dbPTM

ALDOC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ALDOC_HUMAN
UniProt AC	P09972
Protein Name	Fructose-bisphosphate aldolase C
Gene Name	ALDOC
Organism	Homo sapiens (Human).
Sequence Length	364
Subcellular Localization
Protein Description
Protein Sequence	MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIANHAY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPHSYPALSAE ----CCCCCCCCCHH	27.26	24043423
5	Phosphorylation	---MPHSYPALSAEQ ---CCCCCCCCCHHH	6.89	24043423
13	Ubiquitination	PALSAEQKKELSDIA CCCCHHHHHHHCHHC	39.46	-
13	Acetylation	PALSAEQKKELSDIA CCCCHHHHHHHCHHC	39.46	30584453
17	Phosphorylation	AEQKKELSDIALRIV HHHHHHHCHHCHHHH	28.23	30631047
28	Ubiquitination	LRIVAPGKGILAADE HHHHCCCCCCEECCC	41.54	21906983
36	Phosphorylation	GILAADESVGSMAKR CCEECCCHHHHHHHH	32.12	25159151
39	Phosphorylation	AADESVGSMAKRLSQ ECCCHHHHHHHHHHH	17.26	25159151
42	Acetylation	ESVGSMAKRLSQIGV CHHHHHHHHHHHHCC	45.27	25953088
42	Ubiquitination	ESVGSMAKRLSQIGV CHHHHHHHHHHHHCC	45.27	-
42	Malonylation	ESVGSMAKRLSQIGV CHHHHHHHHHHHHCC	45.27	26320211
45	Phosphorylation	GSMAKRLSQIGVENT HHHHHHHHHHCCCCC	24.64	28674151
52	Phosphorylation	SQIGVENTEENRRLY HHHCCCCCHHHHHHH	31.04	23403867
108	Ubiquitination	KGIVVGIKVDKGVVP CCEEEEEEECCCCEE	38.15	-
111	Malonylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	26320211
111	Ubiquitination	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	19413330
111	Acetylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	19413330
115	Ubiquitination	KVDKGVVPLAGTDGE EECCCCEECCCCCCC	17.68	21890473
119	Phosphorylation	GVVPLAGTDGETTTQ CCEECCCCCCCCCCC	34.91	110740371
123	Phosphorylation	LAGTDGETTTQGLDG CCCCCCCCCCCCCCH	40.44	21712546
124	Phosphorylation	AGTDGETTTQGLDGL CCCCCCCCCCCCCHH	16.90	21712546
125	Phosphorylation	GTDGETTTQGLDGLS CCCCCCCCCCCCHHH	28.23	21712546
132	Phosphorylation	TQGLDGLSERCAQYK CCCCCHHHHHHHHHH	28.64	28985074
138	Phosphorylation	LSERCAQYKKDGADF HHHHHHHHHHCCCCH	11.07	-
139	Acetylation	SERCAQYKKDGADFA HHHHHHHHHCCCCHH	32.10	22361407
140	Ubiquitination	ERCAQYKKDGADFAK HHHHHHHHCCCCHHE	57.36	-
147	Acetylation	KDGADFAKWRCVLKI HCCCCHHEEEEEEEE	34.85	19608861
147	Ubiquitination	KDGADFAKWRCVLKI HCCCCHHEEEEEEEE	34.85	21890473
153	Acetylation	AKWRCVLKISERTPS HEEEEEEEECCCCHH	24.64	25953088
153	Ubiquitination	AKWRCVLKISERTPS HEEEEEEEECCCCHH	24.64	-
174	Phosphorylation	NANVLARYASICQQN CHHHHHHHHHHHHHC	10.09	28450419
176	Phosphorylation	NVLARYASICQQNGI HHHHHHHHHHHHCCC	18.24	81018241
178	S-palmitoylation	LARYASICQQNGIVP HHHHHHHHHHCCCCC	2.93	29575903
198	Ubiquitination	ILPDGDHDLKRCQYV CCCCCCCCHHHHHHH	59.64	21890473
200	Acetylation	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	156335
200	Ubiquitination	PDGDHDLKRCQYVTE CCCCCCHHHHHHHHH	58.13	21906983
204	Phosphorylation	HDLKRCQYVTEKVLA CCHHHHHHHHHHHHH	16.99	21082442
206	Phosphorylation	LKRCQYVTEKVLAAV HHHHHHHHHHHHHHH	25.75	28152594
208	Ubiquitination	RCQYVTEKVLAAVYK HHHHHHHHHHHHHHH	32.93	21890473
208	Acetylation	RCQYVTEKVLAAVYK HHHHHHHHHHHHHHH	32.93	30584447
214	Phosphorylation	EKVLAAVYKALSDHH HHHHHHHHHHHCCCC	5.94	7998259
215	Methylation	KVLAAVYKALSDHHV HHHHHHHHHHCCCCE	35.93	-
218	Phosphorylation	AAVYKALSDHHVYLE HHHHHHHCCCCEEEE	39.49	46162185
223	Phosphorylation	ALSDHHVYLEGTLLK HHCCCCEEEECEEEC	8.48	20561515
227	Ubiquitination	HHVYLEGTLLKPNMV CCEEEECEEECCCCC	21.39	21890473
230	Ubiquitination	YLEGTLLKPNMVTPG EEECEEECCCCCCCC	37.14	-
230	Acetylation	YLEGTLLKPNMVTPG EEECEEECCCCCCCC	37.14	25953088
234	Ubiquitination	TLLKPNMVTPGHACP EEECCCCCCCCCCCC	8.10	21890473
235	Phosphorylation	LLKPNMVTPGHACPI EECCCCCCCCCCCCC	16.88	30631047
245	Phosphorylation	HACPIKYTPEEIAMA CCCCCCCCHHHHHHH	21.15	27251275
253	Phosphorylation	PEEIAMATVTALRRT HHHHHHHHHHHHHHC	12.81	27251275
255	Phosphorylation	EIAMATVTALRRTVP HHHHHHHHHHHHCCC	18.67	46162197
260	Phosphorylation	TVTALRRTVPPAVPG HHHHHHHCCCCCCCC	30.81	27251275
269	Phosphorylation	PPAVPGVTFLSGGQS CCCCCCEEEECCCCC	25.44	27251275
272	Phosphorylation	VPGVTFLSGGQSEEE CCCEEEECCCCCHHH	36.36	27251275
276	Phosphorylation	TFLSGGQSEEEASFN EEECCCCCHHHHCCC	50.69	24275569
281	Phosphorylation	GQSEEEASFNLNAIN CCCHHHHCCCCCCCC	20.25	113305393
287	Ubiquitination	ASFNLNAINRCPLPR HCCCCCCCCCCCCCC	3.04	21890473
295	Ubiquitination	NRCPLPRPWALTFSY CCCCCCCCEEEEEEH	20.82	21890473
301	Phosphorylation	RPWALTFSYGRALQA CCEEEEEEHHHHHHH	22.80	29507054
330	Ubiquitination	AATEEFIKRAEVNGL CCCHHHHHHHHHCCE	51.37	2190698
342	Ubiquitination	NGLAAQGKYEGSGED CCEECCCCCCCCCCC	28.22	-
356	Phosphorylation	DGGAAAQSLYIANHA CCCHHHHHEEECCCC	20.58	21945579
358	Phosphorylation	GAAAQSLYIANHAY- CHHHHHEEECCCCC-	11.84	21945579
364	Phosphorylation	LYIANHAY------- EEECCCCC-------	16.13	46162215
417	Ubiquitination	------------------------------------------------------------ ------------------------------------------------------------		21890473

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 ALDOC_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OLA1_HUMAN	OLA1	physical	22939629
MP2K3_HUMAN	MAP2K3	physical	21988832
ERG1_HUMAN	SQLE	physical	21988832
ALDOA_HUMAN	ALDOA	physical	22863883
GNL1_HUMAN	GNL1	physical	22863883
TXND5_HUMAN	TXNDC5	physical	22863883
LNX1_HUMAN	LNX1	physical	25416956
ALDOA_HUMAN	ALDOA	physical	26186194
ACTN4_HUMAN	ACTN4	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26344197
RHG17_HUMAN	ARHGAP17	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
BLMH_HUMAN	BLMH	physical	26344197
CDK2_HUMAN	CDK2	physical	26344197
KCRB_HUMAN	CKB	physical	26344197
KCRU_HUMAN	CKMT1B	physical	26344197
KCRS_HUMAN	CKMT2	physical	26344197
DUT_HUMAN	DUT	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
FUMH_HUMAN	FH	physical	26344197
FKBP7_HUMAN	FKBP7	physical	26344197
LGUL_HUMAN	GLO1	physical	26344197
HCFC1_HUMAN	HCFC1	physical	26344197
INO1_HUMAN	ISYNA1	physical	26344197
SYMM_HUMAN	MARS2	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
PGAM1_HUMAN	PGAM1	physical	26344197
PGAM2_HUMAN	PGAM2	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
PPCE_HUMAN	PREP	physical	26344197
RAE1L_HUMAN	RAE1	physical	26344197
SF01_HUMAN	SF1	physical	26344197
SMAD4_HUMAN	SMAD4	physical	26344197
SODM_HUMAN	SOD2	physical	26344197
STXB1_HUMAN	STXBP1	physical	26344197
UMPS_HUMAN	UMPS	physical	26344197
ALDOA_HUMAN	ALDOA	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
There are no disease associations of PTM sites.

Regulatory Network of ALDOC_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-147, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND MASS SPECTROMETRY.	16916647 [Abstract]