dbPTM

SIAS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIAS_HUMAN
UniProt AC	Q9NR45
Protein Name	Sialic acid synthase
Gene Name	NANS
Organism	Homo sapiens (Human).
Sequence Length	359
Subcellular Localization
Protein Description	Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively..
Protein Sequence	MPLELELCPGRWVGGQHPCFIIAEIGQNHQGDLDVAKRMIRMAKECGADCAKFQKSELEFKFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYRELQRYAEEVGIFFTASGMDEMAVEFLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSGMQSMDTMKQVYQIVKPLNPNFCFLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHETGIAISVAAVALGAKVLERHITLDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTKQLLPCEMACNEKLGKSVVAKVKIPEGTILTMDMLTVKVGEPKGYPPEDIFNLVGKKVLVTVEEDDTIMEELVDNHGKKIKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Glutathionylation	MPLELELCPGRWVGG CCCEEEECCCCCCCC	2.16	22555962
29	Ubiquitination	IAEIGQNHQGDLDVA EEEECCCCCCCHHHH	25.72	22817900
32	Ubiquitination	IGQNHQGDLDVAKRM ECCCCCCCHHHHHHH	32.88	22817900
33	Ubiquitination	GQNHQGDLDVAKRMI CCCCCCCHHHHHHHH	7.94	22817900
52	Ubiquitination	ECGADCAKFQKSELE HHCCCHHHHCHHHHH	55.44	27667366
52	Acetylation	ECGADCAKFQKSELE HHCCCHHHHCHHHHH	55.44	25953088
52	2-Hydroxyisobutyrylation	ECGADCAKFQKSELE HHCCCHHHHCHHHHH	55.44	-
55	Ubiquitination	ADCAKFQKSELEFKF CCHHHHCHHHHHHHC	49.37	21906983
55	Acetylation	ADCAKFQKSELEFKF CCHHHHCHHHHHHHC	49.37	27178108
55	2-Hydroxyisobutyrylation	ADCAKFQKSELEFKF CCHHHHCHHHHHHHC	49.37	-
56	Phosphorylation	DCAKFQKSELEFKFN CHHHHCHHHHHHHCC	36.31	29396449
61	Ubiquitination	QKSELEFKFNRKALE CHHHHHHHCCHHHHC	32.14	29967540
61	2-Hydroxyisobutyrylation	QKSELEFKFNRKALE CHHHHHHHCCHHHHC	32.14	-
61	Acetylation	QKSELEFKFNRKALE CHHHHHHHCCHHHHC	32.14	26822725
65	Ubiquitination	LEFKFNRKALERPYT HHHHCCHHHHCCCCC	59.43	29967540
71	Nitration	RKALERPYTSKHSWG HHHHCCCCCCCCCCC	29.84	-
71	Phosphorylation	RKALERPYTSKHSWG HHHHCCCCCCCCCCC	29.84	28152594
72	Phosphorylation	KALERPYTSKHSWGK HHHCCCCCCCCCCCC	33.70	28152594
73	Phosphorylation	ALERPYTSKHSWGKT HHCCCCCCCCCCCCC	23.64	28152594
74	Acetylation	LERPYTSKHSWGKTY HCCCCCCCCCCCCCC	33.58	26822725
74	Ubiquitination	LERPYTSKHSWGKTY HCCCCCCCCCCCCCC	33.58	29967540
76	Phosphorylation	RPYTSKHSWGKTYGE CCCCCCCCCCCCCCH	41.06	24719451
79	Acetylation	TSKHSWGKTYGEHKR CCCCCCCCCCCHHHH	32.11	19608861
79	Ubiquitination	TSKHSWGKTYGEHKR CCCCCCCCCCCHHHH	32.11	19608861
81	Phosphorylation	KHSWGKTYGEHKRHL CCCCCCCCCHHHHHH	24.81	-
85	Acetylation	GKTYGEHKRHLEFSH CCCCCHHHHHHCCCH	36.89	7692265
102	Ubiquitination	YRELQRYAEEVGIFF HHHHHHHHHHHCCEE	14.52	22817900
105	Ubiquitination	LQRYAEEVGIFFTAS HHHHHHHHCCEEECC	5.54	22817900
118	Ubiquitination	ASGMDEMAVEFLHEL CCCCCHHHHHHHHHC	8.81	22817900
121	Ubiquitination	MDEMAVEFLHELNVP CCHHHHHHHHHCCCC	7.29	22817900
127	Ubiquitination	EFLHELNVPFFKVGS HHHHHCCCCEEECCC	7.36	22817900
130	Ubiquitination	HELNVPFFKVGSGDT HHCCCCEEECCCCCC	5.26	22817900
134	Phosphorylation	VPFFKVGSGDTNNFP CCEEECCCCCCCCCC	36.16	25850435
137	Phosphorylation	FKVGSGDTNNFPYLE EECCCCCCCCCCHHH	35.27	25850435
142	Phosphorylation	GDTNNFPYLEKTAKK CCCCCCCHHHHHCCC	24.29	20090780
145	Ubiquitination	NNFPYLEKTAKKGRP CCCCHHHHHCCCCCC	51.71	21906983
148	Ubiquitination	PYLEKTAKKGRPMVI CHHHHHCCCCCCEEE	62.08	22817900
149	Ubiquitination	YLEKTAKKGRPMVIS HHHHHCCCCCCEEEC	58.66	22817900
153	Sulfoxidation	TAKKGRPMVISSGMQ HCCCCCCEEECCCCC	3.94	30846556
157	Phosphorylation	GRPMVISSGMQSMDT CCCEEECCCCCCHHH	27.45	25599653
159	Sulfoxidation	PMVISSGMQSMDTMK CEEECCCCCCHHHHH	2.62	30846556
161	Phosphorylation	VISSGMQSMDTMKQV EECCCCCCHHHHHHH	15.10	25599653
162	Sulfoxidation	ISSGMQSMDTMKQVY ECCCCCCHHHHHHHH	2.53	30846556
164	Phosphorylation	SGMQSMDTMKQVYQI CCCCCHHHHHHHHHH	20.02	25599653
165	Sulfoxidation	GMQSMDTMKQVYQIV CCCCHHHHHHHHHHH	2.20	30846556
169	Phosphorylation	MDTMKQVYQIVKPLN HHHHHHHHHHHCCCC	7.05	22817900
188	Phosphorylation	FLQCTSAYPLQPEDV EEEECCCCCCCHHHC	12.30	20090780
240	Phosphorylation	KVLERHITLDKTWKG HHHHHEEECCCCCCC	23.84	23312004
243	Ubiquitination	ERHITLDKTWKGSDH HHEEECCCCCCCCCC	60.44	22817900
243	2-Hydroxyisobutyrylation	ERHITLDKTWKGSDH HHEEECCCCCCCCCC	60.44	-
244	Phosphorylation	RHITLDKTWKGSDHS HEEECCCCCCCCCCC	31.88	26657352
246	Acetylation	ITLDKTWKGSDHSAS EECCCCCCCCCCCCC	54.49	27452117
246	Ubiquitination	ITLDKTWKGSDHSAS EECCCCCCCCCCCCC	54.49	22817900
246	Malonylation	ITLDKTWKGSDHSAS EECCCCCCCCCCCCC	54.49	26320211
248	Phosphorylation	LDKTWKGSDHSASLE CCCCCCCCCCCCCCC	28.55	26657352
251	Phosphorylation	TWKGSDHSASLEPGE CCCCCCCCCCCCHHH	25.25	25850435
253	Phosphorylation	KGSDHSASLEPGELA CCCCCCCCCCHHHHH	35.96	25850435
275	Phosphorylation	LVERALGSPTKQLLP HHHHHHCCCCHHHCC	30.19	23401153
277	Phosphorylation	ERALGSPTKQLLPCE HHHHCCCCHHHCCHH	32.87	30266825
278	Ubiquitination	RALGSPTKQLLPCEM HHHCCCCHHHCCHHH	42.19	29967540
285	Sulfoxidation	KQLLPCEMACNEKLG HHHCCHHHHHCCCCC	7.02	21406390
290	Ubiquitination	CEMACNEKLGKSVVA HHHHHCCCCCCCCEE	48.85	32015554
290	Acetylation	CEMACNEKLGKSVVA HHHHHCCCCCCCCEE	48.85	23954790
293	Ubiquitination	ACNEKLGKSVVAKVK HHCCCCCCCCEEEEE	50.98	29967540
294	Phosphorylation	CNEKLGKSVVAKVKI HCCCCCCCCEEEEEC	21.74	28857561
305	Phosphorylation	KVKIPEGTILTMDML EEECCCCCEEEEEEE	15.91	20068231
308	Phosphorylation	IPEGTILTMDMLTVK CCCCCEEEEEEEEEE	13.79	20068231
313	Phosphorylation	ILTMDMLTVKVGEPK EEEEEEEEEECCCCC	16.19	20068231
320	Ubiquitination	TVKVGEPKGYPPEDI EEECCCCCCCCHHHH	67.77	29967540
333	2-Hydroxyisobutyrylation	DIFNLVGKKVLVTVE HHHHHCCCEEEEEEC	32.03	-
333	Ubiquitination	DIFNLVGKKVLVTVE HHHHHCCCEEEEEEC	32.03	29967540
333	Acetylation	DIFNLVGKKVLVTVE HHHHHCCCEEEEEEC	32.03	26051181
338	Phosphorylation	VGKKVLVTVEEDDTI CCCEEEEEECCCCHH	20.31	30257219
344	Phosphorylation	VTVEEDDTIMEELVD EEECCCCHHHHHHHH	34.25	30257219
346	Sulfoxidation	VEEDDTIMEELVDNH ECCCCHHHHHHHHHC	3.39	30846556
355	Acetylation	ELVDNHGKKIKS--- HHHHHCCCCCCC---	43.72	25953088
355	Ubiquitination	ELVDNHGKKIKS--- HHHHHCCCCCCC---	43.72	32015554
356	Acetylation	LVDNHGKKIKS---- HHHHCCCCCCC----	61.02	7692275

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 SIAS_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF4E_HUMAN	EIF4E	physical	22863883
GBP2_HUMAN	GBP2	physical	22863883
AK1A1_HUMAN	AKR1A1	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
AATC_HUMAN	GOT1	physical	26344197
MPI_HUMAN	MPI	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
ANXA5_HUMAN	ANXA5	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435
HPRT_HUMAN	HPRT1	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	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.

Regulatory Network of SIAS_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND MASS SPECTROMETRY.	19608861 [Abstract]