dbPTM

ACLY_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACLY_RAT
UniProt AC	P16638
Protein Name	ATP-citrate synthase
Gene Name	Acly
Organism	Rattus norvegicus (Rat).
Sequence Length	1100
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	MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDTKAQKLLVGVDEKLNAEDIKRHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGSLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMAWAPAIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSATLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVAKGAIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDFVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTREEADEYVDIGALNGVFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Ubiquitination	AISEQTGKELLYKYI HHHHHHCHHHHHHHH	48.88	-
64	Acetylation	VKPDQLIKRRGKLGL CCHHHHHHHHCCCEE	44.64	22902405
68	Ubiquitination	QLIKRRGKLGLVGVN HHHHHHCCCEEEEEE	37.25	-
77	Phosphorylation	GLVGVNLSLDGVKSW EEEEEEECCCHHHHH	21.14	22276854
83	Phosphorylation	LSLDGVKSWLKPRLG ECCCHHHHHHCCCCC	34.92	22673903
86	Ubiquitination	DGVKSWLKPRLGHEA CHHHHHHCCCCCCCC	23.10	-
86	Acetylation	DGVKSWLKPRLGHEA CHHHHHHCCCCCCCC	23.10	22902405
131	Phosphorylation	YATREGDYVLFHHEG EEECCCCEEEEEECC	15.20	25575281
151	Acetylation	DVDTKAQKLLVGVDE CCCHHHHHHHHCCCC	48.96	22902405
159	Acetylation	LLVGVDEKLNAEDIK HHHCCCCCCCHHHHH	42.45	22902405
166	Succinylation	KLNAEDIKRHLLVHA CCCHHHHHHHHHEEC	46.19	26843850
166	Acetylation	KLNAEDIKRHLLVHA CCCHHHHHHHHHEEC	46.19	22902405
230	Ubiquitination	ATADYICKVKWGDIE CCCCEEEEEECCCCC	36.97	-
247	Phosphorylation	PPFGREAYPEEAYIA CCCCCCCCCCCEEEE	13.36	27097102
252	Phosphorylation	EAYPEEAYIADLDAK CCCCCCEEEEECCCC	10.42	27097102
259	Ubiquitination	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	-
259	Acetylation	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	22902405
260	Phosphorylation	IADLDAKSGASLKLT EEECCCCCCCEEEEE	41.11	27097102
263	Phosphorylation	LDAKSGASLKLTLLN CCCCCCCEEEEEEEC	29.57	27097102
265	Ubiquitination	AKSGASLKLTLLNPK CCCCCEEEEEEECCC	36.61	-
267	Phosphorylation	SGASLKLTLLNPKGR CCCEEEEEEECCCCC	27.84	25575281
272	Ubiquitination	KLTLLNPKGRIWTMV EEEEECCCCCEEEEE	60.80	-
322	Phosphorylation	QTYDYAKTILSLMTR HHHHHHHHHHHHHHC	20.98	28432305
325	Phosphorylation	DYAKTILSLMTREKH HHHHHHHHHHHCCCC	16.55	28432305
348	Phosphorylation	GGSIANFTNVAATFK CCCCCCCCHHHHHHH	28.70	23984901
384	Phosphorylation	VRRGGPNYQEGLRVM EECCCCCHHHHCEEE	15.86	126007
445 (in isoform 2)	Phosphorylation	-	33.81	26437020
446 (in isoform 2)	Phosphorylation	-	24.45	26437020
446	Phosphorylation	NASGSTSTPAPSRTA CCCCCCCCCCCCCCC	24.45	2176822
447 (in isoform 2)	Phosphorylation	-	41.77	22276854
450	Phosphorylation	STSTPAPSRTASFSE CCCCCCCCCCCCCCH	44.35	2176822
451 (in isoform 2)	Phosphorylation	-	33.00	26437020
452	Phosphorylation	STPAPSRTASFSESR CCCCCCCCCCCCHHC	30.87	21738781
454	Phosphorylation	PAPSRTASFSESRAD CCCCCCCCCCHHCHH	28.79	23991683
456	Phosphorylation	PSRTASFSESRADEV CCCCCCCCHHCHHHC	31.97	30411139
458	Phosphorylation	RTASFSESRADEVAP CCCCCCHHCHHHCCC	31.41	23991683
477	Phosphorylation	KPAMPQDSVPSPRSL CCCCCCCCCCCCHHH	30.58	23991683
480	Phosphorylation	MPQDSVPSPRSLQGK CCCCCCCCCHHHCCH	30.69	23991683
490	Phosphorylation	SLQGKSATLFSRHTK HHCCHHCCHHHHHHH	35.11	30181290
493	Phosphorylation	GKSATLFSRHTKAIV CHHCCHHHHHHHHHH	26.68	73410221
497	Acetylation	TLFSRHTKAIVWGMQ CHHHHHHHHHHHHHH	29.95	22902405
505	Phosphorylation	AIVWGMQTRAVQGML HHHHHHHHHHHCCCC	16.23	9534837
537	Acetylation	YPFTGDHKQKFYWGH EECCCCCCCCEEECC	60.98	22902405
537	Ubiquitination	YPFTGDHKQKFYWGH EECCCCCCCCEEECC	60.98	-
539	Acetylation	FTGDHKQKFYWGHKE CCCCCCCCEEECCHH	45.27	22902405
545	Ubiquitination	QKFYWGHKEILIPVF CCEEECCHHHHHHHH	42.38	-
545	Acetylation	QKFYWGHKEILIPVF CCEEECCHHHHHHHH	42.38	22902405
553	Acetylation	EILIPVFKNMADAMK HHHHHHHHHHHHHHH	46.15	22902405
578	Phosphorylation	FASLRSAYDSTMETM HHHHHHHHHHHHHHC	16.21	31136869
615	Ubiquitination	LIKKADQKGVTIIGP HHHHHHHCCCEEECC	56.76	-
624	Phosphorylation	VTIIGPATVGGIKPG CEEECCCCCCCCCCC	23.87	28432305
629	Ubiquitination	PATVGGIKPGCFKIG CCCCCCCCCCCEECC	38.34	-
634	Ubiquitination	GIKPGCFKIGNTGGM CCCCCCEECCCCCCH	54.50	-
638	Phosphorylation	GCFKIGNTGGMLDNI CCEECCCCCCHHHHH	29.87	-
649	Ubiquitination	LDNILASKLYRPGSV HHHHHHHHCCCCCCE	43.88	-
651	Phosphorylation	NILASKLYRPGSVAY HHHHHHCCCCCCEEE	20.64	26022182
655	Phosphorylation	SKLYRPGSVAYVSRS HHCCCCCCEEEEECC	13.27	26022182
660	Phosphorylation	PGSVAYVSRSGGMSN CCCEEEEECCCCCCH	14.19	26022182
662	Phosphorylation	SVAYVSRSGGMSNEL CEEEEECCCCCCHHH	31.99	26437020
666	Phosphorylation	VSRSGGMSNELNNII EECCCCCCHHHHHHH	30.35	28689409
676	Phosphorylation	LNNIISRTTDGVYEG HHHHHHCCCCCEEEE	23.58	25575281
677	Phosphorylation	NNIISRTTDGVYEGV HHHHHCCCCCEEEEE	29.64	25575281
681	Phosphorylation	SRTTDGVYEGVAIGG HCCCCCEEEEEEECC	16.70	28432305
731	Acetylation	YKICRGIKEGRLTKP HHHCCCCCCCCCCCC	57.87	22902405
759	Phosphorylation	SSEVQFGHAGACANQ CCCCCCCCHHHHCHH	23.44	-
779	Ubiquitination	VAKNQALKEAGVFVP HHHHHHHHHHCCCCC	48.83	-
819	Phosphorylation	AQEVPPPTVPMDYSW CCCCCCCCCCCCCHH	42.91	22673903
824	Phosphorylation	PPTVPMDYSWARELG CCCCCCCCHHHHHHC	10.40	22673903
825	Phosphorylation	PTVPMDYSWARELGL CCCCCCCHHHHHHCC	15.25	22673903
835	Ubiquitination	RELGLIRKPASFMTS HHHCCCCCCHHHHHH	37.63	-
838	Phosphorylation	GLIRKPASFMTSICD CCCCCCHHHHHHHCC	24.87	25575281
841	Phosphorylation	RKPASFMTSICDERG CCCHHHHHHHCCHHH	16.96	25575281
842	Phosphorylation	KPASFMTSICDERGQ CCHHHHHHHCCHHHC	14.94	25575281
917	Ubiquitination	IICARAGKDLVSSLT EEEECCCHHHHHHHH	47.07	-
943	Ubiquitination	GALDAAAKMFSKAFD HHHHHHHHHHHHHHH	35.43	-
947	Acetylation	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	22902405
947	Ubiquitination	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	-
951	Phosphorylation	MFSKAFDSGIIPMEF HHHHHHHCCCCCHHH	25.99	22673903
961	Acetylation	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	22902405
961	Ubiquitination	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	-
964	Acetylation	EFVNKMKKEGKLIMG HHHHHHHHCCCEEEE	69.10	22902405
967	Acetylation	NKMKKEGKLIMGIGH HHHHHCCCEEEECCC	35.61	22902405
977	Ubiquitination	MGIGHRVKSINNPDM EECCCCHHHCCCHHH	45.64	-
977	Acetylation	MGIGHRVKSINNPDM EECCCCHHHCCCHHH	45.64	22902405
990	Ubiquitination	DMRVQILKDFVKQHF HHHHHHHHHHHHHHC	51.23	-
1076	Acetylation	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	22902405
1079	Acetylation	YLDQKRLKQGLYRHP HHCHHHHHHCCCCCC	46.48	22902405
1099	Phosphorylation	YVLPEHMSM------ HHCCHHCCC------	24.21	23984901

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
446	T	Phosphorylation	Kinase	GSK3A	P18265	PSP
450	S	Phosphorylation	Kinase	GSK3A	P18265	PSP
454	S	Phosphorylation	Kinase	AKT1	P47196	Uniprot
454	S	Phosphorylation	Kinase	AKT2	P47197	Uniprot
454	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
454	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
454	S	Phosphorylation	Kinase	PKA	-	Uniprot
454	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
446	T	Phosphorylation	2176822
Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation state of Ser-454.
450	S	Phosphorylation	2176822
Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation state of Ser-454.
454	S	Phosphorylation	12107176
Phosphorylation on Ser-454 is decreased by prior phosphorylation on the other 2 residues.
454	S	Phosphorylation	12107176
Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation state of Ser-454.
539	K	Acetylation	-
Acetylated at Lys-539, Lys-545 and Lys-553 by KAT2B/PCAF (By similarity).
539	K	ubiquitylation	-
Ubiquitinated at Lys-539, Lys-545 and Lys-553 by UBR4, leading to its degradation (By similarity).
545	K	Acetylation	-
Acetylated at Lys-539, Lys-545 and Lys-553 by KAT2B/PCAF (By similarity).
545	K	ubiquitylation	-
Ubiquitinated at Lys-539, Lys-545 and Lys-553 by UBR4, leading to its degradation (By similarity).
553	K	Acetylation	-
Acetylated at Lys-539, Lys-545 and Lys-553 by KAT2B/PCAF (By similarity).
553	K	ubiquitylation	-
Ubiquitinated at Lys-539, Lys-545 and Lys-553 by UBR4, leading to its degradation (By similarity).

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ACLY_RAT !!

Drug and Disease Associations

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

Regulatory Network of ACLY_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND MASSSPECTROMETRY.	16396499 [Abstract]
"The identification of ATP-citrate lyase as a protein kinase B (Akt)substrate in primary adipocytes."; Berwick D.C., Hers I., Heesom K.J., Moule S.K., Tavare J.M.; J. Biol. Chem. 277:33895-33900(2002). Cited for: PHOSPHORYLATION AT SER-454.	12107176 [Abstract]

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