INTU_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INTU_HUMAN
• UniProt AC: Q9ULD6
• Protein Name: Protein inturned
• Gene Name: INTU
• Organism: Homo sapiens (Human).
• Sequence Length: 942
• Subcellular Localization: Cytoplasm . Cell surface . Cytoplasm, cytoskeleton, cilium basal body . Enriched at the apical surface in ciliated cells..
• Protein Description: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (By similarity). Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies. [PubMed: 27158779]
• Protein Sequence: MASVASCDSRPSSDELPGDPSSQEEDEDYDFEDRVSDSGSYSSASSDYDDLEPEWLDSVQKNGELFYLELSEDEEESLLPETPTVNHVRFSENEIIIEDDYKERKKYEPKLKQFTKILRRKRLLPKRCNKKNSNDNGPVSILKHQSNQKTGVIVQQRYKDVNVYVNPKKLTVIKAKEQLKLLEVLVGIIHQTKWSWRRTGKQGDGERLVVHGLLPGGSAMKSGQVLIGDVLVAVNDVDVTTENIERVLSCIPGPMQVKLTFENAYDVKRETSHPRQKKTQSNTSDLVKLLWGEEVEGIQQSGLNTPHIIMYLTLQLDSETSKEEQEILYHYPMSEASQKLKSVRGIFLTLCDMLENVTGTQVTSSSLLLNGKQIHVAYWKESDKLLLIGLPAEEVPLPRLRNMIENVIQTLKFMYGSLDSAFCQIENVPRLDHFFNLFFQRALQPAKLHSSASPSAQQYDASSAVLLDNLPGVRWLTLPLEIKMELDMALSDLEAADFAELSEDYYDMRRLYTILGSSLFYKGYLICSHLPKDDLIDIAVYCRHYCLLPLAAKQRIGQLIIWREVFPQHHLRPLADSSTEVFPEPEGRYFLLVVGLKHYMLCVLLEAGGCASKAIGSPGPDCVYVDQVKTTLHQLDGVDSRIDERLASSPVPCLSCADWFLTGSREKTDSLTTSPILSRLQGTSKVATSPTCRRTLFGDYSLKTRKPSPSCSSGGSDNGCEGGEDDGFSPHTTPDAVRKQRESQGSDGLEESGTLLKVTKKKSTLPNPFHLGNLKKDLPEKELEIYNTVKLTSGPENTLFHYVALETVQGIFITPTLEEVAQLSGSIHPQLIKNFHQCCLSIRAVFQQTLVEEKKKGLNSGDHSDSAKSVSSLNPVKEHGVLFECSPGNWTDQKKAPPVMAYWVVGRLFLHPKPQELYVCFHDSVTEIAIEIAFKLFFGLTL

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
38	Phosphorylation	FEDRVSDSGSYSSAS CCHHCCCCCCCCCCC	23.33	22468782
48	Phosphorylation	YSSASSDYDDLEPEW CCCCCCCCCCCCHHH	17.19	22468782
58	Phosphorylation	LEPEWLDSVQKNGEL CCHHHHHHHHHCCEE	25.03	22468782
101	Phosphorylation	EIIIEDDYKERKKYE CEEECCCHHHHHHCC	27.37	-
115	Phosphorylation	EPKLKQFTKILRRKR CHHHHHHHHHHHHHC	18.06	26074081
131	Acetylation	LPKRCNKKNSNDNGP CCHHCCCCCCCCCCC	52.17	7933755
133	Phosphorylation	KRCNKKNSNDNGPVS HHCCCCCCCCCCCCE	55.21	-
140	Phosphorylation	SNDNGPVSILKHQSN CCCCCCCEEEEECCC	25.90	24719451
268	Ubiquitination	FENAYDVKRETSHPR ECCCCCCCCCCCCCC	41.44	29967540
271	Phosphorylation	AYDVKRETSHPRQKK CCCCCCCCCCCCCCC	36.05	30243723
272	Phosphorylation	YDVKRETSHPRQKKT CCCCCCCCCCCCCCC	27.09	30243723
410	Phosphorylation	MIENVIQTLKFMYGS HHHHHHHHHHHHHHC	22.31	22210691
455	Phosphorylation	LHSSASPSAQQYDAS CCCCCCCCHHHCCCC	35.89	28555341
512	Phosphorylation	YYDMRRLYTILGSSL HHHHHHHHHHHHCCH	7.02	22817900
521	Phosphorylation	ILGSSLFYKGYLICS HHHCCHHHCCEEEEC	14.59	22817900
524	Phosphorylation	SSLFYKGYLICSHLP CCHHHCCEEEECCCC	6.69	-
541	Phosphorylation	DLIDIAVYCRHYCLL HHHHHHHHHHHHCHH	3.76	-
648	Phosphorylation	RIDERLASSPVPCLS HHHHHHHCCCCCCCH	39.50	24719451
649	Phosphorylation	IDERLASSPVPCLSC HHHHHHCCCCCCCHH	25.06	28348404
667	Ubiquitination	FLTGSREKTDSLTTS HHCCCHHHCCCCCCH	57.43	29967540
668	Phosphorylation	LTGSREKTDSLTTSP HCCCHHHCCCCCCHH	26.52	23186163
670	Phosphorylation	GSREKTDSLTTSPIL CCHHHCCCCCCHHHH	32.61	22199227
672	Phosphorylation	REKTDSLTTSPILSR HHHCCCCCCHHHHHH	29.22	25850435
673	Phosphorylation	EKTDSLTTSPILSRL HHCCCCCCHHHHHHH	37.49	22199227
674	Phosphorylation	KTDSLTTSPILSRLQ HCCCCCCHHHHHHHC	12.52	19664994
678	Phosphorylation	LTTSPILSRLQGTSK CCCHHHHHHHCCCCC	31.50	22199227
684	O-linked_Glycosylation	LSRLQGTSKVATSPT HHHHCCCCCCCCCCC	31.77	30379171
685	Ubiquitination	SRLQGTSKVATSPTC HHHCCCCCCCCCCCH	35.41	29967540
688	Phosphorylation	QGTSKVATSPTCRRT CCCCCCCCCCCHHHH	37.92	23312004
689	Phosphorylation	GTSKVATSPTCRRTL CCCCCCCCCCHHHHH	14.42	23312004
689	O-linked_Glycosylation	GTSKVATSPTCRRTL CCCCCCCCCCHHHHH	14.42	30379171
691	Phosphorylation	SKVATSPTCRRTLFG CCCCCCCCHHHHHHC	20.57	23312004
701	Phosphorylation	RTLFGDYSLKTRKPS HHHHCCCCCCCCCCC	28.29	24719451
757	Ubiquitination	EESGTLLKVTKKKST HHCCCEEEEEECCCC	51.47	29967540
781	Ubiquitination	LKKDLPEKELEIYNT CCCCCCHHHEEEEEE	66.70	29967540
786	Phosphorylation	PEKELEIYNTVKLTS CHHHEEEEEEEECCC	8.73	27642862
788	Phosphorylation	KELEIYNTVKLTSGP HHEEEEEEEECCCCC	11.31	29978859
869	Phosphorylation	DHSDSAKSVSSLNPV CCCCCCCCHHHCCCC	27.27	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of INTU_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INTU_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 INTU_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUZ12_HUMAN	SUZ12	physical	28514442
APBP2_HUMAN	APPBP2	physical	28514442
EED_HUMAN	EED	physical	28514442
EME1_HUMAN	EME1	physical	28514442
RPTOR_HUMAN	RPTOR	physical	28514442
FNTB_HUMAN	FNTB	physical	28514442
AP2M1_HUMAN	AP2M1	physical	28514442
CND3_HUMAN	NCAPG	physical	28514442
TOP2A_HUMAN	TOP2A	physical	28514442
UBB_HUMAN	UBB	physical	28514442
MCRS1_HUMAN	MCRS1	physical	28514442
TPPC4_HUMAN	TRAPPC4	physical	28514442
TF3C1_HUMAN	GTF3C1	physical	28514442
SBDS_HUMAN	SBDS	physical	28514442
RIC8B_HUMAN	RIC8B	physical	28514442
FBW1A_HUMAN	BTRC	physical	28514442
ASPM_HUMAN	ASPM	physical	28514442
EHD3_HUMAN	EHD3	physical	27173435
VPS4A_HUMAN	VPS4A	physical	27173435
SMC4_HUMAN	SMC4	physical	27173435
AFG32_HUMAN	AFG3L2	physical	27173435
PSMD7_HUMAN	PSMD7	physical	27173435
PSMD8_HUMAN	PSMD8	physical	27173435
AAR2_HUMAN	AAR2	physical	27173435
DOCK5_HUMAN	DOCK5	physical	27173435
MCE1_HUMAN	RNGTT	physical	27173435
MAGD2_HUMAN	MAGED2	physical	27173435
YMEL1_HUMAN	YME1L1	physical	27173435
CN37_HUMAN	CNP	physical	27173435
FUZZY_HUMAN	FUZ	physical	27173435
KIFA3_HUMAN	KIFAP3	physical	27173435
KIF3A_HUMAN	KIF3A	physical	27173435

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.