationQELYKEFKGDEILAA
HHHHHHHCCCHHHHH		67.5528112733
216SumoylationQELYKEFKGDEILAA
HHHHHHHCCCHHHHH		67.55-
226AcetylationEILAATMKAPEKKKV
HHHHHHCCCCCHHCC		57.3324469495
226UbiquitinationEILAATMKAPEKKKV
HHHHHHCCCCCHHCC		57.33-
230AcetylationATMKAPEKKKVDKLN
HHCCCCCHHCCCCCC		57.7624469505
231AcetylationTMKAPEKKKVDKLNA
HCCCCCHHCCCCCCC		57.2624469515
232 (in isoform 2)Ubiquitination-67.73-
235AcetylationPEKKKVDKLNAAHYS
CCHHCCCCCCCCHHC		46.7825953088
235UbiquitinationPEKKKVDKLNAAHYS
CCHHCCCCCCCCHHC		46.78-
241PhosphorylationDKLNAAHYSTGKVSA
CCCCCCHHCCCCCCE		11.8227642862
281PhosphorylationQFVKKKGYVRLHTNK
HHHEECCEEEEEECC		7.4128509920
286PhosphorylationKGYVRLHTNKGDLNL
CCEEEEEECCCCEEE		43.1228509920
313UbiquitinationNFIRLCKKHYYDGTI
HHHHHHHHHCCCCCE		35.52-
313 (in isoform 2)Ubiquitination-35.52-
393UbiquitinationSCAYLDKKHTIFGRV
HCEECCCCCEEEEEE		45.72-
395PhosphorylationAYLDKKHTIFGRVVG
EECCCCCEEEEEEEC		27.21-
410SulfoxidationGFDVLTAMENVESDP
CHHHHHHHHHCCCCC		3.0328183972
415PhosphorylationTAMENVESDPKTDRP
HHHHHCCCCCCCCCC		55.73-
459PhosphorylationQLKVAPETKVKSSQP
HCEECCCCCCCCCCC		39.8321406692
460SumoylationLKVAPETKVKSSQPQ
CEECCCCCCCCCCCC		46.10-
460SumoylationLKVAPETKVKSSQPQ
CEECCCCCCCCCCCC		46.10-
462UbiquitinationVAPETKVKSSQPQAG
ECCCCCCCCCCCCCC		46.04-
462 (in isoform 2)Ubiquitination-46.04-
470PhosphorylationSSQPQAGSQGPQTFR
CCCCCCCCCCCCHHH		34.6722210691
482UbiquitinationTFRQGVGKYINPAAT
HHHHCCHHHCCHHHH		40.32-
482AcetylationTFRQGVGKYINPAAT
HHHHCCHHHCCHHHH		40.3219608861
483PhosphorylationFRQGVGKYINPAATK
HHHCCHHHCCHHHHH		10.4527642862
489PhosphorylationKYINPAATKRAAEEE
HHCCHHHHHHHHCCC		24.1422985185
490AcetylationYINPAATKRAAEEEP
HCCHHHHHHHHCCCC		35.0025953088
490UbiquitinationYINPAATKRAAEEEP
HCCHHHHHHHHCCCC		35.00-
495 (in isoform 2)Phosphorylation-71.1723090842
498PhosphorylationRAAEEEPSTSATVPM
HHHCCCCCCCCCCCC		37.9726270265
499PhosphorylationAAEEEPSTSATVPMS
HHCCCCCCCCCCCCC		32.8529759185
500PhosphorylationAEEEPSTSATVPMSK
HCCCCCCCCCCCCCC		26.7026270265
502 (in isoform 2)Phosphorylation-25.5527732954
502PhosphorylationEEPSTSATVPMSKKK
CCCCCCCCCCCCCCC		25.5526270265
505SulfoxidationSTSATVPMSKKKPSR
CCCCCCCCCCCCCCC		8.7921406390
506PhosphorylationTSATVPMSKKKPSRG
CCCCCCCCCCCCCCC		34.9426270265
508 (in isoform 2)Phosphorylation-63.7126434776
511PhosphorylationPMSKKKPSRGFGDFS
CCCCCCCCCCCCCCC		54.6529759185
512MethylationMSKKKPSRGFGDFSS
CCCCCCCCCCCCCCC		53.6554558135
518PhosphorylationSRGFGDFSSW-----
CCCCCCCCCC-----		35.6827251275
519PhosphorylationRGFGDFSSW------
CCCCCCCCC------		36.4824719451
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 PPIL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIL2_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 PPIL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRNL1_MOUSECrnkl1physical
15189447
HS90A_HUMANHSP90AA1physical
15189447
PPIL2_HUMANPPIL2physical
8660300
BASI_HUMANBSGphysical
15946952
A4_HUMANAPPphysical
21832049
PRCC_HUMANPRCCphysical
22365833
ZN830_HUMANZNF830physical
22365833
KANL2_HUMANKANSL2physical
26496610
ZN830_HUMANZNF830physical
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 PPIL2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND MASS SPECTROMETRY.

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