Basic Information
Name | Glycogen debranching enzyme (Glycogen debrancher) [Includes: 4-alpha-glucanotransferase (EC 2.4.1.25) (Oligo-1,4-1,4-glucantransferase); Amylo-alpha-1,6-glucosidase (Amylo-1,6-glucosidase) (EC 3.2.1.33) (Dextrin 6-alpha-D-glucosidase)] |
Uniprot ID | Q06625 |
Systematic gene name | YPR184W |
Standard gene name | GDB1 |
Gene names | GDB1 YPR184W |
Description from SGD | YPR184W GDB1 SGDID:S000006388, Chr XVI from 902044-906654, Genome Release 64-3-1, Verified ORF, "Glycogen debranching enzyme; contains glucanotranferase and alpha-1,6-amyloglucosidase activities; required for glycogen degradation; phosphorylated in mitochondria; activity is inhibited by Igd1p; protein abundance increases in response to DNA replication stress" |
Protein length | 1536 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNRSLLLRLS DTGEPITSCS YGKGVLTLPP IPLPKDAPKD QPLYTVKLLV
SAGSPVARDG LVWTNCPPDH NTPFKRDKFY KKIIHSSFHE DDCIDLNVYA
PGSYCFYLSF RNDNEKLETT RKYYFVALPM LYINDQFLPL NSIALQSVVS
KWLGSDWEPI LSKIAAKNYN MVHFTPLQER GESNSPYSIY DQLQFDQEHF
KSPEDVKNLV EHIHRDLNML SLTDIVFNHT ANNSPWLVEH PEAGYNHITA
PHLISAIELD QELLNFSRNL KSWGYPTELK NIEDLFKIMD GIKVHVLGSL
KLWEYYAVNV QTALRDIKAH WNDESNESYS FPENIKDISS DFVKLASFVK
DNVTEPNFGT LGERNSNRIN VPKFIQLLKL INDGGSDDSE SSLATAQNIL
NEVNLPLYRE YDDDVSEILE QLFNRIKYLR LDDGGPKQGP VTVDVPLTEP
YFTRFKGKDG TDYALANNGW IWNGNPLVDF ASQNSRAYLR REVIVWGDCV
KLRYGKSPED SPYLWERMSK YIEMNAKIFD GFRIDNCHST PIHVGEYFLD
LARKYNPNLY VVAELFSGSE TLDCLFVERL GISSLIREAM QAWSEEELSR
LVHKHGGRPI GSYKFVPMDD FSYPADINLN EEHCFNDSND NSIRCVSEIM
IPKILTATPP HALFMDCTHD NETPFEKRTV EDTLPNAALV ALCSSAIGSV
YGYDEIFPHL LNLVTEKRHY DISTPTGSPS IGITKVKATL NSIRTSIGEK
AYDIEDSEMH VHHQGQYITF HRMDVKSGKG WYLIARMKFS DNDDPNETLP
PVVLNQSTCS LRFSYALERV GDEIPNDDKF IKGIPTKLKE LEGFDISYDD
SKKISTIKLP NEFPQGSIAI FETQQNGVDE SLDHFIRSGA LKATSSLTLE
SINSVLYRSE PEEYDVSAGE GGAYIIPNFG KPVYCGLQGW VSVLRKIVFY
NDLAHPLSAN LRNGHWALDY TISRLNYYSD EAGINEVQNW LRSRFDRVKK
LPSYLVPSYF ALIIGILYGC CRLKAIQLMS RNIGKSTLFV QSLSMTSIQM
VSRMKSTSIL PGENVPSMAA GLPHFSVNYM RCWGRDVFIS LRGMLLTTGR
FDEAKAHILA FAKTLKHGLI PNLLDAGRNP RYNARDAAWF FLQAVQDYVY
IVPDGEKILQ EQVTRRFPLD DTYIPVDDPR AFSYSSTLEE IIYEILSRHA
KGIKFREANA GPNLDRVMTD KGFNVEIHVD WSTGLIHGGS QYNCGTWMDK
MGESEKAGSV GIPGTPRDGA AIEINGLLKS ALRFVIELKN KGLFKFSDVE
TQDGGRIDFT EWNQLLQDNF EKRYYVPEDP SQDADYDVSA KLGVNRRGIY
RDLYKSGKPY EDYQLRPNFA IAMTVAPELF VPEHAIKAIT IADEVLRGPV
GMRTLDPSDY NYRPYYNNGE DSDDFATSKG RNYHQGPEWV WLYGYFLRAF
HHFHFKTSPR CQNAAKEKPS SYLYQQLYYR LKGHRKWIFE SVWAGLTELT
NKDGEVCNDS SPTQAWSSAC LLDLFYDLWD AYEDDS
SAGSPVARDG LVWTNCPPDH NTPFKRDKFY KKIIHSSFHE DDCIDLNVYA
PGSYCFYLSF RNDNEKLETT RKYYFVALPM LYINDQFLPL NSIALQSVVS
KWLGSDWEPI LSKIAAKNYN MVHFTPLQER GESNSPYSIY DQLQFDQEHF
KSPEDVKNLV EHIHRDLNML SLTDIVFNHT ANNSPWLVEH PEAGYNHITA
PHLISAIELD QELLNFSRNL KSWGYPTELK NIEDLFKIMD GIKVHVLGSL
KLWEYYAVNV QTALRDIKAH WNDESNESYS FPENIKDISS DFVKLASFVK
DNVTEPNFGT LGERNSNRIN VPKFIQLLKL INDGGSDDSE SSLATAQNIL
NEVNLPLYRE YDDDVSEILE QLFNRIKYLR LDDGGPKQGP VTVDVPLTEP
YFTRFKGKDG TDYALANNGW IWNGNPLVDF ASQNSRAYLR REVIVWGDCV
KLRYGKSPED SPYLWERMSK YIEMNAKIFD GFRIDNCHST PIHVGEYFLD
LARKYNPNLY VVAELFSGSE TLDCLFVERL GISSLIREAM QAWSEEELSR
LVHKHGGRPI GSYKFVPMDD FSYPADINLN EEHCFNDSND NSIRCVSEIM
IPKILTATPP HALFMDCTHD NETPFEKRTV EDTLPNAALV ALCSSAIGSV
YGYDEIFPHL LNLVTEKRHY DISTPTGSPS IGITKVKATL NSIRTSIGEK
AYDIEDSEMH VHHQGQYITF HRMDVKSGKG WYLIARMKFS DNDDPNETLP
PVVLNQSTCS LRFSYALERV GDEIPNDDKF IKGIPTKLKE LEGFDISYDD
SKKISTIKLP NEFPQGSIAI FETQQNGVDE SLDHFIRSGA LKATSSLTLE
SINSVLYRSE PEEYDVSAGE GGAYIIPNFG KPVYCGLQGW VSVLRKIVFY
NDLAHPLSAN LRNGHWALDY TISRLNYYSD EAGINEVQNW LRSRFDRVKK
LPSYLVPSYF ALIIGILYGC CRLKAIQLMS RNIGKSTLFV QSLSMTSIQM
VSRMKSTSIL PGENVPSMAA GLPHFSVNYM RCWGRDVFIS LRGMLLTTGR
FDEAKAHILA FAKTLKHGLI PNLLDAGRNP RYNARDAAWF FLQAVQDYVY
IVPDGEKILQ EQVTRRFPLD DTYIPVDDPR AFSYSSTLEE IIYEILSRHA
KGIKFREANA GPNLDRVMTD KGFNVEIHVD WSTGLIHGGS QYNCGTWMDK
MGESEKAGSV GIPGTPRDGA AIEINGLLKS ALRFVIELKN KGLFKFSDVE
TQDGGRIDFT EWNQLLQDNF EKRYYVPEDP SQDADYDVSA KLGVNRRGIY
RDLYKSGKPY EDYQLRPNFA IAMTVAPELF VPEHAIKAIT IADEVLRGPV
GMRTLDPSDY NYRPYYNNGE DSDDFATSKG RNYHQGPEWV WLYGYFLRAF
HHFHFKTSPR CQNAAKEKPS SYLYQQLYYR LKGHRKWIFE SVWAGLTELT
NKDGEVCNDS SPTQAWSSAC LLDLFYDLWD AYEDDS
Legend
- X Phoshorylation
- X Monomethylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[45, Phos] | Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications) |
[45, 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) |
[45, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[51, 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) |
[54, 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) |
[155, 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) |
[155, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[162, 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) |
[162, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[350, Mono-CH3] | Wang, K., Zhou, Y.J., Liu, H., Cheng, K., Mao, J., Wang, F., Liu, W., Ye, M., Zhao, Z.K., Zou, H. (2015). Proteomic analysis of protein methylation in the yeast Saccharomyces cerevisiae. J Proteomics 114: 226-233. (Publication) (All modifications) |
[723, 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) |
[724, 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) |
[724, 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) |
[724, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[726, 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) |
[728, 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) |
[1256, 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) |
[1259, 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) |
[1265, 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) |
[1265, 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) |
[1265, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |