dbPTM

ULK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ULK3_HUMAN
UniProt AC	Q6PHR2
Protein Name	Serine/threonine-protein kinase ULK3
Gene Name	ULK3
Organism	Homo sapiens (Human).
Sequence Length	472
Subcellular Localization	Cytoplasm . Localizes to pre-autophagosomal structure during cellular senescence.
Protein Description	Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy..
Protein Sequence	MAGPGWGPPRLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDSDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCQRQYDARVDLWSMGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPLLSRDCRDLLQRLLERDPSRRISFQDFFAHPWVDLEHMPSGESLGRATALVVQAVKKDQEGDSAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTSARDLLREMARDKPRLLAALEVASAAMAKEEAAGGEQDALDLYQHSLGELLLLLAAEPPGRRRELLHTEVQNLMARAEYLKEQVKMRESRWEADTLDKEGLSESVRSSCTLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Methylation	GPGWGPPRLDGFILT CCCCCCCCCCEEEEE	48.85	115387195
13	Phosphorylation	WGPPRLDGFILTERL CCCCCCCEEEEEEEC	18.98	-
17	Phosphorylation	RLDGFILTERLGSGT CCCEEEEEEECCCCC	17.78	20068231
22	Phosphorylation	ILTERLGSGTYATVY EEEEECCCCCEEEEE	32.33	23312004
24	Phosphorylation	TERLGSGTYATVYKA EEECCCCCEEEEEEH	16.22	23663014
25	Phosphorylation	ERLGSGTYATVYKAY EECCCCCEEEEEEHH	12.10	23663014
27	Phosphorylation	LGSGTYATVYKAYAK CCCCCEEEEEEHHCC	17.60	23312004
29	Phosphorylation	SGTYATVYKAYAKKD CCCEEEEEEHHCCCC	5.88	23663014
44	Ubiquitination	TREVVAIKCVAKKSL CCCEEEHHHEEECCC	16.96	-
53	Ubiquitination	VAKKSLNKASVENLL EEECCCCHHHHHHHH	47.54	-
53 (in isoform 3)	Ubiquitination	-	47.54	-
64	Ubiquitination	ENLLTEIEILKGIRH HHHHHHHHHHHCCCC	35.72	-
67 (in isoform 3)	Ubiquitination	-	58.93	-
67	Ubiquitination	LTEIEILKGIRHPHI HHHHHHHHCCCCCCE	58.93	-
78	Ubiquitination	HPHIVQLKDFQWDSD CCCEEEECCCCCCCC	39.13	-
139 (in isoform 3)	Ubiquitination	-	44.20	-
139	Ubiquitination	NISHLDLKPQNILLS CCCCCCCCHHHEEHH	44.20	-
146	Phosphorylation	KPQNILLSSLEKPHL CHHHEEHHHCCCCCC	29.45	20068231
147	Phosphorylation	PQNILLSSLEKPHLK HHHEEHHHCCCCCCC	40.28	20068231
150	Ubiquitination	ILLSSLEKPHLKLAD EEHHHCCCCCCCHHH	42.93	-
165	Phosphorylation	FGFAQHMSPWDEKHV CCCCCCCCCCCHHHC	22.25	17192257
170 (in isoform 3)	Ubiquitination	-	36.22	-
170	Ubiquitination	HMSPWDEKHVLRGSP CCCCCCHHHCCCCCC	36.22	-
176	Phosphorylation	EKHVLRGSPLYMAPE HHHCCCCCCCCCCHH	12.80	17192257
181	Ubiquitination	RGSPLYMAPEMVCQR CCCCCCCCHHHHHHC	5.37	-
219	Phosphorylation	PFASRSFSELEEKIR CCCCCCHHHHHHHHH	42.38	21815630
224	Ubiquitination	SFSELEEKIRSNRVI CHHHHHHHHHHCCCE	33.76	-
224 (in isoform 3)	Ubiquitination	-	33.76	-
235	Ubiquitination	NRVIELPLRPLLSRD CCCEEECCHHHCCHH	16.03	-
294 (in isoform 3)	Ubiquitination	-	59.03	-
300	Phosphorylation	KKDQEGDSAAALSLY HCCCCCCHHHHHHHH	30.57	20643644
305	Phosphorylation	GDSAAALSLYCKALD CCHHHHHHHHHHHHH	16.74	20873877
305	Ubiquitination	GDSAAALSLYCKALD CCHHHHHHHHHHHHH	16.74	-
333	Ubiquitination	RKEAIKAKVGQYVSR HHHHHHHHHHHHHHH	41.73	-
333 (in isoform 3)	Ubiquitination	-	41.73	-
344	Ubiquitination	YVSRAEELKAIVSSS HHHHHHHHHHHHHCH	3.23	-
345	Ubiquitination	VSRAEELKAIVSSSN HHHHHHHHHHHHCHH	39.07	-
345 (in isoform 3)	Ubiquitination	-	39.07	-
349	Phosphorylation	EELKAIVSSSNQALL HHHHHHHHCHHHHHH	23.18	28857561
350	Phosphorylation	ELKAIVSSSNQALLR HHHHHHHCHHHHHHH	23.55	28857561
356	Ubiquitination	SSSNQALLRQGTSAR HCHHHHHHHCCCCHH	4.27	-
361	Phosphorylation	ALLRQGTSARDLLRE HHHHCCCCHHHHHHH	28.29	-
384	Phosphorylation	LAALEVASAAMAKEE HHHHHHHHHHHHHHH	23.03	20643644
439	Phosphorylation	NLMARAEYLKEQVKM HHHHHHHHHHHHHHH	23.30	26330541
441	Ubiquitination	MARAEYLKEQVKMRE HHHHHHHHHHHHHHH	45.24	-
441 (in isoform 3)	Ubiquitination	-	45.24	-
449	Phosphorylation	EQVKMRESRWEADTL HHHHHHHHHHHHHCC	32.12	27251275
455	Phosphorylation	ESRWEADTLDKEGLS HHHHHHHCCCCCCCC	43.85	30266825
456 (in isoform 3)	Ubiquitination	-	10.23	-
458	Ubiquitination	WEADTLDKEGLSESV HHHHCCCCCCCCHHH	57.71	-
462	Phosphorylation	TLDKEGLSESVRSSC CCCCCCCCHHHHHHH	38.39	23401153
464	Phosphorylation	DKEGLSESVRSSCTL CCCCCCHHHHHHHCC	21.32	23401153
469	Ubiquitination	SESVRSSCTLQ---- CHHHHHHHCCC----	4.67	-

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
300	S	Phosphorylation	Kinase	ULK3	Q6PHR2	PSP
350	S	Phosphorylation	Kinase	ULK3	Q6PHR2	PSP
384	S	Phosphorylation	Kinase	ULK3	Q6PHR2	PSP
464	S	Phosphorylation	Kinase	ULK3	Q6PHR2	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ULK3_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 ULK3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR82_HUMAN	WDR82	physical	22939629
AIP_HUMAN	AIP	physical	26186194
FKBP5_HUMAN	FKBP5	physical	26186194
CDC37_HUMAN	CDC37	physical	26186194
FKBP5_HUMAN	FKBP5	physical	28514442
AIP_HUMAN	AIP	physical	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 ULK3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Dual function of UNC-51-like kinase 3 (Ulk3) in the Sonic hedgehogsignaling pathway."; Maloverjan A., Piirsoo M., Kasak L., Peil L., Osterlund T.,Kogerman P.; J. Biol. Chem. 285:30079-30090(2010). Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH SUFU, MUTAGENESIS OFLYS-139, AND PHOSPHORYLATION AT SER-300; SER-350; SER-384 AND SER-464.	20643644 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-176, ANDMASS SPECTROMETRY.	18691976 [Abstract]