dbPTM

ANKS6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANKS6_HUMAN
UniProt AC	Q68DC2
Protein Name	Ankyrin repeat and SAM domain-containing protein 6
Gene Name	ANKS6
Organism	Homo sapiens (Human).
Sequence Length	871
Subcellular Localization	Cell projection, cilium . Cytoplasm . Localizes to the proximal region of the primary cilium in the presence of INVS.
Protein Description	Required for renal function..
Protein Sequence	MGEGGLPPAFQLLLRACDQGDTETARRLLEPGAAEPAERGAEPEAGAEPAGAEVAGPGAAAAGAVGAPVPVDCSDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVDHHHPSGEQLGLGGSRDEPLDITALMAAIQHGHEAVVRLLMEWGADPNHAARTVGWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLVDYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPSHVNLVNGDGATPLMLAAVTGQLALVQLLVERHADVDKQDSVHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMQVNKDKGRPSHQPPLPHSKVRQPWSIPVLPDDKGGLKSWWNRMSNRFRKLKLMQTLPRGLSSNQPLPFSDEPEPALDSTMRAAPQDKTSRSALPDAAPVTKDNGPGSTRGEKEDTLLTTMLRNGAPLTRLPSDKLKAVIPPFLPPSSFELWSSDRSRTRHNGKADPMKTALPQRASRGHPVGGGGTDTTPVRPVKFPSLPRSPASSANSGNFNHSPHSSGGSSGVGVSRHGGELLNRSGGSIDNVLSQIAAQRKKAAGLLEQKPSHRSSPVGPAPGSSPSELPASPAGGSAPVGKKLETSKRPPSGTSTTSKSTSPTLTPSPSPKGHTAESSVSSSSSHRQSKSSGGSSSGTITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNAGKGRERQILQETIHNFHSSFESSASNTRAPGNSPCA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
138	Hydroxylation	LDHGADVNAQNRLGA HHCCCCCCHHHCCCC	36.03	-
247	Ubiquitination	VAQQLVEKGANPDHL HHHHHHHCCCCHHHH	56.71	-
247 (in isoform 4)	Ubiquitination	-	56.71	-
269	Ubiquitination	FEVALDCKHRDLVDY HHHHHHCCCCHHHHH	41.14	-
269 (in isoform 4)	Ubiquitination	-	41.14	-
276	Phosphorylation	KHRDLVDYLDPLTTV CCCHHHHHHCCCCCC	12.91	30457323
387	Phosphorylation	LNQGADVTLRAKNGY HHCCCCEEEEECCCC	15.86	24719451
391	Acetylation	ADVTLRAKNGYTAFD CCEEEEECCCCCCEE	44.46	26051181
423	Acetylation	SVCMQVNKDKGRPSH HHHHHHCCCCCCCCC	63.06	26051181
438	Ubiquitination	QPPLPHSKVRQPWSI CCCCCCCCCCCCCCC	38.10	-
537	Phosphorylation	EKEDTLLTTMLRNGA CCHHHHHHHHHHCCC	17.17	23403867
538	Phosphorylation	KEDTLLTTMLRNGAP CHHHHHHHHHHCCCC	17.74	22210691
551	Phosphorylation	APLTRLPSDKLKAVI CCCCCCCHHHHCHHC	52.55	2466023
596	Methylation	ALPQRASRGHPVGGG CCCCHHHCCCCCCCC	46.59	-
605	Phosphorylation	HPVGGGGTDTTPVRP CCCCCCCCCCCCCCC	33.19	28348404
607	Phosphorylation	VGGGGTDTTPVRPVK CCCCCCCCCCCCCCC	32.60	28555341
608	Phosphorylation	GGGGTDTTPVRPVKF CCCCCCCCCCCCCCC	23.69	25627689
617	Phosphorylation	VRPVKFPSLPRSPAS CCCCCCCCCCCCCCC	54.89	28348404
625	Phosphorylation	LPRSPASSANSGNFN CCCCCCCCCCCCCCC	33.31	28787133
628	Phosphorylation	SPASSANSGNFNHSP CCCCCCCCCCCCCCC	34.53	28787133
657	Phosphorylation	GGELLNRSGGSIDNV HHCHHCCCCCCHHHH	46.57	29255136
660	Phosphorylation	LLNRSGGSIDNVLSQ HHCCCCCCHHHHHHH	30.23	29255136
666	Phosphorylation	GSIDNVLSQIAAQRK CCHHHHHHHHHHHHH	18.43	25850435
688	Phosphorylation	QKPSHRSSPVGPAPG CCCCCCCCCCCCCCC	24.46	25627689
696	Phosphorylation	PVGPAPGSSPSELPA CCCCCCCCCCCCCCC	37.71	25627689
697	Phosphorylation	VGPAPGSSPSELPAS CCCCCCCCCCCCCCC	38.06	24719451
704	Phosphorylation	SPSELPASPAGGSAP CCCCCCCCCCCCCCC	17.22	25159151
714	Acetylation	GGSAPVGKKLETSKR CCCCCCCCCCCCCCC	55.19	26051181
724	Phosphorylation	ETSKRPPSGTSTTSK CCCCCCCCCCCCCCC	58.34	46164483
732	Phosphorylation	GTSTTSKSTSPTLTP CCCCCCCCCCCCCCC	33.61	23403867
733	Phosphorylation	TSTTSKSTSPTLTPS CCCCCCCCCCCCCCC	42.32	26657352
734	Phosphorylation	STTSKSTSPTLTPSP CCCCCCCCCCCCCCC	23.99	25159151
736	Phosphorylation	TSKSTSPTLTPSPSP CCCCCCCCCCCCCCC	42.93	19413330
738	Phosphorylation	KSTSPTLTPSPSPKG CCCCCCCCCCCCCCC	24.97	23403867
740	Phosphorylation	TSPTLTPSPSPKGHT CCCCCCCCCCCCCCC	32.54	23403867
742	Phosphorylation	PTLTPSPSPKGHTAE CCCCCCCCCCCCCCC	43.51	25159151
755	Phosphorylation	AESSVSSSSSHRQSK CCCCCCCCCCCCCCC	28.49	22210691
822	Phosphorylation	LGIKTDGSRQQILAA HCCCCCCCHHHHHHH	29.71	29802988
853	Phosphorylation	ETIHNFHSSFESSAS HHHHHHHHHHHCCCC	32.36	27251275
854	Phosphorylation	TIHNFHSSFESSASN HHHHHHHHHHCCCCC	25.18	27251275

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 ANKS6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
138	N	Hydroxylation		28165004
Hydroxylated at Asn-138, most probably by HIF1AN.

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 ANKS6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
NEK7_HUMAN	NEK7	physical	27173435
DDX1_HUMAN	DDX1	physical	27173435
TIM29_HUMAN	C19orf52	physical	27173435
TIM10_HUMAN	TIMM10	physical	27173435
TIM9_HUMAN	TIMM9	physical	27173435
NEK8_HUMAN	NEK8	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615382	Nephronophthisis 16 (NPHP16)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ANKS6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-736, AND MASSSPECTROMETRY.	19413330 [Abstract]

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