PELI2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PELI2_HUMAN
• UniProt AC: Q9HAT8
• Protein Name: E3 ubiquitin-protein ligase pellino homolog 2
• Gene Name: PELI2
• Organism: Homo sapiens (Human).
• Sequence Length: 420
• Protein Description: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates IL1B-induced IRAK1 'Lys-63'-linked polyubiquitination and possibly 'Lys-48'-linked ubiquitination. May be important for LPS- and IL1B-induced MAP3K7-dependent, but not MAP3K3-dependent, NF-kappa-B activation. Can activate the MAP (mitogen activated protein) kinase pathway leading to activation of ELK1..
• Protein Sequence: MFSPGQEEHCAPNKEPVKYGELVVLGYNGALPNGDRGRRKSRFALYKRPKANGVKPSTVHVISTPQASKAISCKGQHSISYTLSRNQTVVVEYTHDKDTDMFQVGRSTESPIDFVVTDTISGSQNTDEAQITQSTISRFACRIVCDRNEPYTARIFAAGFDSSKNIFLGEKAAKWKNPDGHMDGLTTNGVLVMHPRGGFTEESQPGVWREISVCGDVYTLRETRSAQQRGKLVESETNVLQDGSLIDLCGATLLWRTADGLFHTPTQKHIEALRQEINAARPQCPVGLNTLAFPSINRKEVVEEKQPWAYLSCGHVHGYHNWGHRSDTEANERECPMCRTVGPYVPLWLGCEAGFYVDAGPPTHAFTPCGHVCSEKSAKYWSQIPLPHGTHAFHAACPFCATQLVGEQNCIKLIFQGPID

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
3	Phosphorylation	-----MFSPGQEEHC -----CCCCCCCCCC	27.16	-
36	Methylation	GALPNGDRGRRKSRF CCCCCCCCCCCCCCE	41.75	81452627
38	Methylation	LPNGDRGRRKSRFAL CCCCCCCCCCCCEEE	43.69	115388779
47	Ubiquitination	KSRFALYKRPKANGV CCCEEEECCCCCCCC	64.17	-
50	Acetylation	FALYKRPKANGVKPS EEEECCCCCCCCCCC	59.52	7965575
55	Acetylation	RPKANGVKPSTVHVI CCCCCCCCCCEEEEE	34.35	7965585
63	Phosphorylation	PSTVHVISTPQASKA CCEEEEEECCCCCCC	32.71	28555341
64	Phosphorylation	STVHVISTPQASKAI CEEEEEECCCCCCCC	14.32	-
69	Ubiquitination	ISTPQASKAISCKGQ EECCCCCCCCCCCCE	53.40	-
74	Ubiquitination	ASKAISCKGQHSISY CCCCCCCCCEEEEEE	55.61	-
78	Phosphorylation	ISCKGQHSISYTLSR CCCCCEEEEEEEECC	12.82	30576142
80	Phosphorylation	CKGQHSISYTLSRNQ CCCEEEEEEEECCCC	18.32	30576142
81	Phosphorylation	KGQHSISYTLSRNQT CCEEEEEEEECCCCE	15.27	-
82	Phosphorylation	GQHSISYTLSRNQTV CEEEEEEEECCCCEE	16.09	30576142
84	Phosphorylation	HSISYTLSRNQTVVV EEEEEEECCCCEEEE	22.76	-
88	Phosphorylation	YTLSRNQTVVVEYTH EEECCCCEEEEEEEC	20.86	28555341
151	Phosphorylation	VCDRNEPYTARIFAA ECCCCCCEEEEEEEE	13.57	25839225
164	Ubiquitination	AAGFDSSKNIFLGEK EEECCCCCCEECCHH	59.00	-
171	Ubiquitination	KNIFLGEKAAKWKNP CCEECCHHHHCCCCC	52.42	-
176	Acetylation	GEKAAKWKNPDGHMD CHHHHCCCCCCCCCC	58.87	19608861
219	Phosphorylation	SVCGDVYTLRETRSA EEECCEEEHHHCCHH	21.13	24719451
235	Phosphorylation	QRGKLVESETNVLQD HHCCEEECCCCCCCC	42.09	29978859
237	Phosphorylation	GKLVESETNVLQDGS CCEEECCCCCCCCCC	39.65	29978859
244	Phosphorylation	TNVLQDGSLIDLCGA CCCCCCCCCHHHCCC	30.37	29978859
252	Phosphorylation	LIDLCGATLLWRTAD CHHHCCCEEEEECCC	13.99	29978859
257	Phosphorylation	GATLLWRTADGLFHT CCEEEEECCCCCCCC	19.95	29978859
264	Phosphorylation	TADGLFHTPTQKHIE CCCCCCCCCHHHHHH	22.24	29978859
266	Phosphorylation	DGLFHTPTQKHIEAL CCCCCCCHHHHHHHH	51.94	29978859
268	Ubiquitination	LFHTPTQKHIEALRQ CCCCCHHHHHHHHHH	49.37	-
290	Phosphorylation	QCPVGLNTLAFPSIN CCCCCCCCEECCCCC	25.22	30576142
295	Phosphorylation	LNTLAFPSINRKEVV CCCEECCCCCHHHHH	26.49	30576142

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
290	T	Phosphorylation	Kinase	IRAK1	P51617	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PELI2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PELI2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRAK1_HUMAN	IRAK1	physical	17675297
IRAK4_HUMAN	IRAK4	physical	12860405
IRAK1_HUMAN	IRAK1	physical	12860405
IRAK1_HUMAN	IRAK1	physical	15917247
TRAF6_HUMAN	TRAF6	physical	12804775
NR2C2_HUMAN	NR2C2	physical	12804775
PICAL_HUMAN	PICALM	physical	21988832
THAP7_HUMAN	THAP7	physical	21988832
IRAK1_HUMAN	IRAK1	physical	25027698
UCRI_HUMAN	UQCRFS1	physical	25027698
TRAF6_HUMAN	TRAF6	physical	25027698

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-176, AND MASS SPECTROMETRY.
PubMed: 19608861