dbPTM

ALF_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ALF_YEAST
UniProt AC	P14540
Protein Name	Fructose-bisphosphate aldolase
Gene Name	FBA1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	359
Subcellular Localization
Protein Description	Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis..
Protein Sequence	MGVEQILKRKTGVIVGEDVHNLFTYAKEHKFAIPAINVTSSSTAVAALEAARDSKSPIILQTSNGGAAYFAGKGISNEGQNASIKGAIAAAHYIRSIAPAYGIPVVLHSDHCAKKLLPWFDGMLEADEAYFKEHGEPLFSSHMLDLSEETDEENISTCVKYFKRMAAMDQWLEMEIGITGGEEDGVNNENADKEDLYTKPEQVYNVYKALHPISPNFSIAAAFGNCHGLYAGDIALRPEILAEHQKYTREQVGCKEEKPLFLVFHGGSGSTVQEFHTGIDNGVVKVNLDTDCQYAYLTGIRDYVLNKKDYIMSPVGNPEGPEKPNKKFFDPRVWVREGEKTMGAKITKSLETFRTTNTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	2-Hydroxyisobutyrylation	MGVEQILKRKTGVIV CCHHHHHHHCCCEEE	54.18	-
8	Succinylation	MGVEQILKRKTGVIV CCHHHHHHHCCCEEE	54.18	23954790
10	2-Hydroxyisobutyrylation	VEQILKRKTGVIVGE HHHHHHHCCCEEECC	48.30	-
10	Ubiquitination	VEQILKRKTGVIVGE HHHHHHHCCCEEECC	48.30	17644757
11	Phosphorylation	EQILKRKTGVIVGED HHHHHHCCCEEECCC	40.49	22369663
24	Phosphorylation	EDVHNLFTYAKEHKF CCHHHHHHHHHHCCC	26.24	22369663
25	Phosphorylation	DVHNLFTYAKEHKFA CHHHHHHHHHHCCCE	14.35	22369663
27	2-Hydroxyisobutyrylation	HNLFTYAKEHKFAIP HHHHHHHHHCCCEEE	50.35	-
27	Acetylation	HNLFTYAKEHKFAIP HHHHHHHHHCCCEEE	50.35	24489116
27	Ubiquitination	HNLFTYAKEHKFAIP HHHHHHHHHCCCEEE	50.35	22817900
30	Acetylation	FTYAKEHKFAIPAIN HHHHHHCCCEEEEEE	37.27	24489116
30	Ubiquitination	FTYAKEHKFAIPAIN HHHHHHCCCEEEEEE	37.27	23749301
39	Phosphorylation	AIPAINVTSSSTAVA EEEEEEECCCHHHHH	20.57	25521595
40	Phosphorylation	IPAINVTSSSTAVAA EEEEEECCCHHHHHH	20.29	22369663
41	Phosphorylation	PAINVTSSSTAVAAL EEEEECCCHHHHHHH	23.49	25521595
42	Phosphorylation	AINVTSSSTAVAALE EEEECCCHHHHHHHH	21.83	25521595
43	Phosphorylation	INVTSSSTAVAALEA EEECCCHHHHHHHHH	27.40	22369663
54	Phosphorylation	ALEAARDSKSPIILQ HHHHHHHCCCCEEEE	29.49	22369663
55	Acetylation	LEAARDSKSPIILQT HHHHHHCCCCEEEEE	65.62	24489116
55	Succinylation	LEAARDSKSPIILQT HHHHHHCCCCEEEEE	65.62	23954790
55	Ubiquitination	LEAARDSKSPIILQT HHHHHHCCCCEEEEE	65.62	24961812
56	Phosphorylation	EAARDSKSPIILQTS HHHHHCCCCEEEEEC	25.86	22369663
62	Phosphorylation	KSPIILQTSNGGAAY CCCEEEEECCCCCEE	22.25	22369663
63	Phosphorylation	SPIILQTSNGGAAYF CCEEEEECCCCCEEE	22.10	22369663
69	Phosphorylation	TSNGGAAYFAGKGIS ECCCCCEEECCCCCC	8.07	29136822
73	2-Hydroxyisobutyrylation	GAAYFAGKGISNEGQ CCEEECCCCCCCCCC	50.03	-
73	Acetylation	GAAYFAGKGISNEGQ CCEEECCCCCCCCCC	50.03	24489116
73	Succinylation	GAAYFAGKGISNEGQ CCEEECCCCCCCCCC	50.03	23954790
73	Ubiquitination	GAAYFAGKGISNEGQ CCEEECCCCCCCCCC	50.03	23749301
76	Phosphorylation	YFAGKGISNEGQNAS EECCCCCCCCCCCCC	37.18	22369663
83	Phosphorylation	SNEGQNASIKGAIAA CCCCCCCCHHHHHHH	32.17	22369663
85	2-Hydroxyisobutyrylation	EGQNASIKGAIAAAH CCCCCCHHHHHHHHH	39.53	-
85	Acetylation	EGQNASIKGAIAAAH CCCCCCHHHHHHHHH	39.53	24489116
85	Succinylation	EGQNASIKGAIAAAH CCCCCCHHHHHHHHH	39.53	23954790
85	Ubiquitination	EGQNASIKGAIAAAH CCCCCCHHHHHHHHH	39.53	23749301
93	Phosphorylation	GAIAAAHYIRSIAPA HHHHHHHHHHHHHHH	8.03	21440633
96	Phosphorylation	AAAHYIRSIAPAYGI HHHHHHHHHHHHHCC	17.34	21440633
109	Phosphorylation	GIPVVLHSDHCAKKL CCCEEEECHHHHHHH	25.53	21440633
114	Acetylation	LHSDHCAKKLLPWFD EECHHHHHHHHHHHH	49.72	24489116
114	Succinylation	LHSDHCAKKLLPWFD EECHHHHHHHHHHHH	49.72	23954790
114	Ubiquitination	LHSDHCAKKLLPWFD EECHHHHHHHHHHHH	49.72	22817900
115	Acetylation	HSDHCAKKLLPWFDG ECHHHHHHHHHHHHH	36.41	25381059
115	Ubiquitination	HSDHCAKKLLPWFDG ECHHHHHHHHHHHHH	36.41	22817900
140	Phosphorylation	EHGEPLFSSHMLDLS HHCCCCCCHHCCCCC	27.32	22369663
141	Phosphorylation	HGEPLFSSHMLDLSE HCCCCCCHHCCCCCC	12.94	22369663
147	Phosphorylation	SSHMLDLSEETDEEN CHHCCCCCCCCCHHH	32.81	20377248
150	Phosphorylation	MLDLSEETDEENIST CCCCCCCCCHHHHHH	44.66	22369663
156	Phosphorylation	ETDEENISTCVKYFK CCCHHHHHHHHHHHH	27.60	22369663
157	Phosphorylation	TDEENISTCVKYFKR CCHHHHHHHHHHHHH	19.95	22369663
160	Acetylation	ENISTCVKYFKRMAA HHHHHHHHHHHHHHH	47.30	25381059
179	Phosphorylation	LEMEIGITGGEEDGV HHCHHCCCCCCCCCC	33.64	24909858
198	Phosphorylation	ADKEDLYTKPEQVYN CCHHHHCCCHHHHHH	47.63	28889911
199	Acetylation	DKEDLYTKPEQVYNV CHHHHCCCHHHHHHH	32.76	24489116
199	Ubiquitination	DKEDLYTKPEQVYNV CHHHHCCCHHHHHHH	32.76	24961812
214	Phosphorylation	YKALHPISPNFSIAA HHHHCCCCCCCEEHH	20.45	28889911
218	Phosphorylation	HPISPNFSIAAAFGN CCCCCCCEEHHHHCC	20.25	21440633
246	Ubiquitination	EILAEHQKYTREQVG HHHHHHHCCCHHHCC	50.96	23749301
248	Phosphorylation	LAEHQKYTREQVGCK HHHHHCCCHHHCCCC	34.46	28889911
255	Acetylation	TREQVGCKEEKPLFL CHHHCCCCCCCCEEE	64.08	24489116
255	Succinylation	TREQVGCKEEKPLFL CHHHCCCCCCCCEEE	64.08	23954790
255	Ubiquitination	TREQVGCKEEKPLFL CHHHCCCCCCCCEEE	64.08	23749301
258	Acetylation	QVGCKEEKPLFLVFH HCCCCCCCCEEEEEE	48.38	24489116
258	Ubiquitination	QVGCKEEKPLFLVFH HCCCCCCCCEEEEEE	48.38	24961812
268	Phosphorylation	FLVFHGGSGSTVQEF EEEEECCCCCCHHHH	33.88	22369663
270	Phosphorylation	VFHGGSGSTVQEFHT EEECCCCCCHHHHCC	27.40	20377248
271	Phosphorylation	FHGGSGSTVQEFHTG EECCCCCCHHHHCCC	29.72	20377248
277	Phosphorylation	STVQEFHTGIDNGVV CCHHHHCCCCCCCEE	40.95	22369663
290	Phosphorylation	VVKVNLDTDCQYAYL EEEEECCCCCCHHHH	41.67	22369663
294	Phosphorylation	NLDTDCQYAYLTGIR ECCCCCCHHHHHCCH	11.98	22369663
296	Phosphorylation	DTDCQYAYLTGIRDY CCCCCHHHHHCCHHH	10.40	22369663
298	Phosphorylation	DCQYAYLTGIRDYVL CCCHHHHHCCHHHHC	20.20	20377248
303	Phosphorylation	YLTGIRDYVLNKKDY HHHCCHHHHCCCCCC	9.29	21440633
307	2-Hydroxyisobutyrylation	IRDYVLNKKDYIMSP CHHHHCCCCCCCCCC	42.75	-
307	Acetylation	IRDYVLNKKDYIMSP CHHHHCCCCCCCCCC	42.75	24489116
307	Succinylation	IRDYVLNKKDYIMSP CHHHHCCCCCCCCCC	42.75	23954790
307	Ubiquitination	IRDYVLNKKDYIMSP CHHHHCCCCCCCCCC	42.75	23749301
308	2-Hydroxyisobutyrylation	RDYVLNKKDYIMSPV HHHHCCCCCCCCCCC	55.48	-
308	Acetylation	RDYVLNKKDYIMSPV HHHHCCCCCCCCCCC	55.48	22865919
308	Succinylation	RDYVLNKKDYIMSPV HHHHCCCCCCCCCCC	55.48	23954790
308	Ubiquitination	RDYVLNKKDYIMSPV HHHHCCCCCCCCCCC	55.48	24961812
310	Phosphorylation	YVLNKKDYIMSPVGN HHCCCCCCCCCCCCC	13.85	22369663
313	Phosphorylation	NKKDYIMSPVGNPEG CCCCCCCCCCCCCCC	13.58	22369663
323	Acetylation	GNPEGPEKPNKKFFD CCCCCCCCCCCCCCC	57.96	24489116
323	Succinylation	GNPEGPEKPNKKFFD CCCCCCCCCCCCCCC	57.96	23954790
323	Ubiquitination	GNPEGPEKPNKKFFD CCCCCCCCCCCCCCC	57.96	22817900
326	Acetylation	EGPEKPNKKFFDPRV CCCCCCCCCCCCCCE	60.53	24489116
326	Succinylation	EGPEKPNKKFFDPRV CCCCCCCCCCCCCCE	60.53	23954790
326	Ubiquitination	EGPEKPNKKFFDPRV CCCCCCCCCCCCCCE	60.53	23749301
327	Acetylation	GPEKPNKKFFDPRVW CCCCCCCCCCCCCEE	58.88	22865919
327	Ubiquitination	GPEKPNKKFFDPRVW CCCCCCCCCCCCCEE	58.88	22817900
340	2-Hydroxyisobutyrylation	VWVREGEKTMGAKIT EEEECCCEECCCCCC	55.45	-
340	Acetylation	VWVREGEKTMGAKIT EEEECCCEECCCCCC	55.45	24489116
340	Succinylation	VWVREGEKTMGAKIT EEEECCCEECCCCCC	55.45	23954790
340	Ubiquitination	VWVREGEKTMGAKIT EEEECCCEECCCCCC	55.45	22817900
345	2-Hydroxyisobutyrylation	GEKTMGAKITKSLET CCEECCCCCCCCHHH	45.22	-
345	Acetylation	GEKTMGAKITKSLET CCEECCCCCCCCHHH	45.22	24489116
345	Succinylation	GEKTMGAKITKSLET CCEECCCCCCCCHHH	45.22	23954790
345	Ubiquitination	GEKTMGAKITKSLET CCEECCCCCCCCHHH	45.22	23749301
348	2-Hydroxyisobutyrylation	TMGAKITKSLETFRT ECCCCCCCCHHHHHH	57.42	-
348	Acetylation	TMGAKITKSLETFRT ECCCCCCCCHHHHHH	57.42	24489116
348	Succinylation	TMGAKITKSLETFRT ECCCCCCCCHHHHHH	57.42	23954790
348	Ubiquitination	TMGAKITKSLETFRT ECCCCCCCCHHHHHH	57.42	23749301
349	Phosphorylation	MGAKITKSLETFRTT CCCCCCCCHHHHHHC	23.84	22369663
352	Phosphorylation	KITKSLETFRTTNTL CCCCCHHHHHHCCCC	24.58	22369663
355	Phosphorylation	KSLETFRTTNTL--- CCHHHHHHCCCC---	21.87	22369663
356	Phosphorylation	SLETFRTTNTL---- CHHHHHHCCCC----	23.19	22369663
358	Phosphorylation	ETFRTTNTL------ HHHHHCCCC------	31.58	22369663

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 ALF_YEAST !!

Functions of PTM Sites

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

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 ALF_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSB1_YEAST	SSB1	physical	19536198
GGPPS_YEAST	BTS1	genetic	21623372
COX6_YEAST	COX6	genetic	21623372
QCR1_YEAST	COR1	genetic	21623372
ELO3_YEAST	ELO3	genetic	21623372
ADH3_YEAST	ADH3	genetic	21623372
METC_YEAST	IRC7	genetic	21623372
ACOX_YEAST	POX1	genetic	21623372
CEM1_YEAST	CEM1	genetic	21623372
TPS1_YEAST	TPS1	genetic	21623372
PCKA_YEAST	PCK1	genetic	21623372
ADE_YEAST	AAH1	genetic	21623372
THRC_YEAST	THR4	genetic	21623372
DHOM_YEAST	HOM6	genetic	21623372
RBSK_YEAST	RBK1	genetic	21623372
ODPA_YEAST	PDA1	genetic	21623372
PPT2_YEAST	PPT2	genetic	21623372
CYC1_YEAST	CYC1	genetic	21623372
CYS3_YEAST	CYS3	genetic	21623372
RPC1_YEAST	RPO31	physical	24576411

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ALF_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-41; SER-42;THR-43; SER-54; SER-56; THR-62; SER-63; SER-76; SER-96; SER-147;THR-150; SER-156; THR-157; SER-214; SER-268; THR-290; TYR-294 ANDSER-313, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-313, AND MASSSPECTROMETRY.	17563356 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-24; SER-147;THR-179; SER-268; SER-270; THR-271 AND THR-277, AND MASS SPECTROMETRY.	17287358 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-150; TYR-310 ANDSER-313, AND MASS SPECTROMETRY.	17330950 [Abstract]