| UniProt ID | ACC1_ARATH | |
|---|---|---|
| UniProt AC | Q38970 | |
| Protein Name | Acetyl-CoA carboxylase 1 | |
| Gene Name | ACC1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 2254 | |
| Subcellular Localization | Cytoplasm, cytosol . | |
| Protein Description | Multifunctional enzyme that catalyzes the carboxylation of acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty acid synthesis and in the cytosol in various biosynthetic pathways including fatty acid elongation. Required for very long chain fatty acids elongation. Necessary for embryo and plant development. Plays a central function in embryo morphogenesis, especially in apical meristem development. Involved in cell proliferation and tissue patterning. May act as a repressor of cytokinin response.. | |
| Protein Sequence | MAGSVNGNHSAVGPGINYETVSQVDEFCKALRGKRPIHSILIANNGMAAVKFIRSVRTWAYETFGTEKAILLVGMATPEDMRINAEHIRIADQFVEVPGGTNNNNYANVQLIVEMAEVTRVDAVWPGWGHASENPELPDALDAKGIIFLGPPASSMAALGDKIGSSLIAQAADVPTLPWSGSHVKIPPNSNLVTIPEEIYRQACVYTTEEAIASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGSPIFIMKVASQSRHLEVQLLCDKHGNVSALHSRDCSVQRRHQKIIEEGPITVAPPETVKKLEQAARRLAKSVNYVGAATVEYLYSMDTGEYYFLELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLWQIPEIRRFYGIEHGGGYDSWRKTSVVAFPFDFDKAQSIRPKGHCVAVRVTSEDPDDGFKPTSGRVQELSFKSKPNVWAYFSVKSGGGIHEFSDSQFGHVFAFGESRALAIANMVLGLKEIQIRGEIRTNVDYTIDLLHASDYRDNKIHTGWLDSRIAMRVRAERPPWYLSVVGGALYKASATSAAVVSDYVGYLEKGQIPPKHISLVHSQVSLNIEGSKYTIDVVRGGSGTYRLRMNKSEVVAEIHTLRDGGLLMQLDGKSHVIYAEEEAAGTRLLIDGRTCLLQNDHDPSKLMAETPCKLMRYLISDNSNIDADTPYAEVEVMKMCMPLLSPASGVIHFKMSEGQAMQAGELIANLDLDDPSAVRKAEPFHGSFPRLGLPTAISGRVHQRCAATLNAARMILAGYEHKVDEVVQDLLNCLDSPELPFLQWQECFAVLATRLPKNLRNMLESKYREFESISRNSLTTDFPAKLLKGILEAHLSSCDEKERGALERLIEPLMSLAKSYEGGRESHARVIVHSLFEEYLSVEELFNDNMLADVIERMRQLYKKDLLKIVDIVLSHQGIKNKNKLVLRLMEQLVYPNPAAYRDKLIRFSTLNHTNYSELALKASQLLEQTKLSELRSNIARSLSELEMFTEDGENMDTPKRKSAINERIEDLVSASLAVEDALVGLFDHSDHTLQRRVVETYIRRLYQPYVVKDSVRMQWHRSGLLASWEFLEEHMERKNIGLDDPDTSEKGLVEKRSKRKWGAMVIIKSLQFLPSIISAALRETKHNDYETAGAPLSGNMMHIAIVGINNQMSLLQDSGDEDQAQERVNKLAKILKEEEVSSSLCSAGVGVISCIIQRDEGRTPMRHSFHWSLEKQYYVEEPLLRHLEPPLSIYLELDKLKGYSNIQYTPSRDRQWHLYTVTDKPVPIKRMFLRSLVRQATMNDGFILQQGQDKQLSQTLISMAFTSKCVLRSLMDAMEELELNAHNAAMKPDHAHMFLCILREQQIDDLVPFPRRVEVNAEDEETTVEMILEEAAREIHRSVGVRMHRLGVCEWEVRLWLVSSGLACGAWRVVVANVTGRTCTVHIYREVETPGRNSLIYHSITKKGPLHETPISDQYKPLGYLDRQRLAARRSNTTYCYDFPLAFGTALELLWASQHPGVKKPYKDTLINVKELVFSKPEGSSGTSLDLVERPPGLNDFGMVAWCLDMSTPEFPMGRKLLVIANDVTFKAGSFGPREDAFFLAVTELACAKKLPLIYLAANSGARLGVAEEVKACFKVGWSDEISPENGFQYIYLSPEDHERIGSSVIAHEVKLSSGETRWVIDTIVGKEDGIGVENLTGSGAIAGAYSKAYNETFTLTFVSGRTVGIGAYLARLGMRCIQRLDQPIILTGFSTLNKLLGREVYSSHMQLGGPKIMGTNGVVHLTVSDDLEGVSAILNWLSYIPAYVGGPLPVLAPLDPPERIVEYVPENSCDPRAAIAGVKDNTGKWLGGIFDKNSFIETLEGWARTVVTGRAKLGGIPVGVVAVETQTVMQIIPADPGQLDSHERVVPQAGQVWFPDSAAKTAQALMDFNREELPLFILANWRGFSGGQRDLFEGILQAGSTIVENLRTYRQPVFVYIPMMGELRGGAWVVVDSQINSDYVEMYADETARGNVLEPEGTIEIKFRTKELLECMGRLDQKLISLKAKLQDAKQSEAYANIELLQQQIKAREKQLLPVYIQIATKFAELHDTSMRMAAKGVIKSVVEWSGSRSFFYKKLNRRIAESSLVKNVREASGDNLAYKSSMRLIQDWFCNSDIAKGKEEAWTDDQVFFTWKDNVSNYELKLSELRAQKLLNQLAEIGNSSDLQALPQGLANLLNKVEPSKREELVAAIRKVLG | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 711 | N6-biotinyllysine | YAEVEVMKMCMPLLS CHHHHHHHHHHHHCC | 33.84 | - | |
| 711 | Biotinylation | YAEVEVMKMCMPLLS CHHHHHHHHHHHHCC | 33.84 | - | |
| 1006 | Phosphorylation | LLEQTKLSELRSNIA HHHHHHHHHHHHHHH | 35.82 | 24243849 | |
| 1017 | Phosphorylation | SNIARSLSELEMFTE HHHHHHHHHHHHHCC | 41.19 | 27643528 | |
| 1023 | Phosphorylation | LSELEMFTEDGENMD HHHHHHHCCCCCCCC | 31.68 | 23776212 | |
| 1031 | Phosphorylation | EDGENMDTPKRKSAI CCCCCCCCHHHHHHH | 21.68 | 23776212 | |
| 1192 | Phosphorylation | QMSLLQDSGDEDQAQ HHHHHHCCCCHHHHH | 34.87 | 27531888 | |
| 2143 | Phosphorylation | NRRIAESSLVKNVRE HHHHHHHHHHHHHHH | 28.78 | 25561503 | |
| 2203 | Phosphorylation | SNYELKLSELRAQKL CCCEEEHHHHHHHHH | 32.76 | 24243849 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ACC1_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACC1_ARATH !! | ||||||
* 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 ACC1_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ACC1_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1031 AND SER-1192, ANDIDENTIFICATION BY MASS SPECTROMETRY. | |
