dbPTM

ACLY_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACLY_MOUSE
UniProt AC	Q91V92
Protein Name	ATP-citrate synthase
Gene Name	Acly
Organism	Mus musculus (Mouse).
Sequence Length	1091
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 (By similarity)..
Protein Sequence	MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNTEDIKRHLLVHAPEDKKEVLASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPEGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQGKSATLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVAKGAIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDFVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTREEADEYVDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Ubiquitination	AISEQTGKELLYKYI HHHHHHCHHHHHHHH	48.88	-
20	S-palmitoylation	ELLYKYICTTSAIQN HHHHHHHHHHHHHHH	2.85	28526873
20	S-nitrosylation	ELLYKYICTTSAIQN HHHHHHHHHHHHHHH	2.85	24895380
20	Glutathionylation	ELLYKYICTTSAIQN HHHHHHHHHHHHHHH	2.85	24333276
20	S-nitrosocysteine	ELLYKYICTTSAIQN HHHHHHHHHHHHHHH	2.85	-
52	Phosphorylation	QDHPWLLSQSLVVKP HCCCCHHCCCEECCH	18.62	26060331
54	Phosphorylation	HPWLLSQSLVVKPDQ CCCHHCCCEECCHHH	21.54	26060331
64	Acetylation	VKPDQLIKRRGKLGL CCHHHHHHHHCCCEE	44.64	66698221
68	Ubiquitination	QLIKRRGKLGLVGVN HHHHHHCCCEEEEEE	37.25	-
77	Phosphorylation	GLVGVNLSLDGVKSW EEEEEEECCCHHHHH	21.14	27180971
83	Phosphorylation	LSLDGVKSWLKPRLG ECCCHHHHHHCCCCC	34.92	22817900
94	Phosphorylation	PRLGHEATVGKAKGF CCCCCCCCHHHHHHH	27.14	82570307
131	Phosphorylation	YATREGDYVLFHHEG EEECCCCEEEEEECC	15.20	30635358
148	Ubiquitination	DVGDVDAKAQKLLVG CHHHCCHHHHHHHHC	47.06	-
151	Ubiquitination	DVDAKAQKLLVGVDE HCCHHHHHHHHCCCC	48.96	-
151	Malonylation	DVDAKAQKLLVGVDE HCCHHHHHHHHCCCC	48.96	26320211
159	Ubiquitination	LLVGVDEKLNTEDIK HHHCCCCCCCHHHHH	42.44	-
159	Acetylation	LLVGVDEKLNTEDIK HHHCCCCCCCHHHHH	42.44	66703455
229	S-palmitoylation	DATADYICKVKWGDI CCCCCEEEEEECCCC	3.18	28526873
230	Ubiquitination	ATADYICKVKWGDIE CCCCEEEEEECCCCC	36.97	-
247	Phosphorylation	PPFGREAYPEEAYIA CCCCCCCCCCCEEEE	13.36	75101
252	Phosphorylation	EAYPEEAYIADLDAK CCCCCCEEEEECCCC	10.42	75105
259	Ubiquitination	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	-
259	Acetylation	YIADLDAKSGASLKL EEEECCCCCCCEEEE	49.44	66703851
260	Phosphorylation	IADLDAKSGASLKLT EEECCCCCCCEEEEE	41.11	23737553
263	Phosphorylation	LDAKSGASLKLTLLN CCCCCCCEEEEEEEC	29.57	23737553
265	Ubiquitination	AKSGASLKLTLLNPK CCCCCEEEEEEECCC	36.61	-
267	Phosphorylation	SGASLKLTLLNPKGR CCCEEEEEEECCCCC	27.84	21183079
272	Ubiquitination	KLTLLNPKGRIWTMV EEEEECCCCCEEEEE	60.80	-
325	Phosphorylation	DYAKTILSLMTREKH HHHHHHHHHHHCCCC	16.55	22006019
348	Phosphorylation	GGSIANFTNVAATFK CCCCCCCCHHHHHHH	28.70	30352176
384	Phosphorylation	VRRGGPNYQEGLRVM EECCCCCHHHHCEEE	15.86	75109
442	Phosphorylation	ANFLLNASGSTSTPA HCEEECCCCCCCCCC	32.00	25338131
445	Phosphorylation	LLNASGSTSTPAPSR EECCCCCCCCCCCCC	39.90	21082442
446	Phosphorylation	LNASGSTSTPAPSRT ECCCCCCCCCCCCCC	33.81	28507225
447	Phosphorylation	NASGSTSTPAPSRTA CCCCCCCCCCCCCCC	24.45	19060867
451	Phosphorylation	STSTPAPSRTASFSE CCCCCCCCCCCCCCH	44.35	19060867
453	Phosphorylation	STPAPSRTASFSESR CCCCCCCCCCCCHHC	30.87	25521595
455	Phosphorylation	PAPSRTASFSESRAD CCCCCCCCCCHHCHH	28.79	24925903
457	Phosphorylation	PSRTASFSESRADEV CCCCCCCCHHCHHHC	31.97	24925903
459	Phosphorylation	RTASFSESRADEVAP CCCCCCHHCHHHCCC	31.41	25521595
471	Malonylation	VAPAKKAKPAMPQGK CCCHHHCCCCCCCCC	42.04	26320211
471	Ubiquitination	VAPAKKAKPAMPQGK CCCHHHCCCCCCCCC	42.04	-
478	Acetylation	KPAMPQGKSATLFSR CCCCCCCCCCCCHHH	31.50	23806337
478	Ubiquitination	KPAMPQGKSATLFSR CCCCCCCCCCCCHHH	31.50	-
479	Phosphorylation	PAMPQGKSATLFSRH CCCCCCCCCCCHHHH	33.05	24719451
484	Phosphorylation	GKSATLFSRHTKAIV CCCCCCHHHHHHHHH	26.68	24719451
496	Phosphorylation	AIVWGMQTRAVQGML HHHHHHHHHHHCCCC	16.23	22817900
509	S-palmitoylation	MLDFDYVCSRDEPSV CCCCCEEECCCCCCE	1.94	28526873
521	Phosphorylation	PSVAAMVYPFTGDHK CCEEEEEEECCCCCC	4.59	18779572
524	Phosphorylation	AAMVYPFTGDHKQKF EEEEEECCCCCCCCE	36.88	18779572
528	Ubiquitination	YPFTGDHKQKFYWGH EECCCCCCCCEEECC	60.98	-
530	Acetylation	FTGDHKQKFYWGHKE CCCCCCCCEEECCHH	45.27	-
536	Ubiquitination	QKFYWGHKEILIPVF CCEEECCHHHHHHHH	42.38	-
536	Acetylation	QKFYWGHKEILIPVF CCEEECCHHHHHHHH	42.38	22646827
544	Acetylation	EILIPVFKNMADAMK HHHHHHHHHHHHHHH	46.15	8263617
606	Ubiquitination	LIKKADQKGVTIIGP HHHHHHHCCCEEECC	56.76	-
615	Phosphorylation	VTIIGPATVGGIKPG CEEECCCCCCCCCCC	23.87	1031630257
620	Ubiquitination	PATVGGIKPGCFKIG CCCCCCCCCCCEECC	38.34	-
623	S-palmitoylation	VGGIKPGCFKIGNTG CCCCCCCCEECCCCC	4.21	28526873
623	S-nitrosylation	VGGIKPGCFKIGNTG CCCCCCCCEECCCCC	4.21	22178444
629	Phosphorylation	GCFKIGNTGGMLDNI CCEECCCCCCHHHHH	29.87	-
639	Phosphorylation	MLDNILASKLYRPGS HHHHHHHHHCCCCCC	21.54	27180971
640	Ubiquitination	LDNILASKLYRPGSV HHHHHHHHCCCCCCE	43.88	-
646	Phosphorylation	SKLYRPGSVAYVSRS HHCCCCCCEEEEECC	13.27	29514104
653	Phosphorylation	SVAYVSRSGGMSNEL CEEEEECCCCCCHHH	31.99	25521595
667	Phosphorylation	LNNIISRTTDGVYEG HHHHHHCCCCCEEEE	23.58	26643407
668	Phosphorylation	NNIISRTTDGVYEGV HHHHHCCCCCEEEEE	29.64	26643407
672	Phosphorylation	SRTTDGVYEGVAIGG HCCCCCEEEEEEECC	16.70	25177544
750	Phosphorylation	SSEVQFGHAGACANQ CCCCCCCCHHHHCHH	23.44	-
770	Ubiquitination	VAKNQALKEAGVFVP HHHHHHHHHHCCCCC	48.83	-
815	Phosphorylation	PPTVPMDYSWARELG CCCCCCCCHHHHHHC	10.40	138339
826	Ubiquitination	RELGLIRKPASFMTS HHHCCCCCCHHHHHH	37.63	-
826	Malonylation	RELGLIRKPASFMTS HHHCCCCCCHHHHHH	37.63	26320211
829	Phosphorylation	GLIRKPASFMTSICD CCCCCCHHHHHHHCC	24.87	22817900
835	S-nitrosylation	ASFMTSICDERGQEL HHHHHHHCCHHHCEE	4.44	22178444
850	Phosphorylation	IYAGMPITEVFKEEM EECCCCHHHHHHHHH	21.89	51457861
908	Ubiquitination	IICARAGKDLVSSLT EEEECCCHHHHHHHH	47.07	-
934	Ubiquitination	GALDAAAKMFSKAFD HHHHHHHHHHHHHHH	35.43	-
938	Ubiquitination	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	-
938	Acetylation	AAAKMFSKAFDSGII HHHHHHHHHHHCCCC	41.63	22646811
942	Phosphorylation	MFSKAFDSGIIPMEF HHHHHHHCCCCCHHH	25.99	27180971
952	Ubiquitination	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	-
952	Acetylation	IPMEFVNKMKKEGKL CCHHHHHHHHHCCCE	46.96	22646843
958	Malonylation	NKMKKEGKLIMGIGH HHHHHCCCEEEECCC	35.61	26320211
958	Acetylation	NKMKKEGKLIMGIGH HHHHHCCCEEEECCC	35.61	22646819
968	Ubiquitination	MGIGHRVKSINNPDM EECCCCHHHCCCHHH	45.64	-
968	Malonylation	MGIGHRVKSINNPDM EECCCCHHHCCCHHH	45.64	26320211
968	Acetylation	MGIGHRVKSINNPDM EECCCCHHHCCCHHH	45.64	23806337
969	Phosphorylation	GIGHRVKSINNPDMR ECCCCHHHCCCHHHH	27.91	22817900
981	Ubiquitination	DMRVQILKDFVKQHF HHHHHHHHHHHHHHC	51.23	-
1005	Phosphorylation	LEVEKITTSKKPNLI EEEEECCCCCCCCEE	41.86	18779572
1056	Phosphorylation	GIFVLGRSMGFIGHY CEEEECCCHHHHHHH	22.81	51457853
1067	Acetylation	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	19865989
1067	Ubiquitination	IGHYLDQKRLKQGLY HHHHHCHHHHHHCCC	60.40	-
1070	Ubiquitination	YLDQKRLKQGLYRHP HHCHHHHHHCCCCCC	46.48	-
1070	Malonylation	YLDQKRLKQGLYRHP HHCHHHHHHCCCCCC	46.48	26320211
1090	Phosphorylation	YVLPEHMSM------ HHCCHHCCC------	24.21	21082442

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
455	S	Phosphorylation	Kinase	AKT1	P31750	Uniprot
455	S	Phosphorylation	Kinase	AKT2	Q60823	Uniprot
455	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
455	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
455	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
447	T	Phosphorylation	-
Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity).
451	S	Phosphorylation	-
Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity).
455	S	Phosphorylation	19131326
Phosphorylation on Ser-455 is decreased by prior phosphorylation on the other 2 residues (By similarity).
455	S	Phosphorylation	19131326
Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity).
530	K	Acetylation	-
Acetylated at Lys-530, Lys-536 and Lys-544 by KAT2B/PCAF (By similarity).
530	K	ubiquitylation	-
Ubiquitinated at Lys-530, Lys-536 and Lys-544 by UBR4, leading to its degradation (By similarity).
536	K	Acetylation	-
Acetylated at Lys-530, Lys-536 and Lys-544 by KAT2B/PCAF (By similarity).
536	K	ubiquitylation	-
Ubiquitinated at Lys-530, Lys-536 and Lys-544 by UBR4, leading to its degradation (By similarity).
544	K	Acetylation	-
Acetylated at Lys-530, Lys-536 and Lys-544 by KAT2B/PCAF (By similarity).
544	K	ubiquitylation	-
Ubiquitinated at Lys-530, Lys-536 and Lys-544 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_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of ACLY_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, AND MASSSPECTROMETRY.	17947660 [Abstract]

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