dbPTM

NAGK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NAGK_HUMAN
UniProt AC	Q9UJ70
Protein Name	N-acetyl-D-glucosamine kinase
Gene Name	NAGK
Organism	Homo sapiens (Human).
Sequence Length	344
Subcellular Localization
Protein Description	Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity..
Protein Sequence	MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKAGVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGGVVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGYVKQAMFHYFQVPDRLGILTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQGREIQAQNFFSSFTLMKLRHSSALGGASLGARHIGHLLPMDYSANAIAFYSYTFS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAIYGGVE ------CCCEECCCC	11.54	22223895
5 (in isoform 2)	Phosphorylation	-	11.78	27251275
5	Phosphorylation	---MAAIYGGVEGGG ---CCCEECCCCCCC	11.78	25693802
7 (in isoform 2)	Phosphorylation	-	9.42	27251275
13	Phosphorylation	GGVEGGGTRSEVLLV CCCCCCCCCEEEEEE	34.01	25693802
15	Phosphorylation	VEGGGTRSEVLLVSE CCCCCCCEEEEEECC	31.71	25693802
40 (in isoform 2)	Phosphorylation	-	4.75	22210691
41 (in isoform 2)	Phosphorylation	-	26.20	22210691
44	Ubiquitination	HWLIGTDKCVERINE CEEECCHHHHHHHHH	39.76	-
44	Acetylation	HWLIGTDKCVERINE CEEECCHHHHHHHHH	39.76	25953088
51 (in isoform 2)	Phosphorylation	-	41.98	22210691
59	Ubiquitination	MVNRAKRKAGVDPLV HHHHHHHHCCCCCCC	49.11	-
70	Phosphorylation	DPLVPLRSLGLSLSG CCCCCHHHCCCCCCC	34.18	23927012
74	Phosphorylation	PLRSLGLSLSGGDQE CHHHCCCCCCCCCHH	20.77	29255136
76	Phosphorylation	RSLGLSLSGGDQEDA HHCCCCCCCCCHHHH	37.04	19664994
90	Ubiquitination	AGRILIEELRDRFPY HHHHHHHHHHHHCCC	41.95	-
105	Ubiquitination	LSESYLITTDAAGSI CCCCEEEEECCCCCC	18.94	-
106	Phosphorylation	SESYLITTDAAGSIA CCCEEEEECCCCCCE	19.35	-
116	Phosphorylation	AGSIATATPDGGVVL CCCCEEECCCCCEEE	19.98	-
120	Phosphorylation	ATATPDGGVVLISGT EEECCCCCEEEEECC	17.46	24719451
122	Phosphorylation	ATPDGGVVLISGTGS ECCCCCEEEEECCCC	4.43	19664994
205	Phosphorylation	LGILTHLYRDFDKCR HCHHHHHHHCHHHCC	10.67	14702039
219	Ubiquitination	RFAGFCRKIAEGAQQ CHHHHHHHHHHHHHC	47.66	-
219	Malonylation	RFAGFCRKIAEGAQQ CHHHHHHHHHHHHHC	47.66	26320211
237	Ubiquitination	LSRYIFRKAGEMLGR HHHHHHHHHHHHHHC	50.42	-
251	Phosphorylation	RHIVAVLPEIDPVLF CHHEEEECCCCHHHC	29.87	12112843
265	Ubiquitination	FQGKIGLPILCVGSV CCCCCCCCEEEEHHH	16.58	-
271	Phosphorylation	LPILCVGSVWKSWEL CCEEEEHHHHHHHHH	12.38	28348404
283	Ubiquitination	WELLKEGFLLALTQG HHHHHHCHHHHHHCC	5.46	-
317	Phosphorylation	SSALGGASLGARHIG CHHCCCCCCCHHHHH	30.52	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
76	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
76	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LNX1_HUMAN	LNX1	physical	16189514
NAGK_HUMAN	NAGK	physical	16189514
CD158_HUMAN	CCDC158	physical	16189514
PPHLN_HUMAN	PPHLN1	physical	21900206
SPRE1_HUMAN	SPRED1	physical	21900206
WDR82_HUMAN	WDR82	physical	21900206
FR1OP_HUMAN	FGFR1OP	physical	21900206
SYNE4_HUMAN	SYNE4	physical	21900206
KPYM_HUMAN	PKM	physical	21900206
DC1I1_HUMAN	DYNC1I1	physical	21900206
LENG1_HUMAN	LENG1	physical	21900206
SF3B3_HUMAN	SF3B3	physical	21900206
BCCIP_HUMAN	BCCIP	physical	22863883
CHRD1_HUMAN	CHORDC1	physical	22863883
DX39A_HUMAN	DDX39A	physical	22863883
CH60_HUMAN	HSPD1	physical	22863883
KYNU_HUMAN	KYNU	physical	22863883
LDH6B_HUMAN	LDHAL6B	physical	22863883
LDHA_HUMAN	LDHA	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
SMAP_HUMAN	C11orf58	physical	22863883
SPSY_HUMAN	SMS	physical	22863883
DHSO_HUMAN	SORD	physical	22863883
WDR1_HUMAN	WDR1	physical	22863883
NAGK_HUMAN	NAGK	physical	25416956
ARP10_HUMAN	ACTR10	physical	25416956
ZBT43_HUMAN	ZBTB43	physical	28514442
RAI1_HUMAN	RAI1	physical	28514442
HXB6_HUMAN	HOXB6	physical	28514442
RBM6_HUMAN	RBM6	physical	28514442
SCAF8_HUMAN	SCAF8	physical	28514442
ZIC2_HUMAN	ZIC2	physical	28514442
HNRH1_HUMAN	HNRNPH1	physical	28514442
XRN1_HUMAN	XRN1	physical	28514442
C2CD5_HUMAN	C2CD5	physical	28514442
SETD5_HUMAN	SETD5	physical	28514442
PATL1_HUMAN	PATL1	physical	28514442
PRC2B_HUMAN	PRRC2B	physical	28514442
PPIL2_HUMAN	PPIL2	physical	28514442
CNN2_HUMAN	CNN2	physical	28514442
SF01_HUMAN	SF1	physical	28514442
PIGA_HUMAN	PIGA	physical	28514442
HXB9_HUMAN	HOXB9	physical	28514442
TERF1_HUMAN	TERF1	physical	28514442
ARI1B_HUMAN	ARID1B	physical	28514442
MCM5_HUMAN	MCM5	physical	28514442
ERC6L_HUMAN	ERCC6L	physical	28514442
MCM3_HUMAN	MCM3	physical	28514442
YLPM1_HUMAN	YLPM1	physical	28514442
BCR_HUMAN	BCR	physical	28514442
PPIL4_HUMAN	PPIL4	physical	28514442

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
DB00141	N-Acetyl-D-glucosamine

Regulatory Network of NAGK_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-76, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Identification of the phosphotyrosine proteome from thrombinactivated platelets."; Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,Fitzgerald D.J.; Proteomics 2:642-648(2002). Cited for: PHOSPHORYLATION AT TYR-205.	12112843 [Abstract]