Basic Information
Name | Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)] |
Uniprot ID | P32874 |
Systematic gene name | YMR207C |
Standard gene name | HFA1 |
Gene names | HFA1 YMR207C YM8261.01C YM8325.08C |
Description from SGD | YMR207C HFA1 SGDID:S000004820, Chr XIII from 683564-677193, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon" |
Protein length | 2273 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT
GSQIVRLKGQ RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK
HTRLPPQFIG LNTVESAQPS ILRDFVDLRG GHTVISKILI ANNGIAAVKE
MRSIRKWAYE TFNDEKIIQF VVMATPDDLH ANSEYIRMAD QYVQVPGGTN
NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA SSQRKILFIG
PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD
DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNEDDFIAL
YRQAVNETPG SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR
HQKIIEEAPV TITKPETFQR MERAAIRLGE LVGYVSAGTV EYLYSPKDDK
FYFLELNPRL QVEHPTTEMI SGVNLPATQL QIAMGIPMHM ISDIRKLYGL
DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST GKIHELNFRS
SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI
RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI
ICGAAMKAYV FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL
FNVAQSSEEQ FILSINKSQC EVNVQKLSSD CLLISVDGKC HTVYWKDDIR
GTRLSIDSNT IFLEAELNPT QVISPTPGKL VKYLVRSGDH VFAGQQYAEI
EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS PSKANESSLY
RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK
ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM
KRYLEENTND HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE
KIFENHDIHE ERNLLNLRRK DLTNLKKILC ISLSHANVVA KNKLVTAILH
EYEPLCQDSS KMSLKFRAVI HDLASLESKW AKEVAVKARS VLLRGIFPPI
KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH SNLIQLQDLF
FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
NYLVNSDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV
YEQIHIPEER LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS
KLKVNRITFA FIAANAPAVK FYSFDGTTYD EISQIRNMDP SYEAPLELGK
MSNYKIRSLP TYDSSIRIFE GISKFTPLDK RFFVRKIINS FMYNDQKTTE
ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN IPVHRLEEIV
STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI
ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG
TTYVYDFPGL FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR
EPGLNNIGMV AFEIMVQTPE YPEGRNMIVI SNDITYNIGS FGPREDLFFD
RVTNYARERG IPRIYLAANS GAKLGIAEEL IPLFRVAWND PSDPTKGFQY
LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG FEEGLGVECL
QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII
LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT
WLSYVPAKRD MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN
NFQSGLFDKD SFFETLSGWA KGVIVGRARL GGIPVGVIAV ETKTIEEIIP
ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ TINDFNYGEQ LPLIILANWR
GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE LRGGSWVVID
PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL
RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML
VKGVIRNELE WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD
LLKIVQSWYN DLDVNDDRAV VEFIERNSKK IDKNIEEFEI SLLIDELKKK
FEDRRGNIVL EELTRLVDSK RKR
GSQIVRLKGQ RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK
HTRLPPQFIG LNTVESAQPS ILRDFVDLRG GHTVISKILI ANNGIAAVKE
MRSIRKWAYE TFNDEKIIQF VVMATPDDLH ANSEYIRMAD QYVQVPGGTN
NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA SSQRKILFIG
PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD
DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNEDDFIAL
YRQAVNETPG SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR
HQKIIEEAPV TITKPETFQR MERAAIRLGE LVGYVSAGTV EYLYSPKDDK
FYFLELNPRL QVEHPTTEMI SGVNLPATQL QIAMGIPMHM ISDIRKLYGL
DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST GKIHELNFRS
SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI
RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI
ICGAAMKAYV FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL
FNVAQSSEEQ FILSINKSQC EVNVQKLSSD CLLISVDGKC HTVYWKDDIR
GTRLSIDSNT IFLEAELNPT QVISPTPGKL VKYLVRSGDH VFAGQQYAEI
EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS PSKANESSLY
RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK
ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM
KRYLEENTND HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE
KIFENHDIHE ERNLLNLRRK DLTNLKKILC ISLSHANVVA KNKLVTAILH
EYEPLCQDSS KMSLKFRAVI HDLASLESKW AKEVAVKARS VLLRGIFPPI
KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH SNLIQLQDLF
FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
NYLVNSDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV
YEQIHIPEER LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS
KLKVNRITFA FIAANAPAVK FYSFDGTTYD EISQIRNMDP SYEAPLELGK
MSNYKIRSLP TYDSSIRIFE GISKFTPLDK RFFVRKIINS FMYNDQKTTE
ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN IPVHRLEEIV
STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI
ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG
TTYVYDFPGL FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR
EPGLNNIGMV AFEIMVQTPE YPEGRNMIVI SNDITYNIGS FGPREDLFFD
RVTNYARERG IPRIYLAANS GAKLGIAEEL IPLFRVAWND PSDPTKGFQY
LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG FEEGLGVECL
QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII
LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT
WLSYVPAKRD MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN
NFQSGLFDKD SFFETLSGWA KGVIVGRARL GGIPVGVIAV ETKTIEEIIP
ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ TINDFNYGEQ LPLIILANWR
GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE LRGGSWVVID
PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL
RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML
VKGVIRNELE WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD
LLKIVQSWYN DLDVNDDRAV VEFIERNSKK IDKNIEEFEI SLLIDELKKK
FEDRRGNIVL EELTRLVDSK RKR
Legend
- X Ubiquitination
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[262, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[310, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[865, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[865, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[865, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1214, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[1358, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[1358, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1358, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1361, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[1362, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[1364, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[1364, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1364, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1365, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[1528, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1528, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1853, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1853, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |