Basic Information
Name | Serine/threonine-protein kinase VPS15 (EC 2.7.11.1) (Golgi-retention defective mutant protein 8) (Vacuolar protein sorting-associated protein 15) |
Uniprot ID | P22219 |
Systematic gene name | YBR097W |
Standard gene name | VPS15 |
Gene names | VPS15 GRD8 VAC4 VPL19 YBR097W YBR0825 |
Description from SGD | YBR097W VPS15 SGDID:S000000301, Chr II from 436951-441315, Genome Release 64-3-1, Verified ORF, "Serine/threonine protein kinase involved in vacuolar protein sorting; functions as a membrane-associated complex with Vps34p; active form recruits Vps34p to the Golgi membrane; interacts with the GDP-bound form of Gpa1p; myristoylated; a fraction is localized, with Vps34p, to nuclear pores at nucleus-vacuole junctions and may facilitate transcription elongation for genes positioned at the nuclear periphery" |
Protein length | 1454 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MGAQLSLVVQ ASPSIAIFSY IDVLEEVHYV SQLNSSRFLK TCKALDPNGE
IVIKVFIKPK DQYSLRPFLQ RIRAQSFKLG QLPHVLNYSK LIETNRAGYM
IRQHLKNNLY DRLSLRPYLQ DIELKFIAFQ LLNALKDIHN LNIVHGDIKT
ENILVTSWNW CILTDFAAFI KPVYLPEDNP GEFLFYFDTS KRRTCYLAPE
RFNSKLYQDG KSNNGRLTKE MDIFSLGCVI AEIFAEGRPI FNLSQLFKYK
SNSYDVNREF LMEEMNSTDL RNLVLDMIQL DPSKRLSCDE LLNKYRGIFF
PDYFYTFIYD YFRNLVTMTT STPISDNTCT NSTLEDNVKL LDETTEKIYR
DFSQICHCLD FPLIKDGGEI GSDPPILESY KIEIEISRFL NTNLYFPQNY
HLVLQQFTKV SEKIKSVKEE CALLFISYLS HSIRSIVSTA TKLKNLELLA
VFAQFVSDEN KIDRVVPYFV CCFEDSDQDV QALSLLTLIQ VLTSVRKLNQ
LNENIFVDYL LPRLKRLLIS NRQNTNYLRI VFANCLSDLA IIINRFQEFT
FAQHCNDNSM DNNTEIMESS TKYSAKLIQS VEDLTVSFLT DNDTYVKMAL
LQNILPLCKF FGRERTNDII LSHLITYLND KDPALRVSLI QTISGISILL
GTVTLEQYIL PLLIQTITDS EELVVISVLQ SLKSLFKTGL IRKKYYIDIS
KTTSPLLLHP NNWIRQFTLM IIIEIINKLS KAEVYCILYP IIRPFFEFDV
EFNFKSMISC CKQPVSRSVY NLLCSWSVRA SKSLFWKKII TNHVDSFGNN
RIEFITKNYS SKNYGFNKRD TKSSSSLKGI KTSSTVYSHD NKEIPLTAED
RNWIDKFHII GLTEKDIWKI VALRGYVIRT ARVMAANPDF PYNNSNYRPL
VQNSPPNLNL TNIMPRNIFF DVEFAEESTS EGQDSNLENQ QIYKYDESEK
DSNKLNINGS KQLSTVMDIN GSLIFKNKSI ATTTSNLKNV FVQLEPTSYH
MHSPNHGLKD NANVKPERKV VVSNSYEGDV ESIEKFLSTF KILPPLRDYK
EFGPIQEIVR SPNMGNLRGK LIATLMENEP NSITSSAVSP GETPYLITGS
DQGVIKIWNL KEIIVGEVYS SSLTYDCSST VTQITMIPNF DAFAVSSKDG
QIIVLKVNHY QQESEVKFLN CECIRKINLK NFGKNEYAVR MRAFVNEEKS
LLVALTNLSR VIIFDIRTLE RLQIIENSPR HGAVSSICID EECCVLILGT
TRGIIDIWDI RFNVLIRSWS FGDHAPITHV EVCQFYGKNS VIVVGGSSKT
FLTIWNFVKG HCQYAFINSD EQPSMEHFLP IEKGLEELNF CGIRSLNALS
TISVSNDKIL LTDEATSSIV MFSLNELSSS KAVISPSRFS DVFIPTQVTA
NLTMLLRKMK RTSTHSVDDS LYHHDIINSI STCEVDETPL LVACDNSGLI
GIFQ
IVIKVFIKPK DQYSLRPFLQ RIRAQSFKLG QLPHVLNYSK LIETNRAGYM
IRQHLKNNLY DRLSLRPYLQ DIELKFIAFQ LLNALKDIHN LNIVHGDIKT
ENILVTSWNW CILTDFAAFI KPVYLPEDNP GEFLFYFDTS KRRTCYLAPE
RFNSKLYQDG KSNNGRLTKE MDIFSLGCVI AEIFAEGRPI FNLSQLFKYK
SNSYDVNREF LMEEMNSTDL RNLVLDMIQL DPSKRLSCDE LLNKYRGIFF
PDYFYTFIYD YFRNLVTMTT STPISDNTCT NSTLEDNVKL LDETTEKIYR
DFSQICHCLD FPLIKDGGEI GSDPPILESY KIEIEISRFL NTNLYFPQNY
HLVLQQFTKV SEKIKSVKEE CALLFISYLS HSIRSIVSTA TKLKNLELLA
VFAQFVSDEN KIDRVVPYFV CCFEDSDQDV QALSLLTLIQ VLTSVRKLNQ
LNENIFVDYL LPRLKRLLIS NRQNTNYLRI VFANCLSDLA IIINRFQEFT
FAQHCNDNSM DNNTEIMESS TKYSAKLIQS VEDLTVSFLT DNDTYVKMAL
LQNILPLCKF FGRERTNDII LSHLITYLND KDPALRVSLI QTISGISILL
GTVTLEQYIL PLLIQTITDS EELVVISVLQ SLKSLFKTGL IRKKYYIDIS
KTTSPLLLHP NNWIRQFTLM IIIEIINKLS KAEVYCILYP IIRPFFEFDV
EFNFKSMISC CKQPVSRSVY NLLCSWSVRA SKSLFWKKII TNHVDSFGNN
RIEFITKNYS SKNYGFNKRD TKSSSSLKGI KTSSTVYSHD NKEIPLTAED
RNWIDKFHII GLTEKDIWKI VALRGYVIRT ARVMAANPDF PYNNSNYRPL
VQNSPPNLNL TNIMPRNIFF DVEFAEESTS EGQDSNLENQ QIYKYDESEK
DSNKLNINGS KQLSTVMDIN GSLIFKNKSI ATTTSNLKNV FVQLEPTSYH
MHSPNHGLKD NANVKPERKV VVSNSYEGDV ESIEKFLSTF KILPPLRDYK
EFGPIQEIVR SPNMGNLRGK LIATLMENEP NSITSSAVSP GETPYLITGS
DQGVIKIWNL KEIIVGEVYS SSLTYDCSST VTQITMIPNF DAFAVSSKDG
QIIVLKVNHY QQESEVKFLN CECIRKINLK NFGKNEYAVR MRAFVNEEKS
LLVALTNLSR VIIFDIRTLE RLQIIENSPR HGAVSSICID EECCVLILGT
TRGIIDIWDI RFNVLIRSWS FGDHAPITHV EVCQFYGKNS VIVVGGSSKT
FLTIWNFVKG HCQYAFINSD EQPSMEHFLP IEKGLEELNF CGIRSLNALS
TISVSNDKIL LTDEATSSIV MFSLNELSSS KAVISPSRFS DVFIPTQVTA
NLTMLLRKMK RTSTHSVDDS LYHHDIINSI STCEVDETPL LVACDNSGLI
GIFQ
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
[205, 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) |
[211, 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) |
[826, 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) |
[904, 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) |
[904, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[1003, 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) |
[1032, 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) |