dbPTM

TOLIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOLIP_HUMAN
UniProt AC	Q9H0E2
Protein Name	Toll-interacting protein
Gene Name	TOLLIP
Organism	Homo sapiens (Human).
Sequence Length	274
Subcellular Localization	Cytoplasm .
Protein Description	Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity. [PubMed: 11751856 Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates]
Protein Sequence	MATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVGRLNITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIHCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLRQGKVEDKWYSLSGRQGDDKEGMINLVMSYALLPAAMVMPPQPVVLMPTVYQQGVGYVPITGMPAVCSPGMVPVALPPAAVNAQPRCSEEDLKAIQDMFPNMDQEVIRSVLEAQRGNKDAAINSLLQMGEEP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATTVSTQR ------CCCEECCCC	16.39	22814378
6	Phosphorylation	--MATTVSTQRGPVY --CCCEECCCCCCEE	19.41	-
13	Phosphorylation	STQRGPVYIGELPQD CCCCCCEEEECCCCC	13.32	25884760
25	Phosphorylation	PQDFLRITPTQQQRQ CCCCCCCCCCHHHHH	17.53	26437602
45	Phosphorylation	QAAQQLQYGGAVGTV HHHHHHHCCCCCCCC	26.56	25884760
63	Acetylation	NITVVQAKLAKNYGM EEEEEEHHHHHHHCC	31.70	25953088
63	Ubiquitination	NITVVQAKLAKNYGM EEEEEEHHHHHHHCC	31.70	21890473
63	Ubiquitination	NITVVQAKLAKNYGM EEEEEEHHHHHHHCC	31.70	21906983
66	Ubiquitination	VVQAKLAKNYGMTRM EEEHHHHHHHCCCCC	62.23	21890473
66	Ubiquitination	VVQAKLAKNYGMTRM EEEHHHHHHHCCCCC	62.23	21906983
68	Phosphorylation	QAKLAKNYGMTRMDP EHHHHHHHCCCCCCC	13.94	-
71	Phosphorylation	LAKNYGMTRMDPYCR HHHHHCCCCCCCCHH	20.62	-
76	Phosphorylation	GMTRMDPYCRLRLGY CCCCCCCCHHHHCEE	5.97	-
83	Phosphorylation	YCRLRLGYAVYETPT CHHHHCEEEEEECCC	9.48	19534553
86	Phosphorylation	LRLGYAVYETPTAHN HHCEEEEEECCCCCC	13.10	25839225
96	Malonylation	PTAHNGAKNPRWNKV CCCCCCCCCCCCCCE	69.73	26320211
96	Ubiquitination	PTAHNGAKNPRWNKV CCCCCCCCCCCCCCE	69.73	-
96	Ubiquitination	PTAHNGAKNPRWNKV CCCCCCCCCCCCCCE	69.73	21890473
141	Phosphorylation	THITIPESLRQGKVE EEEECCHHHHCCCCC	24.41	20068231
146	Ubiquitination	PESLRQGKVEDKWYS CHHHHCCCCCCCEEE	33.83	21906983
150	Ubiquitination	RQGKVEDKWYSLSGR HCCCCCCCEEECCCC	34.23	21906983
150	Ubiquitination	RQGKVEDKWYSLSGR HCCCCCCCEEECCCC	34.23	21890473
171	Phosphorylation	GMINLVMSYALLPAA HHHHHHHHHHHHHHH	10.36	-
235	Acetylation	RCSEEDLKAIQDMFP CCCHHHHHHHHHHCC	56.62	90979
235	Ubiquitination	RCSEEDLKAIQDMFP CCCHHHHHHHHHHCC	56.62	-
270	Sulfoxidation	AINSLLQMGEEP--- HHHHHHHCCCCC---	8.02	21406390

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 TOLIP_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHXF2_HUMAN	RHOXF2	physical	16189514
TOM1_HUMAN	TOM1	physical	14563850
SETB1_HUMAN	SETDB1	physical	16169070
ZHX1_HUMAN	ZHX1	physical	16169070
ZBT16_HUMAN	ZBTB16	physical	16169070
TLR2_HUMAN	TLR2	physical	11751856
TLR4_HUMAN	TLR4	physical	11751856
TOLIP_HUMAN	TOLLIP	physical	11751856
IRAK1_HUMAN	IRAK1	physical	10854325
IL1R1_HUMAN	IL1R1	physical	17113392
IRAK1_HUMAN	IRAK1	physical	17113392
CASA1_HUMAN	CSN1S1	physical	20936779
CASB_HUMAN	CSN2	physical	20936779
FRIH_HUMAN	FTH1	physical	20936779
TBX3_HUMAN	TBX3	physical	20936779
BHE40_HUMAN	BHLHE40	physical	20936779
HERP1_HUMAN	HERPUD1	physical	20936779
TM1L1_HUMAN	TOM1L1	physical	20936779
RFOX2_HUMAN	RBFOX2	physical	20936779
N4BP2_HUMAN	N4BP2	physical	20936779
CHD6_HUMAN	CHD6	physical	20936779
TM1L2_HUMAN	TOM1L2	physical	20936779
ITCH_HUMAN	ITCH	physical	21903422
ABCB6_HUMAN	ABCB6	physical	21903422
AN13A_HUMAN	ANKRD13A	physical	21903422
BIRC2_HUMAN	BIRC2	physical	21903422
CSTF1_HUMAN	CSTF1	physical	21903422
DBLOH_HUMAN	DIABLO	physical	21903422
DZIP3_HUMAN	DZIP3	physical	21903422
TCAF1_HUMAN	FAM115A	physical	21903422
IRAK1_HUMAN	IRAK1	physical	21903422
IRAK2_HUMAN	IRAK2	physical	21903422
MAGD1_HUMAN	MAGED1	physical	21903422
NED4L_HUMAN	NEDD4L	physical	21903422
NT5D2_HUMAN	NT5DC2	physical	21903422
PEG10_HUMAN	PEG10	physical	21903422
RNF12_HUMAN	RLIM	physical	21903422
TM1L1_HUMAN	TOM1L1	physical	21903422
WRIP1_HUMAN	WRNIP1	physical	21903422
XIAP_HUMAN	XIAP	physical	21903422
RCAN1_HUMAN	RCAN1	physical	19716405
IRAK1_HUMAN	IRAK1	physical	19716405
TRAF6_HUMAN	TRAF6	physical	19716405
TOLIP_HUMAN	TOLLIP	physical	15388348
IRAK1_HUMAN	IRAK1	physical	15388348
RAC1_HUMAN	RAC1	physical	21291504
TOM1_HUMAN	TOM1	physical	15047686
IRAK1_HUMAN	IRAK1	physical	16107720
CAV1_HUMAN	CAV1	physical	16107720
IRAK1_HUMAN	IRAK1	physical	16024789
SMAD7_HUMAN	SMAD7	physical	23027871
TGFR1_HUMAN	TGFBR1	physical	23027871
TRIP6_HUMAN	TRIP6	physical	22939629
IRAK1_HUMAN	IRAK1	physical	23244239
PINK1_HUMAN	PINK1	physical	23244239
RHXF2_HUMAN	RHOXF2	physical	19447967
DAZP2_HUMAN	DAZAP2	physical	19060904
UBC_HUMAN	UBC	physical	23880770
TM1L1_HUMAN	TOM1L1	physical	21988832
ACPH_HUMAN	APEH	physical	22863883
NMI_HUMAN	NMI	physical	22863883
OXR1_HUMAN	OXR1	physical	22863883
VPS35_HUMAN	VPS35	physical	22863883
UBC_HUMAN	UBC	physical	25042851
ATG8_YEAST	ATG8	physical	25042851
SQSTM_HUMAN	SQSTM1	physical	25042851
NBR1_HUMAN	NBR1	physical	25042851
NTAQ1_HUMAN	WDYHV1	physical	25416956
PR20E_HUMAN	PRR20A	physical	25416956
PR20C_HUMAN	PRR20A	physical	25416956
PR20D_HUMAN	PRR20A	physical	25416956
PR20B_HUMAN	PRR20A	physical	25416956
PR20A_HUMAN	PRR20A	physical	25416956
ODAM_HUMAN	ODAM	physical	21516116
TOM1_HUMAN	TOM1	physical	26320582
ILRL2_HUMAN	IL1RL2	physical	26269592
IRAK1_HUMAN	IRAK1	physical	26673132
TM1L1_HUMAN	TOM1L1	physical	26899482
RNF26_HUMAN	RNF26	physical	27368102

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 TOLIP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND MASSSPECTROMETRY.	19534553 [Abstract]