Basic Information

NameProtein CSF1 (Cold sensitive for fermentation protein 1)
Uniprot IDQ12150
Systematic gene nameYLR087C
Standard gene nameCSF1
Gene namesCSF1 YLR087C
Description from SGDYLR087C CSF1 SGDID:S000004077, Chr XII from 315731-306855, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein required for fermentation at low temperature; plays a role in the maturation of secretory proteins; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies"
Protein length2958
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MEAISQLRGV PLTHQKDFSW VFLVDWILTV VVCLTMIFYM GRIYAYLVSF
ILEWLLWKRA KIKINVETLR VSLLGGRIHF KNLSVIHKDY TISVLEGSLT
WKYWLLNCRK AELIENNKSS SGKKAKLPCK ISVECEGLEI FIYNRTVAYD
NVINLLSKDE RDKFEKYLNE HSFPEPFSDG SSADKLDEDL SESAYTTNSD
ASIVNDRDYQ ETDIGKHPKL LMFLPIELKF SRGSLLLGNK FTPSVMILSY
ESGKGIIDVL PPKERLDLYR NKTQMEFKNF EISIKQNIGY DDAIGLKFKI
DRGKVSKLWK TFVRVFQIVT KPVVPKKTKK SAGTSDDNFY HKWKGLSLYK
ASAGDAKASD LDDVEFDLTN HEYAKFTSIL KCPKVTIAYD VDVPGVVPHG
AHPTIPDIDG PDVGNNGAPP DFALDVQIHG GSICYGPWAQ RQVSHLQRVL
SPVVSRTAKP IKKLPPGSRR IYTLFRMNIS IMEDTTWRIP TRESSKDPEF
LKHYKETNEE YRPFGWMDLR FCKDTYANFN ISVCPTVQGF QNNFHVHFLE
TEIRSSVNHD ILLKSKVFDI DGDIGYPLGW NSKAIWIINM KSEQLEAFLL
REHITLVADT LSDFSAGDPT PYELFRPFVY KVNWEMEGYS IYLNVNDHNI
VNNPLDFNEN CYLSLHGDKL SIDVTVPRES ILGTYTDMSY EISTPMFRMM
LNTPPWNTLN EFMKHKEVGR AYDFTIKGSY LLYSELDIDN VDTLVIECNS
KSTVLHCYGF VMRYLTNVKM NYFGEFFNFV TSEEYTGVLG AREVGDVTTK
SSVADLASTV DSGYQNSSLK NESEDKGPMK RSDLKRTTNE TDIWFTFSVW
DGALILPETI YSFDPCIALH FAELVVDFRS CNYYMDIMAV LNGTSIKRHV
SKQINEVFDF IRRNNGADEQ EHGLLSDLTI HGHRMYGLPP TEPTYFCQWD
INLGDLCIDS DIEFIKGFFN SFYKIGFGYN DLENILLYDT ETINDMTSLT
VHVEKIRIGL KDPVMKSQSV ISAESILFTL IDFENEKYSQ RIDVKIPKLT
ISLNCVMGDG VDTSFLKFET KLRFTNFEQY KDIDKKRSEQ RRYITIHDSP
YHRCPFLLPL FYQDSDTYQN LYGAIAPSSS IPTLPLPTLP DTIDYIIEDI
VGEYATLLET TNPFKNIFAE TPSTMEPSRA SFSEDDNDEE ADPSSFKPVA
FTEDRNHERD NYVVDVSYIL LDVDPLLFIF AKSLLEQLYS ENMVQVLDDI
EIGIVKRLSN LQEGITSISN IDIHIAYLNL IWQETGEEGF ELYLDRIDYQ
MSEKSLEKNR TNKLLEVAAL AKVKTVRVTV NQKKNPDLSE DRPPALSLGI
EGFEVWSSTE DRQVNSLNLT SSDITIDESQ MEWLFEYCSD QGNLIQEVCT
SFNSIQNTRS NSKTELISKL TAASEYYQIS HDPYVITKPA FIMRLSKGHV
RENRSWKIIT RLRHILTYLP DDWQSNIDEV LKEKKYTSAK DAKNIFMSVF
STWRNWEFSD VARSYIYGKL FTAENEKHKQ NLIKKLLKCT MGSFYLTVYG
EGYEVEHNFV VADANLVVDL TPPVTSLPSN REETIEITGR VGSVKGKFSD
RLLKLQDLIP LIAAVGEDDK SDPKKELSKQ FKMNTVLLVD KSELQLVMDQ
TKLMSRTVGG RVSLLWENLK DSTSQAGSLV IFSQKSEVWL KHTSVILGEA
QLRDFSVLAT TEAWSHKPTI LINNQCADLH FRAMSSTEQL VTAITEIRES
LMMIKERIKF KPKSKKKSQF VDQKINTVLS CYFSNVSSEV MPLSPFYIRH
EAKQLDIYFN KFGSNEILLS IWDTDFFMTS HQTKEQYLRF SFGDIEIKGG
ISREGYSLIN VDISISMIKL TFSEPRRIVN SFLQDEKLAS QGINLLYSLK
PLFFSSNLPK KEKQAPSIMI NWTLDTSITY FGVLVPVAST YFVFELHMLL
LSLTNTNNGM LPEETKVTGQ FSIENILFLI KERSLPIGLS KLLDFSIKVS
TLQRTVDTEQ SFQVESSHFR VCLSPDSLLR LMWGAHKLLD LSHYYSRRHA
PNIWNTKMFT GKSDKSKEMP INFRSIHILS YKFCIGWIFQ YGAGSNPGLM
LGYNRLFSAY EKDFGKFTVV DAFFSVANGN TSSTFFSEGN EKDKYNRSFL
PNMQISYWFK RCGELKDWFF RFHGEALDVN FVPSFMDVIE STLQSMRAFQ
ELKKNILDVS ESLRAENDNS YASTSVESAS SSLAPFLDNI RSVNSNFKYD
GGVFRVYTYE DIETKSEPSF EIKSPVVTIN CTYKHDEDKV KPHKFRTLIT
VDPTHNTLYA GCAPLLMEFS ESLQKMIKKH STDEKPNFTK PSSQNVDYKR
LLDQFDVAVK LTSAKQQLSL SCEPKAKVQA DVGFESFLFS MATNEFDSEQ
PLEFSLTLEH TKASIKHIFS REVSTSFEVG FMDLTLLFTH PDVISMYGTG
LVSDLSVFFN VKQLQNLYLF LDIWRFSSIL HTRPVQRTVN KEIEMSSLTS
TNYADAGTEI PWCFTLIFTN VSGDVDLGPS LGMISLRTQR TWLATDHYNE
KRQLLHAFTD GISLTSEGRL SGLFEVANAS WLSEVKWPPE KSKNTHPLVS
TSLNIDDIAV KAAFDYHMFL IGTISNIHFH LHNEKDAKGV LPDLLQVSFS
SDEIILSSTA LVVANILDIY NTIVRMRQDN KISYMETLRD SNPGESRQPI
LYKDILRSLK LLRTDLSVNI SSSKVQISPI SLFDVEVLVI RIDKVSIRSE
THSGKKLKTD LQLQVLDVSA ALSTSKEELD EEVGASIAID DYMHYASKIV
GGTIIDIPKL AVHMTTLQEE KTNNLEYLFA CSFSDKISVR WNLGPVDFIK
EMWTTHVKAL AVRRSQVANI SFGQTEEELE ESIKKEEAAS KFNYIALEEP
QIEVPQIRDL GDATPPMEWF GVNRKKFPKF THQTAVIPVQ KLVYLAEKQY
VKILDDTH

Legend

  • X Phoshorylation
  • X Ubiquitination

Structure

No 3d structure was found in the AlphaFold Protein Structure Database.

References

[349, 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)
[349, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[359, 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)
[359, 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)
[359, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[451, 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)
[455, 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)
[457, 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)
[473, 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)
[473, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[708, 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)
[708, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[799, 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)
[799, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[812, 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)
[812, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[818, 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)
[818, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1181, 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)
[1181, 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)
[1181, 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)
[1181, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1183, 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)
[1183, 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)
[1183, 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)
[1183, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1304, 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)
[1841, 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)
[1841, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[2566, 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)