ANKS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANKS3_HUMAN
• UniProt AC: Q6ZW76
• Protein Name: Ankyrin repeat and SAM domain-containing protein 3
• Gene Name: ANKS3
• Organism: Homo sapiens (Human).
• Sequence Length: 656
• Protein Sequence: MSELSDEASEPELLNRSLSMWHGLGTQVSGEELDVPLDLHTAASIGQYEVVKECVQRRELDLNKKNGGGWTPLMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIQGWTALFHCTSAGHQHMVRFLLDSGANANVREPICGFTPLMEAAAAGHEIIVQYFLNHGVKVDARDHSGATARMLAKQYGHMKIVALMDTYSPSLPKSLYRSPEKYEDLSSSDESCPAPQRQRPCRKKGVSIHEGPRALARITGIGLGGRAPRPRYEQAPPRGYVTFNSSGENPLEEEGLCCRDVTSPINERDVESSSSSSSREEHAFCANLGPVQSSSSSEGLARAQGLSSEASVESNEDSDHACKSSARKQAKSYMKTKNPDSQWPPRAATDREGFLAESSPQTQRAPYSGPQDLAALLEQIGCLKYLQVFEEQDVDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHSSARPPGDALELAYADRLEAEMQELAIQLHKRCEEVEATRGQVCQEQELRAVVESCLLEQDRAREDLQARLRETWALARDAALVLDQLRACQAELSSRVRQDQPPGAATLGLAVPPADSKGWQASLQAMSLPELSGALEDRVREMGQALCLVTQSLEKLQVLNGKKWRET

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
2	Phosphorylation	------MSELSDEAS ------CCCCCHHHC	47.44	25159151
5	Phosphorylation	---MSELSDEASEPE ---CCCCCHHHCCHH	29.38	25159151
9	Phosphorylation	SELSDEASEPELLNR CCCCHHHCCHHHHHH	52.19	25159151
96	Hydroxylation	LEAGVSVNVPTPEGQ HHCCCEEECCCCCCC	26.92	-
201	Phosphorylation	KVDARDHSGATARML CCCCCCCCHHHHHHH	34.12	-
212	Phosphorylation	ARMLAKQYGHMKIVA HHHHHHHHCCEEEEE	14.32	22817900
223	Phosphorylation	KIVALMDTYSPSLPK EEEEEHHCCCCCCCH	16.37	25850435
224	Phosphorylation	IVALMDTYSPSLPKS EEEEHHCCCCCCCHH	17.83	25850435
225	Phosphorylation	VALMDTYSPSLPKSL EEEHHCCCCCCCHHH	15.31	25159151
227	Phosphorylation	LMDTYSPSLPKSLYR EHHCCCCCCCHHHCC	51.90	25850435
233	Phosphorylation	PSLPKSLYRSPEKYE CCCCHHHCCCHHHHH	19.01	22817900
235	Phosphorylation	LPKSLYRSPEKYEDL CCHHHCCCHHHHHCC	24.69	63779713
239	Phosphorylation	LYRSPEKYEDLSSSD HCCCHHHHHCCCCCC	17.02	27732954
243	Phosphorylation	PEKYEDLSSSDESCP HHHHHCCCCCCCCCC	39.87	20363803
244	Phosphorylation	EKYEDLSSSDESCPA HHHHCCCCCCCCCCC	49.45	20363803
245	Phosphorylation	KYEDLSSSDESCPAP HHHCCCCCCCCCCCC	41.86	20363803
248	Phosphorylation	DLSSSDESCPAPQRQ CCCCCCCCCCCCCCC	30.32	27732954
264	Phosphorylation	PCRKKGVSIHEGPRA CCCCCCCCCCCCHHH	27.22	19531433
276	Phosphorylation	PRALARITGIGLGGR HHHHHHHHCCCCCCC	19.73	28555341
302	Phosphorylation	RGYVTFNSSGENPLE CCEEEECCCCCCCCC	35.21	23663014
303	Phosphorylation	GYVTFNSSGENPLEE CEEEECCCCCCCCCC	51.75	23663014
319	Phosphorylation	GLCCRDVTSPINERD CCEECCCCCCCCHHH	32.83	30266825
320	Phosphorylation	LCCRDVTSPINERDV CEECCCCCCCCHHHC	24.51	16964243
364	Phosphorylation	LARAQGLSSEASVES HHHHCCCCCHHHCCC	32.72	23663014
365	Phosphorylation	ARAQGLSSEASVESN HHHCCCCCHHHCCCC	42.07	23663014
368	Phosphorylation	QGLSSEASVESNEDS CCCCCHHHCCCCCCC	23.51	23663014
371	Phosphorylation	SSEASVESNEDSDHA CCHHHCCCCCCCCCH	43.28	23663014
375	Phosphorylation	SVESNEDSDHACKSS HCCCCCCCCCHHHHH	25.72	23663014
381	Phosphorylation	DSDHACKSSARKQAK CCCCHHHHHHHHHHH	29.16	28857561
382	Phosphorylation	SDHACKSSARKQAKS CCCHHHHHHHHHHHH	20.00	28857561
415	Phosphorylation	REGFLAESSPQTQRA CCCCCCCCCCCCCCC	41.53	23663014
416	Phosphorylation	EGFLAESSPQTQRAP CCCCCCCCCCCCCCC	16.72	25159151
419	Phosphorylation	LAESSPQTQRAPYSG CCCCCCCCCCCCCCC	24.33	23663014
541	Phosphorylation	ELRAVVESCLLEQDR HHHHHHHHHHHHCHH	9.84	50565653
651	Ubiquitination	KLQVLNGKKWRET-- HHHHHCCCCCCCC--	48.35	-

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

Oops, there are no upstream regulatory protein records of ANKS3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
5	S	Phosphorylation	Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and Ser-371 occur in a NEK7-dependent manner.	-
96	N	Hydroxylation	Hydroxylated at Asn-96, most probably by HIF1AN.	-
225	S	Phosphorylation	Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and Ser-371 occur in a NEK7-dependent manner.	-
319	T	Phosphorylation	Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and Ser-371 occur in a NEK7-dependent manner.	-
320	S	Phosphorylation	Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and Ser-371 occur in a NEK7-dependent manner.	-
368	S	Phosphorylation	Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and Ser-371 occur in a NEK7-dependent manner.	-
371	S	Phosphorylation	Phosphorylations at Ser-5, Ser-225, Thr-319, Ser-320, Ser-368 and Ser-371 occur in a NEK7-dependent manner.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ANKS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANKS6_HUMAN	ANKS6	physical	27173435
NEK7_HUMAN	NEK7	physical	27173435
NEK8_HUMAN	NEK8	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASSSPECTROMETRY.
PubMed: 16964243

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-5 AND SER-9, ANDMASS SPECTROMETRY.
PubMed: 17081983