ACACB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACACB_MOUSE
• UniProt AC: E9Q4Z2
• Protein Name: Acetyl-CoA carboxylase 2 {ECO:0000250|UniProtKB:O00763}
• Gene Name: Acacb {ECO:0000312|MGI:MGI:2140940}
• Organism: Mus musculus (Mouse).
• Sequence Length: 2448
• Subcellular Localization: Mitochondrion . Nucleus . Endomembrane system . May associate with membranes.
• Protein Description: Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (By similarity). Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (By similarity). Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage. [PubMed: 11283375]
• Protein Sequence: MVLLLFLTCLVFSCLTFSWLKIWGKMTDSKPLTNSKVEANLLSSEESLSASELSGEQLQEHGDHSCLSYRGPRDASQQRNSLPSSCQRPPRNPLSSNDTWPSPELQTNWTAAPGPEVPDANGLSFPARPPSQRTVSPSREDRKQAHIKRQLMTSFILGSLDDNSSDEDPSAGSFQNSSRKSSRASLGTLSQEAALNTSDPESHAPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSGSGLTVEWTEDSRHQGKCISVPEDVYEQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPIPFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYALKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGVILEAGCVVARLELDDPSKVHAAQPFTGELPAQQTLPILGEKLHQVFHGVLENLTNVMSGYCLPEPFFSMKLKDWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFMNTQSIVQLVQRYRSGTRGYMKAVVLDLLRKYLNVEHHFQQAHYDKCVINLREQFKPDMTQVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSDELTSILCELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHENKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAVPISVSNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVQTDTLLFSKACTSLYSEEDSKSLREEPIHILNVAIQCADHMEDEALVPVFRAFVQSKKHILVDYGLRRITFLVAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRDMVMRYGSRLWKLRVLQAEVKINIRQTTSDSAIPIRLFITNESGYYLDISLYREVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVAFKMRFKTPEYPEGRDAVVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLAEEIKQIFQVAWVDPEDPHKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDANLGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSFIPKDNRSPVPITTPSDPIDREIEFTPTKAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDGLRLYEQPILIYIPPCAELRGGSWVVLDSTINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLVGQLGKAQLPDKDRKELEGQLKAREELLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTARTFFYWRLRRLLLEAQVKQEILRASPELNHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSAKDGLRSTIRENINYLKRDSVLKTIQSLVQEHPEVIMDCVAYLSQHLTPAERIQVAQLLSTTESPASS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	Phosphorylation	DSKPLTNSKVEANLL CCCCCCCCHHHHHCC		-
43	Phosphorylation	KVEANLLSSEESLSA HHHHHCCCCHHHCCH		30352176
44	Phosphorylation	VEANLLSSEESLSAS HHHHCCCCHHHCCHH		21183079
47	Phosphorylation	NLLSSEESLSASELS HCCCCHHHCCHHHCC		22817900
49	Phosphorylation	LSSEESLSASELSGE CCCHHHCCHHHCCHH		23567750
51	Phosphorylation	SEESLSASELSGEQL CHHHCCHHHCCHHHH		30352176
54	Phosphorylation	SLSASELSGEQLQEH HCCHHHCCHHHHHHH		30352176
65	Phosphorylation	LQEHGDHSCLSYRGP HHHHCCCCCHHCCCC		21183079
81	Phosphorylation	DASQQRNSLPSSCQR CHHHHHCCCCCCCCC		54885731
84	Phosphorylation	QQRNSLPSSCQRPPR HHHCCCCCCCCCCCC		23140645
85	Phosphorylation	QRNSLPSSCQRPPRN HHCCCCCCCCCCCCC		23140645
86	S-palmitoylation	RNSLPSSCQRPPRNP HCCCCCCCCCCCCCC		26165157
134	Phosphorylation	ARPPSQRTVSPSRED CCCCCCCCCCCCHHH		23140645
136	Phosphorylation	PPSQRTVSPSREDRK CCCCCCCCCCHHHHH		23737553
138	Phosphorylation	SQRTVSPSREDRKQA CCCCCCCCHHHHHHH		23737553
143	Acetylation	SPSREDRKQAHIKRQ CCCHHHHHHHHHHHH		6566457
153	Phosphorylation	HIKRQLMTSFILGSL HHHHHHHHHHHHCCC		23737553
154	Phosphorylation	IKRQLMTSFILGSLD HHHHHHHHHHHCCCC		23737553
159	Phosphorylation	MTSFILGSLDDNSSD HHHHHHCCCCCCCCC		23737553
164	Phosphorylation	LGSLDDNSSDEDPSA HCCCCCCCCCCCCCC		25195567
165	Phosphorylation	GSLDDNSSDEDPSAG CCCCCCCCCCCCCCC		25195567
170	Phosphorylation	NSSDEDPSAGSFQNS CCCCCCCCCCCCCCC		23737553
177	Phosphorylation	SAGSFQNSSRKSSRA CCCCCCCCCCCCCCH		29899451
178	Phosphorylation	AGSFQNSSRKSSRAS CCCCCCCCCCCCCHH		29899451
181	Phosphorylation	FQNSSRKSSRASLGT CCCCCCCCCCHHHHH		9473917
182	Phosphorylation	QNSSRKSSRASLGTL CCCCCCCCCHHHHHH		23567750
185	Phosphorylation	SRKSSRASLGTLSQE CCCCCCHHHHHHCHH		27742792
188	Phosphorylation	SSRASLGTLSQEAAL CCCHHHHHHCHHHHH		27742792
190	Phosphorylation	RASLGTLSQEAALNT CHHHHHHCHHHHHCC		29472430
197	Phosphorylation	SQEAALNTSDPESHA CHHHHHCCCCCCCCC		27742792
198	Phosphorylation	QEAALNTSDPESHAP HHHHHCCCCCCCCCC		9474001
202	Phosphorylation	LNTSDPESHAPTMRP HCCCCCCCCCCCCCC		27742792
206	Phosphorylation	DPESHAPTMRPSMSG CCCCCCCCCCCCCCH		27742792
210	Phosphorylation	HAPTMRPSMSGLHLV CCCCCCCCCCHHHHH		23737553
212	Phosphorylation	PTMRPSMSGLHLVKR CCCCCCCCHHHHHCC		27742792
233	Phosphorylation	LDLHRDFTVASPAEF CCCCCCCEECCHHHH		28066266
236	Phosphorylation	HRDFTVASPAEFVTR CCCCEECCHHHHHHH		27180971
242	Phosphorylation	ASPAEFVTRFGGNRV CCHHHHHHHCCCCCE		28066266
252	Ubiquitination	GGNRVIEKVLIANNG CCCCEEEEEEEECCC		-
290	Phosphorylation	IRFVVMVTPEDLKAN EEEEEECCHHHHHHC		18779572
436	Ubiquitination	EGLQAAEKIGFPLMI HHHHHHHHHCCCEEE		22790023
446	Phosphorylation	FPLMIKASEGGGGKG CCEEEECCCCCCCCC		-
456	Ubiquitination	GGGKGIRKAESAEDF CCCCCCCCCCCCCCC		22790023
459	Phosphorylation	KGIRKAESAEDFPML CCCCCCCCCCCCHHH		27180971
630	Phosphorylation	IPFETPLSPPIARGH CCCCCCCCCCCCCCC		27180971
653	Acetylation	ENPDEGFKPSSGTVQ CCCCCCCCCCCCCEE		42500293
653	Ubiquitination	ENPDEGFKPSSGTVQ CCCCCCCCCCCCCEE		-
715	Phosphorylation	VVALKELSIRGDFRT HHHHHHHCCCCCHHH		18779572
743	Phosphorylation	FQNNDIDTGWLDHLI HCCCCCCCCHHHHHH		-
851	Phosphorylation	DGGLLLSYNGSSYTT CCCEEEEECCCCCEE		51457785
867	Phosphorylation	MKEEVDSYRITIGNK EECCCCEEEEEECCE		22802335
870	Phosphorylation	EVDSYRITIGNKTCV CCCEEEEEECCEEEE		22802335
891	Phosphorylation	PTVLRSPSAGKLMQY CCEEECCCCCCCEEE		30352176
919	Biotinylation	YAEMEVMKMIMTLNV CHHHHHHHHHHCCCC		-
919	N6-biotinyllysine	YAEMEVMKMIMTLNV CHHHHHHHHHHCCCC		-
936	Malonylation	SGRVKYIKRPGVILE CCCEEEECCCEEEEE		26320211
1049	Ubiquitination	RIPAPVEKAVRRVMA CCCHHHHHHHHHHHH		22790023
1155	Phosphorylation	EQFKPDMTQVLDCIF HHHCCCHHHHHHHHH		51457793
1235	Phosphorylation	LRHNQVESIFLSAID CCCCHHHHHHHHHHH		-
1239	Phosphorylation	QVESIFLSAIDMYGH HHHHHHHHHHHHHCC		-
1244	Phosphorylation	FLSAIDMYGHQFCPE HHHHHHHHCCCCCCH		-
1330	Phosphorylation	NRMAVPISVSNPDLL CCEEEEEEECCHHHH		25521595
1332	Phosphorylation	MAVPISVSNPDLLRH EEEEEEECCHHHHHH		25521595
1340	Phosphorylation	NPDLLRHSTELFMDS CHHHHHHHHHHHHCC		25521595
1341	Phosphorylation	PDLLRHSTELFMDSG HHHHHHHHHHHHCCC		25521595
1347	Phosphorylation	STELFMDSGFSPLCQ HHHHHHCCCCHHHHH		21183079
1350	Phosphorylation	LFMDSGFSPLCQRMG HHHCCCCHHHHHHHH		22817900
1395	Phosphorylation	LFSKACTSLYSEEDS HHCHHHHHCCCHHHH		25521595
1403	Ubiquitination	LYSEEDSKSLREEPI CCCHHHHHHHHHCCE		22790023
1518	Acetylation	HLYLGAAKVKEGLEV EEEEECEECCCCCEE		19865905
1520	Ubiquitination	YLGAAKVKEGLEVTD EEECEECCCCCEECC		22790023
1629	Phosphorylation	VKINIRQTTSDSAIP EEEEEEECCCCCCCE		15632237
1631	Phosphorylation	INIRQTTSDSAIPIR EEEEECCCCCCCEEE		15632249
1642	Phosphorylation	IPIRLFITNESGYYL CEEEEEEECCCCEEE		15632261
1695	Ubiquitination	TKDLLQAKRFQAQSL CHHHHHHHHHHHHHC		22790023
1720	Ubiquitination	MFRQALFKLWGSPEK HHHHHHHHHHCCCCC		22790023
1727	Ubiquitination	KLWGSPEKYPKDILT HHHCCCCCCCCCHHH		22790023
1809	Phosphorylation	RASEMARTEGIPQIY HHHHHHHCCCCCCEE		25777480
1816	Phosphorylation	TEGIPQIYLAANSGA CCCCCCEEHHHCCCC		25777480
1821	Phosphorylation	QIYLAANSGARMGLA CEEHHHCCCCCCCHH		25777480
1847	Ubiquitination	VDPEDPHKGFRYLYL CCCCCCCCCEEEEEE		22790023
1871	Ubiquitination	SQNSVHCKHIEDEGE CCCCEEEEECCCCCC		22790023
1889	Ubiquitination	VIVDVIGKDANLGVE EEEEEEECCCCCCCC		22790023
1945	Phosphorylation	RVIQVENSHIILTGA CEEEEECCEEEEECH		22871156
2030	Ubiquitination	EIEFTPTKAPYDPRW CCCCCCCCCCCCCCC		22790023
2107	Phosphorylation	ADPANLDSEAKIIQQ CCCCCCCHHHHHHHH		21183079
2155	Ubiquitination	RGFSGGMKDMYEQML CCCCCCHHHHHHHHH		22790023
2228	Ubiquitination	PEGTVEIKFRKKDLV CCCEEEEEECHHHHH		22790023
2228	Acetylation	PEGTVEIKFRKKDLV CCCEEEEEECHHHHH		66699553
2247	Ubiquitination	RIDPVCKKLVGQLGK HHCHHHHHHHHHHHH		22790023
2270	Malonylation	KELEGQLKAREELLL HHHHHHHHHHHHHHH		26320211
2397	Ubiquitination	RENINYLKRDSVLKT HHHHHHHHHHHHHHH		22790023
2440	Phosphorylation	IQVAQLLSTTESPAS HHHHHHHHCCCCCCC		29472430
2441	Phosphorylation	QVAQLLSTTESPASS HHHHHHHCCCCCCCC		29472430
2442	Phosphorylation	VAQLLSTTESPASS- HHHHHHCCCCCCCC-		29472430
2444	Phosphorylation	QLLSTTESPASS--- HHHHCCCCCCCC---		27180971
2447	Phosphorylation	STTESPASS------ HCCCCCCCC------		30352176
2448	Phosphorylation	TTESPASS------- CCCCCCCC-------		22324799

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
212	S	Phosphorylation	Kinase	AMPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
212	S	Phosphorylation	Phosphorylated by AMPK at Ser-212 inactivates the enzyme.	24913514

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ACACB_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ACACB_MOUSE !!

Drug and Disease Associations

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