dbPTM

ACACA_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACACA_RAT
UniProt AC	P11497
Protein Name	Acetyl-CoA carboxylase 1
Gene Name	Acaca
Organism	Rattus norvegicus (Rat).
Sequence Length	2345
Subcellular Localization	Cytoplasm.
Protein Description	Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase..
Protein Sequence	MDEPSPLAKTLELNQHSRFIIGSVSEDNSEDEISNLVKLDLEEKEGSLSPASVSSDTLSDLGISALQDGLAFHMRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGANNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQDLYEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLFRIKDIRMMYGVSPWGDAPIDFENSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVNLRNSISNFLHSLERGQVLPAHTLLNTVDVELIYEGIKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDGSSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVIAKMQLDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQDIMTSVSGRIPLNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYDVRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASNLNHYGMTHVASVSDVLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFCDSPPQSPTFPESGHTSLYDEDKVPRDEPIHILNVAIKTDGDIEDDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDFRKQVNCEVDQRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQAFLPSPPLPSDILTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMSLKSPEYPDGRDVIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGARIGLAEEIRHMFHVAWVDSEDPYKGYKYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKNVHSSVPLLNSKDPIDRIIEFVPTKAPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAVETRTVELSVPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECSQPVMVYIPPQAELRGGSWVVIDPTINPRHMEMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRRVDPVYIRLAERLGTPELSPTERKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRTFFYWRLRRLLLEDLVKKKIHSANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLVEWLEKQLTEEDGVRSVIEENIKYISRDYVLKQIRSLVQANPEVAMDSIVHMTQHISPTQRAEVVRILSTMDSPST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDEPSPLA -------CCCCCHHH	51.90	-
5	Phosphorylation	---MDEPSPLAKTLE ---CCCCCHHHHHEE	30.42	27097102
17	Phosphorylation	TLELNQHSRFIIGSV HEECCCCCCEEEEEC	21.08	29779826
23	Phosphorylation	HSRFIIGSVSEDNSE CCCEEEEECCCCCCH	16.44	1967580
25	Phosphorylation	RFIIGSVSEDNSEDE CEEEEECCCCCCHHH	40.71	28689409
29	Phosphorylation	GSVSEDNSEDEISNL EECCCCCCHHHHHHH	59.76	23712012
34	Phosphorylation	DNSEDEISNLVKLDL CCCHHHHHHHEECCH	23.28	28551015
47	Phosphorylation	DLEEKEGSLSPASVS CHHHCCCCCCCCCCC	27.11	27097102
49	Phosphorylation	EEKEGSLSPASVSSD HHCCCCCCCCCCCCC	21.81	27097102
52	Phosphorylation	EGSLSPASVSSDTLS CCCCCCCCCCCCCHH	26.39	23984901
54	Phosphorylation	SLSPASVSSDTLSDL CCCCCCCCCCCHHHH	21.72	27097102
55	Phosphorylation	LSPASVSSDTLSDLG CCCCCCCCCCHHHHC	32.24	27097102
57	Phosphorylation	PASVSSDTLSDLGIS CCCCCCCCHHHHCHH	30.06	22673903
59	Phosphorylation	SVSSDTLSDLGISAL CCCCCCHHHHCHHHH	32.64	22673903
64	Phosphorylation	TLSDLGISALQDGLA CHHHHCHHHHHHCHH	22.56	30181290
76	Phosphorylation	GLAFHMRSSMSGLHL CHHHHHHHHHCCCCH	23.87	23991683
77	Phosphorylation	LAFHMRSSMSGLHLV HHHHHHHHHCCCCHH	13.45	23991683
79	Phosphorylation	FHMRSSMSGLHLVKQ HHHHHHHCCCCHHHC	39.90	15461583
95	Phosphorylation	RDRKKIDSQRDFTVA CCCCCCCCCCCCEEC	30.50	29779826
100	Phosphorylation	IDSQRDFTVASPAEF CCCCCCCEECCHHHH	21.32	23984901
103	Phosphorylation	QRDFTVASPAEFVTR CCCCEECCHHHHHHH	21.95	25575281
109	Phosphorylation	ASPAEFVTRFGGNKV CCHHHHHHHCCCCCE	26.12	30181290
157	Phosphorylation	IRFVVMVTPEDLKAN EEEEEECCHHHHHHC	11.67	18779572
378	Phosphorylation	SLFGRDCSVQRRHQK HHHCCCCHHHHHHHH	26.10	30411139
519	Acetylation	ENPDEGFKPSSGTVQ CCCCCCCCCCCCCEE	55.64	22902405
532	Phosphorylation	VQELNFRSNKNVWGY EEEEECCCCCCCCEE	48.28	28689409
581	Phosphorylation	VVALKELSIRGDFRT HHHHHHHCCCCCHHH	16.01	18779572
599	Phosphorylation	YLIKLLETESFQLNR HHHHHHHCCCCCCCC	36.58	30181290
601	Phosphorylation	IKLLETESFQLNRID HHHHHCCCCCCCCCC	26.22	30181290
609	Phosphorylation	FQLNRIDTGWLDRLI CCCCCCCCCHHHHHH	28.08	22673903
785	N6-biotinyllysine	YAEIEVMKMVMTLTA EEHHHHHCHHHHHHH	33.25	-
785	Lipoylation	YAEIEVMKMVMTLTA EEHHHHHCHHHHHHH	33.25	2567668
785	Biotinylation	YAEIEVMKMVMTLTA EEHHHHHCHHHHHHH	33.25	2567668
834	Phosphorylation	QAELHTGSLPQIQST EEEHHCCCCCHHHHH	37.72	-
915	Acetylation	RIPLNVEKSIKKEMA CCCCCHHHHHHHHHH	53.88	22902405
1192 (in isoform 2)	Phosphorylation	-	33.55	-
1195	Phosphorylation	PNRGNIPTLNRMSFA CCCCCCCCCCCCCCH	32.63	29779826
1200	Phosphorylation	IPTLNRMSFASNLNH CCCCCCCCCHHCCCC	17.90	1974251
1203	Phosphorylation	LNRMSFASNLNHYGM CCCCCCHHCCCCCCC	39.58	23984901
1208	Phosphorylation	FASNLNHYGMTHVAS CHHCCCCCCCCCEEE	13.91	23984901
1211	Phosphorylation	NLNHYGMTHVASVSD CCCCCCCCCEEEHHH	14.61	23984901
1215	Phosphorylation	YGMTHVASVSDVLLD CCCCCEEEHHHHHHH	22.51	7915280
1217	Phosphorylation	MTHVASVSDVLLDNA CCCEEEHHHHHHHCC	21.36	23984901
1226	Phosphorylation	VLLDNAFTPPCQRMG HHHHCCCCCCCCCCC	24.74	-
1258	Phosphorylation	VMGCFCDSPPQSPTF HCCCCCCCCCCCCCC	39.39	27097102
1262	Phosphorylation	FCDSPPQSPTFPESG CCCCCCCCCCCCCCC	31.51	27097102
1264	Phosphorylation	DSPPQSPTFPESGHT CCCCCCCCCCCCCCC	58.00	27097102
1268	Phosphorylation	QSPTFPESGHTSLYD CCCCCCCCCCCCCCC	35.79	27097102
1271	Phosphorylation	TFPESGHTSLYDEDK CCCCCCCCCCCCCCC	24.77	27097102
1272	Phosphorylation	FPESGHTSLYDEDKV CCCCCCCCCCCCCCC	21.18	27097102
1274	Phosphorylation	ESGHTSLYDEDKVPR CCCCCCCCCCCCCCC	19.63	27097102
1333	Acetylation	LTFLVAQKDFRKQVN HHHHHCCHHHHHHCC	49.44	-
1356	Phosphorylation	REFPKFFTFRARDKF HHCCCCEEEECCCCC	18.49	25532521
1579	Acetylation	INTPYVTKDLLQSKR ECCCCCCHHHHHCCC	36.01	22902405
1758	Acetylation	YLTPQDYKRVSALNS EECHHHHHHHHHCCC	55.39	22902405
1787	Acetylation	KITDIIGKEEGLGAE EEEECCCCCCCCCCC	42.03	22902405
2126	Acetylation	PEGTVEIKFRKKDLV CCCEEEEEEEHHHHH	26.13	22902405
2134	Acetylation	FRKKDLVKTMRRVDP EEHHHHHHHHHHCCH	43.85	22902405
2152	Phosphorylation	RLAERLGTPELSPTE HHHHHHCCCCCCHHH	20.41	22673903
2156	Phosphorylation	RLGTPELSPTERKEL HHCCCCCCHHHHHHH	28.28	22673903
2158	Phosphorylation	GTPELSPTERKELES CCCCCCHHHHHHHHH	45.08	22673903
2317	Phosphorylation	NPEVAMDSIVHMTQH CHHHHHHHHHHHHCC	17.27	28689409
2322	Phosphorylation	MDSIVHMTQHISPTQ HHHHHHHHCCCCHHH	11.34	28689409
2338	Phosphorylation	AEVVRILSTMDSPST HHHHHHHHCCCCCCC	21.22	27097102
2339	Phosphorylation	EVVRILSTMDSPST- HHHHHHHCCCCCCC-	22.88	27097102
2342	Phosphorylation	RILSTMDSPST---- HHHHCCCCCCC----	15.21	27097102
2344	Phosphorylation	LSTMDSPST------ HHCCCCCCC------	51.18	27097102
2345	Phosphorylation	STMDSPST------- HCCCCCCC-------	46.11	27097102

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
25	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
25	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
29	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
29	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
29	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
77	S	Phosphorylation	Kinase	PKACA	P17612	PSP
77	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
77	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
77	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
79	S	Phosphorylation	Kinase	PRKAA1	P54645	GPS
79	S	Phosphorylation	Kinase	PRKAA2	Q09137	GPS
79	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
79	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
95	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
95	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
1192	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
1200	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
1200	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
1200	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
1200	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
1200	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
1200	S	Phosphorylation	Kinase	PRKAA2	Q09137	GPS
1200	S	Phosphorylation	Kinase	PRKAA1	P54645	GPS
1215	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
1215	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
1215	S	Phosphorylation	Kinase	PRKAA2	Q09137	GPS
1215	S	Phosphorylation	Kinase	PRKAA1	P54645	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
79	S	Phosphorylation	2900138
Phosphorylation at Ser-79 by AMPK inactivates enzyme activity.
1200	S	Phosphorylation	2900138
Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear.
1215	S	Phosphorylation	1346520
Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear.
1262	S	Phosphorylation	-
Phosphorylation on Ser-1262 is required for interaction with BRCA1.

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 ACACA_RAT !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of ACACA_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-79, AND MASSSPECTROMETRY.	16396499 [Abstract]
"Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylaseby the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets."; Davies S.P., Carling D., Munday M.R., Hardie D.G.; Eur. J. Biochem. 203:615-623(1992). Cited for: PHOSPHORYLATION AT SER-79; SER-1200 AND SER-1215.	1346520 [Abstract]
"Acetyl-CoA carboxylase mRNA species with or without inhibitory codingsequence for Ser-1200 phosphorylation."; Kong I.-S., Lopez-Casillas F., Kim K.-H.; J. Biol. Chem. 265:13695-13701(1990). Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1167-1200 (ISOFORMS 1 AND 2), ANDPHOSPHORYLATION AT SER-1200.	1974251 [Abstract]

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