dbPTM

ACLY_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACLY_HUMAN
UniProt AC	P53396
Protein Name	ATP-citrate synthase
Gene Name	ACLY
Organism	Homo sapiens (Human).
Sequence Length	1101
Subcellular Localization	Cytoplasm.
Protein Description	ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine..
Protein Sequence	MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Ubiquitination	----MSAKAISEQTG ----CCCHHHHHHHC	56.39	-
4	2-Hydroxyisobutyrylation	----MSAKAISEQTG ----CCCHHHHHHHC	56.39	-
4	Acetylation	----MSAKAISEQTG ----CCCHHHHHHHC	56.39	25953088
4	Ubiquitination	----MSAKAISEQTG ----CCCHHHHHHHC	56.39	-
10	Phosphorylation	AKAISEQTGKELLYK CHHHHHHHCHHHHHH	46.28	23403867
12	Ubiquitination	AISEQTGKELLYKFI HHHHHHCHHHHHHHH	48.88	-
12	2-Hydroxyisobutyrylation	AISEQTGKELLYKFI HHHHHHCHHHHHHHH	48.88	-
12	Acetylation	AISEQTGKELLYKFI HHHHHHCHHHHHHHH	48.88	26822725
12	Succinylation	AISEQTGKELLYKFI HHHHHHCHHHHHHHH	48.88	23954790
12	Ubiquitination	AISEQTGKELLYKFI HHHHHHCHHHHHHHH	48.88	21890473
12 (in isoform 2)	Ubiquitination	-	48.88	-
17	Ubiquitination	TGKELLYKFICTTSA HCHHHHHHHHHCHHH	28.37	-
17	Acetylation	TGKELLYKFICTTSA HCHHHHHHHHHCHHH	28.37	25953088
17	Ubiquitination	TGKELLYKFICTTSA HCHHHHHHHHHCHHH	28.37	-
20	Glutathionylation	ELLYKFICTTSAIQN HHHHHHHHCHHHHHH	3.70	22555962
20	S-palmitoylation	ELLYKFICTTSAIQN HHHHHHHHCHHHHHH	3.70	29575903
23	Phosphorylation	YKFICTTSAIQNRFK HHHHHCHHHHHHHHC	12.76	21712546
38	Phosphorylation	YARVTPDTDWARLLQ CCEECCCCHHHHHHH	34.34	110746537
58	Ubiquitination	LSQNLVVKPDQLIKR HCCCEECCHHHHHHH	35.08	21890473
58	Acetylation	LSQNLVVKPDQLIKR HCCCEECCHHHHHHH	35.08	26051181
58	Ubiquitination	LSQNLVVKPDQLIKR HCCCEECCHHHHHHH	35.08	21906983
64	Ubiquitination	VKPDQLIKRRGKLGL CCHHHHHHHCCCCCE	44.64	21890473
64	Acetylation	VKPDQLIKRRGKLGL CCHHHHHHHCCCCCE	44.64	25953088
64	Ubiquitination	VKPDQLIKRRGKLGL CCHHHHHHHCCCCCE	44.64	21906983
68	Ubiquitination	QLIKRRGKLGLVGVN HHHHHCCCCCEEEEE	37.25	21890473
68	Acetylation	QLIKRRGKLGLVGVN HHHHHCCCCCEEEEE	37.25	25953088
68	Malonylation	QLIKRRGKLGLVGVN HHHHHCCCCCEEEEE	37.25	26320211
68	Ubiquitination	QLIKRRGKLGLVGVN HHHHHCCCCCEEEEE	37.25	21890473
68 (in isoform 2)	Ubiquitination	-	37.25	-
82	Ubiquitination	NLTLDGVKSWLKPRL EEEHHHHHHHHCCCC	41.25	-
82	Ubiquitination	NLTLDGVKSWLKPRL EEEHHHHHHHHCCCC	41.25	-
83	Phosphorylation	LTLDGVKSWLKPRLG EEHHHHHHHHCCCCC	34.92	9534799
86	Ubiquitination	DGVKSWLKPRLGQEA HHHHHHHCCCCCCCC	23.10	-
86	Acetylation	DGVKSWLKPRLGQEA HHHHHHHCCCCCCCC	23.10	19608861
86	Ubiquitination	DGVKSWLKPRLGQEA HHHHHHHCCCCCCCC	23.10	21906983
94	Phosphorylation	PRLGQEATVGKATGF CCCCCCCCCCHHHCH	29.10	20860994
97	2-Hydroxyisobutyrylation	GQEATVGKATGFLKN CCCCCCCHHHCHHHH	38.14	-
97	Acetylation	GQEATVGKATGFLKN CCCCCCCHHHCHHHH	38.14	25953088
97	Malonylation	GQEATVGKATGFLKN CCCCCCCHHHCHHHH	38.14	26320211
97	Ubiquitination	GQEATVGKATGFLKN CCCCCCCHHHCHHHH	38.14	21906983
97 (in isoform 2)	Ubiquitination	-	38.14	-
99	Phosphorylation	EATVGKATGFLKNFL CCCCCHHHCHHHHCC	31.77	20860994
108	Acetylation	FLKNFLIEPFVPHSQ HHHHCCCCCCCCHHH	34.53	-
108	Ubiquitination	FLKNFLIEPFVPHSQ HHHHCCCCCCCCHHH	34.53	-
112	Ubiquitination	FLIEPFVPHSQAEEF CCCCCCCCHHHCCEE	23.07	21890473
118	Ubiquitination	VPHSQAEEFYVCIYA CCHHHCCEEEEEEEE	45.34	21890473
122	Ubiquitination	QAEEFYVCIYATREG HCCEEEEEEEEECCC	1.03	21890473
131	Phosphorylation	YATREGDYVLFHHEG EEECCCCEEEEEECC	15.20	17360941
148	2-Hydroxyisobutyrylation	DVGDVDAKAQKLLVG CHHHCCHHHHHHHHC	47.06	-
148	Acetylation	DVGDVDAKAQKLLVG CHHHCCHHHHHHHHC	47.06	25953088
148	Ubiquitination	DVGDVDAKAQKLLVG CHHHCCHHHHHHHHC	47.06	21906983
151	2-Hydroxyisobutyrylation	DVDAKAQKLLVGVDE HCCHHHHHHHHCCCC	48.96	-
151	Acetylation	DVDAKAQKLLVGVDE HCCHHHHHHHHCCCC	48.96	23749302
151	Malonylation	DVDAKAQKLLVGVDE HCCHHHHHHHHCCCC	48.96	26320211
151	Ubiquitination	DVDAKAQKLLVGVDE HCCHHHHHHHHCCCC	48.96	21890473
159	Acetylation	LLVGVDEKLNPEDIK HHHCCCCCCCHHHHH	49.45	23749302
159	Ubiquitination	LLVGVDEKLNPEDIK HHHCCCCCCCHHHHH	49.45	-
166	2-Hydroxyisobutyrylation	KLNPEDIKKHLLVHA CCCHHHHHHHHEEEC	46.60	-
166	Ubiquitination	KLNPEDIKKHLLVHA CCCHHHHHHHHEEEC	46.60	-
167	2-Hydroxyisobutyrylation	LNPEDIKKHLLVHAP CCHHHHHHHHEEECC	39.56	-
167	Ubiquitination	LNPEDIKKHLLVHAP CCHHHHHHHHEEECC	39.56	-
177	2-Hydroxyisobutyrylation	LVHAPEDKKEILASF EEECCCCHHHHHHHH	51.12	-
207	Ubiquitination	LEINPLVVTKDGVYV EEECCEEEECCEEEE	7.89	-
210	Ubiquitination	NPLVVTKDGVYVLDL CCEEEECCEEEEEEE	42.28	21890473
213	Nitration	VVTKDGVYVLDLAAK EEECCEEEEEEECHH	10.79	-
213	Phosphorylation	VVTKDGVYVLDLAAK EEECCEEEEEEECHH	10.79	28152594
217	Ubiquitination	DGVYVLDLAAKVDAT CEEEEEEECHHCCCC	4.34	21890473
220	Ubiquitination	YVLDLAAKVDATADY EEEEECHHCCCCCCE	34.73	-
224	Phosphorylation	LAAKVDATADYICKV ECHHCCCCCCEEEEE	18.65	28152594
227	Ubiquitination	KVDATADYICKVKWG HCCCCCCEEEEEECC	13.02	21890473
227	Nitration	KVDATADYICKVKWG HCCCCCCEEEEEECC	13.02	-
227	Phosphorylation	KVDATADYICKVKWG HCCCCCCEEEEEECC	13.02	28152594
229	S-nitrosocysteine	DATADYICKVKWGDI CCCCCEEEEEECCCC	3.18	-
229	S-nitrosylation	DATADYICKVKWGDI CCCCCEEEEEECCCC	3.18	19483679
230	Acetylation	ATADYICKVKWGDIE CCCCEEEEEECCCCC	36.97	25953088
230	Malonylation	ATADYICKVKWGDIE CCCCEEEEEECCCCC	36.97	26320211
230	Ubiquitination	ATADYICKVKWGDIE CCCCEEEEEECCCCC	36.97	21890473
232	2-Hydroxyisobutyrylation	ADYICKVKWGDIEFP CCEEEEEECCCCCCC	30.84	-
232	Ubiquitination	ADYICKVKWGDIEFP CCEEEEEECCCCCCC	30.84	21906983
247	Phosphorylation	PPFGREAYPEEAYIA CCCCCCCCCCCEEEE	13.36	75099
252	Phosphorylation	EAYPEEAYIADLDAK CCCCCCEEEEECCCC	10.42	21406692
259	2-Hydroxyisobutyrylation	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	-
259	Acetylation	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	23954790
259	Ubiquitination	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	21906983
260	Phosphorylation	IADLDAKSGASLKLT EEECCCCCCCEEEEE	41.11	21406692
263	Phosphorylation	LDAKSGASLKLTLLN CCCCCCCEEEEEEEC	29.57	21406692
265	2-Hydroxyisobutyrylation	AKSGASLKLTLLNPK CCCCCEEEEEEECCC	36.61	-
265	Acetylation	AKSGASLKLTLLNPK CCCCCEEEEEEECCC	36.61	25953088
265	Ubiquitination	AKSGASLKLTLLNPK CCCCCEEEEEEECCC	36.61	21906983
267	Ubiquitination	SGASLKLTLLNPKGR CCCEEEEEEECCCCC	27.84	-
267	Phosphorylation	SGASLKLTLLNPKGR CCCEEEEEEECCCCC	27.84	21406692
269	Ubiquitination	ASLKLTLLNPKGRIW CEEEEEEECCCCCEE	9.69	-
272	2-Hydroxyisobutyrylation	KLTLLNPKGRIWTMV EEEEECCCCCEEEEE	60.80	-
272	Ubiquitination	KLTLLNPKGRIWTMV EEEEECCCCCEEEEE	60.80	21906983
275	Ubiquitination	LLNPKGRIWTMVAGG EECCCCCEEEEEECC	4.97	21890473
283	Acetylation	WTMVAGGGASVVYSD EEEEECCCCEEEECC	17.48	-
283	Ubiquitination	WTMVAGGGASVVYSD EEEEECCCCEEEECC	17.48	-
284	Ubiquitination	TMVAGGGASVVYSDT EEEECCCCEEEECCC	11.48	21890473
286	Ubiquitination	VAGGGASVVYSDTIC EECCCCEEEECCCCC	4.67	21890473
291	Ubiquitination	ASVVYSDTICDLGGV CEEEECCCCCCCCCH	19.98	-
317	Phosphorylation	APSEQQTYDYAKTIL CCCCHHHHHHHHHHH	11.56	142167
322	Phosphorylation	QTYDYAKTILSLMTR HHHHHHHHHHHHHHC	20.98	20068231
325	Phosphorylation	DYAKTILSLMTREKH HHHHHHHHHHHCCCC	16.55	20068231
327	Sulfoxidation	AKTILSLMTREKHPD HHHHHHHHHCCCCCC	2.74	21406390
328	Phosphorylation	KTILSLMTREKHPDG HHHHHHHHCCCCCCC	40.75	20068231
345	Ubiquitination	LIIGGSIANFTNVAA EEECCCCCCCCHHHH	13.54	-
359	Ubiquitination	ATFKGIVRAIRDYQG HHHHHHHHHHHHCCC	23.52	21890473
364	Ubiquitination	IVRAIRDYQGPLKEH HHHHHHHCCCCCCCC	12.91	-
364	Phosphorylation	IVRAIRDYQGPLKEH HHHHHHHCCCCCCCC	12.91	28152594
369	2-Hydroxyisobutyrylation	RDYQGPLKEHEVTIF HHCCCCCCCCEEEEE	61.22	-
369	Acetylation	RDYQGPLKEHEVTIF HHCCCCCCCCEEEEE	61.22	23749302
369	Malonylation	RDYQGPLKEHEVTIF HHCCCCCCCCEEEEE	61.22	26320211
369	Ubiquitination	RDYQGPLKEHEVTIF HHCCCCCCCCEEEEE	61.22	-
379	Ubiquitination	EVTIFVRRGGPNYQE EEEEEEECCCCCHHH	49.47	-
379	Methylation	EVTIFVRRGGPNYQE EEEEEEECCCCCHHH	49.47	-
384	Nitration	VRRGGPNYQEGLRVM EECCCCCHHHHCEEE	15.86	-
384	Phosphorylation	VRRGGPNYQEGLRVM EECCCCCHHHHCEEE	15.86	19702290
389	Methylation	PNYQEGLRVMGEVGK CCHHHHCEEEECCCC	27.51	-
391	Sulfoxidation	YQEGLRVMGEVGKTT HHHHCEEEECCCCCC	2.83	30846556
430	Phosphorylation	PIPNQPPTAAHTANF CCCCCCCCHHHHHCE	43.06	26074081
434	Phosphorylation	QPPTAAHTANFLLNA CCCCHHHHHCEEECC	20.69	26074081
442	Phosphorylation	ANFLLNASGSTSTPA HCEEECCCCCCCCCC	32.00	29255136
444	Phosphorylation	FLLNASGSTSTPAPS EEECCCCCCCCCCCC	19.38	29255136
445	Phosphorylation	LLNASGSTSTPAPSR EECCCCCCCCCCCCC	39.90	29255136
446	Phosphorylation	LNASGSTSTPAPSRT ECCCCCCCCCCCCCC	33.81	29255136
447	Phosphorylation	NASGSTSTPAPSRTA CCCCCCCCCCCCCCC	24.45	29255136
451	Phosphorylation	STSTPAPSRTASFSE CCCCCCCCCCCCCCH	44.35	29255136
453	Phosphorylation	STPAPSRTASFSESR CCCCCCCCCCCCHHC	30.87	20201521
455	Phosphorylation	PAPSRTASFSESRAD CCCCCCCCCCHHCHH	28.79	29255136
457	Phosphorylation	PSRTASFSESRADEV CCCCCCCCHHCHHHC	31.97	22167270
459	Phosphorylation	RTASFSESRADEVAP CCCCCCHHCHHHCCC	31.41	23927012
461	Ubiquitination	ASFSESRADEVAPAK CCCCHHCHHHCCCHH	26.96	-
468	Acetylation	ADEVAPAKKAKPAMP HHHCCCHHHCCCCCC	52.81	25953088
468	Ubiquitination	ADEVAPAKKAKPAMP HHHCCCHHHCCCCCC	52.81	21890473
469	Ubiquitination	DEVAPAKKAKPAMPQ HHCCCHHHCCCCCCC	64.84	-
471	Malonylation	VAPAKKAKPAMPQDS CCCHHHCCCCCCCCC	42.04	26320211
471	Ubiquitination	VAPAKKAKPAMPQDS CCCHHHCCCCCCCCC	42.04	-
474	Sulfoxidation	AKKAKPAMPQDSVPS HHHCCCCCCCCCCCC	4.09	21406390
478	Phosphorylation	KPAMPQDSVPSPRSL CCCCCCCCCCCCHHC	30.58	22167270
478 (in isoform 2)	Ubiquitination	-	30.58	-
481	Phosphorylation	MPQDSVPSPRSLQGK CCCCCCCCCHHCCCC	30.69	19664994
484	Phosphorylation	DSVPSPRSLQGKSTT CCCCCCHHCCCCCCC	28.55	23403867
488	Malonylation	SPRSLQGKSTTLFSR CCHHCCCCCCCCHHH	31.50	26320211
488	Ubiquitination	SPRSLQGKSTTLFSR CCHHCCCCCCCCHHH	31.50	21890473
488 (in isoform 2)	Ubiquitination	-	31.50	-
489	Phosphorylation	PRSLQGKSTTLFSRH CHHCCCCCCCCHHHH	33.19	23403867
490	Phosphorylation	RSLQGKSTTLFSRHT HHCCCCCCCCHHHHH	30.88	23403867
491	Phosphorylation	SLQGKSTTLFSRHTK HCCCCCCCCHHHHHH	32.66	23403867
498	Ubiquitination	TLFSRHTKAIVWGMQ CCHHHHHHHHHHHHH	29.95	21906983
504	Sulfoxidation	TKAIVWGMQTRAVQG HHHHHHHHHHHHHCC	1.84	30846556
509	Ubiquitination	WGMQTRAVQGMLDFD HHHHHHHHCCCCCCC	4.56	-
512	Sulfoxidation	QTRAVQGMLDFDYVC HHHHHCCCCCCCEEE	1.49	30846556
525	Ubiquitination	VCSRDEPSVAAMVYP EECCCCCCEEEEEEE	23.49	21890473
529	Sulfoxidation	DEPSVAAMVYPFTGD CCCCEEEEEEECCCC	1.82	30846556
531	Phosphorylation	PSVAAMVYPFTGDHK CCEEEEEEECCCCCC	4.59	119457
532	Ubiquitination	SVAAMVYPFTGDHKQ CEEEEEEECCCCCCC	14.65	21890473
536 (in isoform 2)	Ubiquitination	-	42.63	-
538	Acetylation	YPFTGDHKQKFYWGH EECCCCCCCCEEECC	60.98	23954790
538	Malonylation	YPFTGDHKQKFYWGH EECCCCCCCCEEECC	60.98	26320211
538	Ubiquitination	YPFTGDHKQKFYWGH EECCCCCCCCEEECC	60.98	21906983
540	Acetylation	FTGDHKQKFYWGHKE CCCCCCCCEEECCCH	45.27	23932781
540	Ubiquitination	FTGDHKQKFYWGHKE CCCCCCCCEEECCCH	45.27	23932781
546	2-Hydroxyisobutyrylation	QKFYWGHKEILIPVF CCEEECCCHHHHHHH	42.38	-
546	Acetylation	QKFYWGHKEILIPVF CCEEECCCHHHHHHH	42.38	19608861
546	Ubiquitination	QKFYWGHKEILIPVF CCEEECCCHHHHHHH	42.38	21906983
554	Acetylation	EILIPVFKNMADAMR HHHHHHHHHHHHHHH	46.15	19608861
554	Ubiquitination	EILIPVFKNMADAMR HHHHHHHHHHHHHHH	46.15	23932781
562	Ubiquitination	NMADAMRKHPEVDVL HHHHHHHHCCCHHEE	50.88	-
565	Ubiquitination	DAMRKHPEVDVLINF HHHHHCCCHHEEEEH	51.58	-
574	Phosphorylation	DVLINFASLRSAYDS HEEEEHHHHHHHHHH	21.85	46157797
581	Phosphorylation	SLRSAYDSTMETMNY HHHHHHHHHHHHCCH	19.58	63778937
582	Phosphorylation	LRSAYDSTMETMNYA HHHHHHHHHHHCCHH	19.01	110746553
583	Sulfoxidation	RSAYDSTMETMNYAQ HHHHHHHHHHCCHHH	4.71	30846556
586	Sulfoxidation	YDSTMETMNYAQIRT HHHHHHHCCHHHHHH	1.99	30846556
588	Phosphorylation	STMETMNYAQIRTIA HHHHHCCHHHHHHHH	6.78	51117
590	Ubiquitination	METMNYAQIRTIAII HHHCCHHHHHHHHHH	18.48	21890473
593	Phosphorylation	MNYAQIRTIAIIAEG CCHHHHHHHHHHHCC	19.18	63719025
606	Phosphorylation	EGIPEALTRKLIKKA CCCCHHHHHHHHHHH	32.57	20068231
616	2-Hydroxyisobutyrylation	LIKKADQKGVTIIGP HHHHHHHCCCEEECC	56.76	-
616	Acetylation	LIKKADQKGVTIIGP HHHHHHHCCCEEECC	56.76	26051181
616	Ubiquitination	LIKKADQKGVTIIGP HHHHHHHCCCEEECC	56.76	-
619	Phosphorylation	KADQKGVTIIGPATV HHHHCCCEEECCCCC	18.62	20068231
620 (in isoform 2)	Ubiquitination	-	2.97	-
625	Phosphorylation	VTIIGPATVGGIKPG CEEECCCCCCCCCCC	23.87	20068231
630	Acetylation	PATVGGIKPGCFKIG CCCCCCCCCCCEECC	38.34	26051181
630	Malonylation	PATVGGIKPGCFKIG CCCCCCCCCCCEECC	38.34	26320211
630	Ubiquitination	PATVGGIKPGCFKIG CCCCCCCCCCCEECC	38.34	21890473
633	S-palmitoylation	VGGIKPGCFKIGNTG CCCCCCCCEECCCCC	4.21	29575903
635	Acetylation	GIKPGCFKIGNTGGM CCCCCCEECCCCCCH	54.50	24232461
635	Ubiquitination	GIKPGCFKIGNTGGM CCCCCCEECCCCCCH	54.50	-
639	Phosphorylation	GCFKIGNTGGMLDNI CCEECCCCCCHHHHH	29.87	19060867
642	Sulfoxidation	KIGNTGGMLDNILAS ECCCCCCHHHHHHHH	4.49	21406390
647	Ubiquitination	GGMLDNILASKLYRP CCHHHHHHHHHCCCC	5.73	21890473
649	Phosphorylation	MLDNILASKLYRPGS HHHHHHHHHCCCCCC	21.54	21712546
650	Ubiquitination	LDNILASKLYRPGSV HHHHHHHHCCCCCCE	43.88	-
652	Phosphorylation	NILASKLYRPGSVAY HHHHHHCCCCCCEEE	20.64	20090780
656	Phosphorylation	SKLYRPGSVAYVSRS HHCCCCCCEEEEECC	13.27	28152594
659	Phosphorylation	YRPGSVAYVSRSGGM CCCCCEEEEECCCCC	9.23	110746561
661	Phosphorylation	PGSVAYVSRSGGMSN CCCEEEEECCCCCCH	14.19	22210691
663	Acetylation	SVAYVSRSGGMSNEL CEEEEECCCCCCHHH	31.99	19413330
663	Phosphorylation	SVAYVSRSGGMSNEL CEEEEECCCCCCHHH	31.99	21712546
666	Sulfoxidation	YVSRSGGMSNELNNI EEECCCCCCHHHHHH	4.42	21406390
667	Phosphorylation	VSRSGGMSNELNNII EECCCCCCHHHHHHH	30.35	21712546
673	Ubiquitination	MSNELNNIISRTTDG CCHHHHHHHHCCCCC	2.70	21890473
674	Ubiquitination	SNELNNIISRTTDGV CHHHHHHHHCCCCCE	2.18	21890473
675	Phosphorylation	NELNNIISRTTDGVY HHHHHHHHCCCCCEE	21.56	21712546
677	Ubiquitination	LNNIISRTTDGVYEG HHHHHHCCCCCEEEE	23.58	21890473
677	Phosphorylation	LNNIISRTTDGVYEG HHHHHHCCCCCEEEE	23.58	28152594
678	Phosphorylation	NNIISRTTDGVYEGV HHHHHCCCCCEEEEE	29.64	28152594
682	Phosphorylation	SRTTDGVYEGVAIGG HCCCCCEEEEEEECC	16.70	27273156
691	Ubiquitination	GVAIGGDRYPGSTFM EEEECCCCCCCCCHH	42.70	-
691	Methylation	GVAIGGDRYPGSTFM EEEECCCCCCCCCHH	42.70	-
692	Phosphorylation	VAIGGDRYPGSTFMD EEECCCCCCCCCHHH	19.38	28152594
693	Ubiquitination	AIGGDRYPGSTFMDH EECCCCCCCCCHHHH	31.02	-
695	Phosphorylation	GGDRYPGSTFMDHVL CCCCCCCCCHHHHHH	17.61	28152594
696	Phosphorylation	GDRYPGSTFMDHVLR CCCCCCCCHHHHHHH	28.97	28152594
697	Acetylation	DRYPGSTFMDHVLRY CCCCCCCHHHHHHHC	6.08	-
697	Ubiquitination	DRYPGSTFMDHVLRY CCCCCCCHHHHHHHC	6.08	-
698	Sulfoxidation	RYPGSTFMDHVLRYQ CCCCCCHHHHHHHCC	3.36	30846556
704	Phosphorylation	FMDHVLRYQDTPGVK HHHHHHHCCCCCCEE	13.43	28152594
707	Ubiquitination	HVLRYQDTPGVKMIV HHHHCCCCCCEEEEE	13.35	-
707	Phosphorylation	HVLRYQDTPGVKMIV HHHHCCCCCCEEEEE	13.35	20860994
720	Ubiquitination	IVVLGEIGGTEEYKI EEEEEECCCCCHHHH	32.44	21890473
732	Ubiquitination	YKICRGIKEGRLTKP HHHHCCCCCCCCCCC	57.87	21890473
760	Phosphorylation	SSEVQFGHAGACANQ CCCCCCCCHHHHCHH	23.44	-
780	2-Hydroxyisobutyrylation	VAKNQALKEAGVFVP HHHHHHHHHHCCCCC	48.83	-
780	Ubiquitination	VAKNQALKEAGVFVP HHHHHHHHHHCCCCC	48.83	21906983
806	Acetylation	SVYEDLVANGVIVPA HHHHHHHHCCEEEEC	17.85	-
806	Ubiquitination	SVYEDLVANGVIVPA HHHHHHHHCCEEEEC	17.85	21890473
809	Ubiquitination	EDLVANGVIVPAQEV HHHHHCCEEEECCCC	3.91	-
836	Malonylation	RELGLIRKPASFMTS HHHCCCCCCHHHHHH	37.63	26320211
836	Ubiquitination	RELGLIRKPASFMTS HHHCCCCCCHHHHHH	37.63	-
839	Phosphorylation	GLIRKPASFMTSICD CCCCCCHHHHHHHCC	24.87	28450419
842	Phosphorylation	RKPASFMTSICDERG CCCHHHHHHHCCHHH	16.96	28857561
843	Phosphorylation	KPASFMTSICDERGQ CCHHHHHHHCCHHHC	14.94	20068231
845	Glutathionylation	ASFMTSICDERGQEL HHHHHHHCCHHHCEE	4.44	22555962
854	Phosphorylation	ERGQELIYAGMPITE HHHCEEEECCCCHHH	15.10	21945579
857	Sulfoxidation	QELIYAGMPITEVFK CEEEECCCCHHHHHH	1.33	30846556
908 (in isoform 2)	Ubiquitination	-	35.18	-
918	Ubiquitination	IICARAGKDLVSSLT EEEECCCHHHHHHHH	47.07	21906983
922	Phosphorylation	RAGKDLVSSLTSGLL CCCHHHHHHHHHCCC	27.25	20860994
926	Phosphorylation	DLVSSLTSGLLTIGD HHHHHHHHCCCCCHH	32.51	20860994
930	Phosphorylation	SLTSGLLTIGDRFGG HHHHCCCCCHHHHHH	28.14	20860994
944	Acetylation	GALDAAAKMFSKAFD HHHHHHHHHHHHHHH	35.43	25953088
944	Ubiquitination	GALDAAAKMFSKAFD HHHHHHHHHHHHHHH	35.43	21906983
948	2-Hydroxyisobutyrylation	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	-
948	Acetylation	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	19608861
948	Ubiquitination	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	21906983
952	Phosphorylation	MFSKAFDSGIIPMEF HHHHHHHCCCCCHHH	25.99	9534871
957	Sulfoxidation	FDSGIIPMEFVNKMK HHCCCCCHHHHHHHH	4.38	21406390
962	Ubiquitination	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	21890473
962	Acetylation	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	23954790
962	Malonylation	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	32601280
962	Ubiquitination	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	-
964	Methylation	MEFVNKMKKEGKLIM HHHHHHHHHCCCEEE	49.64	-
964	Ubiquitination	MEFVNKMKKEGKLIM HHHHHHHHHCCCEEE	49.64	-
965	Methylation	EFVNKMKKEGKLIMG HHHHHHHHCCCEEEE	69.10	-
968	Acetylation	NKMKKEGKLIMGIGH HHHHHCCCEEEECCC	35.61	19608861
968	Malonylation	NKMKKEGKLIMGIGH HHHHHCCCEEEECCC	35.61	26320211
968	Ubiquitination	NKMKKEGKLIMGIGH HHHHHCCCEEEECCC	35.61	-
978	2-Hydroxyisobutyrylation	MGIGHRVKSINNPDM EECCCCHHHCCCCHH	45.64	-
978	Acetylation	MGIGHRVKSINNPDM EECCCCHHHCCCCHH	45.64	26051181
978	Malonylation	MGIGHRVKSINNPDM EECCCCHHHCCCCHH	45.64	26320211
978	Ubiquitination	MGIGHRVKSINNPDM EECCCCHHHCCCCHH	45.64	-
979	Phosphorylation	GIGHRVKSINNPDMR ECCCCHHHCCCCHHH	27.91	19060867
981 (in isoform 2)	Ubiquitination	-	62.16	-
986	Methylation	SINNPDMRVQILKDY HCCCCHHHHHHHHHH	25.27	-
988	Ubiquitination	NNPDMRVQILKDYVR CCCHHHHHHHHHHHH	25.57	21890473
991	2-Hydroxyisobutyrylation	DMRVQILKDYVRQHF HHHHHHHHHHHHHHC	48.95	-
991	Acetylation	DMRVQILKDYVRQHF HHHHHHHHHHHHHHC	48.95	25953088
991	Ubiquitination	DMRVQILKDYVRQHF HHHHHHHHHHHHHHC	48.95	21890473
992	Ubiquitination	MRVQILKDYVRQHFP HHHHHHHHHHHHHCC	43.65	21890473
993	Phosphorylation	RVQILKDYVRQHFPA HHHHHHHHHHHHCCC	8.92	29496907
1001	Phosphorylation	VRQHFPATPLLDYAL HHHHCCCCCHHHHHE	18.08	110746577
1006	Phosphorylation	PATPLLDYALEVEKI CCCCHHHHHEEEEEC	17.04	-
1012	Ubiquitination	DYALEVEKITTSKKP HHHEEEEECCCCCCC	50.99	-
1042	Phosphorylation	DMLRNCGSFTREEAD HHHHHCCCCCHHHHH	26.16	21406692
1044	Phosphorylation	LRNCGSFTREEADEY HHHCCCCCHHHHHHH	38.58	21406692
1067	Sulfoxidation	IFVLGRSMGFIGHYL EEEECCCHHHHHHHH	4.97	30846556
1067 (in isoform 2)	Ubiquitination	-	4.97	-
1073	Phosphorylation	SMGFIGHYLDQKRLK CHHHHHHHHCHHHHH	13.53	20090780
1077	2-Hydroxyisobutyrylation	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	-
1077	Acetylation	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	19608861
1077	Malonylation	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	26320211
1077	Ubiquitination	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	21890473
1080	2-Hydroxyisobutyrylation	YLDQKRLKQGLYRHP HHCHHHHHHCCCCCC	46.48	-
1080	Malonylation	YLDQKRLKQGLYRHP HHCHHHHHHCCCCCC	46.48	26320211
1080	Ubiquitination	YLDQKRLKQGLYRHP HHCHHHHHHCCCCCC	46.48	21890473
1084	Phosphorylation	KRLKQGLYRHPWDDI HHHHHCCCCCCCCHH	17.44	75111
1092	Phosphorylation	RHPWDDISYVLPEHM CCCCCHHHHHCCHHC	19.04	28555341
1093	Phosphorylation	HPWDDISYVLPEHMS CCCCHHHHHCCHHCC	13.31	23403867
1100	Phosphorylation	YVLPEHMSM------ HHCCHHCCC------	24.21	22617229
1121	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
131	Y	Phosphorylation	Kinase	LYN	P07948	PSP
227	Y	Phosphorylation	Kinase	SRC	P12931	PSP
227	Y	Phosphorylation	Kinase	LYN	P07948	PSP
252	Y	Phosphorylation	Kinase	SRC	P12931	PSP
252	Y	Phosphorylation	Kinase	LYN	P07948	PSP
384	Y	Phosphorylation	Kinase	LYN	P07948	PSP
447	T	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
447	T	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
447	T	Phosphorylation	Kinase	AKT1	P31749	PSP
451	S	Phosphorylation	Kinase	AKT1	P31749	PSP
451	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
451	S	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
455	S	Phosphorylation	Kinase	AKT2	P31751	Uniprot
455	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
455	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
455	S	Phosphorylation	Kinase	PKA	-	Uniprot
455	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
455	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
659	Y	Phosphorylation	Kinase	LYN	P07948	PSP
682	Y	Phosphorylation	Kinase	LYN	P07948	PSP
682	Y	Phosphorylation	Kinase	SRC	P12931	PSP
1006	Y	Phosphorylation	Kinase	SRC	P12931	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CUL3#KLHL25	Q13618#Q9H0H3	PMID:27664236

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
447	T	Phosphorylation	10653665
Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity).
451	S	Phosphorylation	10653665
Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity).
455	S	Phosphorylation	18669648
Phosphorylation on Ser-455 is decreased by prior phosphorylation on the other 2 residues (By similarity).
455	S	Phosphorylation	18669648
Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity).
540	K	Acetylation	23932781
Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF.
540	K	ubiquitylation	23932781
Ubiquitinated at Lys-540, Lys-546 and Lys-554 by UBR4, leading to its degradation.
546	K	Acetylation	19608861
Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF.
546	K	ubiquitylation	19608861
Ubiquitinated at Lys-540, Lys-546 and Lys-554 by UBR4, leading to its degradation.
554	K	Acetylation	19608861
Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF.
554	K	ubiquitylation	19608861
Ubiquitinated at Lys-540, Lys-546 and Lys-554 by UBR4, leading to its degradation.

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 ACLY_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
MAGD2_HUMAN	MAGED2	physical	22863883
MCM2_HUMAN	MCM2	physical	22863883
MCM6_HUMAN	MCM6	physical	22863883
NUCL_HUMAN	NCL	physical	22863883
UBR4_HUMAN	UBR4	physical	23932781
SIR2_HUMAN	SIRT2	physical	23932781
CISY_HUMAN	CS	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
PNCB_HUMAN	NAPRT	physical	26344197
P210L_HUMAN	NUP210L	physical	26344197
RPE_HUMAN	RPE	physical	26344197
SDHA_HUMAN	SDHA	physical	26344197
SDHB_HUMAN	SDHB	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197

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 ACLY_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-86; LYS-546; LYS-554;LYS-948; LYS-962; LYS-968; LYS-978 AND LYS-1077, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-481 AND TYR-682, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-442; THR-445;THR-447; THR-453; SER-455; SER-478; SER-481; THR-639; SER-663;TYR-682; SER-839; SER-922; SER-979 AND SER-1100, AND MASSSPECTROMETRY.	19369195 [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-455; SER-481 ANDSER-1100, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"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-455 AND SER-481, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131 AND TYR-682, ANDMASS SPECTROMETRY.	15592455 [Abstract]

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